|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5238 |
| Enzyme 1 Name |
Hydroxymethylglutaryl-CoA lyase, mitochondrial |
| Enzyme 1 Synonyms |
- HL
- HMG-CoA lyase
- 3-hydroxy-3-methylglutarate-CoA lyase
|
| Enzyme 1 Gene Name |
HMGCL |
| Enzyme 1 Protein Sequence |
>Hydroxymethylglutaryl-CoA lyase, mitochondrial
MAAMRKALPRRLVGLASLRAVSTSSMGTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLI
DMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAG
AKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKI
SPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQ
ALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLL
EAGNFICQALNRKTSSKVAQATCKL
|
| Enzyme 1 Number of Residues |
325 |
| Enzyme 1 Molecular Weight |
34359.8 |
| Enzyme 1 Theoretical pI |
8.71 |
| Enzyme 1 GO Classification |
| Function |
- carbon-carbon lyase activity
- catalytic activity
- hydroxymethylglutaryl-CoA lyase activity
- lyase activity
- oxo-acid-lyase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in catalytic activity |
| Enzyme 1 Specific Function |
Involved in the catabolism of branched amino acids such as leucine (Probable) |
| Enzyme 1 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 1 Reactions |
- (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate [RN:R01360]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
14714839  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P35914  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
HMGCL_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>978 bp
ATGGCAGCAATGAGGAAGGCGCTTCCGCGGCGACTGGTGGGCTTGGCGTCCCTCCGGGCT
GTCAGCACCTCATCTATGGGCACTTTACCAAAGCGGGTGAAAATTGTGGAAGTTGGTCCC
CGAGATGGACTACAAAATGAAAAGAATATCGTATCTACTCCAGTGAAAATCAAGCTGATA
GACATGCTTTCTGAAGCAGGACTCTCTGTTATAGAAACCACCAGCTTTGTGTCTCCTAAG
TGGGTTCCCCAGATGGGTGACCACACTGAAGTCTTGAAGGGCATTCAGAAGTTTCCTGGC
ATCAACTACCCAGTCCTGACCCCAAATTTGAAAGGCTTCGAGGCAGCGGTTGCTGCTGGA
GCCAAGGAAGTAGTCATCTTTGGAGCTGCCTCAGAGCTCTTCACCAAGAAGAACATCAAT
TGTTCCATAGAGGAGAGTTTTCAGAGGTTTGACGCAATCCTGAAGGCAGCGCAGTCAGCC
AATATTTCTGTGCGGGGGTACGTCTCCTGTGCTCTTGGCTGCCCTTATGAAGGGAAGATC
TCCCCAGCTAAAGTAGCTGAGGTCACCAAGAAGTTCTACTCAATGGGCTGCTACGAGATC
TCCCTGGGGGACACCATTGGTGTGGGCACCCCAGGGATCATGAAAGACATGCTGTCTGCT
GTCATGCAGGAAGTGCCTCTGGCTGCCCTGGCTGTCCACTGCCATGACACCTATGGTCAA
GCCCTGGCCAACACCTTGATGGCCCTGCAGATGGGAGTGAGTGTCGTGGACTCTTCTGTG
GCAGGACTTGGAGGCTGTCCCTACGCACAGGGGGCATCAGGAAACTTGGCCACAGAAGAC
CTGGTCTACATGCTAGAGGGCTTGGGCATTCACACGGGTGTGAATCTCCAGAAGCTTCTG
GAAGCTGGAAACTTTATCTGTCAAGCCCTGAACAGAAAAACTAGCTCCAAAGTGGCTCAG
GCTACCTGTAAACTCTGA
|
| Enzyme 1 GenBank Gene ID |
BC010570  |
| Enzyme 1 GeneCard ID |
HMGCL  |
| Enzyme 1 GenAtlas ID |
HMGCL  |
| Enzyme 1 HGNC ID |
HGNC:5005  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1p36.1-p35 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Mitchell GA, Robert MF, Hruz PW, Wang S, Fontaine G, Behnke CE, Mende-Mueller LM, Schappert K, Lee C, Gibson KM, et al.: 3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency. J Biol Chem. 1993 Feb 25;268(6):4376-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wang SP, Robert MF, Gibson KM, Wanders RJ, Mitchell GA: 3-Hydroxy-3-methylglutaryl CoA lyase (HL): mouse and human HL gene (HMGCL) cloning and detection of large gene deletions in two unrelated HL-deficient patients. Genomics. 1996 Apr 1;33(1):99-104. [PubMed
]
- Tuinstra RL, Miziorko HM: Investigation of conserved acidic residues in 3-hydroxy-3-methylglutaryl-CoA lyase: implications for human disease and for functional roles in a family of related proteins. J Biol Chem. 2003 Sep 26;278(39):37092-8. Epub 2003 Jul 21. [PubMed
]
- Tuinstra RL, Wang CZ, Mitchell GA, Miziorko HM: Evaluation of 3-hydroxy-3-methylglutaryl-coenzyme A lyase arginine-41 as a catalytic residue: use of acetyldithio-coenzyme A to monitor product enolization. Biochemistry. 2004 May 11;43(18):5287-95. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Fu Z, Runquist JA, Forouhar F, Hussain M, Hunt JF, Miziorko HM, Kim JJ: Crystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria. J Biol Chem. 2006 Mar 17;281(11):7526-32. Epub 2005 Dec 5. [PubMed
]
- Roberts JR, Mitchell GA, Miziorko HM: Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue. J Biol Chem. 1996 Oct 4;271(40):24604-9. [PubMed
]
- Mitchell GA, Ozand PT, Robert MF, Ashmarina L, Roberts J, Gibson KM, Wanders RJ, Wang S, Chevalier I, Plochl E, Miziorko H: HMG CoA lyase deficiency: identification of five causal point mutations in codons 41 and 42, including a frequent Saudi Arabian mutation, R41Q. Am J Hum Genet. 1998 Feb;62(2):295-300. [PubMed
]
- Zapater N, Pie J, Lloberas J, Rolland MO, Leroux B, Vidailhet M, Divry P, Hegardt FG, Casals N: Two missense point mutations in different alleles in the 3-hydroxy-3-methylglutaryl coenzyme A lyase gene produce 3-hydroxy-3-methylglutaric aciduria in a French patient. Arch Biochem Biophys. 1998 Oct 15;358(2):197-203. [PubMed
]
- Muroi J, Yorifuji T, Uematsu A, Shigematsu Y, Onigata K, Maruyama H, Nobutoki T, Kitamura A, Nakahata T: Molecular and clinical analysis of Japanese patients with 3-hydroxy-3-methylglutaryl CoA lyase (HL) deficiency. Hum Genet. 2000 Oct;107(4):320-6. [PubMed
]
- Casals N, Gomez-Puertas P, Pie J, Mir C, Roca R, Puisac B, Aledo R, Clotet J, Menao S, Serra D, Asins G, Till J, Elias-Jones AC, Cresto JC, Chamoles NA, Abdenur JE, Mayatepek E, Besley G, Valencia A, Hegardt FG: Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase. J Biol Chem. 2003 Aug 1;278(31):29016-23. Epub 2003 May 13. [PubMed
]
- Mir C, Lopez-Vinas E, Aledo R, Puisac B, Rizzo C, Dionisi-Vici C, Deodato F, Pie J, Gomez-Puertas P, Hegardt FG, Casals N: A single-residue mutation, G203E, causes 3-hydroxy-3-methylglutaric aciduria by occluding the substrate channel in the 3D structural model of HMG-CoA lyase. J Inherit Metab Dis. 2006 Feb;29(1):64-70. [PubMed
]
- Carrasco P, Menao S, Lopez-Vinas E, Santpere G, Clotet J, Sierra AY, Gratacos E, Puisac B, Gomez-Puertas P, Hegardt FG, Pie J, Casals N: C-terminal end and aminoacid Lys48 in HMG-CoA lyase are involved in substrate binding and enzyme activity. Mol Genet Metab. 2007 Jun;91(2):120-7. Epub 2007 Apr 24. [PubMed
]
- Menao S, Lopez-Vinas E, Mir C, Puisac B, Gratacos E, Arnedo M, Carrasco P, Moreno S, Ramos M, Gil MC, Pie A, Ribes A, Perez-Cerda C, Ugarte M, Clayton PT, Korman SH, Serra D, Asins G, Ramos FJ, Gomez-Puertas P, Hegardt FG, Casals N, Pie J: Ten novel HMGCL mutations in 24 patients of different origin with 3-hydroxy-3-methyl-glutaric aciduria. Hum Mutat. 2009 Mar;30(3):E520-9. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5239 |
| Enzyme 2 Name |
ATP-citrate synthase |
| Enzyme 2 Synonyms |
- ATP-citrate (pro-S-)-lyase
- Citrate cleavage enzyme
|
| Enzyme 2 Gene Name |
ACLY |
| Enzyme 2 Protein Sequence |
>ATP-citrate synthase
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
|
| Enzyme 2 Number of Residues |
1101 |
| Enzyme 2 Molecular Weight |
120838.3 |
| Enzyme 2 Theoretical pI |
7.34 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- ATP citrate synthase activity
- CoA-ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleoside binding
- purine nucleoside binding
- succinate-CoA ligase (ADP-forming) activity
- succinate-CoA ligase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- carbohydrate metabolic process
- cellular carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 2 General Function |
Involved in ATP citrate synthase activity |
| Enzyme 2 Specific Function |
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA [RN:R00352]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
13623199  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P53396  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ACLY_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>3306 bp
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCAACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGTCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGAAGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGAGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCCTGGGC
CACCGGCCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTCCTCCTCAAC
GCCAGCGGGAGCACATCGACGCCAGCCCCCAGCAGGACAGCATCTTTTTCTGAGTCCAGG
GCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAAGATTCAGTCCCA
AGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCACACCAAGGCCATT
GTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGACTATGTCTGCTCC
CGAGACGAGCCCTCAGTGGCTGCCATGGTCTACCCTTTCACTGGGGACCACAAGCAGAAG
TTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATGGCTGATGCCATG
AGGAAGCATCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGCTCTGCCTATGAC
AGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATCATAGCTGAAGGC
ATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAGGGAGTGACCATC
ATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATTGGCAACACAGGT
GGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCGCCCAGGCAGCGTGGCCTATGTC
TCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGGACCACGGATGGC
GTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACATTCATGGATCAT
GTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTTGGAGAGATTGGG
GGCACTGAGGAATATAAGATTTGCCGGGGCATCAAGGAGGGCCGCCTCACTAAGCCCATC
GTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTCCAGTTTGGCCAT
GCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAACCAGGCTTTGAAG
GAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATCATCCAGTCTGTA
TACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTGCCGCCCCCAACC
GTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAACCTGCCTCGTTC
ATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGCATGCCCATCACT
GAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGTCCTCGGCCTCCTCTGGTTCCAGAAA
AGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTGACAGCTGATCAC
GGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGAGCTGGGAAAGACCTG
GTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGGGGTGCCTTGGAT
GCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCCATGGAGTTTGTG
AACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGAGTGAAGTCGATA
AACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAGCACTTCCCTGCC
ACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCGAAGAAGCCAAAT
CTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATGCTTAGAAACTGT
GGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCCCTCAATGGCATC
TTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAGAAGAGGCTGAAG
CAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCGGAACACATGAGC
ATGTAA
|
| Enzyme 2 GenBank Gene ID |
BC006195  |
| Enzyme 2 GeneCard ID |
ACLY  |
| Enzyme 2 GenAtlas ID |
ACLY  |
| Enzyme 2 HGNC ID |
HGNC:115  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
17q21.2 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed
]
- Lord KA, Wang XM, Simmons SJ, Bruckner RC, Loscig J, O'Connor B, Bentley R, Smallwood A, Chadwick CC, Stevis PE, Ciccarelli RB: Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells. Protein Expr Purif. 1997 Feb;9(1):133-41. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5240 |
| Enzyme 3 Name |
Histone acetyltransferase p300 |
| Enzyme 3 Synonyms |
- p300 HAT
- E1A-associated protein p300
|
| Enzyme 3 Gene Name |
EP300 |
| Enzyme 3 Protein Sequence |
>Histone acetyltransferase p300
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGD
INQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINS
MVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAA
GNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQ
PLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMP
NMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGE
VRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNA
GDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQM
PTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQ
NPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAAL
KDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPN
AAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSM
AQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNI
PLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTP
TPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPS
LPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSST
EVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELK
TEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVD
PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYK
YCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHF
CEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVL
HHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGE
VTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQE
YGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPP
SEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKE
LPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNK
SSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIP
CDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETR
WHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQ
SLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENK
CPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTG
QQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPG
PPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHL
EPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISP
LKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPI
PGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGG
MSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYP
PQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSP
QQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHV
SPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNS
DLNSNLSQSTLDIH
|
| Enzyme 3 Number of Residues |
2414 |
| Enzyme 3 Molecular Weight |
264159.7 |
| Enzyme 3 Theoretical pI |
8.59 |
| Enzyme 3 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cation binding
- histone acetyltransferase activity
- ion binding
- lysine N-acetyltransferase activity
- metal ion binding
- protein binding
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- covalent chromatin modification
- histone acetylation
- histone modification
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- histone acetyltransferase complex
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- nucleus
- organelle
- protein complex
|
|
| Enzyme 3 General Function |
Involved in transcription cofactor activity |
| Enzyme 3 Specific Function |
Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
56202870  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q09472  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
EP300_HUMAN  |
| Enzyme 3 PDB ID |
1JSP  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>7245 bp
ATGGCCGAGAATGTGGTGGAACCGGGGCCGCCTTCAGCCAAGCGGCCTAAACTCTCATCT
CCGGCCCTCTCGGCGTCCGCCAGCGATGGCACAGATTTTGGCTCTCTATTTGACTTGGAG
CACGACTTACCAGATGAATTAATCAACTCTACAGAATTGGGACTAACCAATGGTGGTGAT
ATTAATCAGCTTCAGACAAGTCTTGGCATGGTACAAGATGCAGCTTCTAAACATAAACAG
CTGTCAGAATTGCTGCGATCTGGTAGTTCCCCTAACCTCAATATGGGAGTTGGTGGCCCA
GGTCAAGTCATGGCCAGCCAGGCCCAACAGAGCAGTCCTGGATTAGGTTTGATAAATAGC
ATGGTCAAAAGCCCAATGACACAGGCAGGCTTGACTTCTCCCAACATGGGGATGGGCACT
AGTGGACCAAATCAGGGTCCTACGCAGTCAACAGGTATGATGAACAGTCCAGTAAATCAG
CCTGCCATGGGAATGAACACAGGGATGAATGCGGGCATGAATCCTGGAATGTTGGCTGCA
GGCAATGGACAAGGGATAATGCCTAATCAAGTCATGAACGGTTCAATTGGAGCAGGCCGA
GGGCGACAGAATATGCAGTACCCAAACCCAGGCATGGGAAGTGCTGGCAACTTACTGACT
GAGCCTCTTCAGCAGGGCTCTCCCCAGATGGGAGGACAAACAGGATTGAGAGGCCCCCAG
CCTCTTAAGATGGGAATGATGAACAACCCCAATCCTTATGGTTCACCATATACTCAGAAT
CCTGGACAGCAGATTGGAGCCAGTGGCCTTGGTCTCCAGATTCAGACAAAAACTGTACTA
TCAAATAACTTATCTCCATTTGCTATGGACAAAAAGGCAGTTCCTGGTGGAGGAATGCCC
AACATGGGTCAACAGCCAGCCCCGCAGGTCCAGCAGCCAGGCCTGGTGACTCCAGTTGCC
CAAGGGATGGGTTCTGGAGCACATACAGCTGATCCAGAGAAGCGCAAGCTCATCCAGCAG
CAGCTTGTTCTCCTTTTGCATGCTCACAAGTGCCAGCGCCGGGAACAGGCCAATGGGGAA
GTGAGGCAGTGCAACCTTCCCCACTGTCGCACAATGAAGAATGTCCTAAACCACATGACA
CACTGCCAGTCAGGCAAGTCTTGCCAAGTGGCACACTGTGCATCTTCTCGACAAATCATT
TCACACTGGAAGAATTGTACAAGACATGATTGTCCTGTGTGTCTCCCCCTCAAAAATGCT
GGTGATAAGAGAAATCAACAGCCAATTTTGACTGGAGCACCCGTTGGACTTGGAAATCCT
AGCTCTCTAGGGGTGGGTCAACAGTCTGCCCCCAACCTAAGCACTGTTAGTCAGATTGAT
CCCAGCTCCATAGAAAGAGCCTATGCAGCTCTTGGACTACCCTATCAAGTAAATCAGATG
CCGACACAACCCCAGGTGCAAGCAAAGAACCAGCAGAATCAGCAGCCTGGGCAGTCTCCC
CAAGGCATGCGGCCCATGAGCAACATGAGTGCTAGTCCTATGGGAGTAAATGGAGGTGTA
GGAGTTCAAACGCCGAGTCTTCTTTCTGACTCAATGTTGCATTCAGCCATAAATTCTCAA
AACCCAATGATGAGTGAAAATGCCAGTGTGCCCTCCCTGGGTCCTATGCCAACAGCAGCT
CAACCATCCACTACTGGAATTCGGAAACAGTGGCACGAAGATATTACTCAGGATCTTCGA
AATCATCTTGTTCACAAACTCGTCCAAGCCATATTTCCTACGCCGGATCCTGCTGCTTTA
AAAGACAGACGGATGGAAAACCTAGTTGCATATGCTCGGAAAGTTGAAGGGGACATGTAT
GAATCTGCAAACAATCGAGCGGAATACTACCACCTTCTAGCTGAGAAAATCTATAAGATC
CAGAAAGAACTAGAAGAAAAACGAAGGACCAGACTACAGAAGCAGAACATGCTACCAAAT
GCTGCAGGCATGGTTCCAGTTTCCATGAATCCAGGGCCTAACATGGGACAGCCGCAACCA
GGAATGACTTCTAATGGCCCTCTACCTGACCCAAGTATGATCCGTGGCAGTGTGCCAAAC
CAGATGATGCCTCGAATAACTCCACAATCTGGTTTGAATCAATTTGGCCAGATGAGCATG
GCCCAGCCCCCTATTGTACCCCGGCAAACCCCTCCTCTTCAGCACCATGGACAGTTGGCT
CAACCTGGAGCTCTCAACCCGCCTATGGGCTATGGGCCTCGTATGCAACAGCCTTCCAAC
CAGGGCCAGTTCCTTCCTCAGACTCAGTTCCCATCACAGGGAATGAATGTAACAAATATC
CCTTTGGCTCCGTCCAGCGGTCAAGCTCCAGTGTCTCAAGCACAAATGTCTAGTTCTTCC
TGCCCGGTGAACTCTCCTATAATGCCTCCAGGGTCTCAGGGGAGCCACATTCACTGTCCC
CAGCTTCCTCAACCAGCTCTTCATCAGAATTCACCCTCGCCTGTACCTAGTCGTACCCCC
ACCCCTCACCATACTCCCCCAAGCATAGGGGCTCAGCAGCCACCAGCAACAACAATTCCA
GCCCCTGTTCCTACACCTCCTGCCATGCCACCTGGGCCACAGTCCCAGGCTCTACATCCC
CCTCCAAGGCAGACACCTACACCACCAACAACACAACTTCCCCAACAAGTGCAGCCTTCA
CTTCCTGCTGCACCTTCTGCTGACCAGCCCCAGCAGCAGCCTCGCTCACAGCAGAGCACA
GCAGCGTCTGTTCCTACCCCAACAGCACCGCTGCTTCCTCCGCAGCCTGCAACTCCACTT
TCCCAGCCAGCTGTAAGCATTGAAGGACAGGTATCAAATCCTCCATCTACTAGTAGCACA
GAAGTGAATTCTCAGGCCATTGCTGAGAAGCAGCCTTCCCAGGAAGTGAAGATGGAGGCC
AAAATGGAAGTGGATCAACCAGAACCAGCAGATACTCAGCCGGAGGATATTTCAGAGTCT
AAAGTGGAAGACTGTAAAATGGAATCTACCGAAACAGAAGAGAGAAGCACTGAGTTAAAA
ACTGAAATAAAAGAGGAGGAAGACCAGCCAAGTACTTCAGCTACCCAGTCATCTCCGGCT
CCAGGACAGTCAAAGAAAAAGATTTTCAAACCAGAAGAACTACGACAGGCACTGATGCCA
ACTTTGGAGGCACTTTACCGTCAGGATCCAGAATCCCTTCCCTTTCGTCAACCTGTGGAC
CCTCAGCTTTTAGGAATCCCTGATTACTTTGATATTGTGAAGAGCCCCATGGATCTTTCT
ACCATTAAGAGGAAGTTAGACACTGGACAGTATCAGGAGCCCTGGCAGTATGTCGATGAT
ATTTGGCTTATGTTCAATAATGCCTGGTTATATAACCGGAAAACATCACGGGTATACAAA
TACTGCTCCAAGCTCTCTGAGGTCTTTGAACAAGAAATTGACCCAGTGATGCAAAGCCTT
GGATACTGTTGTGGCAGAAAGTTGGAGTTCTCTCCACAGACACTGTGTTGCTACGGCAAA
CAGTTGTGCACAATACCTCGTGATGCCACTTATTACAGTTACCAGAACAGGTATCATTTC
TGTGAGAAGTGTTTCAATGAGATCCAAGGGGAGAGCGTTTCTTTGGGGGATGACCCTTCC
CAGCCTCAAACTACAATAAATAAAGAACAATTTTCCAAGAGAAAAAATGACACACTGGAT
CCTGAACTGTTTGTTGAATGTACAGAGTGCGGAAGAAAGATGCATCAGATCTGTGTCCTT
CACCATGAGATCATCTGGCCTGCTGGATTCGTCTGTGATGGCTGTTTAAAGAAAAGTGCA
CGAACTAGGAAAGAAAATAAGTTTTCTGCTAAAAGGTTGCCATCTACCAGACTTGGCACC
TTTCTAGAGAATCGTGTGAATGACTTTCTGAGGCGACAGAATCACCCTGAGTCAGGAGAG
GTCACTGTTAGAGTAGTTCATGCTTCTGACAAAACCGTGGAAGTAAAACCAGGCATGAAA
GCAAGGTTTGTGGACAGTGGAGAGATGGCAGAATCCTTTCCATACCGAACCAAAGCCCTC
TTTGCCTTTGAAGAAATTGATGGTGTTGACCTGTGCTTCTTTGGCATGCATGTTCAAGAG
TATGGCTCTGACTGCCCTCCACCCAACCAGAGGAGAGTATACATATCTTACCTCGATAGT
GTTCATTTCTTCCGTCCTAAATGCTTGAGGACTGCAGTCTATCATGAAATCCTAATTGGA
TATTTAGAATATGTCAAGAAATTAGGTTACACAACAGGGCATATTTGGGCATGTCCACCA
AGTGAGGGAGATGATTATATCTTCCATTGCCATCCTCCTGACCAGAAGATACCCAAGCCC
AAGCGACTGCAGGAATGGTACAAAAAAATGCTTGACAAGGCTGTATCAGAGCGTATTGTC
CATGACTACAAGGATATTTTTAAACAAGCTACTGAAGATAGATTAACAAGTGCAAAGGAA
TTGCCTTATTTCGAGGGTGATTTCTGGCCCAATGTTCTGGAAGAAAGCATTAAGGAACTG
GAACAGGAGGAAGAAGAGAGAAAACGAGAGGAAAACACCAGCAATGAAAGCACAGATGTG
ACCAAGGGAGACAGCAAAAATGCTAAAAAGAAGAATAATAAGAAAACCAGCAAAAATAAG
AGCAGCCTGAGTAGGGGCAACAAGAAGAAACCCGGGATGCCCAATGTATCTAACGACCTC
TCACAGAAACTATATGCCACCATGGAGAAGCATAAAGAGGTCTTCTTTGTGATCCGCCTC
ATTGCTGGCCCTGCTGCCAACTCCCTGCCTCCCATTGTTGATCCTGATCCTCTCATCCCC
TGCGATCTGATGGATGGTCGGGATGCGTTTCTCACGCTGGCAAGGGACAAGCACCTGGAG
TTCTCTTCACTCCGAAGAGCCCAGTGGTCCACCATGTGCATGCTGGTGGAGCTGCACACG
CAGAGCCAGGACCGCTTTGTCTACACCTGCAATGAATGCAAGCACCATGTGGAGACACGC
TGGCACTGTACTGTCTGTGAGGATTATGACTTGTGTATCACCTGCTATAACACTAAAAAC
CATGACCACAAAATGGAGAAACTAGGCCTTGGCTTAGATGATGAGAGCAACAACCAGCAG
GCTGCAGCCACCCAGAGCCCAGGCGATTCTCGCCGCCTGAGTATCCAGCGCTGCATCCAG
TCTCTGGTCCATGCTTGCCAGTGTCGGAATGCCAATTGCTCACTGCCATCCTGCCAGAAG
ATGAAGCGGGTTGTGCAGCATACCAAGGGTTGCAAACGGAAAACCAATGGCGGGTGCCCC
ATCTGCAAGCAGCTCATTGCCCTCTGCTGCTACCATGCCAAGCACTGCCAGGAGAACAAA
TGCCCGGTGCCGTTCTGCCTAAACATCAAGCAGAAGCTCCGGCAGCAACAGCTGCAGCAC
CGACTACAGCAGGCCCAAATGCTTCGCAGGAGGATGGCCAGCATGCAGCGGACTGGTGTG
GTTGGGCAGCAACAGGGCCTCCCTTCCCCCACTCCTGCCACTCCAACGACACCAACTGGC
CAACAGCCAACCACCCCGCAGACGCCCCAGCCCACTTCTCAGCCTCAGCCTACCCCTCCC
AATAGCATGCCACCCTACTTGCCCAGGACTCAAGCTGCTGGCCCTGTGTCCCAGGGTAAG
GCAGCAGGCCAGGTGACCCCTCCAACCCCTCCTCAGACTGCTCAGCCACCCCTTCCAGGG
CCCCCACCTGCAGCAGTGGAAATGGCAATGCAGATTCAGAGAGCAGCGGAGACGCAGCGC
CAGATGGCCCACGTGCAAATTTTTCAAAGGCCAATCCAACACCAGATGCCCCCGATGACT
CCCATGGCCCCCATGGGTATGAACCCACCTCCCATGACCAGAGGTCCCAGTGGGCATTTG
GAGCCAGGGATGGGACCGACAGGGATGCAGCAACAGCCACCCTGGAGCCAAGGAGGATTG
CCTCAGCCCCAGCAACTACAGTCTGGGATGCCAAGGCCAGCCATGATGTCAGTGGCCCAG
CATGGTCAACCTTTGAACATGGCTCCACAACCAGGATTGGGCCAGGTAGGTATCAGCCCA
CTCAAACCAGGCACTGTGTCTCAACAAGCCTTACAAAACCTTTTGCGGACTCTCAGGTCT
CCCAGCTCTCCCCTGCAGCAGCAACAGGTGCTTAGTATCCTTCACGCCAACCCCCAGCTG
TTGGCTGCATTCATCAAGCAGCGGGCTGCCAAGTATGCCAACTCTAATCCACAACCCATC
CCTGGGCAGCCTGGCATGCCCCAGGGGCAGCCAGGGCTACAGCCACCTACCATGCCAGGT
CAGCAGGGGGTCCACTCCAATCCAGCCATGCAGAACATGAATCCAATGCAGGCGGGCGTT
CAGAGGGCTGGCCTGCCCCAGCAGCAACCACAGCAGCAACTCCAGCCACCCATGGGAGGG
ATGAGCCCCCAGGCTCAGCAGATGAACATGAACCACAACACCATGCCTTCACAATTCCGA
GACATCTTGAGACGACAGCAAATGATGCAACAGCAGCAGCAACAGGGAGCAGGGCCAGGA
ATAGGCCCTGGAATGGCCAACCATAACCAGTTCCAGCAACCCCAAGGAGTTGGCTACCCA
CCACAGCAGCAGCAGCGGATGCAGCATCACATGCAACAGATGCAACAAGGAAATATGGGA
CAGATAGGCCAGCTTCCCCAGGCCTTGGGAGCAGAGGCAGGTGCCAGTCTACAGGCCTAT
CAGCAGCGACTCCTTCAGCAACAGATGGGGTCCCCTGTTCAGCCCAACCCCATGAGCCCC
CAGCAGCATATGCTCCCAAATCAGGCCCAGTCCCCACACCTACAAGGCCAGCAGATCCCT
AATTCTCTCTCCAATCAAGTGCGCTCTCCCCAGCCTGTCCCTTCTCCACGGCCACAGTCC
CAGCCCCCCCACTCCAGTCCTTCCCCAAGGATGCAGCCTCAGCCTTCTCCACACCACGTT
TCCCCACAGACAAGTTCCCCACATCCTGGACTGGTAGCTGCCCAGGCCAACCCCATGGAA
CAAGGGCATTTTGCCAGCCCGGACCAGAATTCAATGCTTTCTCAGCTTGCTAGCAATCCA
GGCATGGCAAACCTCCATGGTGCAAGCGCCACGGACCTGGGACTCAGCACCGATAACTCA
GACTTGAATTCAAACCTCTCACAGAGTACACTAGACATACACTAG
|
| Enzyme 3 GenBank Gene ID |
AL035658  |
| Enzyme 3 GeneCard ID |
EP300  |
| Enzyme 3 GenAtlas ID |
EP300  |
| Enzyme 3 HGNC ID |
HGNC:3373  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
22q13.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM: Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 1994 Apr 15;8(8):869-84. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Chaffanet M, Gressin L, Preudhomme C, Soenen-Cornu V, Birnbaum D, Pebusque MJ: MOZ is fused to p300 in an acute monocytic leukemia with t(8;22). Genes Chromosomes Cancer. 2000 Jun;28(2):138-44. [PubMed
]
- Lundblad JR, Kwok RP, Laurance ME, Harter ML, Goodman RH: Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature. 1995 Mar 2;374(6517):85-8. [PubMed
]
- Xu W, Chen H, Du K, Asahara H, Tini M, Emerson BM, Montminy M, Evans RM: A transcriptional switch mediated by cofactor methylation. Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8. [PubMed
]
- Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed
]
- Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed
]
- Arany Z, Huang LE, Eckner R, Bhattacharya S, Jiang C, Goldberg MA, Bunn HF, Livingston DM: An essential role for p300/CBP in the cellular response to hypoxia. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12969-73. [PubMed
]
- Bex F, Yin MJ, Burny A, Gaynor RB: Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300. Mol Cell Biol. 1998 Apr;18(4):2392-405. [PubMed
]
- Fryer CJ, Archer TK: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91. [PubMed
]
- Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, Maudoux F, Calomme C, Burny A, Nakatani Y, Jeang KT, Benkirane M, Van Lint C: HIV-1 tat transcriptional activity is regulated by acetylation. EMBO J. 1999 Nov 1;18(21):6106-18. [PubMed
]
- Miyake S, Sellers WR, Safran M, Li X, Zhao W, Grossman SR, Gan J, DeCaprio JA, Adams PD, Kaelin WG Jr: Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle. Mol Cell Biol. 2000 Dec;20(23):8889-902. [PubMed
]
- MacLellan WR, Xiao G, Abdellatif M, Schneider MD: A novel Rb- and p300-binding protein inhibits transactivation by MyoD. Mol Cell Biol. 2000 Dec;20(23):8903-15. [PubMed
]
- Ko L, Cardona GR, Chin WW: Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc Natl Acad Sci U S A. 2000 May 23;97(11):6212-7. [PubMed
]
- Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F: Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. Virology. 2000 Nov 25;277(2):278-95. [PubMed
]
- Xu X, Chackalaparampil I, Monroy MA, Cannella MT, Pesek E, Chrivia J, Yaciuk P: Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription. J Virol. 2001 Nov;75(21):10033-40. [PubMed
]
- Scoggin KE, Ulloa A, Nyborg JK: The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation. Mol Cell Biol. 2001 Aug;21(16):5520-30. [PubMed
]
- Zhang W, Nisbet JW, Albrecht B, Ding W, Kashanchi F, Bartoe JT, Lairmore MD: Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300. J Virol. 2001 Oct;75(20):9885-95. [PubMed
]
- Gizard F, Lavallee B, DeWitte F, Hum DW: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. J Biol Chem. 2001 Sep 7;276(36):33881-92. Epub 2001 May 10. [PubMed
]
- Vadlamudi RK, Wang RA, Mazumdar A, Kim Y, Shin J, Sahin A, Kumar R: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. J Biol Chem. 2001 Oct 12;276(41):38272-9. Epub 2001 Jul 31. [PubMed
]
- Yamamoto N, Yamamoto S, Inagaki F, Kawaichi M, Fukamizu A, Kishi N, Matsuno K, Nakamura K, Weinmaster G, Okano H, Nakafuku M: Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor. J Biol Chem. 2001 Nov 30;276(48):45031-40. Epub 2001 Sep 19. [PubMed
]
- Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hubscher U, Hottiger MO: Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol Cell. 2001 Jun;7(6):1221-31. [PubMed
]
- Yamamoto H, Kihara-Negishi F, Yamada T, Suzuki M, Nakano T, Oikawa T: Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb. Cell Growth Differ. 2002 Feb;13(2):69-75. [PubMed
]
- Braganca J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S: Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. J Biol Chem. 2002 Mar 8;277(10):8559-65. Epub 2001 Dec 14. [PubMed
]
- Lee YH, Koh SS, Zhang X, Cheng X, Stallcup MR: Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities. Mol Cell Biol. 2002 Jun;22(11):3621-32. [PubMed
]
- Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC: p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity. Cancer Res. 2003 May 15;63(10):2373-8. [PubMed
]
- Hecht A, Stemmler MP: Identification of a promoter-specific transcriptional activation domain at the C terminus of the Wnt effector protein T-cell factor 4. J Biol Chem. 2003 Feb 7;278(6):3776-85. Epub 2002 Nov 22. [PubMed
]
- Ammanamanchi S, Freeman JW, Brattain MG: Acetylated sp3 is a transcriptional activator. J Biol Chem. 2003 Sep 12;278(37):35775-80. Epub 2003 Jun 30. [PubMed
]
- Fujii Y, Kumatori A, Nakamura M: SATB1 makes a complex with p300 and represses gp91(phox) promoter activity. Microbiol Immunol. 2003;47(10):803-11. [PubMed
]
- An W, Kim J, Roeder RG: Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell. 2004 Jun 11;117(6):735-48. [PubMed
]
- Thevenet L, Mejean C, Moniot B, Bonneaud N, Galeotti N, Aldrian-Herrada G, Poulat F, Berta P, Benkirane M, Boizet-Bonhoure B: Regulation of human SRY subcellular distribution by its acetylation/deacetylation. EMBO J. 2004 Aug 18;23(16):3336-45. Epub 2004 Aug 5. [PubMed
]
- Wang H, Fang R, Cho JY, Libermann TA, Oettgen P: Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86. J Biol Chem. 2004 Jun 11;279(24):25241-50. Epub 2004 Apr 8. [PubMed
]
- Thompson PR, Wang D, Wang L, Fulco M, Pediconi N, Zhang D, An W, Ge Q, Roeder RG, Wong J, Levrero M, Sartorelli V, Cotter RJ, Cole PA: Regulation of the p300 HAT domain via a novel activation loop. Nat Struct Mol Biol. 2004 Apr;11(4):308-15. Epub 2004 Mar 7. [PubMed
]
- Aizawa H, Hu SC, Bobb K, Balakrishnan K, Ince G, Gurevich I, Cowan M, Ghosh A: Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. Science. 2004 Jan 9;303(5655):197-202. [PubMed
]
- Roelfsema JH, White SJ, Ariyurek Y, Bartholdi D, Niedrist D, Papadia F, Bacino CA, den Dunnen JT, van Ommen GJ, Breuning MH, Hennekam RC, Peters DJ: Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease. Am J Hum Genet. 2005 Apr;76(4):572-80. Epub 2005 Feb 10. [PubMed
]
- Lee YH, Coonrod SA, Kraus WL, Jelinek MA, Stallcup MR: Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3611-6. Epub 2005 Feb 24. [PubMed
]
- Karanam B, Jiang L, Wang L, Kelleher NL, Cole PA: Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation. J Biol Chem. 2006 Dec 29;281(52):40292-301. Epub 2006 Oct 25. [PubMed
]
- Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed
]
- Hung JJ, Wang YT, Chang WC: Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol Cell Biol. 2006 Mar;26(5):1770-85. [PubMed
]
- Shima Y, Shima T, Chiba T, Irimura T, Pandolfi PP, Kitabayashi I: PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation. Mol Cell Biol. 2008 Dec;28(23):7126-38. Epub 2008 Sep 22. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Huang C, Han Y, Wang Y, Sun X, Yan S, Yeh ET, Chen Y, Cang H, Li H, Shi G, Cheng J, Tang X, Yi J: SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation. EMBO J. 2009 Sep 16;28(18):2748-62. Epub 2009 Aug 13. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ: Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72. [PubMed
]
- Liu X, Wang L, Zhao K, Thompson PR, Hwang Y, Marmorstein R, Cole PA: The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature. 2008 Feb 14;451(7180):846-50. [PubMed
]
- Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y: Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation. Structure. 2009 Feb 13;17(2):202-10. [PubMed
]
- Gayther SA, Batley SJ, Linger L, Bannister A, Thorpe K, Chin SF, Daigo Y, Russell P, Wilson A, Sowter HM, Delhanty JD, Ponder BA, Kouzarides T, Caldas C: Mutations truncating the EP300 acetylase in human cancers. Nat Genet. 2000 Mar;24(3):300-3. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5241 |
| Enzyme 4 Name |
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial |
| Enzyme 4 Synonyms |
- PDHE1-B
|
| Enzyme 4 Gene Name |
PDHB |
| Enzyme 4 Protein Sequence |
>Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEV
AQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAI
DQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNS
EDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVV
SHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFG
VGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
|
| Enzyme 4 Number of Residues |
359 |
| Enzyme 4 Molecular Weight |
39233.1 |
| Enzyme 4 Theoretical pI |
6.63 |
| Enzyme 4 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in catalytic activity |
| Enzyme 4 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 [RN:R01699]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
189053605  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P11177  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ODPB_HUMAN  |
| Enzyme 4 PDB ID |
1NI4  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1080 bp
ATGGCGGCGGTGTCTGGCTTGGTGCGGAGACCCCTTCGGGAGGTCTCCGGGCTGCTGAAG
AGGCGCTTTCACTGGACCGCGCCGGCTGCGCTGCAGGTGACAGTTCGTGATGCTATAAAT
CAGGGTATGGATGAGGAGCTGGAAAGAGATGAGAAGGTATTTCTGCTTGGAGAAGAAGTT
GCCCAGTATGATGGGGCATACAAGGTTAGTCGAGGGCTGTGGAAGAAATATGGAGACAAG
AGGATTATTGACACTCCCATATCAGAGATGGGCTTTGCTGGAATTGCTGTAGGTGCAGCT
ATGGCTGGGTTGCGGCCCATTTGTGAATTTATGACCTTCAATTTCTCCATGCAAGCCATT
GACCAGGTTATAAACTCAGCTGCCAAGACCTACTACATGTCTGGTGGCCTTCAGCCTGTG
CCTATAGTCTTCAGGGGGCCCAATGGTGCCTCAGCAGGTGTAGCTGCCCAGCACTCACAG
TGCTTTGCTGCCTGGTATGGGCACTGCCCAGGCTTAAAGGTGGTCAGTCCCTGGAATTCA
GAGGATGCTAAAGGACTTATTAAATCAGCCATTCGGGATAACAATCCAGTGGTGGTGCTA
GAGAATGAATTGATGTATGGGGTTCCTTTTGAATTTCCTCCGGAAGCTCAGTCAAAAGAT
TTTCTGATTCCTATTGGAAAAGCCAAAATAGAAAGGCAAGGAACACATATAACTGTGGTT
TCCCATTCAAGACCTGTGGGCCACTGCTTAGAAGCTGCAGCAGTGCTATCTAAAGAAGGA
GTTGAATGTGAGGTGATAAATATGCGTACCATTAGACCAATGGACATGGAAACCATAGAA
GCCAGTGTCATGAAGACAAATCATCTTGTAACTGTGGAAGGAGGCTGGCCACAGTTTGGA
GTAGGAGCTGAAATCTGTGCCAGGATCATGGAAGGTCCTGCGTTCAATTTCCTGGATGCT
CCTGCTGTTCGTGTCACTGGTGCTGATGTCCCTATGCCTTATGCAAAGATTCTAGAGGAC
AACTCTATACCTCAGGTCAAAGACATCATATTTGCAATAAAGAAAACATTAAATATTTAG
|
| Enzyme 4 GenBank Gene ID |
AK313022  |
| Enzyme 4 GeneCard ID |
PDHB  |
| Enzyme 4 GenAtlas ID |
PDHB  |
| Enzyme 4 HGNC ID |
HGNC:8808  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3p21.1-p14.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Ho L, Patel MS: Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex. Gene. 1990 Feb 14;86(2):297-302. [PubMed
]
- Chun K, Mackay N, Willard HF, Robinson BH: Isolation, characterization and chromosomal localization of cDNA clones for the E1 beta subunit of the pyruvate dehydrogenase complex. Eur J Biochem. 1990 Dec 12;194(2):587-92. [PubMed
]
- Huh TL, Casazza JP, Huh JW, Chi YT, Song BJ: Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast. J Biol Chem. 1990 Aug 5;265(22):13320-6. [PubMed
]
- Koike K, Urata Y, Koike M: Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene. Proc Natl Acad Sci U S A. 1990 Aug;87(15):5594-7. [PubMed
]
- Koike K, Ohta S, Urata Y, Kagawa Y, Koike M: Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):41-5. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ho L, Javed AA, Pepin RA, Thekkumkara TJ, Raefsky C, Mole JE, Caliendo AM, Kwon MS, Kerr DS, Patel MS: Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex. Biochem Biophys Res Commun. 1988 Feb 15;150(3):904-8. [PubMed
]
- Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65. [PubMed
]
- Muno D, Kominami E, Ishii H, Usui K, Saifuku K, Sakakibara Y, Namihisa T: Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis. Hepatology. 1990 Jan;11(1):16-23. [PubMed
]
- Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS: Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. [PubMed
]
- Brown RM, Head RA, Boubriak II, Leonard JV, Thomas NH, Brown GK: Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency. Hum Genet. 2004 Jul;115(2):123-7. Epub 2004 May 11. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5242 |
| Enzyme 5 Name |
Acetyl-CoA acetyltransferase, cytosolic |
| Enzyme 5 Synonyms |
- Acetyl-CoA transferase-like protein
- Cytosolic acetoacetyl-CoA thiolase
|
| Enzyme 5 Gene Name |
ACAT2 |
| Enzyme 5 Protein Sequence |
>Acetyl-CoA acetyltransferase, cytosolic
MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHV
LAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGME
NMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDK
VAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT
DGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPA
IKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGC
RILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE
|
| Enzyme 5 Number of Residues |
397 |
| Enzyme 5 Molecular Weight |
41350.5 |
| Enzyme 5 Theoretical pI |
6.92 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 5 Specific Function |
2 acetyl-CoA = CoA + acetoacetyl-CoA |
| Enzyme 5 Pathways |
- Benzoate Degradation via CoA Ligation (map00632
)
- Butyrate Metabolism (map00650
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Lysine Degradation (map00310
)
- Propanoate Metabolism (map00640
)
- Pyruvate Metabolism (map00620
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Tryptophan Metabolism (map00380
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 5 Reactions |
- 2 acetyl-CoA = CoA + acetoacetyl-CoA [RN:R00238]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
19880019  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9BWD1  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
THIC_HUMAN  |
| Enzyme 5 PDB ID |
1WL5  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1194 bp
ATGAATGCAGGCTCAGATCCTGTGGTCATCGTCTCGGCGGCGCGGACCATCATAGGTTCC
TTCAATGGTGCCTTAGCTGCTGTTCCTGTCCAGGACCTGGGCTCCACTGTCATCAAAGAA
GTCTTGAAGAGGGCCACTGTGGCTCCGGAAGATGTGTCTGAGGTCATCTTTGGACATGTC
TTGGCAGCAGGCTGTGGGCAGAATCCTGTTAGACAAGCCAGTGTGGGTGCAGGAATTCCC
TACTCTGTTCCAGCATGGAGCTGCCAGATGATCTGTGGGTCAGGCCTAAAAGCTGTGTGC
CTTGCAGTCCAGTCAATAGGGATAGGAGACTCCAGCATTGTGGTTGCAGGAGGCATGGAA
AATATGAGCAAGGCTCCTCACTTGGCTTACTTGAGAACAGGAGTAAAGATAGGTGAGATG
CCACTGACTGACAGTATACTCTGTGATGGTCTTACAGATGCATTTCACAACTGTCATATG
GGTATTACAGCTGAAAATGTAGCCAAAAAATGGCAAGTGAGTAGAGAAGATCAGGACAAG
GTTGCAGTTCTGTCCCAGAACAGGACAGAGAATGCACAGAAAGCTGGCCATTTTGACAAA
GAGATTGTACCAGTTTTGGTGTCAACTAGAAAAGGTCTTATTGAAGTTAAAACAGATGAG
TTTCCTCGCCATGGGAGCAACATAGAAGCCATGTCCAAGCTAAAGCCTTACTTTCTTACT
GATGGAACGGGAACAGTCACCCCAGCCAATGCTTCAGGAATAAATGATGGTGCTGCAGCT
GTCGTTCTTATGAAGAAGTCAGAAGCTGATAAACGTGGGCTTACACCTTTAGCACGGATA
GTTTCCTGGTCCCAAGTGGGTGTGGAGCCTTCCATTATGGGAATAGGACCAATTCCAGCC
ATAAAGCAAGCTGTTACAAAAGCAGGTTGGTCACTGGAAGATGTTGACATATTTGAAATC
AATGAAGCCTTTGCAGCTGTCTCTGCTGCAATAGTTAAAGAACTTGGATTAAACCCAGAG
AAGGTCAATATTGAAGGAGGGGCTATAGCCTTGGGCCACCCTCTTGGAGCATCTGGCTGT
CGAATTCTTGTGACCCTGTTACACACACTGGAGAGAATGGGCGGAAGTCGTGGTGTTGCA
GCCCTGTGCATTGGGGGTGGGATGGGAATAGCAATGTGTGTTCAGAGAGAATGA
|
| Enzyme 5 GenBank Gene ID |
AF356877  |
| Enzyme 5 GeneCard ID |
ACAT2  |
| Enzyme 5 GenAtlas ID |
ACAT2  |
| Enzyme 5 HGNC ID |
HGNC:94  |
| Enzyme 5 Chromosome Location |
6 |
| Enzyme 5 Locus |
6q25.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Song XQ, Fukao T, Yamaguchi S, Miyazawa S, Hashimoto T, Orii T: Molecular cloning and nucleotide sequence of complementary DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase. Biochem Biophys Res Commun. 1994 May 30;201(1):478-85. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Kursula P, Sikkila H, Fukao T, Kondo N, Wierenga RK: High resolution crystal structures of human cytosolic thiolase (CT): a comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I. J Mol Biol. 2005 Mar 18;347(1):189-201. Epub 2005 Jan 19. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5244 |
| Enzyme 6 Name |
Diamine acetyltransferase 2 |
| Enzyme 6 Synonyms |
- Polyamine N-acetyltransferase 2
- Spermidine/spermine N(1)-acetyltransferase 2
- Thialysine N-epsilon-acetyltransferase
|
| Enzyme 6 Gene Name |
SAT2 |
| Enzyme 6 Protein Sequence |
>Diamine acetyltransferase 2
MASVRIREAKEGDCGDILRLIRELAEFEKLSDQVKISEEALRADGFGDNPFYHCLVAEIL
PAPGKLLGPCVVGYGIYYFIYSTWKGRTIYLEDIYVMPEYRGQGIGSKIIKKVAEVALDK
GCSQFRLAVLDWNQRAMDLYKALGAQDLTEAEGWHFFCFQGEATRKLAGK
|
| Enzyme 6 Number of Residues |
170 |
| Enzyme 6 Molecular Weight |
19154.9 |
| Enzyme 6 Theoretical pI |
5.84 |
| Enzyme 6 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 6 Specific Function |
Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine |
| Enzyme 6 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 6 Reactions |
- acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine [RN:R03910]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q96F10  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
SAT2_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>513 bp
ATGGCTTCCGTGCGGATCCGAGAGGCCAAGGAGGGAGACTGTGGAGATATCCTGAGGCTG
ATTCGGGAGCTAGCCGAATTCGAAAAACTCTCGGATCAGGTGAAGATCAGTGAAGAAGCC
CTGAGAGCAGATGGCTTTGGAGACAATCCTTTCTATCACTGTTTGGTAGCAGAGATTCTT
CCAGCGCCCGGGAAGCTACTGGGGCCCTGCGTGGTGGGCTATGGGATATACTATTTCATC
TACAGTACATGGAAGGGACGCACCATTTATCTGGAGGATATCTATGTGATGCCAGAATAT
CGGGGTCAAGGGATTGGTTCCAAAATAATCAAAAAGGTGGCTGAGGTGGCCTTGGATAAG
GGCTGCTCCCAATTCCGCCTGGCCGTCCTGGACTGGAACCAGAGGGCCATGGACTTGTAC
AAGGCCCTAGGAGCCCAAGATCTGACGGAAGCTGAGGGCTGGCACTTCTTCTGCTTTCAA
GGAGAGGCAACGAGAAAGTTGGCAGGAAAGTGA
|
| Enzyme 6 GenBank Gene ID |
AF348524  |
| Enzyme 6 GeneCard ID |
SAT2  |
| Enzyme 6 GenAtlas ID |
SAT2  |
| Enzyme 6 HGNC ID |
HGNC:23160  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
17p13.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Chen Y, Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase. Biochem J. 2003 Aug 1;373(Pt 3):661-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5245 |
| Enzyme 7 Name |
Malonyl-CoA decarboxylase, mitochondrial |
| Enzyme 7 Synonyms |
- MCD
|
| Enzyme 7 Gene Name |
MLYCD |
| Enzyme 7 Protein Sequence |
>Malonyl-CoA decarboxylase, mitochondrial
MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKT
PAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAA
VLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNG
VLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFF
SHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQG
VELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSEC
KEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVA
NFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQV
LSLVAQFQKNSKL
|
| Enzyme 7 Number of Residues |
493 |
| Enzyme 7 Molecular Weight |
55002.9 |
| Enzyme 7 Theoretical pI |
9.26 |
| Enzyme 7 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
- malonyl-CoA decarboxylase activity
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in malonyl-CoA decarboxylase activity |
| Enzyme 7 Specific Function |
Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- malonyl-CoA = acetyl-CoA + CO2 [RN:R00233]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
5732237  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O95822  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
DCMC_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1482 bp
ATGCGAGGCTTCGGGCCAGGCTTGACGGCCAGGCGTCTCCTCCCGCTGCGGTTGCCCCCG
CGGCCGCCCGGGCCCCGGCTGGCGAGCGGGCAGGCGGCCGGCGCCCTGGAGCGGGCCATG
GACGAGCTGCTGCGCCGCGCGGTGCCGCCGACGCCGGCCTACGAGCTGCGCGAGAAGACA
CCGGCGCCCGCCGAGGGTCAGTGCGCGGACTTCGTGAGCTTCTACGGTGGGCTGGCCGAG
ACGGCCCAGCGGGCCGAACTGCTGGGCCGCCTGGCGCGGGGCTTCGGCGTGGACCACGGC
CAGGTGGCGGAGCAGAGCGCCGGCGTGCTCCATCTGCGCCAGCAGCAGCGGGAGTCGGCG
GTGCTGCTGCAGGCCGAGGTCCGGCTGCGCTACGCGCTGGTGCCGCGCTATCGCGGCCTC
TTCCACCACATCAGCAAGCTGGACGGCGGCGTGCGCTTCCTGGTGCAGCTGCGGGCCGAC
CTGCTGGAGGCGCAGGCCCTCAAGCTGGTGGAGGGGCCGGACGTCCGGGAAATGAATGGG
GTGCTGAAAGGAATGCTCTCAGAATGGTTTTCCTCCGGGTTCCTGAACCTAGAACGGGTT
ACCTGGCATTCACCGTGTGAAGTGCTTCAGAAAATCAGTGAGGCTGAGGCTGTGCATCCT
GTAAAAAACTGGATGGACATGAAGCGCCGCGTTGGGCCCTACAGAAGGTGTTACTTCTTT
TCTCACTGTTCGACCCCTGGGGAGCCCCTGGTCGTTTTGCACGTGGCACTGACTGGTGAC
ATCTCCAGCAACATCCAGGCAATCGTGAAGGAACATCCTCCATCAGAAACAGAAGAGAAG
AACAAAATCACTGCTGCGATCTTTTATTCCATCAGCTTGACCCAGCAGGGACTCCAAGGG
GTGGAGCTGGGAACATTCCTCATAAAGCGAGTCGTCAAGGAGTTGCAGAGAGAGTTTCCT
CACCTTGGGGTGTTTTCAAGTCTGTCACCTATACCTGGTTTCACCAAATGGCTTCTGGGG
CTTCTGAACTCGCAAACGAAGGAGCATGGGAGGAATGAACTCTTTACAGATTCGGAATGT
AAGGAAATCTCGGAGATCACAGGTGGCCCCATTAACGAGACCCTCAAGCTCCTCCTCAGC
AGCAGCGAGTGGGTGCAGTCGGAGAAGCTGGTGCGGGCGCTGCAGACTCCGCTGATGAGG
CTGTGCGCCTGGTACCTGTATGGAGAGAAGCACCGCGGCTACGCGCTGAACCCCGTGGCC
AACTTCCACCTGCAGAACGGGGCGGTGCTGTGGCGCATCAACTGGATGGCGGATGTGAGC
CTCAGAGGCATCACCGGCTCCTGCGGCCTGATGGCCAACTACCGCTACTTCCTGGAGGAG
ACGGGCCCCAACAGCACCTCCTACCTCGGCTCCAAGATCATCAAAGCCTCTGAGCAGGTC
CTCAGCCTAGTGGCCCAGTTTCAAAAGAACAGCAAGCTCTGA
|
| Enzyme 7 GenBank Gene ID |
AF090834  |
| Enzyme 7 GeneCard ID |
MLYCD  |
| Enzyme 7 GenAtlas ID |
MLYCD  |
| Enzyme 7 HGNC ID |
HGNC:7150  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
16q24 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- FitzPatrick DR, Hill A, Tolmie JL, Thorburn DR, Christodoulou J: The molecular basis of malonyl-CoA decarboxylase deficiency. Am J Hum Genet. 1999 Aug;65(2):318-26. [PubMed
]
- Sacksteder KA, Morrell JC, Wanders RJ, Matalon R, Gould SJ: MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonyl-CoA decarboxylase deficiency. J Biol Chem. 1999 Aug 27;274(35):24461-8. [PubMed
]
- Gao J, Waber L, Bennett MJ, Gibson KM, Cohen JC: Cloning and mutational analysis of human malonyl-coenzyme A decarboxylase. J Lipid Res. 1999 Jan;40(1):178-82. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5247 |
| Enzyme 8 Name |
Acetyl-CoA carboxylase 2 |
| Enzyme 8 Synonyms |
- ACC-beta
- Biotin carboxylase
|
| Enzyme 8 Gene Name |
ACACB |
| Enzyme 8 Protein Sequence |
>Acetyl-CoA carboxylase 2
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
|
| Enzyme 8 Number of Residues |
2458 |
| Enzyme 8 Molecular Weight |
276538.6 |
| Enzyme 8 Theoretical pI |
6.46 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- CoA carboxylase activity
- acetyl-CoA carboxylase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in acetyl-CoA carboxylase activity |
| Enzyme 8 Specific Function |
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
134142062  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O00763  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ACACB_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>7377 bp
ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGGGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCCCAAGACACCCAGCCAGGCCGAGCCAGCCTCCCACAAA
GGCCCCAAAGATGCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCACCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCCAGCAAGCTGGCTCCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAG
CTGATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTT
GCTGGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCC
CTGGAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGC
ATGTCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGA
GACTTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATC
GAGAAGGTGCTTATTGCCAACAACGGGATTGCCGCCGTGAAGTGCATGCGCTCCATCCGC
AGGTGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTGTGATGGTGACC
CCCGAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGTCCCCGTC
CCAGGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAG
AGAATCCCCGTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTCAGAAAACCCTAAACTT
CCGGAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGTGAGGCCATGTGG
GCCTTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCTGGAGTGGAAGCGGCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGAAGGCTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCCCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATCCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGCAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGATGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGCGTGCCACTGCACCGGCTGAAGGATATCCGG
CTTCTGTATGGAGAGTCACCATGGGGAGTGACTCCCATTTCTTTTGAAACCCCCTCAAAC
CCTCCCCTCGCCCGAGGCCACGTCATTGCCGCCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTG
TGGGGTTACTTCAGCGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGGATTCCCAATTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGGAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCATCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACGACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAGGCGGAGAAACCGGATATCATGCTTGGGGTGGTATGCGGGGCCTTG
AACGTGGCCGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGG
GGCCAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGGA
GGTGTTAAGTACATTCTCAAGGTGGCCCGGCAGTCTCTGACCATGTTCGTTCTCATCATG
AATGGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCC
TACAATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGAATTACC
ATCGGCAATAAGACGTGTGTGTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCC
TCGGCTGGGAAGCTGACACAGTACACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGC
AGCTACGCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGC
CGGGTGAAGTACATCAAGCGTCCAGGTGCCGTGCTGGAAGCAGGCTGCGTGGTGGCCAGG
CTGGAGCTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCT
GCCCAGCAGACACTGCCCATCCTCGGAGAGAAACTGCACCAGGTCTTCCACAGCGTCCTG
GAAAACCTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCCGTTTTTAGCATAAAG
CTGAAGGAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCCGCTGCTG
GAGCTGCAGGAGATCATGACCAGCGTGGCAGGCCGCATCCCCGCCCCTGTGGAGAAGTCT
GTCCGCAGGGTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCC
AGCCAGCAGATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGAT
CGAGAGGTCTTCTTCATCAACACCCAGAGCATCGTGCAGTTGGTCCAGAGATACCGCAGC
GGGATCCGCGGCTATATGAAAACAGTGGTGTTGGATCTCCTGAGAAGATACTTGCGTGTT
GAGCACCATTTTCAGCAAGCCCACTACGACAAGTGTGTGATAAACCTCAGGGAGCAGTTC
AAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCCCACGCACAGGTGGCCAAGAAG
AACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGCCCAGACCCTTCCCTGTCGGAC
GAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGCAAAAGCGAGCACTGCAAAGTG
GCCCTCAGAGCCCGGCAGATCCTGATTGCCTCCCACCTCCCCTCCTACGAGCTGCGGCAT
AACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGCCACCAGTTCTGCCCC
GAGAACCTCAAGAAATTAATACTTTCGGAAACAACCATCTTCGACGTCCTGCCTACTTTC
TTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTTTACGTGCGGAGGGGC
TACATCGCCTATGAGTTAAACAGCCTGCAGCACCGGCAGCTCCCGGACGGCACCTGCGTG
GTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATGACCGTGCCCATCAGC
ATCACCAACCCTGACCTGCTGAGGCACAGCACAGAGCTCTTCATGGACAGCGGCTTCTCC
CCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTCGAGGACTTCACCAGA
AATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCCAAAGACACCCCCCTCTTCAGC
GAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTCAGAGAAGAGCCCATC
CACATTCTGAATGTGTCCATCCAGTGTGCAGACCACCTGGAGGATGAGGCACTGGTGCCG
ATTTTACGGACATTCGTACAGTCCAAGAAAAATATCCTTGTGGATTATGGACTCCGACGA
ATCACATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTCACATTCAGAGCAAGA
GATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCCCTGGCCTTCCAGCTG
GAACTTAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGTGCCAACCACAAGATG
CACCTTTACCTGGGTGCTGCCAAGGTGAAGGAAGGTGTGGAAGTGACGGACCATAGGTTC
TTCATCCGCGCCATCATCAGGCACTCTGACCTGATCACAAAGGAAGCCTCCTTCGAATAC
CTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAGCTGGAGGTGGCGTTC
AATAACACCAGCGTGCGCACCGACTGCAACCACATCTTCCTCAACTTCGTGCCCACTGTC
ATCATGGACCCCTTCAAGATCGAGGAGTCCGTGCGCTACATGGTTATGCGCTACGGCAGC
CGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAACATCCGCCAGACCACC
ACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCGGGCTACTACCTGGAC
ATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATCATGTTTCACTCCTTC
GGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCCTACGTCACCAAGGAT
CTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACCTACATCTATGACTTC
CCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCAGACAAGTATCCCAAA
GACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAGCTGGTGGAGATGAAC
CGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATGAGGTTTAAGACCCAG
GAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATCACCTTTCGCATTGGA
TCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAGATGGCCCGGGCAGAG
GGCATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATTGGCATGGCAGAGGAG
ATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCCCACAAAGGATTTAAA
TACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTGAACTCCGTCCACTGT
AAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGATATCATCGGGAAGGAT
GATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCTGGGGAGTCCTCTCTG
GCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCCATTGGGATTGGGGCC
TACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCCCACATCATCCTCACA
GGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACATCCAACAACCAGCTG
GGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACCGTGCCAGATGACTTT
GAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAGGATAATCACAGCCCT
GTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAATTCCTCCCATCCAGA
GCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCAACTCTGAAGGGAACG
TGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATGGCACCCTGGGCGCAG
ACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGAGTGATTGCTGTGGAG
ACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTGGATTCTGAGGCCAAG
ATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTACAAAACCGCCCAGGCC
GTCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCCAACTGGAGGGGGTTC
TCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGAGCCTACATCGTGGAC
GGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCCGCCCTATGCGGAGCTCCGG
GGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGCATAGAAATGTATGCA
GACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTGGAGATTAAGTTCCGA
AAGAAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTACAAGAAGCTCATGGAA
CAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTGGAGGGCCGGCTAAAG
GCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTGCAGTTCGCCGACTTC
CATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGACATCCTGGAGTGGAAG
ACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTGGAGGACCAGGTCAAG
CAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATCCAGTCCATGCTGCGT
CGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGGGACAACAACCAGGTG
GTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCGCGCTCCACCATCCGT
GAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATCCGAGGCCTGGTTGAA
GAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAGCACATCAGCCCAGCT
GAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCGGCCTCCACCTGA
|
| Enzyme 8 GenBank Gene ID |
NM_001093.3  |
| Enzyme 8 GeneCard ID |
ACACB  |
| Enzyme 8 GenAtlas ID |
ACACB  |
| Enzyme 8 HGNC ID |
HGNC:85  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
12q24.11 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed
]
- Cheng D, Chu CH, Chen L, Feder JN, Mintier GA, Wu Y, Cook JW, Harpel MR, Locke GA, An Y, Tamura JK: Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes. Protein Expr Purif. 2007 Jan;51(1):11-21. Epub 2006 Jun 10. [PubMed
]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed
]
- Cho YS, Lee JI, Shin D, Kim HT, Cheon YH, Seo CI, Kim YE, Hyun YL, Lee YS, Sugiyama K, Park SY, Ro S, Cho JM, Lee TG, Heo YS: Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2. Proteins. 2008 Jan 1;70(1):268-72. [PubMed
]
- Jones S, Zhang X, Parsons DW, Lin JC, Leary RJ, Angenendt P, Mankoo P, Carter H, Kamiyama H, Jimeno A, Hong SM, Fu B, Lin MT, Calhoun ES, Kamiyama M, Walter K, Nikolskaya T, Nikolsky Y, Hartigan J, Smith DR, Hidalgo M, Leach SD, Klein AP, Jaffee EM, Goggins M, Maitra A, Iacobuzio-Donahue C, Eshleman JR, Kern SE, Hruban RH, Karchin R, Papadopoulos N, Parmigiani G, Vogelstein B, Velculescu VE, Kinzler KW: Core signaling pathways in human pancreatic cancers revealed by global genomic analyses. Science. 2008 Sep 26;321(5897):1801-6. Epub 2008 Sep 4. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5248 |
| Enzyme 9 Name |
Pyruvate carboxylase, mitochondrial |
| Enzyme 9 Synonyms |
- Pyruvic carboxylase
- PCB
|
| Enzyme 9 Gene Name |
PC |
| Enzyme 9 Protein Sequence |
>Pyruvate carboxylase, mitochondrial
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
|
| Enzyme 9 Number of Residues |
1178 |
| Enzyme 9 Molecular Weight |
129632.6 |
| Enzyme 9 Theoretical pI |
6.83 |
| Enzyme 9 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleoside binding
- purine nucleoside binding
- pyruvate carboxylase activity
- vitamin binding
|
| Process |
- alcohol metabolic process
- gluconeogenesis
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 9 General Function |
Involved in catalytic activity |
| Enzyme 9 Specific Function |
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate [RN:R00344]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
458236  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P11498  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PYC_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>3537 bp
ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA
|
| Enzyme 9 GenBank Gene ID |
U04641  |
| Enzyme 9 GeneCard ID |
PC  |
| Enzyme 9 GenAtlas ID |
PC  |
| Enzyme 9 HGNC ID |
HGNC:8636  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
11q13.4-q13.5 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [PubMed
]
- MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed
]
- Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Xiang S, Tong L: Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction. Nat Struct Mol Biol. 2008 Mar;15(3):295-302. Epub 2008 Feb 24. [PubMed
]
- Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [PubMed
]
- Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [PubMed
]
- Monnot S, Serre V, Chadefaux-Vekemans B, Aupetit J, Romano S, De Lonlay P, Rival JM, Munnich A, Steffann J, Bonnefont JP: Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency. Hum Mutat. 2009 May;30(5):734-40. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5249 |
| Enzyme 10 Name |
Arylamine N-acetyltransferase 1 |
| Enzyme 10 Synonyms |
- Arylamide acetylase 1
- Monomorphic arylamine N-acetyltransferase
- MNAT
- N-acetyltransferase type 1
- NAT-1
|
| Enzyme 10 Gene Name |
NAT1 |
| Enzyme 10 Protein Sequence |
>Arylamine N-acetyltransferase 1
MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVV
RRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYI
VDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDL
LEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLT
HRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI
|
| Enzyme 10 Number of Residues |
290 |
| Enzyme 10 Molecular Weight |
33898.4 |
| Enzyme 10 Theoretical pI |
6.51 |
| Enzyme 10 GO Classification |
| Function |
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in acetyltransferase activity |
| Enzyme 10 Specific Function |
Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
- acetyl-CoA + an arylamine = CoA + an N-acetylarylamine [RN:R02387]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
2258431  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P18440  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ARY1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>873 bp
ATGGACATTGAAGCATATCTTGAAAGAATTGGCTATAAGAAGTCTAGGAACAAATTGGAC
TTGGAAACATTAACTGACATTCTTCAACACCAGATCCGAGCTGTTCCCTTTGAGAACCTT
AACATCCATTGTGGGGATGCCATGGACTTAGGCTTAGAGGCCATTTTTGATCAAGTTGTG
AGAAGAAATTGGGGTGGATGGTGTCTCCAGGTCAATCATCTTCTGTACTGGGCTCTGACC
ACTATTGGTTTTGAGACCACGATGTTGGGAGGGTATGTTTACAGCACTCCAGCCAAAAAA
TACAGCACTGGCATGATTCACCTTCTCCTGCAGGTGACCATTGATGGCAGGAACTACATT
GTCGATGCTGGGTTTGGACGCTCATACCAGATGTGGCAGCCTCTGGAGTTAATTTCTGGG
AAGGATCAGCCTCAGGTGCCTTGTGTCTTCCGTTTGACGGAAGAGAATGGATTCTGGTAT
CTAGACCAAATCAGAAGGGAACAGTACATTCCAAATGAAGAATTTCTTCATTCTGATCTC
CTAGAAGACAGCAAATACCGAAAAATCTACTCCTTTACTCTTAAGCCTCGAACAATTGAA
GATTTTGAGTCTATGAATACATACCTGCAGACATCTCCATCATCTGTGTTTACTAGTAAA
TCATTTTGTTCCTTGCAGACCCCAGATGGGGTTCACTGTTTGGTGGGCTTCACCCTCACC
CATAGGAGATTCAATTATAAGGACAATACAGATCTAATAGAGTTCAAGACTCTGAGTGAG
GAAGAAATAGAAAAAGTGCTGAAAAATATATTTAATATTTCCTTGCAGAGAAAGCTTGTG
CCCAAACATGGTGATAGATTTTTTACTATTTAG
|
| Enzyme 10 GenBank Gene ID |
AF008204  |
| Enzyme 10 GeneCard ID |
NAT1  |
| Enzyme 10 GenAtlas ID |
NAT1  |
| Enzyme 10 HGNC ID |
HGNC:7645  |
| Enzyme 10 Chromosome Location |
8 |
| Enzyme 10 Locus |
8p22 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Blum M, Grant DM, McBride W, Heim M, Meyer UA: Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression. DNA Cell Biol. 1990 Apr;9(3):193-203. [PubMed
]
- Ohsako S, Deguchi T: Cloning and expression of cDNAs for polymorphic and monomorphic arylamine N-acetyltransferases from human liver. J Biol Chem. 1990 Mar 15;265(8):4630-4. [PubMed
]
- Vatsis KP, Weber WW: Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene locus. Arch Biochem Biophys. 1993 Feb 15;301(1):71-6. [PubMed
]
- Doll MA, Jiang W, Deitz AC, Rustan TD, Hein DW: Identification of a novel allele at the human NAT1 acetyltransferase locus. Biochem Biophys Res Commun. 1997 Apr 28;233(3):584-91. [PubMed
]
- Butcher NJ, Ilett KF, Minchin RF: Functional polymorphism of the human arylamine N-acetyltransferase type 1 gene caused by C190T and G560A mutations. Pharmacogenetics. 1998 Feb;8(1):67-72. [PubMed
]
- Lo-Guidice JM, Allorge D, Chevalier D, Debuysere H, Fazio F, Lafitte LJ, Broly F: Molecular analysis of the N-acetyltransferase 1 gene (NAT1*) using polymerase chain reaction-restriction fragment-single strand conformation polymorphism assay. Pharmacogenetics. 2000 Jun;10(4):293-300. [PubMed
]
- Patin E, Barreiro LB, Sabeti PC, Austerlitz F, Luca F, Sajantila A, Behar DM, Semino O, Sakuntabhai A, Guiso N, Gicquel B, McElreavey K, Harding RM, Heyer E, Quintana-Murci L: Deciphering the ancient and complex evolutionary history of human arylamine N-acetyltransferase genes. Am J Hum Genet. 2006 Mar;78(3):423-36. Epub 2006 Jan 13. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ebisawa T, Deguchi T: Structure and restriction fragment length polymorphism of genes for human liver arylamine N-acetyltransferases. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1252-7. [PubMed
]
- Delomenie C, Goodfellow GH, Krishnamoorthy R, Grant DM, Dupret JM: Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis. Biochem J. 1997 Apr 1;323 ( Pt 1):207-15. [PubMed
]
- Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN: Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases. J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. [PubMed
]
- Hughes NC, Janezic SA, McQueen KL, Jewett MA, Castranio T, Bell DA, Grant DM: Identification and characterization of variant alleles of human acetyltransferase NAT1 with defective function using p-aminosalicylate as an in-vivo and in-vitro probe. Pharmacogenetics. 1998 Feb;8(1):55-66. [PubMed
]
- Lin HJ, Probst-Hensch NM, Hughes NC, Sakamoto GT, Louie AD, Kau IH, Lin BK, Lee DB, Lin J, Frankl HD, Lee ER, Hardy S, Grant DM, Haile RW: Variants of N-acetyltransferase NAT1 and a case-control study of colorectal adenomas. Pharmacogenetics. 1998 Jun;8(3):269-81. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5251 |
| Enzyme 11 Name |
5-aminolevulinate synthase, nonspecific, mitochondrial |
| Enzyme 11 Synonyms |
- ALAS-H
- 5-aminolevulinic acid synthase 1
- Delta-ALA synthase 1
- Delta-aminolevulinate synthase 1
|
| Enzyme 11 Gene Name |
ALAS1 |
| Enzyme 11 Protein Sequence |
>5-aminolevulinate synthase, nonspecific, mitochondrial
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
|
| Enzyme 11 Number of Residues |
640 |
| Enzyme 11 Molecular Weight |
70580.3 |
| Enzyme 11 Theoretical pI |
8.57 |
| Enzyme 11 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 11 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 11 Specific Function |
Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2) |
| Enzyme 11 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 11 Reactions |
- succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 [RN:R00830]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
28583  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P13196  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
HEM1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1923 bp
ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA
|
| Enzyme 11 GenBank Gene ID |
X56351  |
| Enzyme 11 GeneCard ID |
ALAS1  |
| Enzyme 11 GenAtlas ID |
ALAS1  |
| Enzyme 11 HGNC ID |
HGNC:396  |
| Enzyme 11 Chromosome Location |
3 |
| Enzyme 11 Locus |
3p21.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed
]
- Bawden MJ, Borthwick IA, Healy HM, Morris CP, May BK, Elliott WH: Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res. 1987 Oct 26;15(20):8563. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5252 |
| Enzyme 12 Name |
General transcription factor 3C polypeptide 4 |
| Enzyme 12 Synonyms |
- TF3C-delta
- Transcription factor IIIC 90 kDa subunit
- TFIIIC 90 kDa subunit
- TFIIIC90
- Transcription factor IIIC subunit delta
|
| Enzyme 12 Gene Name |
GTF3C4 |
| Enzyme 12 Protein Sequence |
>General transcription factor 3C polypeptide 4
MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKL
QYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKV
GSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRC
LLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQ
RRHSMQTPVRMEWSGICTTQQVKHNNECRDVGSVLLAVLFENGNIAVWQFQLPFVGKESI
SSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPV
ILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWCLLLISKAGLNVHNSHVTG
LHSLPIVSMTADKQNGTVYTCSSDGKVRQLIPIFTDVALKFEHQLIKLSDVFGSVRTHGI
AVSPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLI
DLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPT
HEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAG
GREPMEEKLLEIQGKIEAVEMHLTREHMKRVLGEVYLHTWITENTSIPTRGLCNFLMSDE
EYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSC
QSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF
|
| Enzyme 12 Number of Residues |
822 |
| Enzyme 12 Molecular Weight |
91981.6 |
| Enzyme 12 Theoretical pI |
6.64 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Involved in DNA binding |
| Enzyme 12 Specific Function |
Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 12 Pfam Domain Function |
Not Available |
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
6175593  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9UKN8  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
TF3C4_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>2469 bp
ATGAACACGGCCGACCAGGCCAGGGTGGGGCCCGCGGACGACGGGCCTGCGCCGTCTGGG
GAGGAGGAGGGAGAGGGGGGCGGCGAGGCGGGCGGGAAGGAGCCAGCAGCGGACGCGGCC
CCGGGGCCCAGCGCTGCATTCCGCCTCATGGTGACTCGGCGGGAGCCGGCCGTGAAGCTG
CAGTATGCGGTGAGCGGCCTGGAACCGCTGGCTTGGTCCGAGGACCACCGCGTGTCTGTG
TCCACGGCCCGCAGCATCGCTGTGCTGGAGCTCATCTGCGACGTGCACAACCCGGGCCAG
GACCTGGTTATCCACCGCACCTCGGTGCCCGCACCGCTCAACAGCTGTCTCCTCAAAGTT
GGCTCAAAAACAGAAGTTGCTGAGTGCAAGGAGAAATTCGCCGCCTCCAAGGACCCCACG
GTCAGTCAGACTTTCATGTTGGATAGGGTGTTCAACCCTGAGGGGAAGGCTTTACCACCA
ATGAGAGGATTCAAGTACACCAGCTGGTCTCCCATGGGTTGCGATGCTAATGGCAGGTGC
CTCTTGGCAGCACTGACCATGGACAATCGCCTGACCATCCAGGCAAATCTCAACAGACTG
CAGTGGGTCCAGCTGGTTGACCTGACTGAGATCTATGGAGAACGTCTTTATGAGACCAGT
TACAGGCTCTCTAAAAATGAGGCCCCGGAAGGAAATCTCGGGGATTTTGCTGAGTTTCAG
AGGAGACACAGCATGCAGACCCCAGTCAGAATGGAGTGGTCGGGCATCTGTACCACCCAG
CAGGTCAAGCATAACAACGAAAGCCGGGACGTTGGCAGTGTGCTCCTGGCTGTCCTCTTT
GAAAACGGTAATATCGCCGTGTGGCAGTTTCAGCTGCCGTTTGTAGGAAAAGAATCCATC
TCTTCATGCAACACAATTGAGTCAGGAATCACCTCTCCCAGTGTATTGTTTTGGTGGGAA
TATGAGCACAATAATCGAAAAATGAGTGGCCTTATTGTGGGGAGTGCTTTTGGACCCATA
AAAATTCTTCCTGTCAATCTCAAAGCAGTCAAAGGCTATTTCACTTTAAGGCAGCCTGTT
ATCTTGTGGAAAGAAATGGACCAGTTACCTGTGCACAGTATCAAATGTGTGCCACTTTAT
CATCCTTACCAGAAGTGTAGTTGCAGCTTAGTAGTGGCTGCAAGAGGCTCTTATGTATTT
TGGCGTCTTCTTCTGATCTCCAAAGCAGGGCTGAATCTTCACAATTCCCATGTCACAGGC
CTTCACTCACTGCCAATTGTCTCCATGACTGCAGACAAACAGAATGGAACAGTCTATACT
TGCTCCAGTGACGGAAAGGTGAGGCAGGTGATTCCGATTTTCACAGATGTTGCATTGAAG
TTTGAACACCAGTTGATTAAACTCTCAGATGTGTTTGGCTCAGTGAGGACTCACGGGATA
GCAGTGAAGCCCTGCGGTGCATACCTGGCCATCATCACCACTGAGGGCATGATCAACGGC
CTCCACCCTGTTAACAAAAACTACCAGGTCCAATTTGTTACTCTCAAAACCTTTGAAGAA
GCAGCTGCTCAGCTCCTGGAATCTTCAGTTCAAAACCTTTTTAAGCAGGTAGATTTAATA
GACCTAGTACGCTGGAAGATTTTAAAAGATAAACATATCCCTCAATTTTTACAAGAAGCT
TTGGAAAAAAAGATTGAAAGCAGTGGAGTCACCTATTTTTGGCGTTTTAAGCTTTTCCTC
CTGAGGATTTTATATCAGTCAATGCAGAAAACCCCTTCAGAAGCCTTGTGGAAACCCACC
CATGAGGACTCAAAAATCTTACTAGTGGATTCGCCTGGGATGGGCAATGCTGACGATGAA
CAGCAGGAAGAAGGCACTTCTTCCAAACAGGTGGTGAAGCAAGGCCTGCAGGAGAGGAGC
AAGGAAGGAGATGTAGAGGAGCCCACTGATGACTCGCTCCCCACGACTGGAGATGCTGGA
GGCCGTGAGCCAATGGAAGAGAAACTCCTGGAAATCCAAGGGAAAATCGAAGCTGTGGAG
ATGCACTTGACCAGGGAACACATGAAGCCAGTCTTAGGAGAAGTGTATCTGCACACCTGG
ATCACAGAAAACACTAGCATCCCCACCCGCGGACTCTGTAACTTTTTAATGTCTGATGAA
GAGTATGATGACAGAACTGCACGGGTGCTGATTGGACATATCTCAAAGAAGATGAACAAA
CAGACTTTCCCTGAGCACTGTAGTTTGTGTAAAGAGATCTTGCCATTCACAGATCGCAAA
CAGGCAGTCTGTTCCAATGGCCACATTTGGCTCCGGTGCTTCTTAACCTACCAGTCCTGC
CAGAGTTTGATATATAGAAGGTGTTTGCTCCATGACAGCATTGCCCGGCATCCAGCTCCA
GAAGATCCCGACTGGATTAAGAGGTTACTGCAAAGCCCCTGCCCTTTCTGTGATTCTCCT
GTCTTCTAA
|
| Enzyme 12 GenBank Gene ID |
AF142328  |
| Enzyme 12 GeneCard ID |
GTF3C4  |
| Enzyme 12 GenAtlas ID |
GTF3C4  |
| Enzyme 12 HGNC ID |
HGNC:4667  |
| Enzyme 12 Chromosome Location |
9 |
| Enzyme 12 Locus |
9q34.13 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Hsieh YJ, Kundu TK, Wang Z, Kovelman R, Roeder RG: The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity. Mol Cell Biol. 1999 Nov;19(11):7697-704. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Dumay-Odelot H, Marck C, Durrieu-Gaillard S, Lefebvre O, Jourdain S, Prochazkova M, Pflieger A, Teichmann M: Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC. J Biol Chem. 2007 Jun 8;282(23):17179-89. Epub 2007 Apr 4. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5253 |
| Enzyme 13 Name |
Acyl-coenzyme A thioesterase 12 |
| Enzyme 13 Synonyms |
- Acyl-CoA thioesterase 12
- Acyl-CoA thioester hydrolase 12
- Cytoplasmic acetyl-CoA hydrolase 1
- CACH-1
- hCACH-1
- START domain-containing protein 15
- StARD15
|
| Enzyme 13 Gene Name |
ACOT12 |
| Enzyme 13 Protein Sequence |
>Acyl-coenzyme A thioesterase 12
MERPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQ
FEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKPVGKEK
IHLKPVTLLTEQDHVEHNLAAERRKVRLQHEDTFNNLMKESSKFDDLIFDEEEGAVSTRG
TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPST
VGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWAEGRGRHINSAFLIYNAADDKENLITF
PRIQPISKDDFRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALK
KLAAKRGWEVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHF
VSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVAVKSVILPSVP
PSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCI
QFLENPPDDGFVSTF
|
| Enzyme 13 Number of Residues |
555 |
| Enzyme 13 Molecular Weight |
62033.5 |
| Enzyme 13 Theoretical pI |
6.76 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Lipid transport and metabolism |
| Enzyme 13 Specific Function |
Hydrolyzes acetyl-CoA to acetate and CoA |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- acetyl-CoA + H2O = CoA + acetate [RN:R00227]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
18307694  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q8WYK0  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
ACO12_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1668 bp
ATGGAGCGGCCGGCGCCCGGCGAGGTGGTCATGAGCCAAGCCATCCAGCCGGCGCACGCC
ACTGCGCGCGGCGAGCTGAGCGCGGGGCAGCTGCTCAAGTGGATCGACACCACCGCCTGC
CTGGCGGCTGAGAAACATGCTGGAGTTTCCTGCGTTACAGCCTCAGTGGATGACATACAG
TTTGAGGAGACAGCTAGAGTTGGACAAGTTATAACCATCAAAGCAAAAGTTACTAGAGCA
TTCAGCACAAGCATGGAGATCAGTATCAAGGTCATGGTACAGGATATGCTCACTGGCATT
GAGAAGCTTGTTAGTGTGGCTTTCTCCACATTTGTAGCCAAACCAGTTGGAAAAGAAAAG
ATTCATTTAAAACCAGTCACACTTCTAACTGAACAAGATCATGTGGAACATAATCTGGCT
GCTGAGAGAAGGAAAGTTCGATTACAACATGAAGATACCTTTAACAATTTAATGAAGGAA
AGTAGCAAATTTGATGATCTCATTTTTGATGAAGAGGAAGGAGCGGTTTCCACAAGGGGC
ACCTCCGTTCAGAGCATTGAACTGGTCCTCCCACCCCATGCAAACCATCACGGAAATACA
TTTGGTGGCCAGATTATGGCGTGGATGGAGACAGTGGCTACTATTTCTGCAAGCCGCCTG
TGTTGGGCTCATCCCTTTCTGAAGTCCGTAGATATGTTTAAGTTCCGGGGACCATCTACA
GTTGGAGATCGTCTTGTCTTCACTGCCATTGTCAACAATACATTTCAGACCTGTGTTGAA
GTTGGAGTTCGCGTGGAGGCCTTTGACTGTCAGGAATGGGCCGAGGGCCGAGGGCGTCAC
ATCAACAGTGCTTTTCTCATTTACAATGCTGCTGATGATAAGGAAAATCTCATCACGTTT
CCCAGAATCCAACCCATTTCAAAGGATGATTTCAGACGCTATCGGGGAGCTATTGCACGC
AAGCGAATTCGCCTAGGCAGAAAATATGTTATTTCCCACAAAGAAGAGGTTCCACTTTGC
ATACACTGGGATATCAGCAAGCAGGCATCCCTGAGTGACAGCAATGTGGAGGCCCTCAAA
AAACTGGCAGCCAAAAGGGGTTGGGAGGTTACCAGCACTGTGGAAAAGATAAAAATATAT
ACTCTGGAAGAGCATGATGTTTTATCTGTTTGGGTTGAAAAGCACGTGGGAAGTCCAGCA
CATTTGGCTTATCGTCTCTTGTCTGACTTTACAAAGCGACCTTTGTGGGACCCCCATTTT
GTGTCCTGTGAAGTCATAGACTGGGTGAGTGAAGATGATCAGCTGTATCACATCACCTGT
CCTATACTGAATGATGACAAACCCAAAGACTTGGTAGTACTCGTATCACGAAGAAAACCC
CTCAAAGATGGTAACACTTACACAGTGGCAGTGAAGTCGGTCATTTTGCCATCGGTCCCC
CCGTCTCCACAGTACATCAGAAGTGAAATCATATGTGCCGGATTTCTCATCCATGCTATT
GACAGCAATTCATGCATCGTATCTTACTTTAACCATATGTCTGCTAGCATCCTTCCTTAC
TTTGCTGGAAATCTTGGTGGCTGGTCAAAATCCATTGAAGAAACAGCAGCCTCTTGTATA
CAGTTCTTAGAGAATCCTCCTGATGATGGGTTTGTAAGCACATTTTAA
|
| Enzyme 13 GenBank Gene ID |
AB078619  |
| Enzyme 13 GeneCard ID |
ACOT12  |
| Enzyme 13 GenAtlas ID |
ACOT12  |
| Enzyme 13 HGNC ID |
HGNC:24436  |
| Enzyme 13 Chromosome Location |
5 |
| Enzyme 13 Locus |
5q14.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Suematsu N, Isohashi F: Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase. Acta Biochim Pol. 2006;53(3):553-61. Epub 2006 Sep 2. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5254 |
| Enzyme 14 Name |
Choline O-acetyltransferase |
| Enzyme 14 Synonyms |
- CHOACTase
- ChAT
- Choline acetylase
|
| Enzyme 14 Gene Name |
CHAT |
| Enzyme 14 Protein Sequence |
>Choline O-acetyltransferase
MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPH
PRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMA
AKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQ
QKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLIS
GVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPE
PEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSE
WAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANR
WYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHVTQSSRKLIRADSVSELPAP
RRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQ
LAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLL
KDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQV
PTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRD
LCSLLPPTESKPLATKEKATRPSQGHQP
|
| Enzyme 14 Number of Residues |
748 |
| Enzyme 14 Molecular Weight |
82535.0 |
| Enzyme 14 Theoretical pI |
8.69 |
| Enzyme 14 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in acyltransferase activity |
| Enzyme 14 Specific Function |
Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- acetyl-CoA + choline = CoA + O-acetylcholine [RN:R01023]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
188595670  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P28329  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
CLAT_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>2247 bp
ATGGGGCTGAGGACAGCGAAGAAGAGGGGGCTTGGGGGAGGGGGGAAATGGAAGAGAGAG
GAGGGAGGAGGTACAAGAGGAAGGAGAGAAGTGCGGCCAGCTTGCTTTCTCCAGTCGGGT
GGCCGCGGGGACCCGGGCGACGTCGGAGGCCCTGCCGGGAACCCAGGCTGCAGCCCCCAC
CCCCGCGCTGCGACACGCCCCCCACCCCTTCCGGCTCACACCCCCGCCCACACTCCTGAG
TGGTGCGGTGCAGCGTCGGCCGAGGCAGCAGAGCCGAGGAGAGCAGGTCCACACCTCTGC
ATCCCTGCACCAGGACTCACCAAGACGCCCATCCTGGAAAAGGTCCCCCGTAAGATGGCA
GCAAAAACTCCCAGCAGTGAGGAGTCTGGGCTGCCCAAACTGCCCGTGCCCCCGCTGCAG
CAGACCCTGGCCACGTACCTGCAGTGCATGCGACACTTGGTGTCTGAGGAGCAGTTCAGG
AAGAGCCAGGCCATTGTGCAGCAGTTTGGGGCCCCTGGTGGCCTCGGCGAGACCCTGCAG
CAGAAACTCCTGGAGCGGCAGGAGAAGACAGCCAACTGGGTGTCTGAGTACTGGCTGAAT
GACATGTATCTCAACAACCGCCTGGCCCTGCCTGTCAACTCCAGCCCTGCCGTGATCTTT
GCTCGGCAGCACTTCCCTGGCACCGATGACCAGCTGAGGTTTGCAGCCAGCCTCATCTCT
GGTGTACTCAGCTACAAGGCCCTGCTGGACAGCCACTCCATTCCCACTGACTGTGCCAAA
GGCCAGCTGTCAGGGCAGCCCCTTTGCATGAAGCAATACTATGGGCTCTTCTCCTCCTAC
CGGCTCCCCGGCCATACCCAGGACACGCTGGTGGCTCAGAACAGCAGCATCATGCCGGAG
CCTGAGCACGTCATCGTAGCCTGCTGCAATCAGTTCTTTGTCTTGGATGTTGTCATTAAT
TTCCGCCGTCTCAGTGAGGGGGATCTGTTCACTCAGTTGAGAAAGATAGTCAAAATGGCT
TCCAACGAGGACGAGCGTTTGCCTCCAATTGGCCTGCTGACGTCTGACGGGAGGAGCGAG
TGGGCCGAGGCCAGGACGGTCCTCGTGAAAGACTCCACCAACCGGGACTCGCTGGACATG
ATTGAGCGCTGCATCTGCCTTGTATGCCTGGACGCGCCAGGAGGCGTGGAGCTCAGCGAC
ACCCACAGGGCACTCCAGCTCCTTCACGGCGGAGGCTACAGCAAGAACGGGGCCAATCGC
TGGTACGACAAGTCCCTGCAGTTTGTGGTGGGCCGAGACGGCACCTGCGGTGTGGTGTGC
GAACACTCCCCATTCGATGGCATCGTCCTGGTGCAGTGCACTGAGCATCTGCTCAAGCAC
ATGACGCAGAGCAGCAGGAAGCTGATCCGAGCAGACTCCGTCAGCGAGCTCCCCGCCCCC
CGGAGGCTGCGGTGGAAATGCTCCCCGGAAATTCAAGGCCACTTAGCCTCCTCGGCAGAA
AAACTTCAACGAATAGTAAAGAACCTTGACTTCATTGTCTATAAGTTTGACAACTATGGG
AAAACATTCATTAAGAAGCAGAAATGCAGCCCTGATGCCTTCATCCAGGTGGCCCTCCAG
CTGGCCTTCTACAGGCTCCATCGAAGACTGGTGCCCACCTACGAGAGCGCGTCCATCCGC
CGATTCCAGGAGGGACGCGTGGACAACATCAGATCGGCCACTCCAGAGGCACTGGCTTTT
GTGAGAGCCGTGACTGACCACAAGGCTGCTGTGCCAGCTTCTGAGAAGCTTCTGCTCCTG
AAGGATGCCATCCGTGCCCAGACTGCATACACAGTCATGGCCATAACAGGGATGGCCATT
GACAACCACCTGCTGGCACTGCGGGAGCTGGCCCGGGCCATGTGCAAGGAGCTGCCCGAG
ATGTTCATGGATGAAACCTACCTGATGAGCAACCGGTTTGTCCTCTCCACTAGCCAGGTG
CCCACAACCACGGAGATGTTCTGCTGCTATGGTCCTGTGGTCCCAAATGGGTATGGTGCC
TGCTACAACCCCCAGCCAGAGACCATCCTTTTCTGCATCTCTAGCTTTCACAGCTGCAAA
GAGACTTCTTCTAGCAAGTTTGCAAAAGCTGTGGAAGAAAGCCTCATTGACATGAGAGAC
CTCTGCAGTCTGCTGCCGCCTACTGAGAGCAAGCCATTGGCAACAAAGGAAAAAGCCACG
AGGCCCAGCCAGGGACACCAACCTTGA
|
| Enzyme 14 GenBank Gene ID |
NM_020549.4  |
| Enzyme 14 GeneCard ID |
CHAT  |
| Enzyme 14 GenAtlas ID |
CHAT  |
| Enzyme 14 HGNC ID |
HGNC:1912  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
10q11.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Oda Y, Nakanishi I, Deguchi T: A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells. Brain Res Mol Brain Res. 1992 Dec;16(3-4):287-94. [PubMed
]
- Ohno K, Tsujino A, Brengman JM, Harper CM, Bajzer Z, Udd B, Beyring R, Robb S, Kirkham FJ, Engel AG: Choline acetyltransferase mutations cause myasthenic syndrome associated with episodic apnea in humans. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):2017-22. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lorenzi MV, Trinidad AC, Zhang R, Strauss WL: Two mRNAs are transcribed from the human gene for choline acetyltransferase. DNA Cell Biol. 1992 Oct;11(8):593-603. [PubMed
]
- Toussaint JL, Geoffroy V, Schmitt M, Werner A, Garnier JM, Simoni P, Kempf J: Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions. Genomics. 1992 Feb;12(2):412-6. [PubMed
]
- Hersh LB, Takane K, Gylys K, Moomaw C, Slaughter C: Conservation of amino acid sequences between human and porcine choline acetyltransferase. J Neurochem. 1988 Dec;51(6):1843-5. [PubMed
]
- Cervini R, Rocchi M, DiDonato S, Finocchiaro G: Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene. Neurosci Lett. 1991 Nov 11;132(2):191-4. [PubMed
]
- Kim AR, Rylett RJ, Shilton BH: Substrate binding and catalytic mechanism of human choline acetyltransferase. Biochemistry. 2006 Dec 12;45(49):14621-31. [PubMed
]
- Kraner S, Laufenberg I, Strassburg HM, Sieb JP, Steinlein OK: Congenital myasthenic syndrome with episodic apnea in patients homozygous for a CHAT missense mutation. Arch Neurol. 2003 May;60(5):761-3. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5255 |
| Enzyme 15 Name |
Nuclear receptor coactivator 3 |
| Enzyme 15 Synonyms |
- NCoA-3
- ACTR
- Amplified in breast cancer 1 protein
- AIB-1
- CBP-interacting protein
- pCIP
- Class E basic helix-loop-helix protein 42
- bHLHe42
- Receptor-associated coactivator 3
- RAC-3
- Steroid receptor coactivator protein 3
- SRC-3
- Thyroid hormone receptor activator molecule 1
- TRAM-1
|
| Enzyme 15 Gene Name |
NCOA3 |
| Enzyme 15 Protein Sequence |
>Nuclear receptor coactivator 3
MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDID
NFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQA
LDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNG
VSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGE
DLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRC
IQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDR
HGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLA
DPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNI
MISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLST
LSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKE
SSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVS
SSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGN
VVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQE
KDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLK
SSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGS
SMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPT
LPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQV
SHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPE
LVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMN
QMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTA
GGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQ
QQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQ
PDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQ
FAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC
|
| Enzyme 15 Number of Residues |
1424 |
| Enzyme 15 Molecular Weight |
155292.5 |
| Enzyme 15 Theoretical pI |
7.51 |
| Enzyme 15 GO Classification |
| Function |
- binding
- hormone receptor binding
- molecular transducer activity
- nuclear hormone receptor binding
- protein binding
- receptor binding
- signal transducer activity
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transcription regulator activity
|
| Process |
- biological regulation
- regulation of biological process
- regulation of cellular process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
- signal transduction
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 15 General Function |
Involved in transcription coactivator activity |
| Enzyme 15 Specific Function |
Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit. Interacts with PSMB9 |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
32307126  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9Y6Q9  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
NCOA3_HUMAN  |
| Enzyme 15 PDB ID |
1KBH  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>4275 bp
ATGAGTGGATTAGGAGAAAACTTGGATCCACTGGCCAGTGATTCACGAAAACGCAAATTG
CCATGTGATACTCCAGGACAAGGTCTTACCTGCAGTGGTGAAAAACGGAGACGGGAGCAG
GAAAGTAAATATATTGAAGAATTGGCTGAGCTGATATCTGCCAATCTTAGTGATATTGAC
AATTTCAATGTCAAACCAGATAAATGTGCGATTTTAAAGGAAACAGTAAGACAGATACGT
CAAATAAAAGAGCAAGGAAAAACTATTTCCAATGATGATGATGTTCAAAAAGCCGATGTA
TCTTCTACAGGGCAGGGAGTTATTGATAAAGACTCCTTAGGACCGCTTTTACTTCAGGCA
TTGGATGGTTTCCTATTTGTGGTGAATCGAGACGGAAACATTGTATTTGTATCAGAAAAT
GTCACACAATACCTGCAATATAAGCAAGAGGACCTGGTTAACACAAGTGTTTACAATATC
TTACATGAAGAAGACAGAAAGGATTTTCTTAAGAATTTACCAAAATCTACAGTTAATGGA
GTTTCCTGGACAAATGAGACCCAAAGACAAAAAAGCCATACATTTAATTGCCGTATGTTG
ATGAAAACACCACATGATATTCTGGAAGACATAAACGCCAGTCCTGAAATGCGCCAGAGA
TATGAAACAATGCAGTGCTTTGCCCTGTCTCAGCCACGAGCTATGATGGAGGAAGGGGAA
GATTTGCAATCTTGTATGATCTGTGTGGCACGCCGCATTACTACAGGAGAAAGAACATTT
CCATCAAACCCTGAGAGCTTTATTACCAGACATGATCTTTCAGGAAAGGTTGTCAATATA
GATACAAATTCACTGAGATCCTCCATGAGGCCTGGCTTTGAAGATATAATCCGAAGGTGT
ATTCAGAGATTTTTTAGTCTAAATGATGGGCAGTCATGGTCCCAGAAACGTCACTATCAA
GAAGCTTATCTTAATGGCCATGCAGAAACCCCAGTATATCGATTCTCGTTGGCTGATGGA
ACTATAGTGACTGCACAGACAAAAAGCAAACTCTTCCGAAATCCTGTAACAAATGATCGA
CATGGCTTTGTCTCAACCCACTTCCTTCAGAGAGAACAGAATGGATATAGACCAAACCCA
AATCCTGTTGGACAAGGGATTAGACCACCTATGGCTGGATGCAACAGTTCGGTAGGCGGC
ATGAGTATGTCGCCAAACCAAGGCTTACAGATGCCGAGCAGCAGGGCCTATGGCTTGGCA
GACCCTAGCACCACAGGGCAGATGAGTGGAGCTAGGTATGGGGGTTCCAGTAACATAGCT
TCATTGACCCCTGGGCCAGGCATGCAATCACCATCTTCCTACCAGAACAACAACTATGGG
CTCAACATGAGTAGCCCCCCACATGGGAGTCCTGGTCTTGCCCCAAACCAGCAGAATATC
ATGATTTCTCCTCGTAATCGTGGGAGTCCAAAGATAGCCTCACATCAGTTTTCTCCTGTT
GCAGGTGTGCACTCTCCCATGGCATCTTCTGGCAATACTGGGAACCACAGCTTTTCCAGC
AGCTCTCTCAGTGCCCTGCAAGCCATCAGTGAAGGTGTGGGGACTTCCCTTTTATCTACT
CTGTCATCACCAGGCCCCAAATTGGATAACTCTCCCAATATGAATATTACCCAACCAAGT
AAAGTAAGCAATCAGGATTCCAAGAGTCCTCTGGGCTTTTATTGCGACCAAAATCCAGTG
GAGAGTTCAATGTGTCAGTCAAATAGCAGAGATCACCTCAGTGACAAAGAAAGTAAGGAG
AGCAGTGTTGAGGGGGCAGAGAATCAAAGGGGTCCTTTGGAAAGCAAAGGTCATAAAAAA
TTACTGCAGTTACTTACCTGTTCTTCTGATGACCGGGGTCATTCCTCCTTGACCAACTCC
CCCCTAGATTCAAGTTGTAAAGAATCTTCTGTTAGTGTCACCAGCCCCTCTGGAGTCTCC
TCCTCTACATCTGGAGGAGTATCCTCTACATCCAATATGCATGGGTCACTGTTACAAGAG
AAGCACCGGATTTTGCACAAGTTGCTGCAGAATGGGAATTCACCAGCTGAGGTAGCCAAG
ATTACTGCAGAAGCCACTGGGAAAGACACCAGCAGTATAACTTCTTGTGGGGACGGAAAT
GTTGTCAAGCAGGAGCAGCTAAGTCCTAAGAAGAAGGAGAATAATGCACTTCTTAGATAC
CTGCTGGACAGGGATGATCCTAGTGATGCACTCTCTAAAGAACTACAGCCCCAAGTGGAA
GGAGTGGATAATAAAATGAGTCAGTGCACCAGCTCCACCATTCCTAGCTCAAGTCAAGAG
AAAGACCCTAAAATTAAGACAGAGACAAGTGAAGAGGGATCTGGAGACTTGGATAATCTA
GATGCTATTCTTGGTGATCTGACTAGTTCTGACTTTTACAATAATTCCATATCCTCAAAT
GGTAGTCATCTGGGGACTAAGCAACAGGTGTTTCAAGGAACTAATTCTCTGGGTTTGAAA
AGTTCACAGTCTGTGCAGTCTATTCGTCCTCCATATAACCGAGCAGTGTCTCTGGATAGC
CCTGTTTCTGTTGGCTCAAGTCCTCCAGTAAAAAATATCAGTGCTTTCCCCATGTTACCA
AAGCAACCCATGTTGGGTGGGAATCCAAGAATGATGGATAGTCAGGAAAATTATGGCTCA
AGTATGGGTGGGCCAAACCGAAATGTGACTGTGACTCAGACTCCTTCCTCAGGAGACTGG
GGCTTACCAAACTCAAAGGCCGGCAGAATGGAACCTATGAATTCAAACTCCATGGGAAGA
CCAGGAGGAGATTATAATACTTCTTTACCCAGACCTGCACTGGGTGGCTCTATTCCCACA
TTGCCTCTTCGGTCTAATAGCATACCAGGTGCGAGACCAGTATTGCAACAGCAGCAGCAG
ATGCTTCAAATGAGGCCTGGTGAAATCCCCATGGGAATGGGGGCTAATCCCTATGGCCAA
GCAGCAGCATCTAACCAACTGGGTTCCTGGCCCGATGGCATGTTGTCCATGGAACAAGTT
TCTCATGGCACTCAAAATAGGCCTCTTCTTAGGAATTCCCTGGATGATCTTGTTGGGCCA
CCTTCCAACCTGGAAGGCCAGAGTGACGAAAGAGCATTATTGGACCAGCTGCACACTCTT
CTCAGCAACACAGATGCCACAGGCCTGGAAGAAATTGACAGAGCTTTGGGCATTCCTGAA
CTTGTCAATCAGGGACAGGCATTAGAGCCCAAACAGGATGCTTTCCAAGGCCAAGAAGCA
GCAGTAATGATGGATCAGAAGGCAGGATTATATGGACAGACATACCCAGCACAGGGGCCT
CCAATGCAAGGAGGCTTTCATCTTCAGGGACAATCACCATCTTTTAACTCTATGATGAAT
CAGATGAACCAGCAAGGCAATTTTCCTCTCCAAGGAATGCACCCACGAGCCAACATCATG
AGACCCCGGACAAACACCCCCAAGCAACTTAGAATGCAGCTTCAGCAGAGGCTGCAGGGC
CAGCAGTTTTTGAATCAGAGCCGACAGGCACTTGAATTGAAAATGGAAAACCCTACTGCT
GGTGGTGCTGCGGTGATGAGGCCTATGATGCAGCCCCAGGTGAGCTCCCAGCAGGGTTTT
CTTAATGCTCAAATGGTCGCCCAACGCAGCAGAGAGCTGCTAAGTCATCACTTCCGACAA
CAGAGGGTGGCTATGATGATGCAGCAGCAGCAGCAGCAGCAACAGCAGCAGCAGCAGCAG
CAGCAGCAGCAACAGCAACAGCAACAGCAACAGCAGCAACAGCAGCAAACCCAGGCCTTC
AGCCCACCTCCTAATGTGACTGCTTCCCCCAGCATGGATGGGCTTTTGGCAGGACCCACA
ATGCCACAAGCTCCTCCGCAACAGTTTCCATATCAACCAAATTATGGAATGGGACAACAA
CCAGATCCAGCCTTTGGTCGAGTGTCTAGTCCTCCCAATGCAATGATGTCGTCAAGAATG
GGTCCCTCCCAGAATCCCATGATGCAACACCCGCAGGCTGCATCCATCTATCAGTCCTCA
GAAATGAAGGGCTGGCCATCAGGAAATTTGGCCAGGAACAGCTCCTTTTCCCAGCAGCAG
TTTGCCCACCAGGGGAATCCTGCAGTGTATAGTATGGTGCACATGAATGGCAGCAGTGGT
CACATGGGACAGATGAACATGAACCCCATGCCCATGTCTGGCATGCCTATGGGTCCTGAT
CAGAAATACTGCTGA
|
| Enzyme 15 GenBank Gene ID |
NM_181659.2  |
| Enzyme 15 GeneCard ID |
NCOA3  |
| Enzyme 15 GenAtlas ID |
NCOA3  |
| Enzyme 15 HGNC ID |
HGNC:7670  |
| Enzyme 15 Chromosome Location |
2 |
| Enzyme 15 Locus |
20q12 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW: TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem. 1997 Oct 31;272(44):27629-34. [PubMed
]
- Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed
]
- Anzick SL, Kononen J, Walker RL, Azorsa DO, Tanner MM, Guan XY, Sauter G, Kallioniemi OP, Trent JM, Meltzer PS: AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science. 1997 Aug 15;277(5328):965-8. [PubMed
]
- Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8479-84. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Shirazi SK, Bober MA, Coetzee GA: Polymorphic exonic CAG microsatellites in the gene amplified in breast cancer (AIB1 gene). Clin Genet. 1998 Jul;54(1):102-3. [PubMed
]
- Chen H, Lin RJ, Xie W, Wilpitz D, Evans RM: Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell. 1999 Sep 3;98(5):675-86. [PubMed
]
- Werbajh S, Nojek I, Lanz R, Costas MA: RAC-3 is a NF-kappa B coactivator. FEBS Lett. 2000 Nov 24;485(2-3):195-9. [PubMed
]
- Wu RC, Qin J, Hashimoto Y, Wong J, Xu J, Tsai SY, Tsai MJ, O'Malley BW: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) Coactivator activity by I kappa B kinase. Mol Cell Biol. 2002 May;22(10):3549-61. [PubMed
]
- Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK: BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation. Mol Cell Biol. 2003 Sep;23(17):6210-20. [PubMed
]
- Kino T, Ichijo T, Chrousos GP: FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors. J Steroid Biochem Mol Biol. 2004 Dec;92(5):357-63. Epub 2004 Dec 19. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Zhang H, Sun L, Liang J, Yu W, Zhang Y, Wang Y, Chen Y, Li R, Sun X, Shang Y: The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 2006 Sep 20;25(18):4223-33. Epub 2006 Sep 7. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Zou JX, Revenko AS, Li LB, Gemo AT, Chen HW: ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification. Proc Natl Acad Sci U S A. 2007 Nov 13;104(46):18067-72. Epub 2007 Nov 12. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5256 |
| Enzyme 16 Name |
Histone acetyltransferase KAT2B |
| Enzyme 16 Synonyms |
- Histone acetyltransferase PCAF
- Histone acetylase PCAF
- Lysine acetyltransferase 2B
- P300/CBP-associated factor
- P/CAF
|
| Enzyme 16 Gene Name |
KAT2B |
| Enzyme 16 Protein Sequence |
>Histone acetyltransferase KAT2B
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAA
AGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTP
PRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEED
ADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKE
RQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPR
YETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQ
NSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSG
LEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSA
RDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFD
PKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKH
DILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFS
VIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSK
EPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNR
YYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
|
| Enzyme 16 Number of Residues |
832 |
| Enzyme 16 Molecular Weight |
93012.3 |
| Enzyme 16 Theoretical pI |
9.37 |
| Enzyme 16 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- histone acetyltransferase activity
- lysine N-acetyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- covalent chromatin modification
- histone acetylation
- histone modification
- metabolic process
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 16 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 16 Specific Function |
Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
38173798  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q92831  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
KAT2B_HUMAN  |
| Enzyme 16 PDB ID |
1CM0  |
| Enzyme 16 PDB File |
Show |
| Enzyme 16 3D Structure |
|
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>2499 bp
ATGTCCGAGGCTGGCGGGGCCGGGCCGGGCGGCTGCGGGGCAGGAGCCGGGGCAGGGGCC
GGGCCCGGGGCGCTGCCCCCGCAGCCTGCGGCGCTTCCGCCCGCGCCCCCGCAGGGCTCC
CCCTGCGCCGCTGCCGCCGGGGGCTCGGGCGCCTGCGGTCCGGCGACGGCAGTGGCTGCA
GCGGGCACGGCCGAAGGACCGGGAGGCGGTGGCTCGGCCCGAATCGCCGTGAAGAAAGCG
CAACTACGCTCCGCTCCGCGGGCCAAGAAACTGGAGAAACTCGGAGTGTACTCCGCCTGC
AAGGCCGAGGAGTCTTGTAAATGTAATGGCTGGAAAAACCCTAACCCCTCACCCACTCCC
CCCAGAGCCGACCTGCAGCAAATAATTGTCAGTCTAACAGAATCCTGTCGGAGTTGTAGC
CATGCCCTAGCTGCTCATGTTTCCCACCTGGAGAATGTGTCAGAGGAAGAAATGAACAGA
CTCCTGGGAATAGTATTGGATGTGGAATATCTCTTTACCTGTGTCCACAAGGAAGAAGAT
GCAGATACCAAACAAGTTTATTTCTATCTATTTAAGCTCTTGAGAAAGTCTATTTTACAA
AGAGGAAAACCTGTGGTTGAAGGCTCTTTGGAAAAGAAACCCCCATTTGAAAAACCTAGC
ATTGAACAGGGTGTGAATAACTTTGTGCAGTACAAATTTAGTCACCTGCCAGCAAAAGAA
AGGCAAACAATAGTTGAGTTGGCAAAAATGTTCCTAAACCGCATCAACTATTGGCATCTG
GAGGCACCATCTCAACGAAGACTGCGATCTCCCAATGATGATATTTCTGGATACAAAGAG
AACTACACAAGGTGGCTGTGTTACTGCAACGTGCCACAGTTCTGCGACAGTCTACCTCGG
TACGAAACCACACAGGTGTTTGGGAGAACATTGCTTCGCTCGGTCTTCACTGTTATGAGG
CGACAACTCCTGGAACAAGCAAGACAGGAAAAAGATAAACTGCCTCTTGAAAAACGAACT
CTAATCCTCACTCATTTCCCAAAATTTCTGTCCATGCTAGAAGAAGAAGTATATAGTCAA
AACTCTCCCATCTGGGATCAGGATTTTCTCTCAGCCTCTTCCAGAACCAGCCAGCTAGGC
ATCCAAACAGTTATCAATCCACCTCCTGTGGCTGGGACAATTTCATACAATTCAACCTCA
TCTTCCCTTGAGCAGCCAAACGCAGGGAGCAGCAGTCCTGCCTGCAAAGCCTCTTCTGGA
CTTGAGGCAAACCCAGGAGAAAAGAGGAAAATGACTGATTCTCATGTTCTGGAGGAGGCC
AAGAAACCCCGAGTTATGGGGGATATTCCGATGGAATTAATCAACGAGGTTATGTCTACC
ATCACGGACCCTGCAGCAATGCTTGGACCAGAGACCAATTTTCTGTCAGCACACTCGGCC
AGGGATGAGGCGGCAAGGTTGGAAGAGCGCAGGGGTGTAATTGAATTTCACGTGGTTGGC
AATTCCCTCAACCAGAAACCAAACAAGAAGATCCTGATGTGGCTGGTTGGCCTACAGAAC
GTTTTCTCCCACCAGCTGCCCCGAATGCCAAAAGAATACATCACACGGCTCGTCTTTGAC
CCGAAACACAAAACCCTTGCTTTAATTAAAGATGGCCGTGTTATTGGTGGTATCTGTTTC
CGTATGTTCCCATCTCAAGGATTCACAGAGATTGTCTTCTGTGCTGTAACCTCAAATGAG
CAAGTCAAGGGCTATGGAACACACCTGATGAATCATTTGAAAGAATATCACATAAAGCAT
GACATCCTGAACTTCCTCACATATGCAGATGAATATGCAATTGGATACTTTAAGAAACAG
GGTTTCTCCAAAGAAATTAAAATACCTAAAACCAAATATGTTGGCTATATCAAGGATTAT
GAAGGAGCCACTTTAATGGGATGTGAGCTAAATCCACGGATCCCGTACACAGAATTTTCT
GTCATCATTAAAAAGCAGAAGGAGATAATTAAAAAACTGATTGAAAGAAAACAGGCACAA
ATTCGAAAAGTTTACCCTGGACTTTCATGTTTTAAAGATGGAGTTCGACAGATTCCTATA
GAAAGCATTCCTGGAATTAGAGAGACAGGCTGGAAACCGAGTGGAAAAGAGAAAAGTAAA
GAGCCCAGAGACCCTGACCAGCTTTACAGCACGCTCAAGAGCATCCTCCAGCAGGTGAAG
AGCCATCAAAGCGCTTGGCCCTTCATGGAACCTGTGAAGAGAACAGAAGCTCCAGGATAT
TATGAAGTTATAAGGTTCCCCATGGATCTGAAAACCATGAGTGAACGCCTCAAGAATAGG
TACTACGTGTCTAAGAAATTATTCATGGCAGACTTACAGCGAGTCTTTACCAATTGCAAA
GAGTACAACCCCCCTGAGAGTGAATACTACAAATGTGCCAATATCCTGGAGAAATTCTTC
TTCAGTAAAATTAAGGAAGCTGGATTAATTGACAAGTGA
|
| Enzyme 16 GenBank Gene ID |
BC060823  |
| Enzyme 16 GeneCard ID |
KAT2B  |
| Enzyme 16 GenAtlas ID |
KAT2B  |
| Enzyme 16 HGNC ID |
HGNC:8638  |
| Enzyme 16 Chromosome Location |
3 |
| Enzyme 16 Locus |
3p24 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996 Nov 29;87(5):953-9. [PubMed
]
- Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW: TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J Biol Chem. 1997 Oct 31;272(44):27629-34. [PubMed
]
- Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW: Steroid receptor coactivator-1 is a histone acetyltransferase. Nature. 1997 Sep 11;389(6647):194-8. [PubMed
]
- Zhang W, Bieker JJ: Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9855-60. [PubMed
]
- Harrod R, Kuo YL, Tang Y, Yao Y, Vassilev A, Nakatani Y, Giam CZ: p300 and p300/cAMP-responsive element-binding protein associated factor interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone acetyltransferase/activator-enhancer complex. J Biol Chem. 2000 Apr 21;275(16):11852-7. [PubMed
]
- Chakraborty S, Senyuk V, Sitailo S, Chi Y, Nucifora G: Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. J Biol Chem. 2001 Nov 30;276(48):44936-43. Epub 2001 Sep 21. [PubMed
]
- Bres V, Tagami H, Peloponese JM, Loret E, Jeang KT, Nakatani Y, Emiliani S, Benkirane M, Kiernan RE: Differential acetylation of Tat coordinates its interaction with the co-activators cyclin T1 and PCAF. EMBO J. 2002 Dec 16;21(24):6811-9. [PubMed
]
- Zhao Q, Cumming H, Cerruti L, Cunningham JM, Jane SM: Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1. J Biol Chem. 2004 Oct 1;279(40):41477-86. Epub 2004 Jul 24. [PubMed
]
- Gangisetty O, Lauffart B, Sondarva GV, Chelsea DM, Still IH: The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases. Oncogene. 2004 Apr 1;23(14):2559-63. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM: Structure and ligand of a histone acetyltransferase bromodomain. Nature. 1999 Jun 3;399(6735):491-6. [PubMed
]
- Mujtaba S, He Y, Zeng L, Farooq A, Carlson JE, Ott M, Verdin E, Zhou MM: Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain. Mol Cell. 2002 Mar;9(3):575-86. [PubMed
]
- Zhu P, Zhou W, Wang J, Puc J, Ohgi KA, Erdjument-Bromage H, Tempst P, Glass CK, Rosenfeld MG: A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol Cell. 2007 Aug 17;27(4):609-21. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5257 |
| Enzyme 17 Name |
Carnitine O-acetyltransferase |
| Enzyme 17 Synonyms |
- Carnitine acetylase
- Carnitine acetyltransferase
- CAT
- CrAT
|
| Enzyme 17 Gene Name |
CRAT |
| Enzyme 17 Protein Sequence |
>Carnitine O-acetyltransferase
MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSE
EEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSP
GVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSC
RVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSS
LQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVY
RSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIE
YTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKD
FPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVK
AMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMD
TSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNA
ARLAHYLEKALLDMRALLQSHPRAKL
|
| Enzyme 17 Number of Residues |
626 |
| Enzyme 17 Molecular Weight |
70857.1 |
| Enzyme 17 Theoretical pI |
8.63 |
| Enzyme 17 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in acyltransferase activity |
| Enzyme 17 Specific Function |
Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
- acetyl-CoA + carnitine = CoA + O-acetylcarnitine [RN:R02396]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
55958023  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P43155  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
CACP_HUMAN  |
| Enzyme 17 PDB ID |
1S5O  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1881 bp
ATGTTAGCCTTCGCTGCCAGGACCGTGGTGAAGCCTCTGGGCTTCCTGAAGCCCTTCTCC
TTGATGAAGGCTTCCAGCCGCTTCAAGGCACACCAGGATGCACTGCCACGGCTGCCCGTG
CCCCCTCTCCAGCAGTCCCTGGACCACTACCTGAAGGCGCTGCAGCCCATCGTGAGTGAG
GAGGAGTGGGCCCACACCAAGCAGCTGGTGGATGAGTTTCAGGCCTCAGGAGGTGTAGGG
GAGCGCCTGCAGAAGGGGCTGGAGCGTCGGGCCAGGAAGACGGAGAACTGGCTGTCTGAG
TGGTGGCTCAAGACCGCCTACCTCCAGTACCGCCAGCCTGTGGTCATCTACTCGAGCCCA
GGCGTGATGCTACCCAAGCAGGACTTCGTGGACCTGCAGGGTCAGCTCCGATTTGCTGCC
AAACTCATTGAGGGTGTGTTGGATTTCAAGGTCATGATTGACAACGAGACCCTGCCCGTG
GAGTACCTGGGGGGGAAGCCACTGTGCATGAACCAGTACTATCAGATCTTGTCCTCCTGC
CGAGTGCCGGGCCCCAAGCAGGACACAGTCAGCAACTTCAGCAAGACCAAGAAGCCTCCC
ACGCACATCACCGTGGTACACAACTACCAGTTTTTTGAGCTGGATGTGTACCACAGTGAC
GGGACACCCCTCACTGCGGATCAGATCTTTGTGCAGCTGGAGAAGATCTGGAACTCATCC
CTACAGACCAACAAGGAGCCTGTGGGCATCCTCACCTCCAACCACCGCAACTCCTGGGCC
AAGGCATACAACACCCTCATCAAAGACAAGGTGAACCGGGATTCCGTGCGCTCCATCCAG
AAGAGCATCTTCACCGTGTGCCTAGATGCAACCATGCCCAGGGTCTCAGAAGACGTGTAC
CGCAGCCACGTGGCAGGCCAGATGCTGCATGGGGGCGGCAGCAGGCTCAACAGCGGCAAC
CGCTGGTTCGACAAGACGCTGCAGTTCATCGTGGCAGAAGATGGCTCCTGTGGGCTTGTG
TACGAGCATGCTGCAGCGGAGGGGCCCCCTATTGTCACCCTTCTGGACTATGTCATCGAG
TACACGAAGAAACCCGAGCTTGTGCGGTCTCCCCTGGTGCCCCTGCCCATGCCCAAGAAG
CTGCGGTTCAACATCACCCCCGAGATCAAGAGCGACATCGAGAAGGCCAAGCAGAACCTC
AGCATCATGATCCAGGACCTGGATATCACCGTGATGGTGTTCCACCATTTTGGAAAAGAC
TTCCCCAAGTCGGAGAAGCTAAGCCCAGATGCCTTCATCCAGATGGCTTTGCAGCTGGCC
TACTACAGGATCTACGGACAGGCATGTGCCACCTATGAAAGTGCCTCCCTGCGCATGTTT
CACCTGGGCCGCACCGACACCATCCGCTCGGCTTCCATGGACTCACTCACCTTTGTCAAG
GCCATGGATGACTCCAGCGTCACGGAGCACCAGAAGGTGGAGCTGCTGCGGAAGGCCGTG
CAGGCCCACCGAGGCTACACCGACCGGGCCATCCGCGGGGAGGCCTTTGATCGACACCTG
CTGGGCCTGAAGCTGCAGGCCATCGAGGACCTGGTGAGCATGCCCGACATCTTCATGGAC
ACCTCCTACGCCATCGCCATGCACTTCCACCTCTCCACCAGCCAGGTCCCTGCCAAGACA
GACTGTGTCATGTTCTTCGGGCCCGTGGTCCCCGACGGCTACGGTGTCTGCTATAACCCC
ATGGAGGCCCACATCAACTTCTCCCTGTCGGCCTACAACAGCTGCGCGGAGACCAACGCC
GCCCGCCTGGCGCATTACCTGGAGAAGGCGCTCCTGGACATGCGTGCCCTGCTGCAGAGC
CACCCCCGGGCCAAGCTCTGA
|
| Enzyme 17 GenBank Gene ID |
AL158151  |
| Enzyme 17 GeneCard ID |
CRAT  |
| Enzyme 17 GenAtlas ID |
CRAT  |
| Enzyme 17 HGNC ID |
HGNC:2342  |
| Enzyme 17 Chromosome Location |
9 |
| Enzyme 17 Locus |
9q34.1 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Corti O, DiDonato S, Finocchiaro G: Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations. Biochem J. 1994 Oct 1;303 ( Pt 1):37-41. [PubMed
]
- Corti O, Finocchiaro G, Rossi E, Zuffardi O, DiDonato S: Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. Genomics. 1994 Sep 1;23(1):94-9. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Wu D, Govindasamy L, Lian W, Gu Y, Kukar T, Agbandje-McKenna M, McKenna R: Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer. J Biol Chem. 2003 Apr 11;278(15):13159-65. Epub 2003 Jan 31. [PubMed
]
- Govindasamy L, Kukar T, Lian W, Pedersen B, Gu Y, Agbandje-McKenna M, Jin S, McKenna R, Wu D: Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase. J Struct Biol. 2004 Jun;146(3):416-24. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5258 |
| Enzyme 18 Name |
Diamine acetyltransferase 1 |
| Enzyme 18 Synonyms |
- Polyamine N-acetyltransferase 1
- Putrescine acetyltransferase
- Spermidine/spermine N(1)-acetyltransferase 1
- SSAT
- SSAT-1
|
| Enzyme 18 Gene Name |
SAT1 |
| Enzyme 18 Protein Sequence |
>Diamine acetyltransferase 1
MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVP
KEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRC
RCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE
|
| Enzyme 18 Number of Residues |
171 |
| Enzyme 18 Molecular Weight |
20023.8 |
| Enzyme 18 Theoretical pI |
4.82 |
| Enzyme 18 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 18 Specific Function |
Enzyme which catalyzes the acetylation of polyamines. Substrate specificity:norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine |
| Enzyme 18 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 18 Reactions |
- acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine [RN:R03910]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P21673  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
SAT1_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>516 bp
ATGGCTAAATTCGTGATCCGCCCAGCCACTGCCGCCGACTGCAGTGACATACTGCGGCTG
ATCAAGGAGCTGGCTAAATATGAATACATGGAAGAACAAGTAATCTTAACTGAAAAAGAT
CTGCTAGAAGATGGTTTTGGAGAGCACCCCTTTTACCACTGCCTGGTTGCAGAAGTGCCG
AAAGAGCACTGGACTCCGGAAGGACACAGCATTGTTGGTTTTGCCATGTACTATTTTACC
TATGACCCGTGGATTGGCAAGTTATTGTATCTTGAGGACTTCTTCGTGATGAGTGATTAT
AGAGGCTTTGGCATAGGATCAGAAATTCTGAAGAATCTAAGCCAGGTTGCAATGAGGTGT
CGCTGCAGCAGCATGCACTTCTTGGTAGCAGAATGGAATGAACCATCCATCAACTTCTAT
AAAAGAAGAGGTGCTTCTGATCTGTCCAGTGAAGAGGGTTGGAGACTGTTCAAGATCGAC
AAGGAGTACTTGCTAAAAATGGCAACAGAGGAGTGA
|
| Enzyme 18 GenBank Gene ID |
M77693  |
| Enzyme 18 GeneCard ID |
SAT1  |
| Enzyme 18 GenAtlas ID |
SAT1  |
| Enzyme 18 HGNC ID |
HGNC:10540  |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Casero RA Jr, Celano P, Ervin SJ, Applegren NB, Wiest L, Pegg AE: Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. J Biol Chem. 1991 Jan 15;266(2):810-4. [PubMed
]
- Xiao L, Celano P, Mank AR, Pegg AE, Casero RA Jr: Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase. Biochem Biophys Res Commun. 1991 Aug 30;179(1):407-15. [PubMed
]
- Xiao L, Celano P, Mank AR, Griffin C, Jabs EW, Hawkins AL, Casero RA Jr: Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1). Biochem Biophys Res Commun. 1992 Sep 30;187(3):1493-502. [PubMed
]
- Xiao L, Casero RA Jr: Differential transcription of the human spermidine/spermine N1-acetyltransferase (SSAT) gene in human lung carcinoma cells. Biochem J. 1996 Jan 15;313 ( Pt 2):691-6. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Casero RA Jr, Celano P, Ervin SJ, Wiest L, Pegg AE: High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma. Biochem J. 1990 Sep 15;270(3):615-20. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Bewley MC, Graziano V, Jiang J, Matz E, Studier FW, Pegg AE, Coleman CS, Flanagan JM: Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target. Proc Natl Acad Sci U S A. 2006 Feb 14;103(7):2063-8. Epub 2006 Feb 2. [PubMed
]
- Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS: Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. Biochemistry. 2007 Jun 19;46(24):7187-95. Epub 2007 May 22. [PubMed
]
- Zhu YQ, Zhu DY, Yin L, Zhang Y, Vonrhein C, Wang DC: Crystal structure of human spermidine/spermine N1-acetyltransferase (hSSAT): the first structure of a new sequence family of transferase homologous superfamily. Proteins. 2006 Jun 1;63(4):1127-31. [PubMed
]
- Oosterwijk JC, Richard G, van der Wielen MJ, van de Vosse E, Harth W, Sandkuijl LA, Bakker E, van Ommen GJ: Molecular genetic analysis of two families with keratosis follicularis spinulosa decalvans: refinement of gene localization and evidence for genetic heterogeneity. Hum Genet. 1997 Oct;100(5-6):520-4. [PubMed
]
- Gimelli G, Giglio S, Zuffardi O, Alhonen L, Suppola S, Cusano R, Lo Nigro C, Gatti R, Ravazzolo R, Seri M: Gene dosage of the spermidine/spermine N(1)-acetyltransferase ( SSAT) gene with putrescine accumulation in a patient with a Xp21.1p22.12 duplication and keratosis follicularis spinulosa decalvans (KFSD). Hum Genet. 2002 Sep;111(3):235-41. Epub 2002 Aug 1. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5259 |
| Enzyme 19 Name |
Serotonin N-acetyltransferase |
| Enzyme 19 Synonyms |
- Serotonin acetylase
- Aralkylamine N-acetyltransferase
- AA-NAT
|
| Enzyme 19 Gene Name |
AANAT |
| Enzyme 19 Protein Sequence |
>Serotonin N-acetyltransferase
MSTQSTHPLKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVL
GVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLMQESLTLHRSGGHIAH
LHVLAVHRAFRQQGRGPILLWRYLHHLGSQPAVRRAALMCEDALVPFYERFSFHAVGPCA
ITVGSLTFMELHCSLRGHPFLRRNSGC
|
| Enzyme 19 Number of Residues |
207 |
| Enzyme 19 Molecular Weight |
23343.8 |
| Enzyme 19 Theoretical pI |
7.57 |
| Enzyme 19 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 19 Specific Function |
Catalyzes the N-acetylation of serotonin into N- acetylserotonin. Controls the night/day rhythm of melatonin production in the pineal gland. Has a relative affinity for hydroxylated versus non-hydroxylated arylalkylamines |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine [RN:R03760]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q16613  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
SNAT_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>624 bp
ATGTCCACGCAGAGCACCCACCCCCTGAAACCTGAGGCCCCACGTCTGCCACCTGGGATC
CCCGAGTCCCCGAGCTGTCAGCGGCGCCACACACTCCCTGCCAGTGAGTTTCGCTGCCTC
ACCCCGGAGGACGCTGTCAGCGCCTTTGAGATCGAGCGTGAAGCCTTCATCTCCGTCTTG
GGCGTCTGCCCCCTGTACCTGGATGAGATCCGGCACTTCCTGACCCTATGTCCAGAGCTG
TCCCTGGGCTGGTTCGAGGAGGGCTGCCTTGTGGCCTTCATCATCGGCTCGCTCTGGGAC
AAGGAGAGACTCATGCAGGAGTCACTGACGCTGCACAGGTCTGGGGGCCACATAGCCCAC
CTGCATGTGCTGGCCGTGCACCGCGCCTTCCGGCAGCAGGGCAGGGGCCCCATCCTGCTG
TGGCGCTACCTGCACCACCTGGGCAGCCAGCCGGCCGTGCGCCGGGCCGCGCTCATGTGC
GAGGACGCGCTGGTACCCTTCTATGAGAGGTTCAGCTTCCACGCCGTGGGCCCCTGCGCC
ATCACCGTGGGCTCCCTCACCTTCATGGAGCTCCACTGCTCCCTGCGGGGCCACCCCTTC
CTGCGCAGGAACAGCGGCTGCTGA
|
| Enzyme 19 GenBank Gene ID |
U40347  |
| Enzyme 19 GeneCard ID |
AANAT  |
| Enzyme 19 GenAtlas ID |
AANAT  |
| Enzyme 19 HGNC ID |
HGNC:19  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
17q25 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR: The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression. Genomics. 1996 May 15;34(1):76-84. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Coon SL, Weller JL, Korf HW, Namboodiri MA, Rollag M, Klein DC: cAmp regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation. J Biol Chem. 2001 Jun 29;276(26):24097-107. Epub 2001 Apr 19. [PubMed
]
- Konturek SJ, Konturek PC, Brzozowski T, Bubenik GA: Role of melatonin in upper gastrointestinal tract. J Physiol Pharmacol. 2007 Dec;58 Suppl 6:23-52. [PubMed
]
- Hohjoh H, Takasu M, Shishikura K, Takahashi Y, Honda Y, Tokunaga K: Significant association of the arylalkylamine N-acetyltransferase ( AA-NAT) gene with delayed sleep phase syndrome. Neurogenetics. 2003 Apr;4(3):151-3. Epub 2002 Nov 29. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5260 |
| Enzyme 20 Name |
3-ketoacyl-CoA thiolase, mitochondrial |
| Enzyme 20 Synonyms |
- Acetyl-CoA acyltransferase
- Beta-ketothiolase
- Mitochondrial 3-oxoacyl-CoA thiolase
- T1
|
| Enzyme 20 Gene Name |
ACAA2 |
| Enzyme 20 Protein Sequence |
>3-ketoacyl-CoA thiolase, mitochondrial
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
|
| Enzyme 20 Number of Residues |
397 |
| Enzyme 20 Molecular Weight |
41923.8 |
| Enzyme 20 Theoretical pI |
8.21 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 20 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 20 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 20 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
12804931  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P42765  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
THIM_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1194 bp
ATGGCTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTGCTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
|
| Enzyme 20 GenBank Gene ID |
BC001918  |
| Enzyme 20 GeneCard ID |
ACAA2  |
| Enzyme 20 GenAtlas ID |
ACAA2  |
| Enzyme 20 HGNC ID |
HGNC:83  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
18q21.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5262 |
| Enzyme 21 Name |
Testis-specific chromodomain protein Y 1 |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
CDY1 |
| Enzyme 21 Protein Sequence |
>Testis-specific chromodomain protein Y 1
MASQEFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQTE
KQKKLTWTTTSRIFSNNARRRTSRSTKANYSKNSPKTPVTDKHHRSKNRKLFAASKNVRR
KAASILSDTKNMEIINSTIETLAPDSPFDHKTVSGFQKLEKLDPIAADQQDTVVFKVTEG
KLLRDPLSRPGAEQTGIQNKTQIHPLMSQMSGSVTASMATGSATRKGIVVLIDPLAANGT
TDMHTSVPRVKGGQRNITDDSRDQPFIKKMHFTIRLTESASTYRDIVVKKEDGFTQIVLS
TRSTEKNALNTEVIKEIVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVKHLRNNRNT
ASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTTF
GQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQIK
ELASYNPIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESMLKYVENKIDEF
|
| Enzyme 21 Number of Residues |
540 |
| Enzyme 21 Molecular Weight |
60472.6 |
| Enzyme 21 Theoretical pI |
9.61 |
| Enzyme 21 GO Classification |
| Function |
- binding
- catalytic activity
- chromatin binding
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin assembly or disassembly
- chromatin organization
- chromosome organization
- metabolic process
- organelle organization
|
| Component |
- chromatin
- chromosomal part
- intracellular membrane-bounded organelle
- intracellular organelle part
- membrane-bounded organelle
- nucleus
- organelle
- organelle part
|
|
| Enzyme 21 General Function |
Involved in chromatin binding |
| Enzyme 21 Specific Function |
Has histone acetyltransferase activity, with a preference for histone H4 |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
25453481  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9Y6F8  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
CDY1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1623 bp
ATGGCTTCCCAGGAGTTTGAGGTTGAAGCTATTGTTGACAAAAGACAGGATAAAAATGGG
AATACACAGTATTTGGTTCGGTGGAAAGGTTATGACAAACAGGATGACACTTGGGAACCA
GAGCAGCACCTCATGAACTGTGAAAAATGTGTACATGATTTTAATAGACGACAGACTGAA
AAACAGAAAAAACTGACATGGACTACAACCAGTAGAATTTTTTCAAACAATGCCAGAAGA
AGAACTTCCAGATCTACAAAAGCAAACTATTCTAAGAACTCTCCTAAAACGCCAGTGACT
GATAAACACCACAGGTCCAAAAACCGCAAGTTATTTGCTGCCAGCAAGAACGTTAGGAGA
AAGGCAGCTTCAATTCTCTCCGACACAAAGAATATGGAGATAATAAATTCAACTATTGAG
ACCCTTGCACCTGACAGCCCCTTTGACCACAAAACTGTGAGTGGCTTTCAGAAACTTGAG
AAACTGGACCCTATTGCAGCAGATCAGCAGGACACGGTGGTCTTCAAGGTGACAGAAGGG
AAACTCCTCCGGGACCCTTTGTCACGTCCTGGTGCAGAACAGACTGGAATACAGAACAAG
ACTCAGATACACCCACTAATGTCGCAGATGTCTGGCTCAGTTACTGCTTCTATGGCCACA
GGTTCAGCTACCCGAAAGGGTATAGTGGTATTAATAGACCCATTAGCAGCCAATGGGACA
ACAGACATGCATACCTCAGTTCCAAGAGTGAAAGGTGGGCAAAGAAATATTACTGATGAC
AGCAGAGACCAGCCTTTTATCAAGAAGATGCACTTCACCATAAGGCTAACAGAAAGTGCC
AGCACATACAGAGACATTGTAGTGAAGAAAGAGGATGGATTCACCCAGATAGTGCTATCA
ACTAGATCGACAGAAAAAAATGCACTGAATACAGAAGTAATTAAAGAAATAGTTAATGCT
CTGAATAGCGCTGCTGCAGATGACAGCAAGCTCGTGCTGTTCAGTGCAGCTGGAAGTGTC
TTTTGCTGCGGTCTTGATTTTGGGTACTTTGTGAAGCACTTAAGGAATAACAGAAACACA
GCAAGCCTTGAAATGGTGGACACCATCAAGAACTTTGTGAATACTTTTATTCAATTTAAA
AAGCCTATTGTTGTATCAGTCAATGGCCCTGCGATTGGACTAGGTGCATCCATCCTGCCT
CTTTGTGATCTCGTGTGGGCTAATGAAAAGGCTTGGTTCCAAACCCCTTATACGACCTTT
GGACAGAGTCCAGATGGCTGTTCTTCTATTACATTCCCCAAAATGATGGGTAAAGCATCT
GCCAATGAAATGTTAATTGCTGGGCGAAAGCTGACAGCAAGGGAGGCATGCGCCAAAGGC
CTGGTCTCTCAGGTATTTTTGACTGGAACTTTCACCCAAGAGGTTATGATTCAAATTAAG
GAGCTTGCCTCATACAATCCAATTGTACTGGAAGAATGTAAGGCCCTCGTTCGCTGTAAT
ATTAAGTTGGAGTTGGAACAGGCCAATGAGAGAGAGTGTGAGGTGCTGAGGAAGATCTGG
AGCTCAGCCCAAGGGATAGAATCCATGTTAAAGTATGTTGAAAATAAAATTGATGAGTTT
TAA
|
| Enzyme 21 GenBank Gene ID |
NM_170723.1  |
| Enzyme 21 GeneCard ID |
CDY1  |
| Enzyme 21 GenAtlas ID |
CDY1  |
| Enzyme 21 HGNC ID |
HGNC:1809  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Lahn BT, Page DC: Functional coherence of the human Y chromosome. Science. 1997 Oct 24;278(5338):675-80. [PubMed
]
- Lahn BT, Page DC: Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome. Nat Genet. 1999 Apr;21(4):429-33. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lahn BT, Tang ZL, Zhou J, Barndt RJ, Parvinen M, Allis CD, Page DC: Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis. Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8707-12. Epub 2002 Jun 18. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5264 |
| Enzyme 22 Name |
Fatty acid synthase |
| Enzyme 22 Synonyms |
- [Acyl-carrier-protein] S-acetyltransferase
- [Acyl-carrier-protein] S-malonyltransferase
- 3-oxoacyl-[acyl-carrier-protein] synthase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
- Enoyl-[acyl-carrier-protein] reductase
- Oleoyl-[acyl-carrier-protein] hydrolase
|
| Enzyme 22 Gene Name |
FASN |
| Enzyme 22 Protein Sequence |
>Fatty acid synthase
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
|
| Enzyme 22 Number of Residues |
2511 |
| Enzyme 22 Molecular Weight |
273424.1 |
| Enzyme 22 Theoretical pI |
6.41 |
| Enzyme 22 GO Classification |
| Function |
- acyl carrier activity
- amino acid binding
- binding
- carboxylic acid binding
- catalytic activity
- cation binding
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- oxidoreductase activity
- phosphopantetheine binding
- substrate-specific transporter activity
- transferase activity
- transition metal ion binding
- transporter activity
- zinc ion binding
|
| Process |
- biosynthetic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in transferase activity |
| Enzyme 22 Specific Function |
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- a (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = a hexadec-2-enoyl-[acyl-carrier protein] + H2O [RN:R04462]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
41872631  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P49327  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
FAS_HUMAN  |
| Enzyme 22 PDB ID |
1XKT  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>7536 bp
ATGGAGGAGGTGGTGATTGCCGGCATGTCCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCGGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGTCACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAATGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCCGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
CGGGTGTACGCCACCATCCTGAACGCCGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCCTCAGGGGATATCCAGGAGCAGCTCATCCGCTCGTTGTACCAGTCGGCC
GGAGTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGCACAGGCACCAAGGTGGGC
GACCCCCAGGAGCTGAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTG
CTCATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTGGCAGCC
CTGGCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCAT
AGCCCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCC
CTGCCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACGTG
CACATCATCCTGAGGCCCAACACGCAGCCGCCCCCCGCACCCGCCCCACATGCCACCCTG
CCCCGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAG
GGCCTCCGGCACAGCCAGGACCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTC
CCCGCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGCGCGGTGGCCCA
GAGGTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGC
ACACAGTGGCGCGGGATGGGGCTGAGCCTCATGCGCCTGGACCGCTTCCGAGATTCCATC
CTACGCTCCGATGAGGCTGTGAAGCCATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGC
ACAGACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAG
ATAGGCCTCATAGACCTGCTGAGCTGCATGGGGCTGAGGCCAGATGGCATCGTCGGCCAC
TCCCTGGGGGAGGTGGCCTGTGGCTACGCCGACGGCTGCCTGTCCCAGGAGGAGGCCGTC
CTCGCTGCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCATCTCCCGCCGGGCGCCATG
GCAGCCGTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCGGGCGTGGTGCCC
GCCTGCCACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAG
TTCGTGGAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATG
GCCTTCCACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAG
GTGATCCGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCC
CAGTGGCACAGCAGCCTGGCACGCACGTCCTCCGCCGAGTACAATGTCAACAACCTGGTG
AGCCCTGTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAG
ATCGCGCCCCACGCCCTGCTGCAGGCTGTCCTGAAGCGTGGCCTGAAGCCGAGCTGCACC
ATCATCCCCCTGATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATC
GGCAGGCTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAG
TTCCCAGCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTG
GCCTGGGACGTGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCGCC
ATCTACAACATCGACACCAGCTCCGAGTCTCCTGACCACTACCTGGTGGACCACACCCTC
GACGGTCGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCC
CGCGCCCTGGGCCTGGGCGTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCTGCAC
CAGGCCACCATCCTGCCCAAGACTGGGACAGTGTCCCTGGAGGTACGGCTCCTGGAGGCC
TCCCGTGCCTTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAG
TGGGATGACCCTGACCCCAGGCTCTTCGACCACCCGGAAAGCCCCACCCCCAACCCCACG
GAGCCCCTCTTCCTGGCCCAGGCTGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGAC
TACGGCCCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTG
CTGTGGAAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGC
TCGGCCAAGCACGGCCTGTACCTGCCCACCCGTGTCACCGCCATCCACATCGACCCTGCC
ACCCACAGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTG
AGCAGGTGGCTGAGGGTCACAGTGGCCGGAGGCGTCCACATCTCCGGGCTCCACACTGAG
TCGGCCCCGCGGCGGCAGCAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACT
CCCCACACGGAGGAGGGGTGCCTGTCTGAGCGCGCTGCCCTGCAGGAGGAGCTGCAACTG
TGCAAGGGGCTGGTGCAGGCACTGCAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTG
GTGCCCGGACTGGATGGGGCCCAGATCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGG
CTGTTGTCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAG
GTGCTGGCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGAC
TCCCCGGCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATG
AAGGTGGTGGAGGTGCTGGCTGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTC
AGCCCCCATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTG
GAGGCTGCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCA
GACCCTGCCCCCAGCGCCCTGGGCAGCGCCGACCTCCTGGTGTGCAACTGTGCTGTGGCT
GCCCTCGGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGC
TTTCTGCTCCTGCACACACTGCTCCGGGGGCACCCCCTCGGGGACATCGTGGCCTTCCTC
ACCTCCACTGAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTC
TTCTCCAGGGTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCTCCACGCTC
TTCCTGTGCCGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACC
AGCTTCCGCTGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCT
GTGTGGCTGAAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTC
CGCCGAGAGCCCGGCGGGAACCGCCTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACC
TCCCACGTCCCGGAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGAC
CTGGTGATGAACGTCTACCGCGACGGGGCCTGGGGGGCTTTCCGCCACTTCCTGCTGGAG
GAGGACAAGCCTGAGGAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGAC
CTGTCCTCCATCCGCTGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGC
GCCCAGCTCTGCACGGTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACT
GGCAAGCTGTCCCCTGATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGT
ATGGAGTTCTCGGGCCGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAG
GGCCTGGCCACCTCTGTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGG
ACGCTGGAGGAGGCGGCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTG
GTGCGTGGGCGGGTGCGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTG
GGCCAGGCCGCCATCGCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGG
TCGGCTGAGAAGCGGGCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTC
GCCAACTCCCGGGACACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGC
GTTGACCTGGTCTTGAACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTG
GCTACGCACGGTCGCTTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTC
GGCATGGCTATCTTCCTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTC
AACGAGAGCAGTGCTGACTGGCGGGAGGTGTGGGCGCTTGTGCAGGCCGGCATCCGGGAT
GGGGTGGTACGGCCCCTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTC
CGCTACATGGCCCAAGGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAG
CCGGAGGCAGTGCTGAAGGGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTC
TGCCCGGCCCACAAGAGCTACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTG
GCGCAGTGGCTGATACAGCGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATC
CGGACAGGCTACCAGGCCAAGCAGGTCCGCCGGTGGAGGCGCCAGGGCGTACAGGTGCAG
GTGTCCACCAGCAACATCAGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCG
CAGCTTGGGCCCGTGGGCGGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTG
GAGAACCAGACCCCAGAGTTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTG
AACCTGGACAGGGTGACCCGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCC
TCTGTGAGCTGCGGGCGTGGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCC
ATGGAGCGTATCTGTGAGAAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGG
GGCGCCATCGGCGACGTGGGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTC
AGTGGCACGCTGCCCCAGCGCATGGCGTCCTGCCTGGAGGTGCTGGACCTCTTCCTGAAC
CAGCCCCACATGGTCCTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGAC
AGGGACAGCCAGCGGGACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTG
GCTGCTGTCAACCTGGACAGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGTG
GAGGTGCGCCAGACGCTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGG
CAACTCACGCTCCGGAAACTGCAGGAGCTGTCCTCAAAGGCGGATGAGGCCAGCGAGCTG
GCATGCCCCACGCCCAAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGC
TCCCTGCTGGTGAACCCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCG
GAGCGGCCCCTGTTCCTGGTGCACCCAATCGAGGGCTCCACCACCGTGTTCCACAGCCTG
GCCTCCCGGCTCAGCATCCCCACCTATGGCCTGCAGTGCACCCGAGCTGCGCCCCTTGAC
AGCATCCACAGCCTGGCTGCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGC
CCCTACCGCGTGGCCGGCTACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAG
CTGCAGGCCCAGCAGAGCCCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCG
CCCACCTACGTACTGGCCTACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTGAG
GCTGAGGCTGAGACGGAGGCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCAC
AACAGGGTGCTGGAGGCGCTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCC
GTGGACCTGATCATCAAGAGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCC
CGGTCCTTCTACTACAAGCTGCGTGCCGCTGAGCAGTACACACCCAAGGCCAAGTACCAT
GGCAACGTGATGCTACTGCGCGCCAAGACGGGTGGCGCCTACGGCGAGGACCTGGGCGCG
GACTACAACCTCTCCCAGGTATGCGACGGGAAAGTATCCGTCCACGTCATCGAGGGTGAC
CACCGCACGCTGCTGGAGGGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCC
CTGGCTGAGCCACGCGTGAGCGTGCGGGAGGGCTAG
|
| Enzyme 22 GenBank Gene ID |
NM_004104.4  |
| Enzyme 22 GeneCard ID |
FASN  |
| Enzyme 22 GenAtlas ID |
FASN  |
| Enzyme 22 HGNC ID |
HGNC:3594  |
| Enzyme 22 Chromosome Location |
1 |
| Enzyme 22 Locus |
17q25 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed
]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed
]
- Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Brink J, Ludtke SJ, Yang CY, Gu ZW, Wakil SJ, Chiu W: Quaternary structure of human fatty acid synthase by electron cryomicroscopy. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):138-43. Epub 2001 Dec 26. [PubMed
]
- Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA: Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15567-72. Epub 2004 Oct 26. [PubMed
]
- Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U: Mechanism and substrate recognition of human holo ACP synthase. Chem Biol. 2007 Nov;14(11):1243-53. [PubMed
]
- Pemble CW 4th, Johnson LC, Kridel SJ, Lowther WT: Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat Struct Mol Biol. 2007 Aug;14(8):704-9. Epub 2007 Jul 8. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5265 |
| Enzyme 23 Name |
Histone acetyltransferase KAT5 |
| Enzyme 23 Synonyms |
- 60 kDa Tat-interactive protein
- Tip60
- Histone acetyltransferase HTATIP
- HIV-1 Tat interactive protein
- Lysine acetyltransferase 5
- cPLA(2)-interacting protein
|
| Enzyme 23 Gene Name |
KAT5 |
| Enzyme 23 Protein Sequence |
>Histone acetyltransferase KAT5
MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTH
ERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPK
EREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAV
AAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRH
RLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTIS
FFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKE
STEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQ
TILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDI
VDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW
|
| Enzyme 23 Number of Residues |
513 |
| Enzyme 23 Molecular Weight |
58581.4 |
| Enzyme 23 Theoretical pI |
8.64 |
| Enzyme 23 GO Classification |
| Function |
- binding
- catalytic activity
- chromatin binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin assembly or disassembly
- chromatin organization
- chromosome organization
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
|
| Component |
- chromatin
- chromosomal part
- intracellular membrane-bounded organelle
- intracellular organelle part
- membrane-bounded organelle
- nucleus
- organelle
- organelle part
|
|
| Enzyme 23 General Function |
Involved in chromatin binding |
| Enzyme 23 Specific Function |
Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
27802679  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q92993  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
KAT5_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1542 bp
ATGGCGGAGGTGGGGGAGATAATCGAGGGCTGCCGCCTACCCGTGCTGCGGCGGAACCAG
GACAACGAAGATGAGTGGCCCCTGGCCGAGATCCTGAGCGTGAAGGACATCAGTGGCCGG
AAGCTTTTCTACGTCCATTACATTGACTTCAACAAACGTCTGGATGAATGGGTGACGCAT
GAGCGGCTGGACCTAAAGAAGATCCAGTTCCCCAAGAAAGAGGCCAAGACCCCCACTAAG
AACGGACTTCCTGGGTCCCGTCCTGGCTCTCCAGAGAGAGAGGTGCCGGCCTCGGCGCAG
GCCAGCGGGAAGACCTTGCCAATCCCGGTCCAGATCACACTCCGCTTCAACCTGCCCAAG
GAGCGGGAGGCCATTCCCGGTGGCGAGCCTGACCAGCCGCTCTCCTCCAGCTCCTGCCTG
CAGCCCAACCACCGCTCAACGAAACGGAAGGTGGAGGTGGTTTCACCAGCAACTCCAGTG
CCCAGCGAGACAGCCCCGGCCTCGGTTTTTCCCCAGAATGGAGCCGCCCGTAGGGCAGTG
GCAGCCCAGCCAGGACGGAAGCGAAAATCGAATTGTTTGGGCACTGATGAGGACTCCCAG
GACAGCTCTGATGGAATACCGTCAGCACCACGCATGACTGGCAGCCTGGTGTCTGATCGA
AGCCACGACGACATCGTCACCCGGATGAAGAACATTGAGTGCATTGAGCTGGGCCGGCAC
CGCCTCAAGCCGTGGTACTTCTCCCCGTACCCACAGGAACTCACCACATTGCCTGTCCTC
TACCTGTGCGAGTTCTGCCTCAAGTACGGCCGTAGTCTCAAGTGTCTTCAGCGTCATTTG
ACCAAGTGTGACCTACGACATCCTCCAGGCAATGAGATTTACCGCAAGGGCACCATCTCC
TTCTTTGAGATTGATGGACGTAAGAACAAGAGTTATTCCCAGAACCTGTGTCTTTTGGCC
AAGTGTTTCCTTGACCATAAGACACTGTACTATGACACAGACCCTTTCCTCTTCTACGTC
ATGACAGAGTATGACTGTAAGGGCTTCCACATCGTGGGCTACTTCTCCAAGGAGAAAGAA
TCAACGGAAGACTACAATGTGGCCTGCATCCTAACCCTGCCTCCCTACCAGCGCCGGGGC
TACGGCAAGCTGCTGATCGAGTTCAGCTATGAACTCTCCAAAGTGGAAGGGAAAACAGGG
ACCCCTGAGAAGCCCCTCTCAGACCTTGGCCTCCTATCCTATCGAAGCTACTGGTCCCAG
ACCATCCTGGAGATCCTGATGGGGCTGAAGTCGGAGAGCGGGGAGAGGCCACAGATCACC
ATCAATGAGATTAGTGAAATCACCAGCATCAAGAAGGAGGATGTCATCTCCACTCTGCAG
TACCTCAATCTCATCAACTACTACAAGGGCCAGTACATCCTCACACTGTCAGAGGACATC
GTGGATGGCCATGAGCGGGCCATGCTCAAGCGGCTCCTGCGGATCGACTCCAAGTGTCTG
CACTTCACTCCCAAGGACTGGAGCAAGAGGGGGAAGTGGTGA
|
| Enzyme 23 GenBank Gene ID |
AY214165  |
| Enzyme 23 GeneCard ID |
KAT5  |
| Enzyme 23 GenAtlas ID |
KAT5  |
| Enzyme 23 HGNC ID |
HGNC:5275  |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
11q13 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G: Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology. 1996 Feb 15;216(2):357-66. [PubMed
]
- Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed
]
- Legube G, Trouche D: Identification of a larger form of the histone acetyl transferase Tip60. Gene. 2003 May 22;310:161-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cai Y, Jin J, Tomomori-Sato C, Sato S, Sorokina I, Parmely TJ, Conaway RC, Conaway JW: Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. J Biol Chem. 2003 Oct 31;278(44):42733-6. Epub 2003 Sep 8. [PubMed
]
- Kimura A, Horikoshi M: Tip60 acetylates six lysines of a specific class in core histones in vitro. Genes Cells. 1998 Dec;3(12):789-800. [PubMed
]
- Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y: Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell. 2000 Aug 18;102(4):463-73. [PubMed
]
- Lee HJ, Chun M, Kandror KV: Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling. J Biol Chem. 2001 May 18;276(20):16597-600. Epub 2001 Mar 21. [PubMed
]
- Legube G, Linares LK, Lemercier C, Scheffner M, Khochbin S, Trouche D: Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation. EMBO J. 2002 Apr 2;21(7):1704-12. [PubMed
]
- Frank SR, Parisi T, Taubert S, Fernandez P, Fuchs M, Chan HM, Livingston DM, Amati B: MYC recruits the TIP60 histone acetyltransferase complex to chromatin. EMBO Rep. 2003 Jun;4(6):575-80. [PubMed
]
- Lemercier C, Legube G, Caron C, Louwagie M, Garin J, Trouche D, Khochbin S: Tip60 acetyltransferase activity is controlled by phosphorylation. J Biol Chem. 2003 Feb 14;278(7):4713-8. Epub 2002 Dec 4. [PubMed
]
- Xiao H, Chung J, Kao HY, Yang YC: Tip60 is a co-repressor for STAT3. J Biol Chem. 2003 Mar 28;278(13):11197-204. Epub 2003 Jan 27. [PubMed
]
- Doyon Y, Cote J: The highly conserved and multifunctional NuA4 HAT complex. Curr Opin Genet Dev. 2004 Apr;14(2):147-54. [PubMed
]
- Legube G, Linares LK, Tyteca S, Caron C, Scheffner M, Chevillard-Briet M, Trouche D: Role of the histone acetyl transferase Tip60 in the p53 pathway. J Biol Chem. 2004 Oct 22;279(43):44825-33. Epub 2004 Aug 13. [PubMed
]
- Panchenko MV, Zhou MI, Cohen HT: von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity. J Biol Chem. 2004 Dec 31;279(53):56032-41. Epub 2004 Oct 22. [PubMed
]
- Doyon Y, Selleck W, Lane WS, Tan S, Cote J: Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol Cell Biol. 2004 Mar;24(5):1884-96. [PubMed
]
- Taubert S, Gorrini C, Frank SR, Parisi T, Fuchs M, Chan HM, Livingston DM, Amati B: E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1. Mol Cell Biol. 2004 May;24(10):4546-56. [PubMed
]
- Berns K, Hijmans EM, Mullenders J, Brummelkamp TR, Velds A, Heimerikx M, Kerkhoven RM, Madiredjo M, Nijkamp W, Weigelt B, Agami R, Ge W, Cavet G, Linsley PS, Beijersbergen RL, Bernards R: A large-scale RNAi screen in human cells identifies new components of the p53 pathway. Nature. 2004 Mar 25;428(6981):431-7. [PubMed
]
- Col E, Caron C, Chable-Bessia C, Legube G, Gazzeri S, Komatsu Y, Yoshida M, Benkirane M, Trouche D, Khochbin S: HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses. EMBO J. 2005 Jul 20;24(14):2634-45. Epub 2005 Jul 7. [PubMed
]
- Sun Y, Jiang X, Chen S, Fernandes N, Price BD: A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13182-7. Epub 2005 Sep 2. [PubMed
]
- Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J: ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. [PubMed
]
- Miyajima N, Maruyama S, Bohgaki M, Kano S, Shigemura M, Shinohara N, Nonomura K, Hatakeyama S: TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells. Cancer Res. 2008 May 1;68(9):3486-94. [PubMed
]
- Cheng Z, Ke Y, Ding X, Wang F, Wang H, Wang W, Ahmed K, Liu Z, Xu Y, Aikhionbare F, Yan H, Liu J, Xue Y, Yu J, Powell M, Liang S, Wu Q, Reddy SE, Hu R, Huang H, Jin C, Yao X: Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response. Oncogene. 2008 Feb 7;27(7):931-41. Epub 2007 Aug 20. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5266 |
| Enzyme 24 Name |
Acetyl-coenzyme A synthetase, cytoplasmic |
| Enzyme 24 Synonyms |
- Acetate--CoA ligase
- Acetyl-CoA synthetase
- ACS
- AceCS
- Acyl-CoA synthetase short-chain family member 2
- Acyl-activating enzyme
|
| Enzyme 24 Gene Name |
ACSS2 |
| Enzyme 24 Protein Sequence |
>Acetyl-coenzyme A synthetase, cytoplasmic
MGLPEERVRSGSGSRGQEEAGAGGRARSWSPPPEVSRSAHVPSLQRYRELHRRSVEEPRE
FWGDIAKEFYWKTPCPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDK
VAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAC
ARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEK
GFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDLWWHELMQEAGDEC
EPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIG
WITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFG
DEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPG
ATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTY
FKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV
GHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG
KIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
|
| Enzyme 24 Number of Residues |
701 |
| Enzyme 24 Molecular Weight |
78579.1 |
| Enzyme 24 Theoretical pI |
6.43 |
| Enzyme 24 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in acetate-CoA ligase activity |
| Enzyme 24 Specific Function |
Activates acetate so that it can be used for lipid synthesis or for energy generation |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA [RN:R00235]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
Not Available |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9NR19  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
ACSA_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>2106 bp
ATGGGGCTTCCTGAGGAGCGGGTCCGGAGCGGCAGCGGGAGCCGGGGCCAGGAGGAAGCT
GGAGCCGGAGGCCGGGCGCGGAGTTGGTCTCCGCCGCCCGAGGTCAGCCGCTCCGCGCAC
GTCCCCTCGCTGCAGCGCTACCGCGAGCTGCACCGGCGCTCCGTGGAGGAGCCGCGGGAA
TTCTGGGGAGACATTGCCAAGGAATTTTACTGGAAGACTCCATGCCCTGGCCCATTCCTT
CGGTACAACTTTGATGTGACTAAAGGGAAAATCTTCATTGAGTGGATGAAAGGAGCAACT
ACCAACATCTGCTACAATGTACTGGATCGAAATGTCCATGAGAAAAAGCTTGGAGATAAA
GTTGCTTTTTACTGGGAGGGCAATGAGCCAGGGGAGACCACTCAGATCACATACCATCAG
CTTCTGGTCCAAGTGTGTCAGTTCAGCAATGTTCTCCGAAAACAGGGCATTCAGAAGGGG
GACCGAGTGGCCATCTACATGCCTATGATCCCAGAGCTTGTGGTGGCCATGCTGGCATGT
GCCCGCATTGGGGCTTTGCACTCCATTGTGTTTGCAGGCTTCTCTTCAGAGTCTCTATGT
GAACGGATCTTGGATTCCAGCTGCAGTCTTCTCATCACTACAGATGCCTTCTACAGGGGG
GAAAAGCTTGTGAACCTGAAGGAGCTGGCTGACGAGGCCCTGCAGAAGTGTCAGGAGAAG
GGTTTCCCAGTAAGATGCTGCATTGTGGTCAAGCACCTGGGGCGGGCAGAGCTCGGCATG
GGTGACTCCACCAGCCAGTCCCCCCCAATTAAGAGGTCATGCCCAGATGTGCAGATCTCA
TGGAACCAAGGGATTGACTTGTGGTGGCATGAGCTCATGCAAGAGGCAGGGGATGAGTGT
GAGCCCGAGTGGTGTGATGCCGAGGACCCACTCTTCATCCTGTACACCAGTGGCTCCACA
GGCAAACCCAAGGGTGTGGTTCACACAGTTGGGGGCTACATGCTCTATGTAGCCACAACC
TTCAAGTATGTGTTTGACTTCCATGCAGAGGATGTGTTCTGGTGCACGGCAGACATTGGT
TGGATCACTGGTCATTCCTACGTCACCTATGGGCCACTGGCCAATGGTGCCACCAGTGTT
TTGTTTGAGGGGATTCCCACATATCCGGACGTGAACCGCCTGTGGAGCATTGTGGACAAA
TACAAGGTGACCAAGTTCTACACAGCACCCACAGCCATCCGTCTGCTCATGAAGTTTGGA
GATGAGCCTGTCACCAAGCATAGCCGGGCATCCTTGCAGGTGTTAGGCACAGTGGGTGAA
CCCATCAACCCTGAGGCCTGGCTATGGTACCACCGGGTGGTAGGTGCCCAGCGCTGCCCC
ATCGTGGACACCTTCTGGCAAACAGAGACAGGTGGCCACATGTTGACTCCCCTTCCTGGT
GCCACACCCATGAAACCCGGTTCTGCTACTTTCCCATTCTTTGGTGTAGCTCCTGCAATC
CTGAATGAGTCCGGGGAAGAGTTGGAAGGTGAAGCTGAAGGTTATCTGGTGTTCAAGCAG
CCCTGGCCAGGGATCATGCGCACAGTCTATGGGAACCACGAACGCTTTGAGACAACCTAC
TTTAAGAAGTTTCCTGGATACTATGTTACAGGAGATGGCTGCCAGCGGGACCAGGATGGC
TATTACTGGATCACTGGCAGGATTGATGACATGCTCAATGTATCTGGACACCTGCTGAGT
ACAGCAGAGGTGGAGTCAGCACTTGTGGAACATGAGGCTGTTGCAGAGGCAGCTGTGGTG
GGCCACCCTCATCCTGTGAAGGGTGAATGCCTCTACTGCTTTGTCACCTTGTGTGATGGC
CACACCTTCAGCCCCAAGCTCACCGAGGAGCTCAAGAAGCAGATTAGAGAAAAGATTGGC
CCCATTGCCACACCAGACTACATCCAGAATGCACCTGGCTTGCCTAAAACCCGCTCAGGG
AAAATCATGAGGCGAGTGCTTCGGAAGATTGCTCAGAATGACCATGACCTCGGGGACATG
TCTACTGTGGCTGACCCATCTGTCATCAGTCACCTCTTCAGCCACCGCTGCCTGACCATC
CAGTGA
|
| Enzyme 24 GenBank Gene ID |
AF263614  |
| Enzyme 24 GeneCard ID |
ACSS2  |
| Enzyme 24 GenAtlas ID |
ACSS2  |
| Enzyme 24 HGNC ID |
HGNC:15814  |
| Enzyme 24 Chromosome Location |
2 |
| Enzyme 24 Locus |
20q11.22 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Luong A, Hannah VC, Brown MS, Goldstein JL: Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J Biol Chem. 2000 Aug 25;275(34):26458-66. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5267 |
| Enzyme 25 Name |
Acetyl-CoA acetyltransferase, mitochondrial |
| Enzyme 25 Synonyms |
- Acetoacetyl-CoA thiolase
- T2
|
| Enzyme 25 Gene Name |
ACAT1 |
| Enzyme 25 Protein Sequence |
>Acetyl-CoA acetyltransferase, mitochondrial
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLS
LLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT
TINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIV
KDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV
TVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADA
AKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVV
LANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGAS
AMLIQKL
|
| Enzyme 25 Number of Residues |
427 |
| Enzyme 25 Molecular Weight |
45199.2 |
| Enzyme 25 Theoretical pI |
9.21 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 25 Specific Function |
Plays a major role in ketone body metabolism |
| Enzyme 25 Pathways |
- Benzoate Degradation via CoA Ligation (map00632
)
- Butyrate Metabolism (map00650
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Lysine Degradation (map00310
)
- Propanoate Metabolism (map00640
)
- Pyruvate Metabolism (map00620
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Tryptophan Metabolism (map00380
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 25 Reactions |
- 2 acetyl-CoA = CoA + acetoacetyl-CoA [RN:R00238]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P24752  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
THIL_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1284 bp
ATGGCTGTGCTGGCGGCACTTCTGCGCAGCGGCGCCCGCAGCCGCAGCCCCCTGCTCCGG
AGGCTGGTGCAGGAAATAAGATATGTGGAACGGAGTTATGTATCAAAACCCACTTTGAAG
GAAGTGGTCATAGTAAGTGCTACAAGAACACCCATTGGATCTTTTTTAGGCAGCCTTTCC
TTGCTGCCAGCCACTAAGCTTGGTTCCATTGCAATTCAGGGAGCCATTGAAAAGGCAGGG
ATTCCAAAAGAAGAAGTGAAAGAAGCATACATGGGTAATGTTCTACAAGGAGGTGAAGGA
CAAGCTCCTACAAGGCAGGCAGTATTGGGTGCAGGCTTACCTATTTCTACTCCATGTACC
ACCATAAACAAAGTTTGTGCTTCAGGAATGAAAGCCATCATGATGGCCTCTCAAAGTCTT
ATGTGTGGACATCAGGATGTGATGGTGGCAGGTGGGATGGAGAGCATGTCCAATGTTCCA
TATGTAATGAACAGAGGATCAACACCATATGGTGGGGTAAAGCTTGAAGATTTGATTGTA
AAAGACGGGCTAACTGATGTCTACAATAAAATTCATATGGGCAGCTGTGCTGAGAATACA
GCAAAGAAGCTGAATATTGCACGAAATGAACAGGACGCTTATGCTATTAATTCTTATACC
AGAAGTAAAGCAGCATGGGAAGCTGGGAAATTTGGAAATGAAGTTATTCCTGTCACAGTT
ACAGTAAAAGGTCAACCAGATGTAGTGGTGAAAGAAGATGAAGAATATAAACGTGTTGAT
TTTAGCAAAGTTCCAAAGCTGAAGACAGTTTTCCAGAAAGAAAATGGCACAGTAACAGCT
GCCAATGCCAGTACACTGAATGATGGAGCAGCTGCTCTGGTTCTCATGACGGCAGATGCA
GCGAAGAGGCTCAATGTTACACCACTGGCAAGAATAGTAGCATTTGCTGACGCTGCTGTA
GAACCTATTGATTTTCCAATTGCTCCTGTATATGCTGCATCTATGGTTCTTAAAGATGTG
GGATTGAAAAAAGAAGATATTGCAATGTGGGAAGTAAATGAAGCCTTTAGTCTGGTTGTA
CTAGCAAACATTAAAATGTTGGAGATTGATCCCCAAAAAGTGAATATCAATGGAGGAGCT
GTTTCTCTGGGACATCCAATTGGGATGTCTGGAGCCAGGATTGTTGGTCATTTGACTCAT
GCCTTGAAGCAAGGAGAATACGGTCTTGCCAGTATTTGCAATGGAGGAGGAGGTGCTTCT
GCCATGCTAATTCAGAAGCTGTAG
|
| Enzyme 25 GenBank Gene ID |
D90228  |
| Enzyme 25 GeneCard ID |
ACAT1  |
| Enzyme 25 GenAtlas ID |
ACAT1  |
| Enzyme 25 HGNC ID |
HGNC:93  |
| Enzyme 25 Chromosome Location |
1 |
| Enzyme 25 Locus |
11q22.3 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Fukao T, Yamaguchi S, Kano M, Orii T, Fujiki Y, Osumi T, Hashimoto T: Molecular cloning and sequence of the complementary DNA encoding human mitochondrial acetoacetyl-coenzyme A thiolase and study of the variant enzymes in cultured fibroblasts from patients with 3-ketothiolase deficiency. J Clin Invest. 1990 Dec;86(6):2086-92. [PubMed
]
- Kano M, Fukao T, Yamaguchi S, Orii T, Osumi T, Hashimoto T: Structure and expression of the human mitochondrial acetoacetyl-CoA thiolase-encoding gene. Gene. 1991 Dec 30;109(2):285-90. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Haapalainen AM, Merilainen G, Pirila PL, Kondo N, Fukao T, Wierenga RK: Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function. Biochemistry. 2007 Apr 10;46(14):4305-21. Epub 2007 Mar 20. [PubMed
]
- Fukao T, Yamaguchi S, Orii T, Hashimoto T: Molecular basis of beta-ketothiolase deficiency: mutations and polymorphisms in the human mitochondrial acetoacetyl-coenzyme A thiolase gene. Hum Mutat. 1995;5(2):113-20. [PubMed
]
- Fukao T, Yamaguchi S, Orii T, Schutgens RB, Osumi T, Hashimoto T: Identification of three mutant alleles of the gene for mitochondrial acetoacetyl-coenzyme A thiolase. A complete analysis of two generations of a family with 3-ketothiolase deficiency. J Clin Invest. 1992 Feb;89(2):474-9. [PubMed
]
- Fukao T, Yamaguchi S, Tomatsu S, Orii T, Frauendienst-Egger G, Schrod L, Osumi T, Hashimoto T: Evidence for a structural mutation (347Ala to Thr) in a German family with 3-ketothiolase deficiency. Biochem Biophys Res Commun. 1991 Aug 30;179(1):124-9. [PubMed
]
- Wakazono A, Fukao T, Yamaguchi S, Hori T, Orii T, Lambert M, Mitchell GA, Lee GW, Hashimoto T: Molecular, biochemical, and clinical characterization of mitochondrial acetoacetyl-coenzyme A thiolase deficiency in two further patients. Hum Mutat. 1995;5(1):34-42. [PubMed
]
- Fukao T, Nakamura H, Song XQ, Nakamura K, Orii KE, Kohno Y, Kano M, Yamaguchi S, Hashimoto T, Orii T, Kondo N: Characterization of N93S, I312T, and A333P missense mutations in two Japanese families with mitochondrial acetoacetyl-CoA thiolase deficiency. Hum Mutat. 1998;12(4):245-54. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5268 |
| Enzyme 26 Name |
Nuclear receptor coactivator 1 |
| Enzyme 26 Synonyms |
- NCoA-1
- Class E basic helix-loop-helix protein 74
- bHLHe74
- Protein Hin-2
- RIP160
- Renal carcinoma antigen NY-REN-52
- Steroid receptor coactivator 1
- SRC-1
|
| Enzyme 26 Gene Name |
NCOA1 |
| Enzyme 26 Protein Sequence |
>Nuclear receptor coactivator 1
MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSL
SVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEAL
DGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNG
VPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQ
SCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFF
QPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMG
IHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINR
QQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNQGQASSQSSNPSLNLNNSPMEGTG
ISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTS
LQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASILNEMIQSDN
SSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSC
TGTSNSASANSSGGSCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVS
VTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQ
MDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAV
TSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAIN
QSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKL
VQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPSPTANLPSPFQGMVRQKPSLGT
MPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQF
AATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSF
GNNLPPSSGLPVQMGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLAN
RNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPI
PPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVS
MAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTE
ADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLT
E
|
| Enzyme 26 Number of Residues |
1441 |
| Enzyme 26 Molecular Weight |
156755.4 |
| Enzyme 26 Theoretical pI |
6.10 |
| Enzyme 26 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- histone acetyltransferase activity
- hormone receptor binding
- lysine N-acetyltransferase activity
- molecular transducer activity
- nuclear hormone receptor binding
- protein binding
- receptor binding
- signal transducer activity
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transcription regulator activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- biological regulation
- regulation of biological process
- regulation of cellular process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
- signal transduction
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 26 General Function |
Involved in transcription coactivator activity |
| Enzyme 26 Specific Function |
Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3 |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
62702258  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q15788  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
NCOA1_HUMAN  |
| Enzyme 26 PDB ID |
1OJ5  |
| Enzyme 26 PDB File |
Show |
| Enzyme 26 3D Structure |
|
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>4326 bp
ATGAGTGGCCTCGGGGACAGTTCATCCGACCCTGCTAACCCAGACTCACATAAGAGGAAA
GGATCGCCATGTGACACACTGGCATCAAGCACGGAAAAGAGGCGCAGGGAGCAAGAAAAT
AAATATTTAGAAGAACTAGCTGAGTTACTGTCTGCCAACATTAGTGACATTGACAGCTTG
AGTGTAAAACCAGACAAATGCAAGATTTTGAAGAAAACAGTCGATCAGATACAGCTAATG
AAGAGAATGGAACAAGAGAAATCAACAACTGATGACGATGTACAGAAATCAGACATCTCA
TCAAGTAGTCAAGGAGTGATAGAAAAGGAATCCTTGGGACCTCTTCTTTTGGAGGCTTTG
GATGGATTTTTCTTTGTTGTGAACTGTGAAGGGAGAATTGTATTTGTGTCAGAGAATGTA
ACCAGCTACTTAGGTTACAATCAGGAGGAATTAATGAATACGAGCGTCTACAGCATACTG
CACGTGGGGGATCATGCAGAATTTGTGAAGAATCTGCTACCAAAATCACTAGTAAATGGA
GTTCCTTGGCCTCAAGAGGCAACACGACGAAATAGCCATACCTTTAACTGCAGGATGCTA
ATTCACCCTCCAGATGAGCCAGGGACCGAGAACCAAGAAGCTTGCCAGCGTTATGAAGTA
ATGCAGTGTTTCACTGTGTCACAGCCAAAATCAATTCAAGAGGATGGAGAAGATTTCCAG
TCATGTCTGATTTGTATTGCACGGCGATTACCTCGGCCTCCAGCTATTACGGGTGTAGAA
TCCTTTATGACCAAGCAAGATACTACAGGTAAAATCATCTCTATTGATACTAGTTCCCTG
AGAGCTGCTGGCAGAACTGGTTGGGAAGATTTAGTGAGGAAGTGCATTTATGCTTTTTTC
CAACCTCAGGGCAGAGAACCATCTTATGCCAGACAGCTGTTCCAAGAAGTGATGACTCGT
GGCACTGCCTCCAGCCCCTCCTATAGATTCATATTGAATGATGGGACAATGCTTAGCGCC
CACACCAAGTGTAAACTTTGCTACCCTCAAAGTCCAGACATGCAACCTTTCATCATGGGA
ATTCATATCATCGACAGGGAGCACAGTGGGCTTTCTCCTCAAGATGACACTAATTCTGGA
ATGTCAATTCCCCGAGTAAATCCCTCGGTCAATCCTAGTATCTCTCCAGCTCATGGTGTG
GCTCGTTCATCCACATTGCCACCATCCAACAGCAACATGGTATCCACCAGAATAAACCGC
CAGCAGAGCTCAGACCTTCATAGCAGCAGTCATAGTAATTCTAGCAACAGCCAAGGAAGT
TTCGGATGCTCACCCGGAAGTCAGATTGTAGCCAATGTTGCCTTAAACCAAGGACAGGCC
AGTTCACAGAGCAGTAATCCCTCTTTAAACCTCAATAATTCTCCTATGGAAGGTACAGGA
ATATCCCTAGCACAGTTCATGTCTCCAAGGAGACAGGTTACTTCTGGATTGGCAACAAGG
CCCAGGATGCCAAACAATTCCTTTCCTCCTAATATTTCGACATTAAGCTCTCCCGTTGGC
ATGACAAGTAGTGCCTGTAATAATAATAACCGATCTTATTCAAACATCCCAGTAACATCT
TTACAGGGTATGAATGAAGGACCCAATAACTCCGTTGGCTTCTCTGCCAGTTCTCCAGTC
CTCAGGCAGATGAGCTCACAGAATTCACCTAGCAGATTAAATATACAACCAGCAAAAGCT
GAGTCCAAAGATAACAAAGAGATTGCCTCAATTTTAAATGAAATGATTCAATCTGACAAC
AGCTCTAGTGATGGCAAACCTCTGGATTCAGGGCTTCTGCATAACAATGACAGACTTTCA
GATGGAGACAGTAAATACTCTCAAACCAGTCACAAACTAGTGCAGCTTTTGACAACAACT
GCCGAACAGCAGTTACGGCATGCTGATATAGACACAAGCTGCAAAGATGTCCTGTCTTGC
ACAGGCACTTCCAACTCTGCCTCTGCTAACTCTTCAGGAGGTTCTTGTCCCTCTTCTCAT
AGCTCATTGACAGAACGGCATAAAATTCTACACCGGCTCTTACAGGAGGGTAGCCCCTCA
GATATCACCACTTTGTCTGTCGAGCCTGATAAAAAGGACAGTGCATCTACTTCTGTGTCA
GTGACTGGACAGGTACAAGGAAACTCCAGTATAAAACTAGAACTGGATGCTTCAAAGAAA
AAAGAATCAAAAGACCATCAGCTCCTACGCTATCTTTTAGATAAAGATGAGAAAGATTTA
AGATCAACTCCAAACCTGAGCCTGGATGATGTAAAGGTGAAAGTGGAAAAGAAAGAACAG
ATGGATCCATGTAATACAAACCCAACCCCAATGACCAAACCCACTCCTGAGGAAATAAAA
CTGGAGGCCCAGAGCCAGTTTACAGCTGACCTTGACCAGTTTGATCAGTTACTGCCCACG
CTGGAGAAGGCAGCACAGTTGCCAGGCTTATGTGAGACAGACAGGATGGATGGTGCGGTC
ACCAGTGTAACCATCAAATCGGAGATCCTGCCAGCTTCACTTCAGTCCGCCACTGCCAGA
CCCACTTCCAGGCTAAATAGATTACCTGAGCTGGAATTGGAAGCAATTGATAACCAATTT
GGACAACCAGGAACAGGCGATCAGATTCCATGGACAAATAATACAGTGACAGCTATAAAT
CAGAGTAAATCAGAAGACCAGTGTATTAGCTCACAATTAGATGAGCTTCTCTGTCCACCC
ACAACAGTAGAAGGGAGAAATGATGAGAAGGCTCTTCTTGAACAGCTGGTATCCTTCCTT
AGTGGCAAAGATGAAACTGAGCTAGCTGAACTAGACAGAGCTCTGGGAATTGACAAACTT
GTTCAGGGGGGTGGATTAGATGTATTATCAGAGAGATTTCCACCACAACAAGCAACGCCA
CCTTTGATCATGGAAGAAAGACCCAACCTTTATTCCCAGCCTTACTCTTCTCCTTCTCCT
ACTGCCAATCTCCCTAGCCCTTTCCAAGGCATGGTCAGGCAAAAACCTTCACTGGGGACG
ATGCCTGTTCAAGTAACACCTCCCCGAGGTGCTTTTTCACCTGGCATGGGCATGCAGCCC
AGGCAAACTCTAAACAGACCTCCGGCTGCACCTAACCAGCTTCGACTTCAACTACAGCAG
CGATTACAGGGACAACAGCAGTTGATACACCAAAATCGGCAAGCTATCTTAAACCAGTTT
GCAGCAACTGCTCCTGTTGGCATCAATATGAGATCAGGCATGCAACAGCAAATTACACCT
CAGCCACCCCTGAATGCTCAAATGTTGGCACAACGTCAGCGGGAACTGTACAGTCAACAG
CACCGACAGAGGCAGCTAATACAGCAGCAAAGAGCCATGCTTATGAGGCAGCAAAGCTTT
GGGAACAACCTCCCTCCCTCATCTGGACTACCAGTTCAAATGGGGAACCCCCGTCTTCCT
CAGGGTGCTCCACAGCAATTCCCCTATCCACCAAACTATGGTACAAATCCAGGAACCCCA
CCTGCTTCTACCAGCCCGTTTTCACAACTAGCAGCAAATCCTGAAGCATCCTTGGCCAAC
CGCAACAGCATGGTGAGCAGAGGCATGACAGGAAACATAGGAGGACAGTTTGGCACTGGA
ATCAATCCTCAGATGCAGCAGAATGTCTTCCAGTATCCAGGAGCAGGAATGGTTCCCCAA
GGTGAGGCCAACTTTGCTCCATCTCTAAGCCCTGGGAGCTCCATGGTGCCGATGCCAATC
CCTCCTCCTCAGAGTTCTCTTCTCCAGCAAACTCCACCTGCCTCCGGGTATCAGTCACCA
GACATGAAGGCCTGGCAGCAAGGAGCGATAGGAAACAACAATGTGTTCAGTCAAGCTGTC
CAGAACCAGCCCACGCCTGCACAGCCAGGAGTATACAACAACATGAGCATCACCGTTTCC
ATGGCAGGTGGAAATACGAATGTTCAGAACATGAACCCAATGATGGCCCAGATGCAGATG
AGCTCTTTGCAGATGCCAGGAATGAACACTGTGTGCCCTGAGCAGATAAATGATCCCGCA
CTGAGACACACAGGCCTCTACTGCAACCAGCTCTCATCCACTGACCTTCTCAAAACAGAA
GCAGATGGAACCCAGCAGGTGCAACAGGTTCAGGTGTTTGCTGACGTCCAGTGTACAGTG
AATCTGGTAGGCGGGGACCCTTACCTGAACCAGCCTGGTCCACTGGGAACTCAAAAGCCC
ACGTCAGGACCACAGACCCCCCAGGCCCAGCAGAAGAGCCTCCTTCAGCAGCTACTGACT
GAATAA
|
| Enzyme 26 GenBank Gene ID |
AC013459  |
| Enzyme 26 GeneCard ID |
NCOA1  |
| Enzyme 26 GenAtlas ID |
NCOA1  |
| Enzyme 26 HGNC ID |
HGNC:7668  |
| Enzyme 26 Chromosome Location |
2 |
| Enzyme 26 Locus |
2p23 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Takeshita A, Yen PM, Misiti S, Cardona GR, Liu Y, Chin WW: Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator. Endocrinology. 1996 Aug;137(8):3594-7. [PubMed
]
- Kalkhoven E, Valentine JE, Heery DM, Parker MG: Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 1998 Jan 2;17(1):232-43. [PubMed
]
- Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai MJ, Edwards DP, O'Malley BW: The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J Biol Chem. 1998 May 15;273(20):12101-8. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Onate SA, Tsai SY, Tsai MJ, O'Malley BW: Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science. 1995 Nov 24;270(5240):1354-7. [PubMed
]
- Raineri I, Soler M, Senn HP: Analysis of human immunodeficiency virus type 1 promoter insertion in vivo. Virology. 1995 Apr 1;208(1):359-64. [PubMed
]
- Wachtel M, Dettling M, Koscielniak E, Stegmaier S, Treuner J, Simon-Klingenstein K, Buhlmann P, Niggli FK, Schafer BW: Gene expression signatures identify rhabdomyosarcoma subtypes and detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1. Cancer Res. 2004 Aug 15;64(16):5539-45. [PubMed
]
- Hayashi Y, Ohmori S, Ito T, Seo H: A splicing variant of Steroid Receptor Coactivator-1 (SRC-1E): the major isoform of SRC-1 to mediate thyroid hormone action. Biochem Biophys Res Commun. 1997 Jul 9;236(1):83-7. [PubMed
]
- Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW: Steroid receptor coactivator-1 is a histone acetyltransferase. Nature. 1997 Sep 11;389(6647):194-8. [PubMed
]
- Jenster G, Spencer TE, Burcin MM, Tsai SY, Tsai MJ, O'Malley BW: Steroid receptor induction of gene transcription: a two-step model. Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7879-84. [PubMed
]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed
]
- Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed
]
- Liu Z, Wong J, Tsai SY, Tsai MJ, O'Malley BW: Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and receptor-dependent cell-free transcription of chromatin. Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9485-90. [PubMed
]
- Rowan BG, Weigel NL, O'Malley BW: Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway. J Biol Chem. 2000 Feb 11;275(6):4475-83. [PubMed
]
- Chauchereau A, Georgiakaki M, Perrin-Wolff M, Milgrom E, Loosfelt H: JAB1 interacts with both the progesterone receptor and SRC-1. J Biol Chem. 2000 Mar 24;275(12):8540-8. [PubMed
]
- Carrero P, Okamoto K, Coumailleau P, O'Brien S, Tanaka H, Poellinger L: Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol Cell Biol. 2000 Jan;20(1):402-15. [PubMed
]
- Giraud S, Bienvenu F, Avril S, Gascan H, Heery DM, Coqueret O: Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a. J Biol Chem. 2002 Mar 8;277(10):8004-11. Epub 2001 Dec 31. [PubMed
]
- Litterst CM, Pfitzner E: An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1. J Biol Chem. 2002 Sep 27;277(39):36052-60. Epub 2002 Jul 22. [PubMed
]
- Chauchereau A, Amazit L, Quesne M, Guiochon-Mantel A, Milgrom E: Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1. J Biol Chem. 2003 Apr 4;278(14):12335-43. Epub 2003 Jan 14. [PubMed
]
- Litterst CM, Kliem S, Marilley D, Pfitzner E: NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL motif in the alpha-helical region of the STAT5 transactivation domain. J Biol Chem. 2003 Nov 14;278(46):45340-51. Epub 2003 Sep 3. [PubMed
]
- Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK: BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation. Mol Cell Biol. 2003 Sep;23(17):6210-20. [PubMed
]
- Verma S, Ismail A, Gao X, Fu G, Li X, O'Malley BW, Nawaz Z: The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors. Mol Cell Biol. 2004 Oct;24(19):8716-26. [PubMed
]
- Zhang H, Sun L, Liang J, Yu W, Zhang Y, Wang Y, Chen Y, Li R, Sun X, Shang Y: The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 2006 Sep 20;25(18):4223-33. Epub 2006 Sep 7. [PubMed
]
- He Y, Simons SS Jr: STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression. Mol Cell Biol. 2007 Feb;27(4):1467-85. Epub 2006 Nov 20. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998 Sep 10;395(6698):137-43. [PubMed
]
- Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed
]
- Greschik H, Wurtz JM, Sanglier S, Bourguet W, van Dorsselaer A, Moras D, Renaud JP: Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol Cell. 2002 Feb;9(2):303-13. [PubMed
]
- Razeto A, Ramakrishnan V, Litterst CM, Giller K, Griesinger C, Carlomagno T, Lakomek N, Heimburg T, Lodrini M, Pfitzner E, Becker S: Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain. J Mol Biol. 2004 Feb 13;336(2):319-29. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5269 |
| Enzyme 27 Name |
Hydroxymethylglutaryl-CoA synthase, mitochondrial |
| Enzyme 27 Synonyms |
- HMG-CoA synthase
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
|
| Enzyme 27 Gene Name |
HMGCS2 |
| Enzyme 27 Protein Sequence |
>Hydroxymethylglutaryl-CoA synthase, mitochondrial
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALE
VYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLP
WDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWM
ESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYD
FYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIF
HTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKAS
QDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASF
FSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPG
DTNSLFPGTWYLERVDEQHRRKYARRPV
|
| Enzyme 27 Number of Residues |
508 |
| Enzyme 27 Molecular Weight |
56634.9 |
| Enzyme 27 Theoretical pI |
8.28 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- hydroxymethylglutaryl-CoA synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- cellular lipid metabolic process
- isoprenoid biosynthetic process
- isoprenoid metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Involved in hydroxymethylglutaryl-CoA synthase activity |
| Enzyme 27 Specific Function |
This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase |
| Enzyme 27 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 27 Reactions |
- acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA [RN:R01978]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
56205097  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P54868  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
HMCS2_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1527 bp
ATGCAGCGTCTGTTGACTCCAGTGAAGCGCATTCTGCAACTGACAAGAGCGGTGCAGGAA
ACCTCCCTCACACCTGCTCGCCTGCTCCCAGTAGCCCACCAAAGGTTTTCTACAGCCTCT
GCTGTCCCCCTGGCCAAAACAGATACTTGGCCAAAGGACGTGGGCATCCTGGCCCTGGAG
GTCTACTTCCCAGCCCAATATGTGGACCAAACTGACCTGGAGAAGTATAACAATGTGGAA
GCAGGAAAGTATACAGTGGGCTTGGGCCAGACCCGTATGGGCTTCTGCTCAGTCCAAGAG
GACATCAACTCCCTGTGCCTGACGGTGGTGCAACGGCTGATGGAGCGCATACAGCTCCCA
TGGGACTCTGTGGGCAGGCTGGAAGTAGGCACTGAGACCATCATTGACAAGTCCAAAGCT
GTCAAAACAGTGCTCATGGAACTCTTCCAGGATTCAGGCAATACTGATATTGAGGGCATA
GATACCACCAATGCCTGCTACGGTGGTACTGCCTCCCTCTTCAATGCTGCCAACTGGATG
GAGTCCAGTTCCTGGGATGGTCGTTATGCCATGGTGGTCTGTGGAGACATTGCCGTCTAT
CCCAGTGGTAATGCTCGTCCCACAGGTGGGGCCGGAGCTGTGGCTATGCTGATTGGGCCC
AAGGCCCCTCTGGCCCTGGAGCGAGGGCTGAGGGGAACCCATATGGAGAATGTGTATGAC
TTCTACAAACCAAATTTGGCCTCGGAGTACCCAATAGTGGATGGGAAGCTTTCCATCCAG
TGCTACTTGCGGGCCTTGGATCGATGTTACACATCATACCGTAAAAAAATCCAGAATCAG
TGGAAGCAAGCTGGCAGCGATCGACCCTTCACCCTTGACGATTTACAGTACATGATCTTT
CATACACCCTTTTGCAAGATGGTCCAGAAGTCTCTGGCTCGCCTGATGTTCAATGACTTC
CTGTCAGCCAGCAGTGACACACAAACCAGCTTATATAAGGGGCTGGAGGCTTTCGGGGGG
CTAAAGCTGGAAGACACCTACACCAACAAGGACCTGGATAAAGCACTTCTAAAGGCCTCT
CAGGACATGTTCGACAAGAAAACCAAGGCTTCCCTTTACCTCTCCACTCACAATGGGAAC
ATGTACACCTCATCCCTGTACGGGTGCCTGGCCTCGCTTCTGTCCCACCACTCTGCCCAA
GAACTGGCTGGCTCCAGGATTGGTGCCTTCTCTTATGGCTCTGGTTTAGCAGCAAGTTTC
TTTTCATTTCGAGTATCCCAGGATGCTGCTCCAGGCTCTCCCCTGGACAAGTTGGTGTCC
AGCACATCAGACCTGCCAAAACGCCTAGCCTCCCGAAAGTGTGTGTCTCCTGAGGAGTTC
ACAGAAATAATGAACCAAAGAGAGCAATTCTACCATAAGGTGAATTTCTCCCCACCTGGT
GACACAAACAGCCTTTTCCCAGGTACTTGGTACCTGGAGCGAGTGGACGAGCAGCATCGC
CGAAAGTATGCCCGGCGTCCCGTCTAA
|
| Enzyme 27 GenBank Gene ID |
AL589734  |
| Enzyme 27 GeneCard ID |
HMGCS2  |
| Enzyme 27 GenAtlas ID |
HMGCS2  |
| Enzyme 27 HGNC ID |
HGNC:5008  |
| Enzyme 27 Chromosome Location |
1 |
| Enzyme 27 Locus |
1p13-p12 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Mascaro C, Buesa C, Ortiz JA, Haro D, Hegardt FG: Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. Arch Biochem Biophys. 1995 Mar 10;317(2):385-90. [PubMed
]
- Boukaftane Y, Mitchell GA: Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene. Gene. 1997 Aug 22;195(2):121-6. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Boukaftane Y, Duncan A, Wang S, Labuda D, Robert MF, Sarrazin J, Schappert K, Mitchell GA: Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution. Genomics. 1994 Oct;23(3):552-9. [PubMed
]
- Camarero N, Mascaro C, Mayordomo C, Vilardell F, Haro D, Marrero PF: Ketogenic HMGCS2 Is a c-Myc target gene expressed in differentiated cells of human colonic epithelium and down-regulated in colon cancer. Mol Cancer Res. 2006 Sep;4(9):645-53. Epub 2006 Aug 28. [PubMed
]
- Aledo R, Zschocke J, Pie J, Mir C, Fiesel S, Mayatepek E, Hoffmann GF, Casals N, Hegardt FG: Genetic basis of mitochondrial HMG-CoA synthase deficiency. Hum Genet. 2001 Jul;109(1):19-23. [PubMed
]
- Bouchard L, Robert MF, Vinarov D, Stanley CA, Thompson GN, Morris A, Leonard JV, Quant P, Hsu BY, Boneh A, Boukaftane Y, Ashmarina L, Wang S, Miziorko H, Mitchell GA: Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase deficiency: clinical course and description of causal mutations in two patients. Pediatr Res. 2001 Mar;49(3):326-31. [PubMed
]
- Wolf NI, Rahman S, Clayton PT, Zschocke J: Mitochondrial HMG-CoA synthase deficiency: identification of two further patients carrying two novel mutations. Eur J Pediatr. 2003 Apr;162(4):279-80. Epub 2003 Feb 11. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5271 |
| Enzyme 28 Name |
Acetyl-coenzyme A synthetase 2-like, mitochondrial |
| Enzyme 28 Synonyms |
- Acetate--CoA ligase 2
- Acetyl-CoA synthetase 2
- AceCS2
- Acyl-CoA synthetase short-chain family member 1
|
| Enzyme 28 Gene Name |
ACSS1 |
| Enzyme 28 Protein Sequence |
>Acetyl-coenzyme A synthetase 2-like, mitochondrial
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
|
| Enzyme 28 Number of Residues |
689 |
| Enzyme 28 Molecular Weight |
74856.1 |
| Enzyme 28 Theoretical pI |
7.11 |
| Enzyme 28 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 28 General Function |
Involved in acetate-CoA ligase activity |
| Enzyme 28 Specific Function |
Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions. Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2) |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA [RN:R00235]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
24659677  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q9NUB1  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
ACS2L_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>2070 bp
ATGGCGGCGCGCACCCTGGGCCGCGGCGTCGGGAGGCTGCTGGGCAGCCTGCGAGGGCTC
TCGGGGCAGCCCGCGCGGCCGCCGTGCGGGGTGAGCGCGCCGCGCAGGGCGGCCTCGGGA
CCCTCGGGCAGCGCTCCCGCAGTTGCAGCAGCAGCAGCACAGCCAGGCTCGTATCCCGCG
CTGAGTGCACAGGCAGCCCGGGAGCCGGCCGCCTTCTGGGGGCCTCTGGCGCGGGACACT
CTCGTGTGGGACACCCCCTACCACACCGTCTGGGACTGCGACTTCAGCACTGGCAAGATC
GGCTGGTTCCTGGGAGGCCAGTTAAATGTCTCTGTCAACTGCTTGGACCAGCATGTTCGG
AAGTCCCCCGAGAGCGTTGCTTTGATCTGGGAGCGCGATGAGCCTGGAACGGAAGTGAGG
ATCACCTACAGGGAACTACTGGAGACCACGTGCCGCCTGGCCAACACGCTGAAGAGGCAT
GGAGTCCACCGTGGGGACCGTGTTGCCATCTACATGCCCGTGTCCCCATTGGCTGTGGCA
GCAATGCTGGCCTGTGCCAGGATCGGAGCTGTCCACACAGTCATCTTTGCTGGCTTCAGT
GCGGAGTCCTTGGCTGGGAGGATCAATGATGCCAAGTGCAAGGTGGTTATCACCTTCAAC
CAAGGACTCCGGGGTGGGCGCGTGGTGGAGCTGAAGAAAATAGTGGATGAGGCTGTGAAG
CACTGCCCCACCGTGCAGCATGTCCTGGTGGCTCACAGGACAGACAACAAGGTCCACATG
GGGGATCTGGACGTCCCGCTGGAGCAGGAAATGGCCAAGGAGGACCCTGTTTGCGCCCCA
GAGAGCATGGGCAGTGAGGACATGCTCTTCATGCTGTACACCTCAGGGAGCACCGGAATG
CCCAAGGGCATCGTCCATACCCAGGCAGGCTACCTGCTCTATGCCGCCCTGACTCACAAG
CTTGTGTTTGACCACCAGCCAGGTGACATCTTTGGCTGTGTGGCCGACATCGGTTGGATT
ACAGGACACAGCTACGTGGTGTATGGGCCTCTCTGCAATGGTGCCACCAGCGTCCTTTTT
GAGAGCACCCCAGTTTATCCCAATGCTGGTCGGTACTGGGAGACAGTAGAGAGGTTGAAG
ATCAATCAGTTCTATGGCGCCCCAACGGCTGTCCGGCTGTTGCTGAAATACGGTGATGCC
TGGGTGAAGAAGTATGATCGCTCCTCCCTGCGGACCCTGGGGTCAGTGGGAGAGCCCATC
AACTGTGAGGCCTGGGAGTGGCTTCACAGGGTGGTGGGGGACAGCAGGTGCACGCTGGTG
GACACCTGGTGGCAGACAGAAACAGGTGGCATCTGCATCGCACCACGGCCCTCGGAAGAA
GGGGCGGAAATCCTCCCTGCCATGGCGATGAGGCCCTTCTTTGGCATCGTCCCCGTCCTC
ATGGATGAGAAGGGCAGCGTCATGGAGGGCAGCAACGTCTCCGGGGCCCTGTGCATCTCC
CAGGCCTGGCCGGGCATGGCCAGGACCATCTATGGCGACCACCAGCGATTTGTGGACGCC
TACTTCAAGGCCTACCCAGGCTATTACTTCACTGGAGACGGGGCTTACCGAACTGAGGGC
GGCTATTACCAGATCACAGGGCGGATGGATGATGTCATCAACATCAGTGGCCACCGGCTG
GGGACCGCAGAGATTGAGGACGCCATCGCCGACCACCCTGCAGTACCAGAAAGTGCTGTC
ATTGGCTACCCCCACGACATCAAAGGAGAAGCTGCCTTTGCCTTCATTGTGGTGAAAGAT
AGTGCGGGTGACTCAGATGTGGTGGTGCAGGAGCTCAAGTCCATGGTGGCCACCAAGATC
GCCAAATATGCTGTGCCTGATGAGATCCTGGTGGTGAAACGTCTTCCAAAAACCAGGTCT
GGGAAGGTCATGCGGCGGCTCCTGAGGAAGATCATCACTAGTGAGGCCCAGGAGCTGGGA
GACACTACCACCTTGGAGGACCCCAGCATCATCGCAGAGATCCTGAGTGTCTACCAGAAG
TGCAAGGACAAGCAGGCTGCTGCTAAGTGA
|
| Enzyme 28 GenBank Gene ID |
BC039261  |
| Enzyme 28 GeneCard ID |
ACSS1  |
| Enzyme 28 GenAtlas ID |
ACSS1  |
| Enzyme 28 HGNC ID |
HGNC:16091  |
| Enzyme 28 Chromosome Location |
2 |
| Enzyme 28 Locus |
20p11.23-p11.21 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E: Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10224-9. Epub 2006 Jun 20. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB: Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem. 2009 Sep 4;284(36):24394-405. Epub 2009 Jun 16. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5272 |
| Enzyme 29 Name |
Citrate synthase, mitochondrial |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
CS |
| Enzyme 29 Protein Sequence |
>Citrate synthase, mitochondrial
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVV
GQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLF
WLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESN
FARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNF
TNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPL
HGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQ
REFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYY
TVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
|
| Enzyme 29 Number of Residues |
466 |
| Enzyme 29 Molecular Weight |
51712.0 |
| Enzyme 29 Theoretical pI |
8.53 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- citrate (Si)-synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- carbohydrate metabolic process
- cellular carbohydrate metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- primary metabolic process
- tricarboxylic acid cycle
|
| Component |
| — |
|
| Enzyme 29 General Function |
Involved in transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer |
| Enzyme 29 Specific Function |
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- acetyl-CoA + H2O + oxaloacetate = citrate + CoA [RN:R00351]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
3288815  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
O75390  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
CISY_HUMAN  |
| Enzyme 29 PDB ID |
4CTS  |
| Enzyme 29 PDB File |
Show |
| Enzyme 29 3D Structure |
|
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1401 bp
ATGGCTTTACTTACTGCGGCCGCCCGGCTCTTGGGAACCAAGAATGCATCTTGTCTTGTT
CTTGCAGCCCGGCATGCTAGTGCTTCCTCCACGAATTTGAAAGACATATTGGCTGACCTG
ATACCTAAGGAGCAGGCCAGAATTAAGACTTTCAGGCAGCAACATGGCAAGACGGTGGTG
GGCCAAATCACTGTGGACATGATGTATGGTGGCATGAGAGGCATGAAGGGATTGGTGTAT
GAAACATCAGTTCTTGATCCTGATGAGGGCATCCGTTTCCGAGGCTTTAGTATCCCTGAA
TGCCAGAAACTGCTACCCAAGGCTAAGGGTGGGGAAGAACCCCTGCCTGAGGGCTTATTT
TGGCTGCTGGTAACTGGATGTATCCCAACAGAGGAACAGGTATCTTGGCTCTCAAAAGAG
TGGGCAAAGAGGGCAGCTCTGCCTTCCCATGTGGTCACCATGCTGGACAACTTTCCCACC
AATCTACACCCCATGTCTCAGCTGAGTGCAGCTGTTACAGCCCTCAACAGTGAAAGTAAC
TTTGCCCAAGCATATGCACGGGGTATCAGCCGAACCAAGTACTGGGAGTTGATTTATGAA
GATTCTGTGGATCTAATAGCAAAGCTACCTTGTGTTGCAGCAAAGATCTACCGAAATCTC
TACTGGGAAGGCAGCGGTATTGGGGCCATTGACTCTAACCTGGACTGGTCTCACAATTTC
ACCAACATGTTAGGCTATACTGATCATCAGTTCACTGAGCTCATGCGCCTGTACCTCACC
ATCCACAGTGACCATGAGGGTGGCAATGTAAGTGCCCATACCAGCCACTTGGTGGGCAGT
GCCCTTTCCGACCCTTACCTGTCCTTTGCAGCAGCCATGAACGGGCTGGCAGGGCCTCTC
CATGGACTGGCAAATCAGGAAGTGCTTGTCTGGCTAACACAGCTGCAGAAGGAAGTTGGC
AAAGATGTGTCAGATGAGAAGTTACGAGACTACATCTGGAACACACTCAACTCAGGACGG
GTTGTTCCAGGCTATGGCCATGCAGTACTAAGGAAGACTGATCCGCGATATACCTGTCAG
CGAGAGTTTGCTCTGAAACACCTGCCTAATGACCCCATGTTTAAGTTGGTTGCTCAGCTG
TACAAGATTGTGCCCAATGTCCTCTTAGAGCAGGGTAAAGCCAAGAATCCTTGGCCCAAT
GTAGATGCTCACAGTGGGGTGCTGCTCCAGTATTATGGCATGACGGAGATGAATTACTAC
ACGGTCCTGTTTGGGGTGTCACGAGCATTGGGTGTACTGGCACAGCTCATCTGGAGCCGA
GCCTTAGGCTTCCCTCTAGAAAGGCCCAAGTCCATGAGCACAGAGGGTCTGATGAAGTTT
GTGGACTCTAAGTCAGGGTAA
|
| Enzyme 29 GenBank Gene ID |
AF047042  |
| Enzyme 29 GeneCard ID |
CS  |
| Enzyme 29 GenAtlas ID |
CS  |
| Enzyme 29 HGNC ID |
HGNC:2422  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
12q13.2 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Goldenthal MJ, Marin-Garcia J, Ananthakrishnan R: Cloning and molecular analysis of the human citrate synthase gene. Genome. 1998 Oct;41(5):733-8. [PubMed
]
- Liu Q, Yu L, Han XF, Fu Q, Zhang JX, Tang H, Zhao SY: [Cloning and tissue expression pattern analysis of the human citrate synthase cDNA] Shi Yan Sheng Wu Xue Bao. 2000 Sep;33(3):207-14. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5273 |
| Enzyme 30 Name |
Testis-specific chromodomain protein Y 2 |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
CDY2A |
| Enzyme 30 Protein Sequence |
>Testis-specific chromodomain protein Y 2
MASQEFEVEAIVDKRQDKNGNTQYLVRWKGYDKQDDTWEPEQHLMNCEKCVHDFNRRQTE
KQKKLTWTTTSRIFSNNARRRTSRSTKANYSKNSPKTPVTDKHHRSKNCKLFAASKNVRR
KAASTLSDTKNMEIINSTIETLAPDSPFDHKKTVSGFQKLEKLDPIAADQQDTVVFKVTE
GKLLRDPLSHPGAEQTGIQNKTQMHPLMSQMSGSVTASMATGSATRKGIVVLIDPLAANG
TTDMHTSVPRVKGGQRNITDDSRGQPFIKKMHFTIRLTESAITYRDIVVKKEDGFTQIVL
STRSTEKNALNTEVIKEMVNALNSAAADDSKLVLFSAAGSVFCCGLDFGYFVRHLRNDRN
TASLEMVDTIKNFVNTFIQFKKPIVVSVNGPAIGLGASILPLCDLVWANEKAWFQTPYTT
FGQSPDGCSSITFPKMMGKASANEMLIAGRKLTAREACAKGLVSQVFLTGTFTQEVMIQI
KELASYNAIVLEECKALVRCNIKLELEQANERECEVLRKIWSSAQGIESMLKYVENKIDE
F
|
| Enzyme 30 Number of Residues |
541 |
| Enzyme 30 Molecular Weight |
60523.7 |
| Enzyme 30 Theoretical pI |
9.42 |
| Enzyme 30 GO Classification |
| Function |
- binding
- catalytic activity
- chromatin binding
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin assembly or disassembly
- chromatin organization
- chromosome organization
- metabolic process
- organelle organization
|
| Component |
- chromatin
- chromosomal part
- intracellular membrane-bounded organelle
- intracellular organelle part
- membrane-bounded organelle
- nucleus
- organelle
- organelle part
|
|
| Enzyme 30 General Function |
Involved in chromatin binding |
| Enzyme 30 Specific Function |
May have histone acetyltransferase activity |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
4558754  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q9Y6F7  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
CDY2_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1626 bp
ATGGCTTCCCAGGAGTTTGAGGTTGAAGCTATTGTTGACAAAAGACAGGATAAAAATGGG
AATACACAGTATTTGGTTCGGTGGAAAGGTTATGACAAACAGGATGACACTTGGGAACCA
GAGCAGCACCTCATGAACTGTGAAAAATGTGTACATGATTTTAATAGACGACAGACTGAA
AAACAGAAAAAACTGACATGGACTACAACCAGTAGAATTTTTTCAAACAATGCCAGAAGA
AGAACTTCCAGATCTACAAAAGCAAACTATTCTAAGAACTCTCCTAAAACTCCAGTGACT
GATAAACACCACAGGTCCAAAAACTGCAAGTTATTTGCTGCCAGCAAGAACGTTAGGAGA
AAGGCAGCTTCAACTCTCTCCGACACAAAGAATATGGAGATAATAAATTCAACTATTGAG
ACCCTTGCACCTGACAGCCCCTTTGACCACAAGAAAACTGTGAGTGGCTTTCAGAAACTT
GAGAAACTGGACCCTATTGCAGCAGATCAGCAGGACACGGTGGTCTTCAAGGTGACAGAA
GGGAAACTCCTCCGGGACCCTTTGTCACATCCTGGTGCAGAACAGACTGGAATACAGAAC
AAGACTCAGATGCACCCACTAATGTCGCAGATGTCTGGCTCAGTTACTGCTTCTATGGCC
ACAGGTTCAGCTACCCGAAAGGGTATAGTGGTATTAATAGACCCATTAGCAGCCAATGGG
ACAACAGACATGCATACCTCAGTTCCAAGAGTGAAAGGTGGGCAAAGAAATATTACTGAT
GACAGCAGAGGCCAGCCTTTTATCAAGAAGATGCACTTCACCATAAGGCTAACAGAAAGT
GCCATCACATACAGAGACATTGTAGTGAAGAAAGAGGATGGATTCACCCAGATAGTGCTA
TCAACTAGATCGACAGAAAAAAATGCACTGAATACAGAAGTAATTAAAGAAATGGTTAAT
GCTCTGAATAGCGCTGCTGCAGATGACAGCAAGCTCGTGCTGTTCAGTGCAGCTGGAAGT
GTCTTTTGCTGCGGTCTTGATTTTGGGTACTTTGTGAGGCACTTAAGGAATGACAGAAAC
ACAGCAAGCCTTGAAATGGTGGACACCATCAAGAACTTTGTGAATACTTTTATTCAATTT
AAAAAGCCTATTGTTGTATCAGTCAATGGCCCTGCCATTGGACTAGGTGCATCCATCCTG
CCTCTTTGTGATCTCGTGTGGGCTAATGAAAAGGCTTGGTTCCAAACCCCTTATACGACC
TTTGGACAGAGTCCAGATGGCTGTTCTTCTATTACATTCCCCAAAATGATGGGTAAAGCA
TCTGCCAATGAAATGTTAATTGCTGGGCGAAAGCTGACAGCACGGGAGGCATGCGCCAAA
GGCCTGGTCTCTCAGGTATTTTTGACTGGAACTTTCACCCAAGAGGTTATGATTCAAATT
AAGGAGCTTGCCTCATACAATGCAATTGTACTGGAAGAATGTAAGGCCCTCGTTCGCTGT
AATATTAAGTTGGAGTTGGAACAGGCCAATGAGAGAGAGTGTGAGGTGCTGAGGAAGATC
TGGAGCTCAGCCCAAGGGATAGAATCCATGTTAAAGTATGTTGAAAATAAAATTGATGAG
TTTTAA
|
| Enzyme 30 GenBank Gene ID |
AF080598  |
| Enzyme 30 GeneCard ID |
CDY2A  |
| Enzyme 30 GenAtlas ID |
CDY2A  |
| Enzyme 30 HGNC ID |
HGNC:1810  |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Lahn BT, Page DC: Retroposition of autosomal mRNA yielded testis-specific gene family on human Y chromosome. Nat Genet. 1999 Apr;21(4):429-33. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5274 |
| Enzyme 31 Name |
3-ketoacyl-CoA thiolase, peroxisomal |
| Enzyme 31 Synonyms |
- Acetyl-CoA acyltransferase
- Beta-ketothiolase
- Peroxisomal 3-oxoacyl-CoA thiolase
|
| Enzyme 31 Gene Name |
ACAA1 |
| Enzyme 31 Protein Sequence |
>3-ketoacyl-CoA thiolase, peroxisomal
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIP
MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSI
TVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPI
LGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLR
LPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFE
YPGN
|
| Enzyme 31 Number of Residues |
424 |
| Enzyme 31 Molecular Weight |
44291.6 |
| Enzyme 31 Theoretical pI |
8.55 |
| Enzyme 31 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 31 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 31 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 31 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
23874  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P09110  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
THIK_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1275 bp
ATGCAGAGGCTGCAGGTAGTGCTGGGCCACCTGAGGGGTCCGGCCGATTCCGGCTGGATG
CCGCAGGCCGCGCCTTGCCTGAGCGGTGCCCCGCAGGCCTCGGCCGCGGACGTGGTGGTG
GTGCACGGGCGGCGCACGGCCATCTGCCGGGCGGGCCGCGGCGGCTTCAAGGACACCACC
CCCGACGAGCTTCTCTCGGCAGTCATGACCGCGGTTCTCAAGGACGTGAATCTGAGGCCG
GAACAGCTGGGGGACATCTGTGTCGGAAATGTGCTGCAGCCTGGGGCCGGGGCAATCATG
GCCCGAATCGCCCAGTTTCTGAGTGACATCCCGGAGACTGTGCCTTTGTCCACTGTCAAT
AGACAGTGCTCGTCGGGGCTACAGGCAGTGGCCAGCATAGCAGGTGGCATCAGAAATGGG
TCTTATGACATTGGCATGGCCTGTGGGGTGGAGTCCATGTCCCTGGCTGACAGAGGGAAC
CCTGGAAATATTACTTCGCGCTTGATGGAGAAGGAGAAGGCCAGAGATTGCCTGATTCCT
ATGGGGATAACCTCTGAGAATGTGGCTGAGCGGTTTGGCATTTCACGGGAGAAGCAGGAT
ACCTTTGCCCTGGCTTCCCAGCAGAAGGCAGCAAGAGCCCAGAGCAAGGGCTGTTTCCAA
GCTGAGATTGTGCCTGTGACCACCACGGTCCATGATGACAAGGGCACCAAGAGGAGCATC
ACTGTGACCCAGGATGAGGGTATCCGCCCCAGCACCACCATGGAGGGCCTGGCCAAACTG
AAGCCTGCCTTCAAGAAAGATGGTTCTACCACAGCTGGAAACTCTAGCCAGGTGAGTGAT
GGGGCAGCTGCCATCCTGCTGGCCCGGAGGTCCAAGGCAGAAGAGTTGGGCCTTCCCATC
CTTGGGGTCCTGAGGTCTTATGCAGTGGTTGGGGTCCCACCTGACATCATGGGCATTGGA
CCTGCCTATGCCATCCCAGTAGCTTTGCAAAAAGCAGGGCTGACAGTGAGTGACGTGGAC
ATCTTCGAGATCAATGAGGCCTTTGCAAGCCAGGCTGCCTACTGTGTGGAGAAGCTACGA
CTCCCCCCTGAGAAGGTGAACCCCCTGGGGGGTGCAGTGGCCTTAGGGCACCCACTGGGC
TGCACTGGGGCACGACAGGTCATCACGCTGCTCAATGAGCTGAAGCGCCGTGGGAAGAGG
GCATACGGAGTGGTGTCCATGTGCATCGGGACTGGAATGGGAGCCGCTGCCGTCTTTGAA
TACCCTGGGAACTGA
|
| Enzyme 31 GenBank Gene ID |
X12966  |
| Enzyme 31 GeneCard ID |
ACAA1  |
| Enzyme 31 GenAtlas ID |
ACAA1  |
| Enzyme 31 HGNC ID |
HGNC:82  |
| Enzyme 31 Chromosome Location |
3 |
| Enzyme 31 Locus |
3p23-p22 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Bout A, Teunissen Y, Hashimoto T, Benne R, Tager JM: Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase. Nucleic Acids Res. 1988 Nov 11;16(21):10369. [PubMed
]
- Fairbairn LJ, Tanner MJ: Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase. Nucleic Acids Res. 1989 May 11;17(9):3588. [PubMed
]
- Bout A, Franse MM, Collins J, Blonden L, Tager JM, Benne R: Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient. Biochim Biophys Acta. 1991 Aug 27;1090(1):43-51. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5275 |
| Enzyme 32 Name |
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial |
| Enzyme 32 Synonyms |
- PDHE1-A type I
|
| Enzyme 32 Gene Name |
PDHA1 |
| Enzyme 32 Protein Sequence |
>Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS
|
| Enzyme 32 Number of Residues |
390 |
| Enzyme 32 Molecular Weight |
43295.3 |
| Enzyme 32 Theoretical pI |
8.14 |
| Enzyme 32 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
- pyruvate dehydrogenase (acetyl-transferring) activity
- pyruvate dehydrogenase activity
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- oxidation reduction
- small molecule metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 32 General Function |
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| Enzyme 32 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 [RN:R01699]
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
Not Available |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P08559  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
ODPA_HUMAN  |
| Enzyme 32 PDB ID |
1NI4  |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1173 bp
ATGAGGAAGATGCTCGCCGCCGTCTCCCGCGTGCTGTCTGGCGCTTCTCAGAAGCCGGCA
AGCAGAGTGCTGGTAGCATCCCGTAATTTTGCAAATGATGCTACATTTGAAATTAAGAAA
TGTGACCTTCACCGGCTGGAAGAAGGCCCTCCTGTCACAACAGTGCTCACCAGGGAGGAT
GGGCTCAAATACTACAGGATGATGCAGACTGTACGCCGAATGGAGTTGAAAGCAGATCAG
CTGTATAAACAGAAAATTATTCGTGGTTTCTGTCACTTGTGTGATGGTCAGGAAGCTTGC
TGTGTGGGCCTGGAGGCCGGCATCAACCCCACAGACCATCTCATCACAGCCTACCGGGCT
CACGGCTTTACTTTCACCCGGGGCCTTTCCGTCCGAGAAATTCTCGCAGAGCTTACAGGA
CGAAAAGGAGGTTGTGCTAAAGGGAAAGGAGGATCGATGCACATGTATGCCAAGAACTTC
TACGGGGGCAATGGCATCGTGGGAGCGCAGGTGCCCCTGGGCGCTGGGATTGCTCTAGCC
TGTAAGTATAATGGAAAAGATGAGGTCTGCCTGACTTTATATGGCGATGGTGCTGCTAAC
CAGGGCCAGATATTCGAAGCTTACAACATGGCAGCTTTGTGGAAATTACCTTGTATTTTC
ATCTGTGAGAATAATCGCTATGGAATGGGAACGTCTGTTGAGAGAGCGGCAGCCAGCACT
GATTACTACAAGAGAGGCGATTTCATTCCTGGGCTGAGAGTGGATGGAATGGATATCCTG
TGCGTCCGAGAGGCAACAAGGTTTGCTGCTGCCTATTGTAGATCTGGGAAGGGGCCCATC
CTGATGGAGCTGCAGACTTACCGTTACCACGGACACAGTATGAGTGACCCTGGAGTCAGT
TACCGTACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGTGACCCTATTATGCTTCTC
AAGGACAGGATGGTGAACAGCAATCTTGCCAGTGTGGAAGAACTAAAGGAAATTGATGTG
GAAGTGAGGAAGGAGATTGAGGATGCTGCCCAGTTTGCCACGGCCGATCCTGAGCCACCT
TTGGAAGAGCTGGGCTACCACATCTACTCCAGCGACCCACCTTTTGAAGTTCGTGGTGCC
AATCAGTGGATCAAGTTTAAGTCAGTCAGTTAA
|
| Enzyme 32 GenBank Gene ID |
M24848  |
| Enzyme 32 GeneCard ID |
PDHA1  |
| Enzyme 32 GenAtlas ID |
PDHA1  |
| Enzyme 32 HGNC ID |
HGNC:8806  |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Koike K, Urata Y, Matsuo S, Koike M: Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit. Gene. 1990 Sep 14;93(2):307-11. [PubMed
]
- Ho L, Wexler ID, Liu TC, Thekkumkara TJ, Patel MS: Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5330-4. [PubMed
]
- Dahl HH, Hunt SM, Hutchison WM, Brown GK: The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J Biol Chem. 1987 May 25;262(15):7398-403. [PubMed
]
- Maragos C, Hutchison WM, Hayasaka K, Brown GK, Dahl HH: Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex. J Biol Chem. 1989 Jul 25;264(21):12294-8. [PubMed
]
- De Meirleir L, MacKay N, Lam Hon Wah AM, Robinson BH: Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex. J Biol Chem. 1988 Feb 5;263(4):1991-5. [PubMed
]
- Koike K, Ohta S, Urata Y, Kagawa Y, Koike M: Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):41-5. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Harris EE, Hey J: X chromosome evidence for ancient human histories. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3320-4. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS: Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. [PubMed
]
- Dahl HH, Brown GK, Brown RM, Hansen LL, Kerr DS, Wexler ID, Patel MS, De Meirleir L, Lissens W, Chun K, et al.: Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene. Hum Mutat. 1992;1(2):97-102. [PubMed
]
- Hansen LL, Brown GK, Kirby DM, Dahl HH: Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency. J Inherit Metab Dis. 1991;14(2):140-51. [PubMed
]
- De Meirleir L, Lissens W, Vamos E, Liebaers I: Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit. Hum Genet. 1992 Mar;88(6):649-52. [PubMed
]
- Dahl HH, Hansen LL, Brown RM, Danks DM, Rogers JG, Brown GK: X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation. J Inherit Metab Dis. 1992;15(6):835-47. [PubMed
]
- Ito M, Huq AH, Naito E, Saijo T, Takeda E, Kuroda Y: Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein. J Inherit Metab Dis. 1992;15(6):848-56. [PubMed
]
- Matthews PM, Marchington DR, Squier M, Land J, Brown RM, Brown GK: Molecular genetic characterization of an X-linked form of Leigh's syndrome. Ann Neurol. 1993 Jun;33(6):652-5. [PubMed
]
- Chun K, MacKay N, Petrova-Benedict R, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex. Hum Mol Genet. 1993 Apr;2(4):449-54. [PubMed
]
- Matthews PM, Brown RM, Otero LJ, Marchington DR, LeGris M, Howes R, Meadows LS, Shevell M, Scriver CR, Brown GK: Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients. Brain. 1994 Jun;117 ( Pt 3):435-43. [PubMed
]
- Hansen LL, Horn N, Dahl HH, Kruse TA: Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit. Hum Mol Genet. 1994 Jun;3(6):1021-2. [PubMed
]
- Dahl HH, Brown GK: Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit. Hum Mutat. 1994;3(2):152-5. [PubMed
]
- Awata H, Endo F, Tanoue A, Kitano A, Matsuda I: Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia. J Inherit Metab Dis. 1994;17(2):189-95. [PubMed
]
- Chun K, MacKay N, Petrova-Benedict R, Federico A, Fois A, Cole DE, Robertson E, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex. Am J Hum Genet. 1995 Mar;56(3):558-69. [PubMed
]
- Takakubo F, Cartwright P, Hoogenraad N, Thorburn DR, Collins F, Lithgow T, Dahl HH: An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am J Hum Genet. 1995 Oct;57(4):772-80. [PubMed
]
- Hemalatha SG, Kerr DS, Wexler ID, Lusk MM, Kaung M, Du Y, Kolli M, Schelper RL, Patel MS: Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit. Hum Mol Genet. 1995 Feb;4(2):315-8. [PubMed
]
- Lissens W, De Meirleir L, Seneca S, Benelli C, Marsac C, Poll-The BT, Briones P, Ruitenbeek W, van Diggelen O, Chaigne D, Ramaekers V, Liebaers I: Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency. Hum Mutat. 1996;7(1):46-51. [PubMed
]
- Tripatara A, Kerr DS, Lusk MM, Kolli M, Tan J, Patel MS: Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS). Hum Mutat. 1996;8(2):180-2. [PubMed
]
- Naito E, Ito M, Yokota I, Saijo T, Matsuda J, Osaka H, Kimura S, Kuroda Y: Biochemical and molecular analysis of an X-linked case of Leigh syndrome associated with thiamin-responsive pyruvate dehydrogenase deficiency. J Inherit Metab Dis. 1997 Aug;20(4):539-48. [PubMed
]
- Otero LJ, Brown RM, Brown GK: Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity. Hum Mutat. 1998;12(2):114-21. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5276 |
| Enzyme 33 Name |
Acetyl-CoA carboxylase 1 |
| Enzyme 33 Synonyms |
- ACC-alpha
- Biotin carboxylase
|
| Enzyme 33 Gene Name |
ACACA |
| Enzyme 33 Protein Sequence |
>Acetyl-CoA carboxylase 1
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST
|
| Enzyme 33 Number of Residues |
2346 |
| Enzyme 33 Molecular Weight |
265551.7 |
| Enzyme 33 Theoretical pI |
6.32 |
| Enzyme 33 GO Classification |
| Function |
- ATP binding
- CoA carboxylase activity
- acetyl-CoA carboxylase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Involved in acetyl-CoA carboxylase activity |
| Enzyme 33 Specific Function |
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
38679967  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q13085  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
ACACA_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>7041 bp
ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCTGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGTTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTAGCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCATGTCT
GGCTTGCACCTAGTAAAGCAGGGCCGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTTATTGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCAGTGCCTGGA
GGACCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTACAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAGCCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTACAGGCA
GCTGAGGAAGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTCAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTGGAATTGAATCCT
CGGCTGCAGGTAGAGCACCCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCTGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCCTGGGGTGATTCTCCCATTGATTTTGAAGATTCTGCACACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGATTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAGGCAATTTCAAACATGGTGGTGGCTTTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAGATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACAGGCTGAGCGACCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTGGCA
GATGTGAGCCTGCGGAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCTGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTATACTACGTATATGAAAGAGGAAGTGGATAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCT
GAGATTGAGGTAATGAAGATGGTAATGACCTTAACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGACCTGGAGCAGCTCTTGACCCTGGCTGTGTACTAGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACGGCACTCAGAGGCGAGAAACTCCATCGAGTGTTCCATTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAGCGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTTCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTCCGAGAAGAGAATAAAAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTCACTGATGAGCTGCTG
AATATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGAGCTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTATGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGTGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTA
CTGTTGGACAACTCATTCACTCCACCTTGTCAGCGGATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTGATGGGCTGCTTCTCTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACTGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTTACCCAGCAAAATAAAGCTACCCTGGTT
GACCATGGGATCCGGCGCCTTACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAATGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCTTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTCTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAACAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACATACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCCACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGACCTTTAAAAGTCCTGAATATCCAGAAGGCCGAGATATCATTGTTATT
GGCAATGACATCACATACCGAATTGGGTCCTTTGGGCCTCAAGAGGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCAGAAGGTATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
CCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCAGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATTGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTGCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTAATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTATGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGATGACTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTGCACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATACGATCCTCGATGGATGCTAGCAGGC
CGTCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACTGTGGTGGTTGGTAGAGCCAGGCTAGGAGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGAACAGTAGAACTAAGTATCCCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCAGGCTGGCCAGGTTTGGTTCCCA
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTGCCTCTG
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTACGACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGAGGGAGTGCTGCCAGCCTGTGCTGGTT
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATTGACTCCTCCATC
AACCCCCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACAGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTAAGCACAGCTGAG
CGGAAGGAGTTGGAGAACAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCCATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACACCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGGCTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAATGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGGCGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGAGCAGAAGTCATACGGATCCTCTCCACA
ATGGATTCCCCTTCCACGTAG
|
| Enzyme 33 GenBank Gene ID |
NM_198836.1  |
| Enzyme 33 GeneCard ID |
ACACA  |
| Enzyme 33 GenAtlas ID |
ACACA  |
| Enzyme 33 HGNC ID |
HGNC:84  |
| Enzyme 33 Chromosome Location |
1 |
| Enzyme 33 Locus |
17q21 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed
]
- Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed
]
- Sinilnikova OM, Ginolhac SM, Magnard C, Leone M, Anczukow O, Hughes D, Moreau K, Thompson D, Coutanson C, Hall J, Romestaing P, Gerard JP, Bonadona V, Lasset C, Goldgar DE, Joulin V, Venezia ND, Lenoir GM: Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility. Carcinogenesis. 2004 Dec;25(12):2417-24. Epub 2004 Aug 27. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Travers MT, Vallance AJ, Clegg RA, Thomson R, Price NT, Barber MC: Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspects. Biochim Biophys Acta. 2003 Nov 15;1634(3):97-106. [PubMed
]
- Travers MT, Cambot M, Kennedy HT, Lenoir GM, Barber MC, Joulin V: Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes. Genomics. 2005 Jan;85(1):71-84. [PubMed
]
- Magnard C, Bachelier R, Vincent A, Jaquinod M, Kieffer S, Lenoir GM, Venezia ND: BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains. Oncogene. 2002 Oct 3;21(44):6729-39. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Moreau K, Dizin E, Ray H, Luquain C, Lefai E, Foufelle F, Billaud M, Lenoir GM, Venezia ND: BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase. J Biol Chem. 2006 Feb 10;281(6):3172-81. Epub 2005 Dec 2. [PubMed
]
- Ray H, Moreau K, Dizin E, Callebaut I, Venezia ND: ACCA phosphopeptide recognition by the BRCT repeats of BRCA1. J Mol Biol. 2006 Jun 16;359(4):973-82. Epub 2006 Apr 25. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed
]
- Blom W, de Muinck Keizer SM, Scholte HR: Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty acid synthesis. N Engl J Med. 1981 Aug 20;305(8):465-6. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5277 |
| Enzyme 34 Name |
Trifunctional enzyme subunit beta, mitochondrial |
| Enzyme 34 Synonyms |
- TP-beta
- 3-ketoacyl-CoA thiolase
- Acetyl-CoA acyltransferase
- Beta-ketothiolase
|
| Enzyme 34 Gene Name |
HADHB |
| Enzyme 34 Protein Sequence |
>Trifunctional enzyme subunit beta, mitochondrial
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
|
| Enzyme 34 Number of Residues |
474 |
| Enzyme 34 Molecular Weight |
51294.0 |
| Enzyme 34 Theoretical pI |
9.94 |
| Enzyme 34 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 34 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 34 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 34 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 34 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
Not Available |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P55084  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
ECHB_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1425 bp
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
|
| Enzyme 34 GenBank Gene ID |
D16481  |
| Enzyme 34 GeneCard ID |
HADHB  |
| Enzyme 34 GenAtlas ID |
HADHB  |
| Enzyme 34 HGNC ID |
HGNC:4803  |
| Enzyme 34 Chromosome Location |
2 |
| Enzyme 34 Locus |
2p23 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed
]
- Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Middleton B: The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase. Biochem Soc Trans. 1994 May;22(2):427-31. [PubMed
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Kamijo T, Wanders RJ, Saudubray JM, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest. 1994 Apr;93(4):1740-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed
]
- Spiekerkoetter U, Sun B, Khuchua Z, Bennett MJ, Strauss AW: Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations. Hum Mutat. 2003 Jun;21(6):598-607. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
5278 |
| Enzyme 35 Name |
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial |
| Enzyme 35 Synonyms |
- AKB ligase
- Aminoacetone synthase
- Glycine acetyltransferase
|
| Enzyme 35 Gene Name |
GCAT |
| Enzyme 35 Protein Sequence |
>2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRV
DGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIA
RFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLD
MADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLG
PTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPP
AVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLAS
RMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
|
| Enzyme 35 Number of Residues |
419 |
| Enzyme 35 Molecular Weight |
45284.6 |
| Enzyme 35 Theoretical pI |
8.11 |
| Enzyme 35 GO Classification |
| Function |
- C-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- glycine C-acetyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Involved in glycine C-acetyltransferase activity |
| Enzyme 35 Specific Function |
Acetyl-CoA + glycine = CoA + 2-amino-3- oxobutanoate |
| Enzyme 35 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 35 Reactions |
- acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate [RN:R00371]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
Not Available |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
O75600  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
KBL_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1260 bp
ATGTGGCCTGGGAACGCCTGGCGCGCCGCACTCTTCTGGGTGCCCCGCGGCCGCCGCGCA
CAGTCAGCGCTGGCCCAGCTGCGTGGCATTCTGGAGGGGGAGCTGGAAGGCATCCGCGGA
GCTGGCACTTGGAAGAGTGAGCGGGTCATCACGTCCCGTCAGGGGCCGCACATCCGCGTG
GACGGCGTCTCCGGAGGAATCCTCAACTTCTGTGCCAACAACTACCTGGGCCTGAGCAGC
CACCCTGAGGTGATTCAGGCAGGTCTGCAGGCTCTGGAGGAGTTTGGAGCTGGCCTTAGC
TCGGTCCGCTTCATCTGTGGAACCCAGAGCATCCACAAGAATCTAGAAGCAAAAATAGCC
CGCTTCCACCAGCGGGAGGATGCCATCCTCTATCCCAGCTGTTATGACGCCAACGCCGGC
CTCTTTGAGGCCCTGCTGACCCCAGAGGACGCAGTCCTGTCGGACGAGCTGAACCATGCC
TCCATCATCGACGGCATCCGGCTGTGCAAGGCCCACAAGTACCGCTATCGCCACCTGGAC
ATGGCCGACCTAGAAGCCAAGCTGCAGGAGGCCCAGAAGCATCGGCTGCGCCTGGTGGCC
ACCGATGGGGCCTTTTCCATGGATGGCGACATCGCACCCCTGCAGGAGATCTGCTGCCTC
GCCTCTAGATATGGTGCCCTGGTCTTCATGGATGAATGCCATGCCACTGGTTTCCTGGGG
CCCACAGGACGGGGCACAGATGAGCTGCTGGGTGTGATGGACCAGGTCACCATCATCAAC
TCCACCCTGGGGAAGGCCCTGGGTGGAGCATCAGGGGGCTACACGACAGGGCCTGGGCCC
CTGGTGTCACTGCTGCGGCAGCGCGCCCGGCCATACCTCTTCTCCAACAGTCTGCCACCT
GCTGTCGTTGGCTGCGCCTCCAAGGCCCTAGATCTGCTGATGGGGAGTAACACCATTGTC
CAGTCTATGGCTGCCAAGACCCAGAGGTTCCGTAGTAAGATGGAAGCTGCTGGCTTCACT
ATCTCAGGAGCCAGTCACCCCATCTGCCCTGTGATGCTGGGTGATGCCCGGCTGGCCTCT
CGCATGGCGGATGACATGCTGAAGAGAGGCATCTTTGTCATCGGGTTCAGCTACCCCGTG
GTCCCCAAGGGCAAGGCCCGGATCCGGGTACAGATCTCAGCAGTGCATAGCGAGGAAGAC
ATTGACCGCTGCGTGGAGGCCTTCGTGGAAGTGGGGCGACTGCACGGGGCACTGCCCTGA
|
| Enzyme 35 GenBank Gene ID |
AF077740  |
| Enzyme 35 GeneCard ID |
GCAT  |
| Enzyme 35 GenAtlas ID |
GCAT  |
| Enzyme 35 HGNC ID |
HGNC:4188  |
| Enzyme 35 Chromosome Location |
2 |
| Enzyme 35 Locus |
22q13.1 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Edgar AJ, Polak JM: Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur J Biochem. 2000 Mar;267(6):1805-12. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
5279 |
| Enzyme 36 Name |
Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial |
| Enzyme 36 Synonyms |
- PDHE1-A type II
|
| Enzyme 36 Gene Name |
PDHA2 |
| Enzyme 36 Protein Sequence |
>Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGL
KYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG
VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACK
YKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDY
YKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYR
TREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE
ELGHHIYSSDSSFEVRGANPWIKFKSVS
|
| Enzyme 36 Number of Residues |
388 |
| Enzyme 36 Molecular Weight |
42932.9 |
| Enzyme 36 Theoretical pI |
8.56 |
| Enzyme 36 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
- pyruvate dehydrogenase (acetyl-transferring) activity
- pyruvate dehydrogenase activity
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- oxidation reduction
- small molecule metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 36 General Function |
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| Enzyme 36 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 36 Pathways |
|
| Enzyme 36 Reactions |
- pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 [RN:R01699]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
Not Available |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
P29803  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
ODPAT_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>1167 bp
ATGCTGGCCGCCTTCATCTCCCGCGTGTTGAGGCGAGTTGCCCAGAAATCAGCTCGCAGA
GTGCTGGTGGCATCCCGTAACTCCTCAAATGACGCTACATTTGAAATTAAGAAATGTGAT
CTTTATCTGTTGGAAGAGGGTCCCCCTGTCACTACAGTGCTCACTAGGGCGGAGGGGCTT
AAATACTACAGGATGATGCTGACTGTTCGCCGCATGGAATTGAAGGCAGATCAGCTGTAC
AAACAGAAATTCATTCGCGGTTTCTGTCACCTGTGCGATGGTCAGGAAGCTTGTTGCGTG
GGCCTTGAGGCCGGCATAAACCCCTCGGATCACGTCATTACATCCTATAGGGCTCATGGT
GTGTGCTATACTCGGGGACTTTCTGTCCGATCCATTCTCGCAGAGCTGACGGGAAGAAGA
GGAGGTTGTGCTAAAGGAAAAGGAGGATCGATGCATATGTATACCAAGAACTTCTATGGG
GGCAATGGCATCGTCGGTGCACAGGGCCCCCTGGGCGCTGGCATTGCTCTGGCCTGTAAA
TATAAAGGAAACGATGAGATCTGTTTGACTTTATATGGGGATGGCGCTGCGAATCAGGGG
CAGATAGCCGAAGCTTTCAATATGGCAGCTTTATGGAAATTACCTTGTGTTTTCATCTGT
GAGAATAACCTATATGGAATGGGAACATCTACTGAGAGAGCAGCAGCCAGCCCTGATTAC
TACAAGAGGGGCAATTTTATCCCTGGGCTAAAGGTCGATGGAATGGATGTTCTGTGTGTT
CGTGAGGCAACAAAATTTGCAGCTAACTACTGTAGATCTGGAAAGGGGCCCATACTGATG
GAGCTGCAAACCTACCGTTATCATGGACACAGTATGAGTGATCCTGGAGTCAGTTATCGT
ACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGGGATCCTATAATAATTCTCCAAGAT
AGAATGGTAAACAGCAAGCTCGCCACTGTGGAAGAATTAAAGGAAATTGGGGCTGAGGTG
AGGAAAGAAATTGATGATGCTGCCCAGTTTGCTACCACTGATCCTGAGCCACATTTGGAA
GAATTAGGCCATCACATCTACAGCAGTGATTCATCTTTTGAAGTTCGTGGTGCAAATCCA
TGGATCAAGTTTAAGTCCGTCAGTTAA
|
| Enzyme 36 GenBank Gene ID |
AK313872  |
| Enzyme 36 GeneCard ID |
PDHA2  |
| Enzyme 36 GenAtlas ID |
PDHA2  |
| Enzyme 36 HGNC ID |
HGNC:8807  |
| Enzyme 36 Chromosome Location |
4 |
| Enzyme 36 Locus |
4q22-q23 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Dahl HH, Brown RM, Hutchison WM, Maragos C, Brown GK: A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4. Genomics. 1990 Oct;8(2):225-32. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
5280 |
| Enzyme 37 Name |
Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial |
| Enzyme 37 Synonyms |
- MMSDH
- Malonate-semialdehyde dehydrogenase [acylating]
- Aldehyde dehydrogenase family 6 member A1
|
| Enzyme 37 Gene Name |
ALDH6A1 |
| Enzyme 37 Protein Sequence |
>Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIH
NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA
KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCA
GIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG
QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKEN
TLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLIT
PQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFG
PVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLP
MFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR
|
| Enzyme 37 Number of Residues |
535 |
| Enzyme 37 Molecular Weight |
57839.3 |
| Enzyme 37 Theoretical pI |
8.69 |
| Enzyme 37 GO Classification |
| Function |
- catalytic activity
- methylmalonate-semialdehyde dehydrogenase (acylating) activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
|
| Process |
- branched chain family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- oxidation reduction
- valine metabolic process
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in oxidoreductase activity |
| Enzyme 37 Specific Function |
Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA |
| Enzyme 37 Pathways |
- Propanoate Metabolism (map00640
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 37 Reactions |
- 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH [RN:R00922]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
6164678  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q02252  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
MMSA_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>1608 bp
ATGGCGGCGCTATTGGCGGCGGCGGCAGTGCGAGCCCGGATCCTGCAGGTTTCTTCCAAG
GTGAAATCCAGTCCCACCTGGTATTCAGCATCTTCCTTCTCTTCTTCAGTGCCAACTGTA
AAGCTCTTCATTGGTGGGAAATTCGTTGAATCCAAAAGTGACAAATGGATCGATATCCAC
AACCCAGCCACCAATGAGGTCATTGGTCGGGTCCCTCAGGCCACCAAGGCAGAAATGGAT
GCAGCCATTGCTTCCTGCAAACGTGCTTTTCCTGCATGGGCAGACACTTCAGTATTAAGC
CGCCAGCAGGTCTTGCTCCGCTATCAACAACTTATTAAAGAAAACTTGAAAGAAATTGCC
AAGTTAATCACATTGGAACAAGGGAAGACCCTAGCTGATGCTGAAGGAGATGTATTTCGA
GGCCTTCAGGTGGTTGAGCATGCCTGTAGTGTGACATCCCTCATGATGGGAGAGACCATG
CCATCCATCACCAAAGACATGGACCTTTATTCCTACCGTCTGCCTCTGGGAGTGTGTGCA
GGCATTGCTCCATTCAATTTTCCTGCCATGATCCCCCTTTGGATGTTTCCCATGGCCATG
GTGTGTGGAAATACCTTCCTAATGAAACCATCTGAGCGAGTCCCTGGAGCAACTATGCTT
CTTGCTAAGTTGCTCCAGGATTCTGGTGCCCCTGATGGAACATTAAACATCATCCATGGA
CAGCATGAAGCTGTAAATTTTATTTGCGATCATCCGGACATCAAAGCAATCAGCTTTGTG
GGATCCAACAAGGCAGGAGAGTATATCTTCGAGAGAGGATCAAGACATGGCAAGAGGGTT
CAAGCCAATATGGGAGCCAAGAACCATGGGGTAGTCATGCCAGATGCCAATAAGGAAAAT
ACCCTGAACCAGCTGGTTGGGGCAGCATTTGGAGCTGCTGGTCAGCGCTGCATGGCTCTT
TCAACAGCAGTCCTTGTGGGAGAAGCCAAGAAGTGGCTGCCAGAGCTGGTGGAGCATGCC
AAAAACCTGAGAGTCAATGCAGGAGATCAGCCTGGAGCTGATCTTGGCCCTCTGATCACT
CCCCAGGCCAAAGAGCGAGTCTGTAATCTGATTGATAGTGGAACAAAGGAGGGAGCTTCC
ATCCTTCTTGATGGACGAAAAATTAAAGTGAAAGGCTATGAAAATGGCAACTTTGTTGGA
CCAACCATCATCTCGAATGTCAAGCCAAATATGACCTGTTACAAAGAGGAGATTTTTGGT
CCAGTTCTTGTGGTTCTGGAGACAGAAACATTGGATGAAGCCATCCAGATTGTAAATAAC
AACCCATATGGAAATGGAACTGCCATCTTCACCACCAATGGAGCCACTGCTCGGAAATAT
GCCCACTTGGTGGATGTTGGACAGGTGGGAGTGAATGTCCCCATTCCAGTGCCTTTGCCA
ATGTTCTCATTCACCGGCTCTCGATCCTCCTTCAGGGGAGACACCAATTTCTATGGCAAA
CAGGGCATCCAATTCTACACTCAGTTAAAGACCATTACTTCTCAGTGGAAAGAAGAAGAT
GCTACTCTTTCCTCACCTGCTGTTGTCATGCCTACCATGGGCCGTTAG
|
| Enzyme 37 GenBank Gene ID |
AF148505  |
| Enzyme 37 GeneCard ID |
ALDH6A1  |
| Enzyme 37 GenAtlas ID |
ALDH6A1  |
| Enzyme 37 HGNC ID |
HGNC:7179  |
| Enzyme 37 Chromosome Location |
1 |
| Enzyme 37 Locus |
14q24.3 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Chambliss KL, Gray RG, Rylance G, Pollitt RJ, Gibson KM: Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency. J Inherit Metab Dis. 2000 Jul;23(5):497-504. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kedishvili NY, Popov KM, Rougraff PM, Zhao Y, Crabb DW, Harris RA: CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. J Biol Chem. 1992 Sep 25;267(27):19724-9. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
5281 |
| Enzyme 38 Name |
Glucosamine 6-phosphate N-acetyltransferase |
| Enzyme 38 Synonyms |
- Phosphoglucosamine acetylase
- Phosphoglucosamine transacetylase
|
| Enzyme 38 Gene Name |
GNPNAT1 |
| Enzyme 38 Protein Sequence |
>Glucosamine 6-phosphate N-acetyltransferase
MKPDETPMFDPSLLKEVDWSQNTATFSPAISPTHPGEGLVLRPLCTADLNRGFFKVLGQL
TETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVE
DVVVSDECRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENYMCR
RFLK
|
| Enzyme 38 Number of Residues |
184 |
| Enzyme 38 Molecular Weight |
20749.0 |
| Enzyme 38 Theoretical pI |
8.12 |
| Enzyme 38 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 38 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 38 Specific Function |
Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate [RN:R02058]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
21748766  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q96EK6  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
GNA1_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>555 bp
ATGAAACCTGATGAAACTCCTATGTTTGACCCAAGTCTACTCAAAGAAGTGGACTGGAGT
CAGAATACAGCTACATTTTCTCCAGCCATTTCCCCAACACATCCTGGAGAAGGCTTGGTT
TTGAGGCCTCTTTGTACTGCTGACTTAAATAGAGGTTTTTTTAAGGTATTGGGTCAGCTA
ACAGAGACTGGAGTTGTCAGCCCTGAACAATTTATGAAATCTTTTGAGCATATGAAGAAA
TCTGGGGATTATTATGTTACAGTTGTAGAAGATGTGACTCTAGGACAGATTGTTGCTACG
GCAACTCTGATTATAGAACATAAATTCATCCATTCCTGTGCTAAGAGAGGAAGAGTAGAA
GATGTTGTTGTTAGTGATGAATGCAGAGGAAAGCAGCTTGGCAAATTGTTATTATCAACC
CTTACTTTGCTAAGCAAGAAACTGAACTGTTACAAGATTACCCTTGAATGTCTACCACAA
AATGTTGGTTTCTATAAAAAGTTTGGATATACTGTATCTGAAGAAAACTACATGTGTCGG
AGGTTTCTAAAGTAA
|
| Enzyme 38 GenBank Gene ID |
AK090577  |
| Enzyme 38 GeneCard ID |
GNPNAT1  |
| Enzyme 38 GenAtlas ID |
GNPNAT1  |
| Enzyme 38 HGNC ID |
HGNC:19980  |
| Enzyme 38 Chromosome Location |
1 |
| Enzyme 38 Locus |
14q22.1 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wang J, Liu X, Liang YH, Li LF, Su XD: Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1. FEBS Lett. 2008 Sep 3;582(20):2973-8. Epub 2008 Aug 7. [PubMed
]
- Hurtado-Guerrero R, Raimi OG, Min J, Zeng H, Vallius L, Shepherd S, Ibrahim AF, Wu H, Plotnikov AN, van Aalten DM: Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase. Biochem J. 2008 Oct 15;415(2):217-23. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
5282 |
| Enzyme 39 Name |
Hydroxymethylglutaryl-CoA synthase, cytoplasmic |
| Enzyme 39 Synonyms |
- HMG-CoA synthase
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
|
| Enzyme 39 Gene Name |
HMGCS1 |
| Enzyme 39 Protein Sequence |
>Hydroxymethylglutaryl-CoA synthase, cytoplasmic
MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCT
DREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDI
EGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALL
IGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKI
HAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEA
FGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQY
SPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAP
DVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEG
VGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH
|
| Enzyme 39 Number of Residues |
520 |
| Enzyme 39 Molecular Weight |
57293.1 |
| Enzyme 39 Theoretical pI |
5.05 |
| Enzyme 39 GO Classification |
| Function |
- catalytic activity
- hydroxymethylglutaryl-CoA synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- cellular lipid metabolic process
- isoprenoid biosynthetic process
- isoprenoid metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 39 General Function |
Involved in hydroxymethylglutaryl-CoA synthase activity |
| Enzyme 39 Specific Function |
This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase |
| Enzyme 39 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 39 Reactions |
- acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA [RN:R01978]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
30009  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q01581  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
HMCS1_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1563 bp
ATGCCTGGATCACTTCCTTTGAATGCAGAAGCTTGCTGGCCAAAAGATGTGGGAATTGTT
GCCCTTGAGATCTATTTTCCTTCTCAATATGTTGATCAAGCAGAGTTGGAAAAATATGAT
GGTGTAGATGCTGGAAAGTATACCATTGGCTTGGGCCAGGCCAAGATGGGCTTCTGCACA
GATAGAGAAGATATTAACTCTCTTTGCATGACTGTGGTTCAGAATCTTATGGAGAGAAAT
AACCTTTCCTATGATTGCATTGGGCGGCTGGAAGTTGGAACAGAGACAATCATCGACAAA
TCAAAGTCTGTGAAGACTAATTTGATGCAGCTGTTTGAAGAGTCTGGGAATACAGATATA
GAAGGAATCGACACAACTAATGCATGCTATGGAGGCACAGCTGCTGTCTTCAATGCTGTT
AACTGGATTGAGTCCAGCTCTTGGGATGGACGGTATGCCCTGGTAGTTGCAGGAGATATT
GCTGTATATGCCACAGGAAATGCTAGACCTACAGGTGGAGTTGGAGCAGTAGCTCTGCTA
ATTGGGCCAAATGCTCCTTTAATTTTTGAACGAGGGCTTCGTGGGACACATATGCAACAT
GCCTATGATTTTTACAAGCCTGATATGCTATCTGAATATCCTATAGTAGATGGAAAACTC
TCCATACAGTGCTACCTCAGTGCATTAGACCGCTGCTATTCTGTCTACTGCAAAAAGATC
CATGCCCAGTGGCAGAAAGAGGCAAATGATAACGATTTTACCTTGAATGATTTTGGCTTC
ATGATCTTTCACTCACCATATTGTAAACTGGTTCAGAAATCTCTAGCTCGGATGTTGCTG
AATGACTTCCTTAATGACCAGAATAGAGATAAAAATAGTATCTATAGTGGCCTGAAGGCC
TTTGGGGATGTTAAGTTAGAAGACACCTACTTTGATAGAGATGTGGAGAAGGCATTTATG
AAGGCTAGCTCTGAACTCTTCAGTCAGAAAACAAAGGCATCTTTACTTGTATCAAATCAA
AATGGAAATATGTACACATCTTCAGTATATGGTTCCCTTGCATCTGTTCTAGCACAGTAC
TCACCTCAGCATTTAGCAGGGAAGAGAATTGGAGTGTTTTCTTATGGTTCTGGTTTGGCT
GCCACTCTGTACTCTCTTAAAGTCACACAAGATGCTACACCGGGGTCTGCTCTTGATAAA
ATAACAGCAAGTTTATGTGATCTTAAATCAAGGCTTGATTCAAGAACTGGTGTGGCACAA
GATGTCTTCGCTGAAAACATGAAGCTCAGAGAGGACACCCATCATTTGGTCAACTATATT
CCCCAGGGTTCAATAGATTCACTCTTTGAAGGAACGTGGTACTTAGTTAGGGTGGATGAA
AAGCACAGAAGAACTTACGCTCGGCGTCCCACTCCAAATGATGACACTTTGGATGAAGGA
GTAGGACTTGTGCATTCAAACATAGCAACTGAGCATATTCCAAGCCCTGCCAAGAAAGTA
CCAAGACTCCCTGCTACAGCAGCAGAACCTGAAGCAGCAGTTATTAGTAATGGGGTATGG
TAA
|
| Enzyme 39 GenBank Gene ID |
X66435  |
| Enzyme 39 GeneCard ID |
HMGCS1  |
| Enzyme 39 GenAtlas ID |
HMGCS1  |
| Enzyme 39 HGNC ID |
HGNC:5007  |
| Enzyme 39 Chromosome Location |
5 |
| Enzyme 39 Locus |
5p14-p13 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Russ AP, Ruzicka V, Maerz W, Appelhans H, Gross W: Amplification and direct sequencing of a cDNA encoding human cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase. Biochim Biophys Acta. 1992 Oct 20;1132(3):329-31. [PubMed
]
- Rokosz LL, Boulton DA, Butkiewicz EA, Sanyal G, Cueto MA, Lachance PA, Hermes JD: Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes. Arch Biochem Biophys. 1994 Jul;312(1):1-13. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
5283 |
| Enzyme 40 Name |
Dihydrolipoyl dehydrogenase, mitochondrial |
| Enzyme 40 Synonyms |
- Dihydrolipoamide dehydrogenase
- Glycine cleavage system L protein
|
| Enzyme 40 Gene Name |
DLD |
| Enzyme 40 Protein Sequence |
>Dihydrolipoyl dehydrogenase, mitochondrial
MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF
|
| Enzyme 40 Number of Residues |
509 |
| Enzyme 40 Molecular Weight |
54176.9 |
| Enzyme 40 Theoretical pI |
7.95 |
| Enzyme 40 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- dihydrolipoyl dehydrogenase activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
- purine nucleoside binding
|
| Process |
- cell redox homeostasis
- cellular homeostasis
- cellular process
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 40 General Function |
Involved in oxidoreductase activity |
| Enzyme 40 Specific Function |
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction |
| Enzyme 40 Pathways |
|
| Enzyme 40 Reactions |
- protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ [RN:R08550]
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
91199540  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
P09622  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
DLDH_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1530 bp
ATGCAGAGCTGGAGTCGTGTGTACTGCTCCTTGGCCAAGAGAGGCCATTTCAATCGAATA
TCTCATGGCCTACAGGGACTTTCTGCAGTGCCTCTGAGAACTTACGCAGATCAGCCGATT
GATGCTGATGTAACAGTTATAGGTTCTGGTCCTGGAGGATATGTTGCTGCTATTAAAGCT
GCCCAGTTAGGCTTCAAGACAGTCTGCATTGAGAAAAATGAAACACTTGGTGGAACATGC
TTGAATGTTGGTTGTATTCCTTCTAAGGCTTTATTGAACAACTCTCATTATTACCATATG
GCCCATGGAAAAGATTTTGCATCTAGAGGAATTGAAATGTCCGAAGTTCGCTTGAATTTA
GACAAGATGATGGAGCAGAAGAGTACTGCAGTAAAAGCTTTAACAGGTGGAATTGCCCAC
TTATTCAAACAGAATAAGGTTGTTCATGTCAATGGATATGGAAAGATAACTGGCAAAAAT
CAAGTCACTGCTACGAAAGCTGATGGCGGCACTCAGGTTATTGATACAAAGAACATTCTT
ATAGCCACGGGTTCAGAAGTTACTCCTTTTCCTGGAATCACGATAGATGAAGATACAATA
GTGTCATCTACAGGTGCTTTATCTTTAAAAAAAGTTCCAGAAAAGATGGTTGTTATTGGT
GCAGGAGTAATAGGTGTAGAATTGGGTTCAGTTTGGCAAAGACTTGGTGCAGATGTGACA
GCAGTTGAATTTTTAGGTCATGTAGGTGGAGTTGGAATTGATATGGAGATATCTAAAAAC
TTTCAACGCATCCTTCAAAAACAGGGGTTTAAATTTAAATTGAATACAAAGGTTACTGGT
GCTACCAAGAAGTCAGATGGAAAAATTGATGTTTCTATTGAAGCTGCTTCTGGTGGTAAA
GCTGAAGTTATCACTTGTGATGTACTCTTGGTTTGCATTGGCCGACGACCCTTTACTAAG
AATTTGGGACTAGAAGAGCTGGGAATTGAACTAGATCCCAGAGGTAGAATTCCAGTCAAT
ACCAGATTTCAAACTAAAATTCCAAATATCTATGCCATTGGTGATGTAGTTGCTGGTCCA
ATGCTGGCTCACAAAGCAGAGGATGAAGGCATTATCTGTGTTGAAGGAATGGCTGGTGGT
GCTGTGCACATTGACTACAATTGTGTGCCATCAGTGATTTACACACACCCTGAAGTTGCT
TGGGTTGGCAAATCAGAAGAGCAGTTGAAAGAAGAGGGTATTGAGTACAAAGTTGGGAAA
TTCCCATTTGCTGCTAACAGCAGAGCTAAGACAAATGCTGACACAGATGGCATGGTGAAG
ATCCTTGGGCAGAAATCGACAGACAGAGTACTGGGAGCACATATTCTTGGACCAGGTGCT
GGAGAAATGGTAAATGAAGCTGCTCTTGCTTTGGAATATGGAGCATCCTGTGAAGATATA
GCTAGAGTCTGTCATGCACATCCGACCTTATCAGAAGCTTTTAGAGAAGCAAATCTTGCT
GCGTCATTTGGCAAATCAATCAACTTTTGA
|
| Enzyme 40 GenBank Gene ID |
NM_000108.3  |
| Enzyme 40 GeneCard ID |
DLD  |
| Enzyme 40 GenAtlas ID |
DLD  |
| Enzyme 40 HGNC ID |
HGNC:2898  |
| Enzyme 40 Chromosome Location |
7 |
| Enzyme 40 Locus |
7q31-q32 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Otulakowski G, Robinson BH: Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J Biol Chem. 1987 Dec 25;262(36):17313-8. [PubMed
]
- Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1422-6. [PubMed
]
- Feigenbaum AS, Robinson BH: The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Johanning GL, Morris JI, Madhusudhan KT, Samols D, Patel MS: Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10964-8. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. [PubMed
]
- Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS: How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J Biol Chem. 2006 Jan 6;281(1):648-55. Epub 2005 Nov 1. [PubMed
]
- Brautigam CA, Wynn RM, Chuang JL, Machius M, Tomchick DR, Chuang DT: Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure. 2006 Mar;14(3):611-21. Epub 2006 Jan 26. [PubMed
]
- Liu TC, Kim H, Arizmendi C, Kitano A, Patel MS: Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5186-90. [PubMed
]
- Hong YS, Kerr DS, Craigen WJ, Tan J, Pan Y, Lusk M, Patel MS: Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency. Hum Mol Genet. 1996 Dec;5(12):1925-30. [PubMed
]
- Shaag A, Saada A, Berger I, Mandel H, Joseph A, Feigenbaum A, Elpeleg ON: Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews. Am J Med Genet. 1999 Jan 15;82(2):177-82. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
5284 |
| Enzyme 41 Name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial |
| Enzyme 41 Synonyms |
- 70 kDa mitochondrial autoantigen of primary biliary cirrhosis
- PBC
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- M2 antigen complex 70 kDa subunit
- Pyruvate dehydrogenase complex component E2
- PDC-E2
- PDCE2
|
| Enzyme 41 Gene Name |
DLAT |
| Enzyme 41 Protein Sequence |
>Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCG
WTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKIN
EGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYT
LDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEK
KVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI
SAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPL
AKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVF
TDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFI
IKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAND
VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPA
DNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL
|
| Enzyme 41 Number of Residues |
647 |
| Enzyme 41 Molecular Weight |
68996.0 |
| Enzyme 41 Theoretical pI |
7.94 |
| Enzyme 41 GO Classification |
| Function |
- S-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- dihydrolipoyllysine-residue acetyltransferase activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
- pyruvate metabolic process
|
| Component |
- macromolecular complex
- protein complex
- pyruvate dehydrogenase complex
|
|
| Enzyme 41 General Function |
Involved in acyltransferase activity |
| Enzyme 41 Specific Function |
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 41 Pathways |
|
| Enzyme 41 Reactions |
- acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine [RN:R02569]
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
62898924  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
P10515  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
ODP2_HUMAN  |
| Enzyme 41 PDB ID |
1FYC  |
| Enzyme 41 PDB File |
Show |
| Enzyme 41 3D Structure |
|
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1944 bp
ATGTGGCGCGTCTGTGCGCGACGGGCTCAGAATGTAGCCCCATGGGCGGGACTCGAGGCT
CGGTGGACGGCCTTGCAGGAGGTACCCGGAACTCCACGAGTGACCTCGCGATCTGGCCCG
GCTCCCGTTCGTCGCAACAGCGTGACTACAGGGTATGGCGGGGTCCGGGCACTGTGCGGC
TGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGCTTACTGCTGCAGCTTTTGGGGTCG
CCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAGAAGGTTCCATTGCCTTCTCTTTCC
CCCACAATGCAGGCAGGCACCATAGCCCGTTGGGAAAAAAAAGAGGGAGACAAAATCAAT
GAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAAGCCACTGTTGGATTTGAGAGCCTG
GAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAAGGTACCAGGGATGTTCCCATCGGA
GCGATCATCTGTATCACAGTTGGCAAGCCTGAGGATATTGAGGCCTTTAAAAATTATACA
CTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCCCCAGCACCAACCCCTGCTGCCACT
GCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGTAGCTCATATCCCCCTCACATGCAG
GTACTTCTTCCTGCCCTCTCTCCCACCATGACCATGGGCACAGTTCAGAGATGGGAAAAA
AAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTGGCAGAGATAGAAACTGACAAAGCC
ACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTGGCAAAAATCCTGGTCCCTGAAGGC
ACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATCATTGTAGAAAAAGAGGCAGATATA
TCAGCATTTGCTGACTATAGGCCAACCGAAGTAACAGATTTAAAACCACAAGCGCCACCA
CCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACTCCCCAGCCTTTAGCTCCTACACCT
TCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAGGGAAGGGTGTTTGTTAGCCCTCTT
GCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTTACACAAGTAAAAGGGACAGGACCA
GATGGTAGAATCACCAAGAAGGATATCGACTCTTTTGTGCCTAGTAAAGTTGCTCCTGCT
CCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATGGCACCAGTTCCTACAGGTGTCTTC
ACAGATATCCCAATCAGCAACATTCGTCGGGTTATTGCACAGCGATTAATGCAATCAAAG
CAAACCATACCTCATTATTACCTTTCTATCAATGTAAATATGGGAGAAGTTTTGTTGGTA
CGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGCAAAATTTCTGTCAATGACTTCATC
ATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCCGAAGCAAATTCTTCTTGGATGGAC
ACAGTTATAAGACAAAATCATGTTGTTGATGTCAGTGTTGCGGTCAGTACTCCTGCAGGA
CTCATCACACCTATTGTGTTTAATGCACATATAAAAGGAGTGGAAACCATTGCTAATGAT
GTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAACTACAGCCACATGAATTCCAGGGT
GGCACTTTTACGATCTCCAATTTAGGAATGTTTGGAATTAAGAATTTCTCTGCTATTATT
AACCCACCTCAAGCATGTATTTTGGCAATTGGTGCTTCAGAGGATAAACTGGTCCCTGCA
GATAATGAAAAAGGGTTTGATGTGGCTAGCATGATGTCTGTTACACTCAGTTGTGATCAC
CGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTTGCTGAGTTTAGAAAGTACCTTGAA
AAACCTATCACTATGTTGTTGTAA
|
| Enzyme 41 GenBank Gene ID |
AK223596  |
| Enzyme 41 GeneCard ID |
DLAT  |
| Enzyme 41 GenAtlas ID |
DLAT  |
| Enzyme 41 HGNC ID |
HGNC:2896  |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
11q23.1 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Coppel RL, McNeilage LJ, Surh CD, Van de Water J, Spithill TW, Whittingham S, Gershwin ME: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7317-21. [PubMed
]
- Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 1988 Nov 21;240(1-2):45-8. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ: Three-dimensional structure of the major autoantigen in primary biliary cirrhosis. Gastroenterology. 1998 Jul;115(1):139-46. [PubMed
]
- Head RA, Brown RM, Zolkipli Z, Shahdadpuri R, King MD, Clayton PT, Brown GK: Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency. Ann Neurol. 2005 Aug;58(2):234-41. [PubMed
]
- Kato M, Chuang JL, Tso SC, Wynn RM, Chuang DT: Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex. EMBO J. 2005 May 18;24(10):1763-74. Epub 2005 Apr 28. [PubMed
]
- Devedjiev Y, Steussy CN, Vassylyev DG: Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications. J Mol Biol. 2007 Jul 13;370(3):407-16. Epub 2007 May 10. [PubMed
]
- Kato M, Li J, Chuang JL, Chuang DT: Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol. Structure. 2007 Aug;15(8):992-1004. Epub 2007 Aug 2. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
5334 |
| Enzyme 42 Name |
Long-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 42 Synonyms |
- LCAD
|
| Enzyme 42 Gene Name |
ACADL |
| Enzyme 42 Protein Sequence |
>Long-chain specific acyl-CoA dehydrogenase, mitochondrial
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
|
| Enzyme 42 Number of Residues |
430 |
| Enzyme 42 Molecular Weight |
47655.3 |
| Enzyme 42 Theoretical pI |
7.89 |
| Enzyme 42 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 42 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 42 Specific Function |
Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor |
| Enzyme 42 Pathways |
|
| Enzyme 42 Reactions |
- acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
177962  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
P28330  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
ACADL_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1293 bp
ATGGCCGCACGCCTTCTCCGAGGGTCCCTACGCGTCCTGGGCGGCCACCGTGCGCCGCGC
CAGCTGCCCGCCGCGCGATGTTCTCATTCCGGAGGGGAAGAACGTCTAGAAACTCCTTCT
GCTAAAAAATTAACAGATATAGGAATTCGAAGAATCTTTTCTCCAGAGCATGACATTTTC
CGGAAAAGTGTAAGGAAGTTTTTCCAAGAAGAAGTGATTCCTCATCACTCAGAATGGGAG
AAAGCTGGAGAAGTAAGTAGGGAGGTTTGGGAAAAAGCTGGAAAACAAGGACTGCTTGGT
GTCAATATTGCAGAGCATCTTGGTGGAATTGGAGGGGATCTGTACTCCGCAGCTATTGTC
TGGGAGGAGCAAGCTTATTCAAATTGTTCAGGCCCAGGTTTTAGTATTCATTCAGGTATT
GTCATGTCCTATATTACAAACCATGGCTCAGAAGAACAGATTAAGCACTTTATTCCCCAG
ATGACTGCAGGCAAATGTATTGGTGCAATAGCAATGACAGAGCCTGGAGCTGGAAGTGAC
TTACAGGGAATAAAAACAAATGCTAAAAAGGATGGAAGTGACTGGATTCTCAATGGAAGC
AAGGTGTTCATCAGTAATGGGTCATTAAGTGATGTTGTGATTGTAGTTGCGGTCACAAAT
CATGAAGCTCCCTCCCCTGCCCATGGTATTAGCCTTTTTCTGGTGGAAAATGGAATGAAA
GGATTTATCAAGGGACGAAAGCTACATAAAATGGGATTAAAAGCCCAGGATACCGCAGAA
CTATTCTTTGAAGATATACGGTTGCCAGCTAGTGCCCTACTTGGAGAAGAGAATAAAGGC
TTCTATTACATCATGAAAGAGCTTCCACAGGAAAGGCTGTTAATTGCTGATGTGGCAATT
TCAGCTAGTGAATTCATGTTTGAAGAAACCAGGAACTATGTTAAACAAAGAAAAGCTTTT
GGCAAAACAGTTGCTCACCTACAGACAGTGCAACATAAATTAGCAGAATTAAAAACACAT
ATATGTGTAACCCGAGCATTTGTGGACAACTGTCTCCAGCTGCATGAAGCGAAACGTTTG
GACTCCGCCACTGCTTGCATGGCGAAATATTGGGCATCTGAGTTACAAAATAGTGTAGCT
TACGACTGTGTACAGCTCCATGGAGGTTGGGGATACATGTGGGAGTACCCAATTGCAAAA
GCTTATGTGGATGCCAGAGTTCAGCCAATCTATGGTGGTACAAATGAAATAATGAAGGAG
CTGATTGCAAGAGAGATTGTCTTTGACAAGTAG
|
| Enzyme 42 GenBank Gene ID |
M74096  |
| Enzyme 42 GeneCard ID |
ACADL  |
| Enzyme 42 GenAtlas ID |
ACADL  |
| Enzyme 42 HGNC ID |
HGNC:88  |
| Enzyme 42 Chromosome Location |
2 |
| Enzyme 42 Locus |
2q34-q35 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1991 Nov;11(3):609-20. [PubMed
]
- Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1992 Mar;12(3):626. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
5335 |
| Enzyme 43 Name |
Short-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 43 Synonyms |
- SCAD
- Butyryl-CoA dehydrogenase
|
| Enzyme 43 Gene Name |
ACADS |
| Enzyme 43 Protein Sequence |
>Short-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQV
DKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN
SLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLN
GTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTAN
LIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF
GAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
|
| Enzyme 43 Number of Residues |
412 |
| Enzyme 43 Molecular Weight |
44296.7 |
| Enzyme 43 Theoretical pI |
8.12 |
| Enzyme 43 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 43 Specific Function |
Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor |
| Enzyme 43 Pathways |
- Butyrate Metabolism (map00650
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 43 Reactions |
- butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor [RN:R01178]
|
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
337928  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P16219  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
ACADS_HUMAN  |
| Enzyme 43 PDB ID |
1JQI  |
| Enzyme 43 PDB File |
Show |
| Enzyme 43 3D Structure |
|
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1239 bp
ATGGCCGCCGCGCTGCTCGCCCGGGCCTCGGGCCCTGCCCGCAGAGCTCTCTGTCCTAGG
GCCTGGCGGCAGTTACACACCATCTACCAGTCTGTGGAACTGCCCGAGACACACCAGATG
TTGCTCCAGACATGCCGGGACTTTGCCGAGAAGGAGTTGTTTCCCATTGCAGCCCAGGTG
GATAAGGAACATCTCTTCCCAGCGGCTCAGGTGAAGAAGATGGGCGGGCTTGGGCTTCTG
GCCATGGACGTGCCCGAGGAGCTTGGCGGTGCTGGCCTCGATTACCTGGCCTACGCCATC
GCCATGGAGGAGATCAGCCGTGGCTGCGCCTCCACCGGAGTCATCATGAGTGTCAACAAC
TCTCTCTACCTGGGGCCCATCTTGAAGTTTGGCTCCAAGGAGCAGAAGCAGGCGTGGGTC
ACGCCTTTCACCAGTGGTGACAAAATTGGCTGCTTTGCCCTCAGCGAACCAGGGAACGGC
AGTGATGCAGGAGCTGCGTCCACCACCGCCCGGGCCGAGGGCGACTCATGGGTTCTGAAT
GGAACCAAAGCCTGGATCACCAATGCCTGGGAGGCTTCGGCTGCCGTGGTCTTTGCCAGC
ACGGACAGAGCCCTGCAAAACAAGGGCATCAGTGCCTTCCTGGTCCCCATGCCAACGCCT
GGGCTCACGTTGGGGAAGAAAGAAGACAAGCTGGGCATCCGGGGCTCATCCACGGCCAAC
CTCATCTTTGAGGACTGTCGCATCCCCAAGGACAGCATCCTGGGGGAGCCAGGGATGGGC
TTCAAGATAGCCATGCAAACCCTGGACATGGGCCGCATCGGCATCGCCTCCCAGGCCCTG
GGCATTGCCCAGACCGCCCTCGATTGTGCTGTGAACTACGCTGAGAATCGCATGGCCTTC
GGGGCGCCCCTCACCAAGCTCCAGGTCATCCAGTTCAAGTTGGCAGACATGGCCCTGGCC
CTGGAGAGTGCCCGGCTGCTGACCTGGCGCGCTGCCATGCTGAAGGATAACAAGAAGCCT
TTCATCAAGGAGGCAGCCATGGCCAAGCTGGCCGCCTCGGAGGCCGCGACCGCCATCAGC
CACCAGGCCATCCAGATCCTGGGCGGCATGGGCTACGTGACAGAGATGCCGGCAGAGCGG
CACTACCGCGACGCCCGCATCACTGAGATCTACGAGGGCACCAGCGAAATCCAGCGGCTG
GTGATCGCCGGGCATCTGCTCAGGAGCTACCGGAGCTGA
|
| Enzyme 43 GenBank Gene ID |
M26393  |
| Enzyme 43 GeneCard ID |
ACADS  |
| Enzyme 43 GenAtlas ID |
ACADS  |
| Enzyme 43 HGNC ID |
HGNC:90  |
| Enzyme 43 Chromosome Location |
1 |
| Enzyme 43 Locus |
12q22-qter |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Naito E, Ozasa H, Ikeda Y, Tanaka K: Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1989 May;83(5):1605-13. [PubMed
]
- Corydon MJ, Andresen BS, Bross P, Kjeldsen M, Andreasen PH, Eiberg H, Kolvraa S, Gregersen N: Structural organization of the human short-chain acyl-CoA dehydrogenase gene. Mamm Genome. 1997 Dec;8(12):922-6. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed
]
- Naito E, Indo Y, Tanaka K: Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1990 May;85(5):1575-82. [PubMed
]
- Gregersen N, Winter VS, Corydon MJ, Corydon TJ, Rinaldo P, Ribes A, Martinez G, Bennett MJ, Vianey-Saban C, Bhala A, Hale DE, Lehnert W, Kmoch S, Roig M, Riudor E, Eiberg H, Andresen BS, Bross P, Bolund LA, Kolvraa S: Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet. 1998 Apr;7(4):619-27. [PubMed
]
- Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N: Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
5336 |
| Enzyme 44 Name |
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 44 Synonyms |
- MCAD
|
| Enzyme 44 Gene Name |
ACADM |
| Enzyme 44 Protein Sequence |
>Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEI
IPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ
TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNM
GQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEAT
KYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF
AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK
N
|
| Enzyme 44 Number of Residues |
421 |
| Enzyme 44 Molecular Weight |
46588.0 |
| Enzyme 44 Theoretical pI |
8.51 |
| Enzyme 44 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 44 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 44 Specific Function |
This enzyme is specific for acyl chain lengths of 4 to 16 |
| Enzyme 44 Pathways |
|
| Enzyme 44 Reactions |
- acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
177964  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P11310  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
ACADM_HUMAN  |
| Enzyme 44 PDB ID |
1T9G  |
| Enzyme 44 PDB File |
Show |
| Enzyme 44 3D Structure |
|
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1266 bp
ATGGCAGCGGGGTTCGGGCGATGCTGCAGGGTCCTGAGAAGTATTTCTCGTTTTCATTGG
AGATCACAGCATACAAAAGCCAATCGACAACGTGAACCAGGATTAGGATTTAGTTTTGAG
TTCACCGAACAGCAGAAAGAATTTCAAGCTACTGCTCGTAAATTTGCCAGAGAGGAAATC
ATCCCAGTGGCTGCAGAATATGATAAAACTGGTGAATATCCAGTCCCCCTAATTAGAAGA
GCCTGGGAACTTGGTTTAATGAACACACACATTCCAGAGAACTGTGGAGGTCTTGGACTT
GGAACTTTTGATGCTTGTTTAATTAGTGAAGAATTGGCTTATGGATGTACAGGGGTTCAG
ACTGCTATTGAAGGAAATTCTTTGGGGCAAATGCCTATTATTATTGCTGGAAATGATCAA
CAAAAGAAGAAGTATTTGGGGAGAATGACTGAGGAGCCATTGATGTGTGCTTATTGTGTA
ACAGAACCTGGAGCAGGCTCTGATGTAGCTGGTATAAAGACCAAAGCAGAAAAGAAAGGA
GATGAGTATATTATTAATGGTCAGAAGATGTGGATAACCAACGGAGGAAAAGCTAATTGG
TATTTTTTATTGGCACGTTCTGATCCAGATCCTAAAGCTCCTGCTAATAAAGCCTTTACT
GGATTCATTGTGGAAGCAGATACCCCAGGAATTCAGATTGGGAGAAAGGAATTAAACATG
GGCCAGCGATGTTCAGATACTAGAGGAATTGTCTTCGAAGATGTGAAAGTGCCTAAAGAA
AATGTTTTAATTGGTGACGGAGCTGGTTTCAAAGTTGCAATGGGAGCTTTTGATAAAACC
AGACCTGTAGTAGCTGCTGGTGCTGTTGGATTAGCACAAAGAGCTTTGGATGAAGCTACC
AAGTATGCCCTGGAAAGGAAAACTTTCGGAAAGCTACTTGTAGAGCACCAAGCAATATCA
TTTATGCTGGCTGAAATGGCAATGAAAGTTGAACTAGCTAGAATGAGTTACCAGAGAGCA
GCTTGGGAGGTTGATTCTGGTCGTCGAAATACCTATTATGCTTCTATTGCAAAGGCATTT
GCTGGAGATATTGCAAATCAGTTAGCTACTGATGCTGTGCAGATACTTGGAGGCAATGGA
TTTAATACAGAATATCCTGTAGAAAAACTAATGAGGGATGCCAAAATCTATCAGATTTAT
GAAGGTACTTCACAAATTCAAAGACTTATTGTAGCCCGTGAACACATTGACAAGTACAAA
AATTAA
|
| Enzyme 44 GenBank Gene ID |
M16827  |
| Enzyme 44 GeneCard ID |
ACADM  |
| Enzyme 44 GenAtlas ID |
ACADM  |
| Enzyme 44 HGNC ID |
HGNC:89  |
| Enzyme 44 Chromosome Location |
1 |
| Enzyme 44 Locus |
1p31 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- Kelly DP, Kim JJ, Billadello JJ, Hainline BE, Chu TW, Strauss AW: Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4068-72. [PubMed
]
- Zhang ZF, Kelly DP, Kim JJ, Zhou YQ, Ogden ML, Whelan AJ, Strauss AW: Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene. Biochemistry. 1992 Jan 14;31(1):81-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR: Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. [PubMed
]
- Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D: Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J Biol Chem. 2004 Jul 30;279(31):32904-12. Epub 2004 May 24. [PubMed
]
- Toogood HS, van Thiel A, Scrutton NS, Leys D: Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. [PubMed
]
- Tanaka K, Yokota I, Coates PM, Strauss AW, Kelly DP, Zhang Z, Gregersen N, Andresen BS, Matsubara Y, Curtis D, et al.: Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. Hum Mutat. 1992;1(4):271-9. [PubMed
]
- Yokota I, Indo Y, Coates PM, Tanaka K: Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. [PubMed
]
- Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW: Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. [PubMed
]
- Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K: Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. [PubMed
]
- Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.: Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. [PubMed
]
- Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D: Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. [PubMed
]
- Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.: Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. [PubMed
]
- Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW: Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. [PubMed
]
- Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW: A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. [PubMed
]
- Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N: The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. [PubMed
]
- Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S: Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. [PubMed
]
- Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR: Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. [PubMed
]
- Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N: Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. [PubMed
]
- Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E: Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. [PubMed
]
- Albers S, Levy HL, Irons M, Strauss AW, Marsden D: Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
5378 |
| Enzyme 45 Name |
Peroxisomal acyl-coenzyme A oxidase 1 |
| Enzyme 45 Synonyms |
- AOX
- Palmitoyl-CoA oxidase
- Straight-chain acyl-CoA oxidase
- SCOX
|
| Enzyme 45 Gene Name |
ACOX1 |
| Enzyme 45 Protein Sequence |
>Peroxisomal acyl-coenzyme A oxidase 1
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
|
| Enzyme 45 Number of Residues |
660 |
| Enzyme 45 Molecular Weight |
74423.0 |
| Enzyme 45 Theoretical pI |
8.29 |
| Enzyme 45 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 45 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 45 Specific Function |
Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs |
| Enzyme 45 Pathways |
|
| Enzyme 45 Reactions |
- acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
|
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
14250616  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
Q15067  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
ACOX1_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1983 bp
ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACCCGGCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAATTTTGTGCACCGAGGGCGGCCTGAGCCTCTG
GATCTTCACTTGGGCATGTTCCTGCCCACCTTGCTTCACCAGGCAACTGCGGAGCAGCAG
GAGCGCTTCTTCATGCCCGCCTGGAACTTGGAGATCATTGGCACTTATGCCCAGACAGAG
ATGGGTCATGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGGAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAATCGGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGCACATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATGAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTGCCACTATGTGGTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA
|
| Enzyme 45 GenBank Gene ID |
BC008767  |
| Enzyme 45 GeneCard ID |
ACOX1  |
| Enzyme 45 GenAtlas ID |
ACOX1  |
| Enzyme 45 HGNC ID |
HGNC:119  |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
17q24-q25|17q25.1 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed
]
- Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed
]
- Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed
]
- Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Suzuki Y, Iai M, Kamei A, Tanabe Y, Chida S, Yamaguchi S, Zhang Z, Takemoto Y, Shimozawa N, Kondo N: Peroxisomal acyl CoA oxidase deficiency. J Pediatr. 2002 Jan;140(1):128-30. [PubMed
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
5396 |
| Enzyme 46 Name |
Peroxisomal acyl-coenzyme A oxidase 2 |
| Enzyme 46 Synonyms |
- 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase
- 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase
- Trihydroxycoprostanoyl-CoA oxidase
- THCA-CoA oxidase
- THCCox
|
| Enzyme 46 Gene Name |
ACOX2 |
| Enzyme 46 Protein Sequence |
>Peroxisomal acyl-coenzyme A oxidase 2
MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSY
PEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHR
VFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVI
HSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGD
IGPKMDFDQTDNGFLQLNHVRVPRENMLSRFAQVLPDGTYVKLGTAQSNYLPMVVVRVEL
LSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFL
AVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKL
SGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAP
DLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHL
QAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGA
QVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNT
QENPAYEEYIRPLLQSWRSKL
|
| Enzyme 46 Number of Residues |
681 |
| Enzyme 46 Molecular Weight |
76826.1 |
| Enzyme 46 Theoretical pI |
7.59 |
| Enzyme 46 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 46 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 46 Specific Function |
Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
- (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor [RN:R07374]
|
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
1780991  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q99424  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
ACOX2_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>2046 bp
ATGGGCAGCCCAGTGCACCGAGTGTCATTGGGGGATACCTGGAGCAGGCAAATGCACCCC
GACATAGAGAGCGAGAGGTATATGCAGTCCTTTGACGTGGAACGGCTCACCAACATCCTT
GATGGAGGTGCCCAGAACACTGCACTCCGCAGGAAAGTTGAGAGCATCATCCACAGTTAC
CCGGAGTTTAGCTGTAAGGACAATTATTTCATGACCCAGAATGAGCGTTATAAGGCTGCC
ATGCGGAGGGCATTCCACATCCGGTTGATAGCTCGGCGCCTGGGTTGGTTAGAAGATGGT
CGTGAATTAGGCTACGCTTACAGAGCCCTTTCTGGAGACGTGGCCTTAAATATACACAGA
GTCTTCGTGAGAGCCCTCAGGAGCCTGGGCTCAGAGGAGCAGATTGCCAAATGGGACCCA
CTCTGCAAAAACATCCAGATCATCGCAACGTATGCACAGACAGAGTTGGGACATGGGACA
TATCTTCAGGGCCTGGAGACTGAAGCCACCTATGACGCAGCCACCCAGGAGTTTGTGATA
CACAGCCCCACGCTGACTGCCACCAAATGGTGGCCTGGAGACTTGGGACGGTCAGCCACC
CATGCCCTGGTCCAGGCCCAGCTGATCTGCTCAGGAGCCAGGCGGGGCATGCACGCTTTT
ATTGTGCCAATCCGGAGTCTTCAGGACCACACCCCACTGCCAGGAATCATCATTGGGGAC
ATCGGACCCAAGATGGACTTTGATCAAACAGACAATGGCTTCCTGCAGCTGAACCATGTG
CGGGTCCCCAGGGAGAACATGCTGAGTCGCTTTGCACAGGTCTTGCCAGATGGCACCTAC
GTCAAACTCGGTACAGCACAGAGCAACTACCTTCCCATGGTGGTGGTGCGGGTGGAGCTG
CTGTCAGGGGAGATCCTCCCTATACTGCAGAAGGCCTGTGTCATCGCCATGCGCTACTCG
GTCATCCGCCGCCAATCCCGGCTCCGGCCCAGTGACCCAGAGGCAAAGGTCCTGGACTAC
CAGACACAACAGCAGAAACTCTTTCCTCAGCTGGCCATCAGTTATGCCTTCCATTTCCTG
GCAGTCAGCCTCTTGGAGTTCTTCCAGCACTCCTACACTGCCATTCTGAACCAAGACTTC
AGCTTCCTGCCTGAGCTCCACGCGCTGAGCACGGGCATGAAGGCCATGATGTCAGAATTC
TGCACCCAGGGAGCTGAGATGTGCCGCAGGGCCTGTGGCGGACATGGCTACTCAAAGCTG
AGTGGCCTGCCATCACTGGTCACCAAATTGTCGGCCTCCTGCACCTACGAGGGTGAGAAC
ACAGTGCTCTACCTGCAGGTGGCCAGGTTCCTGGTGAAGAGCTACCTGCAGACTCAGATG
TCCCCTGGCTCCACGCCACAGAGATCTCTCTCTCCATCTGTCGCATATCTCACCGCACCT
GACCTGGCCAGGTGTCCAGCCCAGAGGGCAGCCGACTTCCTCTGCCCGGAGCTCTACACC
ACGGCCTGGGCACATGTGGCAGTAAGGCTCATAAAGGACTCAGTGCAGCATTTACAGACC
CTGACGCAATCCGGAGCTGACCAGCACGAGGCTTGGAACCAGACCACTGTCATACACCTC
CAGGCTGCTAAGGTGCACTGCTACTATGTCACTGTGAAGGGTTTTACAGAAGCTCTGGAG
AAACTAGAAAATGAACCAGCGATTCAGCAGGTGCTCAAGCGCCTCTGTGACCTCCATGCC
ATACATGGAATCTTGACTAACTCGGGTGACTTTCTCCATGACGCCTTCCTGTCTGGTGCC
CAAGTGGACATGGCAAGAACAGCCTACCTGGACCTGCTCCGCCTGATCCGGAAGGATGCC
ATCCTGTTAACTGATGCTTTTGACTTCACCGATCAGTGTTTAAATTCAGCCCTTGGCTGT
TATGATGGAAACGTCTACGAACGCCTGTTCCAGTGGGCTCAGAAGTCACCAACCAATACT
CAGGAGAACCCTGCCTATGAGGAATATATAAGACCACTTTTACAAAGTTGGAGATCCAAG
CTATGA
|
| Enzyme 46 GenBank Gene ID |
X95190  |
| Enzyme 46 GeneCard ID |
ACOX2  |
| Enzyme 46 GenAtlas ID |
ACOX2  |
| Enzyme 46 HGNC ID |
HGNC:120  |
| Enzyme 46 Chromosome Location |
3 |
| Enzyme 46 Locus |
3p14.3 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Baumgart E, Vanhooren JC, Fransen M, Marynen P, Puype M, Vandekerckhove J, Leunissen JA, Fahimi HD, Mannaerts GP, van Veldhoven PP: Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13748-53. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
5398 |
| Enzyme 47 Name |
Isovaleryl-CoA dehydrogenase, mitochondrial |
| Enzyme 47 Synonyms |
- IVD
|
| Enzyme 47 Gene Name |
IVD |
| Enzyme 47 Protein Sequence |
>Isovaleryl-CoA dehydrogenase, mitochondrial
MATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEH
LAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG
AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA
EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKL
DKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLD
HTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGV
ILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA
DFH
|
| Enzyme 47 Number of Residues |
423 |
| Enzyme 47 Molecular Weight |
46319.0 |
| Enzyme 47 Theoretical pI |
8.31 |
| Enzyme 47 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 47 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 47 Specific Function |
3-methylbutanoyl-CoA + acceptor = 3-methylbut- 2-enoyl-CoA + reduced acceptor |
| Enzyme 47 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 47 Reactions |
- 3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor [RN:R04096]
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
306897  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P26440  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
IVD_HUMAN  |
| Enzyme 47 PDB ID |
1IVH  |
| Enzyme 47 PDB File |
Show |
| Enzyme 47 3D Structure |
|
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>1272 bp
ATGGCGACTGCGACTCGGCTGCTGGGGTGGCGTGTGGCGAGCTGGAGGCTGCGGCCGCCG
CTTGCCGGCTTCGTTTCCCAGCGGGCCCACTCGCTTTTGCCCGTGGACGATGCAATCAAT
GGGCTAAGCGAGGAGCAGAGGCAGCTTCGTCAGACCATGGCTAAGTTCCTTCAGGAGCAC
CTGGCCCCCAAGGCCCAGGAGATCGATCGCAGCAATGAGTTCAAGAACCTGCGAGAATTT
TGGAAGCAGCTGGGGAACCTGGGCGTATTGGGCATCACAGCCCCTGTTCAGTATGGCGGC
TCCGGCCTGGGCTACCTGGAGCATGTGCTGGTGATGGAGGAGATATCCCGAGCTTCCGGA
GCAGTGGGGCTCAGTTACGGTGCCCACTCCAACCTCTGCATCAACCAGCTTGTACGCAAT
GGGAATGAGGCCCAGAAAGAGAAGTATCTCCCGAAGCTGATCAGTGGTGAGTACATCGGA
GCCCTGGCCATGAGTGAGCCCAATGCAGGCTCTGATGTTGTCTCTATGAAGCTCAAAGCG
GAAAAGAAAGGAAATCACTACATCCTGAATGGCAACAAGTTCTGGATCACTAATGGCCCT
GATGCTGACGTCCTGATTGTCTATGCCAAGACAGATCTGGCTGCTGTGCCAGCTTCTCGG
GGCATCACAGCCTTCATTGTGGAGAAGGGTATGCCTGGCTTTAGCACCTCTAAGAAGCTG
GACAAGCTGGGGATGAGGGGCTCTAACACCTGTGAGCTAATCTTTGAAGACTGCAAGATT
CCTGCTGCCAACATCCTGGGCCATGAGAATAAGGGTGTCTACGTGCTGATGAGTGGGCTG
GACCTGGAGCGGCTGGTGCTGGCCGGGGGGCCTCTTGGGCTCATGCAAGCGGTCCTGGAC
CACACCATTCCCTACCTGCACGTGAGGGAAGCCTTTGGCCAGAAGATCGGCCACTTCCAG
TTGATGCAGGGGAAGATGGCTGACATGTACACCCGCCTCATGGCGTGTCGGCAGTATGTC
TACAATGTCGCCAAGGCCTGCGATGAGGGCCATTGCACTGCTAAGGACTGTGCAGGTGTG
ATTCTTTACTCAGCTGAGTGTGCTACACAGGTAGCCCTGGACGGCATTCAGTGTTTTGGT
GGCAATGGCTACATCAATGACTTTCCCATGGGCCGCTTTCTTCGAGATGCCAAGCTGTAT
GAGATAGGGGCTGGGACCAGCGAGGTGAGGCGGCTGGTCATCGGCAGAGCCTTCAATGCA
GACTTTCACTAG
|
| Enzyme 47 GenBank Gene ID |
M34192  |
| Enzyme 47 GeneCard ID |
IVD  |
| Enzyme 47 GenAtlas ID |
IVD  |
| Enzyme 47 HGNC ID |
HGNC:6186  |
| Enzyme 47 Chromosome Location |
1 |
| Enzyme 47 Locus |
15q14-q15 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
- Matsubara Y, Ito M, Glassberg R, Satyabhama S, Ikeda Y, Tanaka K: Nucleotide sequence of messenger RNA encoding human isovaleryl-coenzyme A dehydrogenase and its expression in isovaleric acidemia fibroblasts. J Clin Invest. 1990 Apr;85(4):1058-64. [PubMed
]
- Vockley J, Rogan PK, Anderson BD, Willard J, Seelan RS, Smith DI, Liu W: Exon skipping in IVD RNA processing in isovaleric acidemia caused by point mutations in the coding region of the IVD gene. Am J Hum Genet. 2000 Feb;66(2):356-67. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Parimoo B, Tanaka K: Structural organization of the human isovaleryl-CoA dehydrogenase gene. Genomics. 1993 Mar;15(3):582-90. [PubMed
]
- Vockley J, Nagao M, Parimoo B, Tanaka K: The variant human isovaleryl-CoA dehydrogenase gene responsible for type II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire second coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors. J Biol Chem. 1992 Feb 5;267(4):2494-501. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Mohsen AW, Vockley J: Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase. Biochemistry. 1995 Aug 15;34(32):10146-52. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Tiffany KA, Roberts DL, Wang M, Paschke R, Mohsen AW, Vockley J, Kim JJ: Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,. Biochemistry. 1997 Jul 15;36(28):8455-64. [PubMed
]
- Vockley J, Parimoo B, Tanaka K: Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia. Am J Hum Genet. 1991 Jul;49(1):147-57. [PubMed
]
- Mohsen AW, Anderson BD, Volchenboum SL, Battaile KP, Tiffany K, Roberts D, Kim JJ, Vockley J: Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia. Biochemistry. 1998 Jul 14;37(28):10325-35. [PubMed
]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
5424 |
| Enzyme 48 Name |
Peroxisomal acyl-coenzyme A oxidase 3 |
| Enzyme 48 Synonyms |
- Branched-chain acyl-CoA oxidase
- BRCACox
- Pristanoyl-CoA oxidase
|
| Enzyme 48 Gene Name |
ACOX3 |
| Enzyme 48 Protein Sequence |
>Peroxisomal acyl-coenzyme A oxidase 3
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
|
| Enzyme 48 Number of Residues |
700 |
| Enzyme 48 Molecular Weight |
77628.3 |
| Enzyme 48 Theoretical pI |
7.27 |
| Enzyme 48 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 48 General Function |
Involved in oxidoreductase activity, acting on the CH-CH group of donors |
| Enzyme 48 Specific Function |
Oxidizes the CoA-esters of 2-methyl-branched fatty acids |
| Enzyme 48 Pathways |
|
| Enzyme 48 Reactions |
- acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
2326549  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
O15254  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
ACOX3_HUMAN  |
| Enzyme 48 PDB ID |
Not Available |
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>2103 bp
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG
|
| Enzyme 48 GenBank Gene ID |
Y11411  |
| Enzyme 48 GeneCard ID |
ACOX3  |
| Enzyme 48 GenAtlas ID |
ACOX3  |
| Enzyme 48 HGNC ID |
HGNC:121  |
| Enzyme 48 Chromosome Location |
4 |
| Enzyme 48 Locus |
4p15.3 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
5434 |
| Enzyme 49 Name |
Glutaryl-CoA dehydrogenase, mitochondrial |
| Enzyme 49 Synonyms |
- GCD
|
| Enzyme 49 Gene Name |
GCDH |
| Enzyme 49 Protein Sequence |
>Glutaryl-CoA dehydrogenase, mitochondrial
MALRGVSVRLLSRGPGLHVLRTWVSSAAQTEKGGRTQSQLAKSSRPEFDWQDPLVLEEQL
TTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSS
VAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLT
EPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEK
GMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWG
VLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQD
KAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIH
ALILGRAITGIQAFTASK
|
| Enzyme 49 Number of Residues |
438 |
| Enzyme 49 Molecular Weight |
48126.7 |
| Enzyme 49 Theoretical pI |
8.15 |
| Enzyme 49 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 49 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 49 Specific Function |
Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive |
| Enzyme 49 Pathways |
|
| Enzyme 49 Reactions |
- glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor [RN:R02488]
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
Not Available |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q92947  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
GCDH_HUMAN  |
| Enzyme 49 PDB ID |
1SIR  |
| Enzyme 49 PDB File |
Show |
| Enzyme 49 3D Structure |
|
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>1317 bp
ATGGCCCTGAGAGGCGTCTCCGTGCGGCTGCTGAGCCGCGGACCCGGCCTGCACGTCCTT
CGCACGTGGGTCTCGTCGGCGGCGCAGACCGAGAAAGGCGGGAGAACACAGAGCCAACTG
GCTAAGTCCTCGCGTCCCGAGTTTGACTGGCAGGACCCGCTGGTGCTGGAGGAGCAGCTG
ACCACAGATGAGATCCTCATCAGGGACACCTTCCGCACCTACTGCCAGGAGAGACTCATG
CCTCGCATCCTGTTGGCCAATCGCAACGAAGTTTTTCATCGGGAGATCATTTCGGAGATG
GGGGAGTTGGGTGTGCTGGGCCCCACCATCAAAGGATATGGCTGTGCTGGGGTTTCGTCT
GTGGCCTATGGGCTCCTGGCCCGAGAGCTGGAGCGGGTGGACAGTGGCTACAGGTCGGCG
ATGAGTGTCCAGTCCTCCCTCGTCATGCACCCTATCTATGCCTATGGCAGCGAGGAACAG
CGGCAGAAGTACCTGCCCCAGCTGGCCAAGGGGGAGCTCCTGGGCTGCTTCGGGCTCACA
GAGCCCAACAGCGGAAGTGACCCCAGCAGCATGGAGACCAGAGCCCACTACAACTCATCC
AACAAGAGCTACACCCTCAATGGGACCAAGACCTGGATCACGAACTCGCCTATGGCCGAT
CTGTTTGTAGTGTGGGCTCGGTGTGAAGATGGCTGCATTCGGGGCTTCCTGCTGGAGAAG
GGGATGCGGGGTCTCTCGGCCCCCAGGATCCAGGGCAAGTTCTCGCTGCGGGCCTCAGCC
ACAGGCATGATCATCATGGACGGTGTGGAGGTGCCAGAGGAGAATGTGCTCCCTGGTGCA
TCCAGCCTGGGGGGTCCCTTCGGCTGCCTGAACAACGCCCGGTACGGCATCGCGTGGGGC
GTGCTTGGAGCTTCGGAGTTCTGCTTGCACACAGCCCGGCAGTACGCCCTCGACAGGATG
CAGTTTGGTGTCCCACTGGCCAGGAACCAGCTGATTCAGAAGAAGCTGGCAGACATGCTC
ACTGAGATTACCCTGGGCCTTCACGCCTGCCTGCAGCTCGGCCGCTTGAAGGACCAGGAC
AAGGCTGCCCCCGAGATGGTTTCTCTGCTGAAGAGGAATAACTGTGGGAAAGCCCTGGAC
ATCGCCCGCCAGGCCCGAGACATGCTGGGGGGGAATGGGATTTCTGACGAGTATCACGTG
ATCCGGCACGCCATGAACCTGGAGGCCGTGAACACCTACGAAGGTACACATGACATTCAC
GCCCTGATCCTTGGGAGAGCTATCACGGGAATCCAGGCGTTCACGGCCAGCAAGTGA
|
| Enzyme 49 GenBank Gene ID |
U69141  |
| Enzyme 49 GeneCard ID |
GCDH  |
| Enzyme 49 GenAtlas ID |
GCDH  |
| Enzyme 49 HGNC ID |
HGNC:4189  |
| Enzyme 49 Chromosome Location |
1 |
| Enzyme 49 Locus |
19p13.2 |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 General References |
- Goodman SI, Kratz LE, Frerman FE: Pork and human cDNAs encoding glutaryl-CoA dehydrogenase. Prog Clin Biol Res. 1992;375:169-73. [PubMed
]
- Goodman SI, Kratz LE, DiGiulio KA, Biery BJ, Goodman KE, Isaya G, Frerman FE: Cloning of glutaryl-CoA dehydrogenase cDNA, and expression of wild type and mutant enzymes in Escherichia coli. Hum Mol Genet. 1995 Sep;4(9):1493-8. [PubMed
]
- Schwartz M, Christensen E, Superti-Furga A, Brandt NJ: The human glutaryl-CoA dehydrogenase gene: report of intronic sequences and of 13 novel mutations causing glutaric aciduria type I. Hum Genet. 1998 Apr;102(4):452-8. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Goodman SI, Stein DE, Schlesinger S, Christensen E, Schwartz M, Greenberg CR, Elpeleg ON: Glutaryl-CoA dehydrogenase mutations in glutaric acidemia (type I): review and report of thirty novel mutations. Hum Mutat. 1998;12(3):141-4. [PubMed
]
- Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ: Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry. 2004 Aug 3;43(30):9674-84. [PubMed
]
- Rao KS, Fu Z, Albro M, Narayanan B, Baddam S, Lee HJ, Kim JJ, Frerman FE: The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate. Biochemistry. 2007 Dec 18;46(50):14468-77. Epub 2007 Nov 17. [PubMed
]
- Biery BJ, Stein DE, Morton DH, Goodman SI: Gene structure and mutations of glutaryl-coenzyme A dehydrogenase: impaired association of enzyme subunits that is due to an A421V substitution causes glutaric acidemia type I in the Amish. Am J Hum Genet. 1996 Nov;59(5):1006-11. [PubMed
]
- Anikster Y, Shaag A, Joseph A, Mandel H, Ben-Zeev B, Christensen E, Elpeleg ON: Glutaric aciduria type I in the Arab and Jewish communities in Israel. Am J Hum Genet. 1996 Nov;59(5):1012-8. [PubMed
]
- Muhlhausen C, Christensen E, Schwartz M, Muschol N, Ullrich K, Lukacs Z: Severe phenotype despite high residual glutaryl-CoA dehydrogenase activity: a novel mutation in a Turkish patient with glutaric aciduria type I. J Inherit Metab Dis. 2003;26(7):713-4. [PubMed
]
- Keyser B, Muhlhausen C, Dickmanns A, Christensen E, Muschol N, Ullrich K, Braulke T: Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH). Hum Mol Genet. 2008 Dec 15;17(24):3854-63. Epub 2008 Sep 5. [PubMed
]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
5458 |
| Enzyme 50 Name |
Hepatic triacylglycerol lipase |
| Enzyme 50 Synonyms |
- HL
- Hepatic lipase
- Lipase member C
|
| Enzyme 50 Gene Name |
LIPC |
| Enzyme 50 Protein Sequence |
>Hepatic triacylglycerol lipase
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
|
| Enzyme 50 Number of Residues |
499 |
| Enzyme 50 Molecular Weight |
55880.1 |
| Enzyme 50 Theoretical pI |
9.37 |
| Enzyme 50 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 50 General Function |
Involved in catalytic activity |
| Enzyme 50 Specific Function |
Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin |
| Enzyme 50 Pathways |
|
| Enzyme 50 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
194097335  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
P11150  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
LIPC_HUMAN  |
| Enzyme 50 PDB ID |
Not Available |
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACCCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTTCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTCAAGATCCAGTTC
ATCAACCAAACTGAGACACCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
|
| Enzyme 50 GenBank Gene ID |
NM_000236.2  |
| Enzyme 50 GeneCard ID |
LIPC  |
| Enzyme 50 GenAtlas ID |
LIPC  |
| Enzyme 50 HGNC ID |
HGNC:6619  |
| Enzyme 50 Chromosome Location |
1 |
| Enzyme 50 Locus |
15q21-q23 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 General References |
- Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed
]
- Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed
]
- Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed
]
- Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed
]
- Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tiebel O, Gehrisch S, Pietzsch J, Gromeier S, Jaross W: 18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. Hum Mutat. 1998;12(3):216. [PubMed
]
- Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed
]
- Todorova B, Kubaszek A, Pihlajamaki J, Lindstrom J, Eriksson J, Valle TT, Hamalainen H, Ilanne-Parikka P, Keinanen-Kiukaanniemi S, Tuomilehto J, Uusitupa M, Laakso M: The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish Diabetes Prevention Study. J Clin Endocrinol Metab. 2004 May;89(5):2019-23. [PubMed
]
- Grarup N, Andreasen CH, Andersen MK, Albrechtsen A, Sandbaek A, Lauritzen T, Borch-Johnsen K, Jorgensen T, Schmitz O, Hansen T, Pedersen O: The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects. J Clin Endocrinol Metab. 2008 Jun;93(6):2294-9. Epub 2008 Mar 25. [PubMed
]
- Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
5475 |
| Enzyme 51 Name |
Diacylglycerol O-acyltransferase 1 |
| Enzyme 51 Synonyms |
- ACAT-related gene product 1
- Diglyceride acyltransferase
|
| Enzyme 51 Gene Name |
DGAT1 |
| Enzyme 51 Protein Sequence |
>Diacylglycerol O-acyltransferase 1
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVG
SGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQV
VSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPA
AVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHT
VSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWM
VPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREF
YRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVS
VPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLN
YEAPAAEA
|
| Enzyme 51 Number of Residues |
488 |
| Enzyme 51 Molecular Weight |
55277.7 |
| Enzyme 51 Theoretical pI |
9.60 |
| Enzyme 51 GO Classification |
Not Available |
| Enzyme 51 General Function |
Involved in diacylglycerol O-acyltransferase activity |
| Enzyme 51 Specific Function |
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly |
| Enzyme 51 Pathways |
|
| Enzyme 51 Reactions |
- acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
|
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
- 104-124
130-150
166-186
189-209
282-302
332-352
406-426
428-448
453-473
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
29170487  |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
O75907  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
DGAT1_HUMAN  |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
>1467 bp
ATGGGCGACCGCGGCAGCTCCCGGCGCCGGAGGACAGGGTCGCGGCCCTCGAGCCACGGC
GGCGGCGGGCCTGCGGCGGCGGAAGAGGAGGTGCGGGACGCCGCTGCGGGCCCCGACGTG
GGAGCCGCGGGGGACGCGCCAGCCCCGGCCCCCAACAAGGACGGAGACGCCGGCGTGGGC
AGCGGCCACTGGGAGCTGAGGTGCCATCGCCTGCAGGATTCTTTATTCAGCTCTGACAGT
GGCTTCAGCAACTACCGTGGCATCCTGAACTGGTGTGTGGTGATGCTGATCTTGAGCAAT
GCCCGGTTATTTCTGGAGAACCTCATCAAGTATGGCATCCTGGTGGACCCCATCCAGGTG
GTTTCTCTGTTCCTGAAGGATCCCTATAGCTGGCCCGCCCCATGCCTGGTTATTGCGGCC
AATGTCTTTGCTGTGGCTGCATTCCAGGTTGAGAAGCGCCTGGCGGTGGGTGCCCTGACG
GAGCAGGCGGGACTGCTGCTGCACGTGGCCAACCTGGCCACCATTCTGTGTTTCCCAGCG
GCTGTGGTCTTACTGGTTGAGTCTATCACTCCAGTGGGCTCCCTGCTGGCGCTGATGGCG
CACACCATCCTCTTCCTCAAGCTCTTCTCCTACCGCGACGTCAACTCATGGTGCCGCAGG
GCCAGGGCCAAGGCTGCCTCTGCAGGGAAGAAGGCCAGCAGTGCTGCTGCCCCGCACACC
GTGAGCTACCCGGACAATCTGACCTACCGCGATCTCTACTACTTCCTCTTCGCCCCCACC
TTGTGCTACGAGCTCAACTTTCCCCGCTCTCCCCGCATCCGGAAGCGCTTTCTGCTGCGA
CGGATCCTTGAGATGCTGTTCTTCACCCAGCTCCAGGTGGGGCTGATCCAGCAGTGGATG
GTCCCCACCATCCAGAACTCCATGAAGCCCTTCAAGGACATGGACTACTCACGCATCATC
GAGCGCCTCCTGAAGCTGGCGGTCCCCAATCACCTCATCTGGCTCATCTTCTTCTACTGG
CTCTTCCACTCCTGCCTGAATGCCGTGGCTGAGCTCATGCAGTTTGGAGACCGGGAGTTC
TACCGGGACTGGTGGAACTCCGAGTCTGTCACCTACTTCTGGCAGAACTGGAACATCCCT
GTGCACAAGTGGTGCATCAGACACTTCTACAAGCCCATGCTTCGACGGGGCAGCAGCAAG
TGGATGGCCAGGACAGGGGTGTTCCTGGCCTCGGCCTTCTTCCACGAGTACCTGGTGAGC
GTCCCTCTGCGAATGTTCCGCCTCTGGGCGTTCACGGGCATGATGGCTCAGATCCCACTG
GCCTGGTTCGTGGGCCGCTTTTTCCAGGGCAACTATGGCAACGCAGCTGTGTGGCTGTCG
CTCATCATCGGACAGCCAATAGCCGTCCTCATGTACGTCCACGACTACTACGTGCTCAAC
TATGAGGCCCCAGCGGCAGAGGCCTGA
|
| Enzyme 51 GenBank Gene ID |
AB057815  |
| Enzyme 51 GeneCard ID |
DGAT1  |
| Enzyme 51 GenAtlas ID |
DGAT1  |
| Enzyme 51 HGNC ID |
HGNC:2843  |
| Enzyme 51 Chromosome Location |
8 |
| Enzyme 51 Locus |
8q24.3 |
| Enzyme 51 SNPs |
SNPJam Report  |
| Enzyme 51 General References |
- Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
5534 |
| Enzyme 52 Name |
2-oxoisovalerate dehydrogenase subunit beta, mitochondrial |
| Enzyme 52 Synonyms |
- Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
- BCKDE1B
- BCKDH E1-beta
|
| Enzyme 52 Gene Name |
BCKDHB |
| Enzyme 52 Protein Sequence |
>2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
MAVVAAAAGWLLRLRAAGAEGHWRRLPGAGLARGFLHPAATVEDAAQRRQVAHFTFQPDP
EPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVF
NTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSL
TIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEP
KILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCE
VIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRV
CGYDTPFPHIFEPFYIPDKWKCYDALRKMINY
|
| Enzyme 52 Number of Residues |
392 |
| Enzyme 52 Molecular Weight |
43122.1 |
| Enzyme 52 Theoretical pI |
6.24 |
| Enzyme 52 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 52 General Function |
Involved in catalytic activity |
| Enzyme 52 Specific Function |
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 52 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 52 Reactions |
- 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 [RN:R01701]
|
| Enzyme 52 Pfam Domain Function |
|
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
179362  |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
P21953  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
ODBB_HUMAN  |
| Enzyme 52 PDB ID |
1X80  |
| Enzyme 52 PDB File |
Show |
| Enzyme 52 3D Structure |
|
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
>1179 bp
ATGGCGGTTGTAGCGGCGGCTGCCGGCTGGCTACTCAGGCTCAGGGCGGCAGGGGCTGAG
GGGCACTGGCGTCGGCTTCCTGGCGCGGGGCTGGCGCGGGGCTTTTTGCACCCCGCCGCG
ACTGTCGAGGATGCGGCCCAGAGGCGGCAGGTGGCTCATTTTACTTTCCAGCCAGATCCG
GAGCCCCGGGAGTACGGGCAAACTCAGAAAATGAATCTTTTCCAGTCTGTAACAAGTGCC
TTGGATAACTCATTGGCCAAAGATCCTACTGCAGTAATATTTGGTGAAGATGTTGCCTTT
GGTGGAGTCTTTAGATGCACTGTTGGCTTGCGAGACAAATATGGAAAAGATAGAGTTTTT
AATACCCCATTGTGTGAACAAGGAATTGTTGGATTTGGAATCGGAATTGCGGTCACTGGA
GCTACTGCCATTGCGGAAATTCAGTTTGCAGATTATATTTTCCCTGCATTTGATCAGATT
GTTAATGAAGCTGCCAAGTATCGCTATCGCTCTGGGGATCTTTTTAACTGTGGAAGCCTC
ACTATCCGGTCCCCTTGGGGCTGTGTTGGTCATGGGGCTCTCTATCATTCTCAGAGTCCT
GAAGCATTTTTTGCCCATTGCCCAGGAATCAAGGTGGTTATACCCAGAAGCCCTTTCCAG
GCCAAAGGACTTCTTTTGTCATGCATAGAGGATAAAAATCCTTGTATATTTTTTGAACCT
AAAATACTTTACAGGGCAGCAGCGGAAGAAGTCCCTATAGAACCATACAACATCCCACTG
TCCCAGGCCGAAGTCATACAGGAAGGGAGTGATGTTACTCTAGTTGCCTGGGGCACTCAG
GTTCATGTGATCCGAGAGGTAGCTTCCATGGCAAAAGAAAAGCTTGGAGTGTCTTGTGAA
GTCATTGATCTGAGGACTATAATACCTTGGGATGTGGACACAATTTGTAAGTCTGTGATC
AAAACAGGGCGACTGCTAATCAGTCACGAGGCTCCCTTGACAGGCGGCTTTGCATCGGAA
ATCAGCTCTACAGTTCAGGAGGAATGTTTCTTGAACCTAGAGGCTCCTATATCAAGAGTA
TGTGGTTATGACACACCATTTCCTCACATTTTTGAACCATTCTACATCCCAGACAAATGG
AAGTGTTATGATGCCCTTCGAAAAATGATCAACTATTGA
|
| Enzyme 52 GenBank Gene ID |
M55575  |
| Enzyme 52 GeneCard ID |
BCKDHB  |
| Enzyme 52 GenAtlas ID |
BCKDHB  |
| Enzyme 52 HGNC ID |
HGNC:987  |
| Enzyme 52 Chromosome Location |
6 |
| Enzyme 52 Locus |
6q14.1 |
| Enzyme 52 SNPs |
SNPJam Report  |
| Enzyme 52 General References |
- Nobukuni Y, Mitsubuchi H, Endo F, Akaboshi I, Asaka J, Matsuda I: Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease. J Clin Invest. 1990 Jul;86(1):242-7. [PubMed
]
- Chuang JL, Cox RP, Chuang DT: Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences. Am J Hum Genet. 1996 Jun;58(6):1373-7. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Chuang JL, Cox RP, Chuang DT: Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1990 Mar 26;262(2):305-9. [PubMed
]
- Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed
]
- Edelmann L, Wasserstein MP, Kornreich R, Sansaricq C, Snyderman SE, Diaz GA: Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population. Am J Hum Genet. 2001 Oct;69(4):863-8. Epub 2001 Aug 16. [PubMed
]
|
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
5535 |
| Enzyme 53 Name |
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial |
| Enzyme 53 Synonyms |
- Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
- BCKDE1A
- BCKDH E1-alpha
|
| Enzyme 53 Gene Name |
BCKDHA |
| Enzyme 53 Protein Sequence |
>2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAE
FIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILY
ESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYG
NISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGA
ASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDG
NDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHP
ISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQL
RKQQESLARHLQTYGEHYPLDHFDK
|
| Enzyme 53 Number of Residues |
445 |
| Enzyme 53 Molecular Weight |
50470.6 |
| Enzyme 53 Theoretical pI |
8.41 |
| Enzyme 53 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
|
| Process |
|
| Component |
| — |
|
| Enzyme 53 General Function |
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| Enzyme 53 Specific Function |
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 53 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 53 Reactions |
- 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 [RN:R01701]
|
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
29391  |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
P12694  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
ODBA_HUMAN  |
| Enzyme 53 PDB ID |
1U5B  |
| Enzyme 53 PDB File |
Show |
| Enzyme 53 3D Structure |
|
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>1338 bp
ATGGCGGTAGCGATCGCTGCAGCGAGGGTCTGGCGGCTAAACCGTGGTTTGAGCCAGGCT
GCCCTCCTGCTGCTGCGGCAGCCTGGGGCTCGGGGACTGGCTAGATCTCACCCCCCCAGG
CAGCAGCAGCAGTTTTCATCTCTGGATGACAAGCCCCAGTTCCCAGGGGCCTCGGCGGAG
TTTATAGATAAGTTGGAATTCATCCAGCCCAACGTCATCTCTGGAATCCCCATCTACCGC
GTCATGGACCGGCAAGGCCAGATCATCAACCCCAGCGAGGACCCCCACCTGCCGAAGGAG
AAGGTGCTGAAGCTCTACAAGAGCATGACACTGCTTAACACCATGGACCGCATCCTCTAT
GAGTCTCAGCGGCAGGGCCGGATCTCCTTCTACATGACCAACTATGGTGAGGAGGGCACG
CACGTGGGGAGTGCCGCCGCCCTGGACAACACGGACCTGGTGTTTGGCCAGTACCGGGAG
GCAGGTGTGCTGATGTATCGGGACTACCCCCTGGAACTATTCATGGCCCAGTGCTATGGC
AACATCAGTGACTTGGGCAAGGGGCGCCAGATGCCTGTCCACTACGGCTGCAAGGAACGC
CACTTCGTCACTATCTCCTCTCCACTGGCCACGCAGATCCCTCAGGCGGTGGGGGCGGCG
TACGCAGCCAAGCGGGCCAATGCCAACAGGGTCGTCATCTGTTACTTCGGCGAGGGGGCA
GCCAGTGAGGGGGACGCCCATGCCGGCTTCAACTTCGCTGCCACACTTGAGTGCCCCATC
ATCTTCTTCTGCCGGAACAATGGCTACGCCATCTCCACGCCCACCTCTGAGCAGTATCGC
GGCGATGGCATTGCAGCACGAGGCCCCGGGTATGGCATCATGTCAATCCGCGTGGATGGT
AATGATGTGTTTGCCGTATACAACGCCACAAAGGAGGCCCGACGGCGGGCTGTGGCAGAG
AACCAGCCCTTTCTCATCGAGGCCATGACCTACAGGATCGGGCACCACAGCACCAGTGAC
GACAGTTCAGCGTACCGCTCGGTGGATGAGGTCAATTACTGGGATAAACAGGACCACCCC
ATCTCCCGGCTGCGGCACTATCTGCTGAGCCAAGGCTGGTGGGATGAGGAGCAGGAGAAG
GCCTGGAGGAAGCAGTCCCGCAGGAAGGTGATGGAGGCCTTTGAGCAGGCCGAGCGGAAG
CCCAAACCCAACCCCAACCTGCTCTTCTCAGACGTGTATCAGGAGATGCCCGCCCAGCTC
CGCAAGCAGCAGGAGTCTCTGGCCCGCCACCTGCAGACCTACGGGGAGCACTACCCACTG
GATCACTTCGATAAGTGA
|
| Enzyme 53 GenBank Gene ID |
Z14093  |
| Enzyme 53 GeneCard ID |
BCKDHA  |
| Enzyme 53 GenAtlas ID |
BCKDHA  |
| Enzyme 53 HGNC ID |
HGNC:986  |
| Enzyme 53 Chromosome Location |
1 |
| Enzyme 53 Locus |
19q13.1-q13.2 |
| Enzyme 53 SNPs |
SNPJam Report  |
| Enzyme 53 General References |
- McKean MC, Winkeler KA, Danner DJ: Nucleotide sequence of the 5' end including the initiation codon of cDNA for the E1 alpha subunit of the human branched chain alpha-ketoacid dehydrogenase complex. Biochim Biophys Acta. 1992 Nov 15;1171(1):109-12. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Fisher CW, Chuang JL, Griffin TA, Lau KS, Cox RP, Chuang DT: Molecular phenotypes in cultured maple syrup urine disease cells. Complete E1 alpha cDNA sequence and mRNA and subunit contents of the human branched chain alpha-keto acid dehydrogenase complex. J Biol Chem. 1989 Feb 25;264(6):3448-53. [PubMed
]
- Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1991 Jun 17;284(1):34-8. [PubMed
]
- Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex (1991) FEBS Letters 284, 34-38. FEBS Lett. 1991 Oct 21;291(2):376-7. [PubMed
]
- Zhang B, Crabb DW, Harris RA: Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase. Gene. 1988 Sep 15;69(1):159-64. [PubMed
]
- Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- AEvarsson A, Chuang JL, Wynn RM, Turley S, Chuang DT, Hol WG: Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure. 2000 Mar 15;8(3):277-91. [PubMed
]
- Chuang JL, Fisher CR, Cox RP, Chuang DT: Molecular basis of maple syrup urine disease: novel mutations at the E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid dehydrogenase complex. Am J Hum Genet. 1994 Aug;55(2):297-304. [PubMed
]
- Zhang B, Edenberg HJ, Crabb DW, Harris RA: Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease. J Clin Invest. 1989 Apr;83(4):1425-9. [PubMed
]
- Matsuda I, Nobukuni Y, Mitsubuchi H, Indo Y, Endo F, Asaka J, Harada A: A T-to-A substitution in the E1 alpha subunit gene of the branched-chain alpha-ketoacid dehydrogenase complex in two cell lines derived from Menonite maple syrup urine disease patients. Biochem Biophys Res Commun. 1990 Oct 30;172(2):646-51. [PubMed
]
- Fisher CR, Fisher CW, Chuang DT, Cox RP: Occurrence of a Tyr393----Asn (Y393N) mutation in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population. Am J Hum Genet. 1991 Aug;49(2):429-34. [PubMed
]
- Fisher CR, Chuang JL, Cox RP, Fisher CW, Star RA, Chuang DT: Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1 alpha impedes assembly of the E1 component of branched-chain alpha-keto acid dehydrogenase complex. J Clin Invest. 1991 Sep;88(3):1034-7. [PubMed
]
- Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed
]
- Chuang JL, Davie JR, Chinsky JM, Wynn RM, Cox RP, Chuang DT: Molecular and biochemical basis of intermediate maple syrup urine disease. Occurrence of homozygous G245R and F364C mutations at the E1 alpha locus of Hispanic-Mexican patients. J Clin Invest. 1995 Mar;95(3):954-63. [PubMed
]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
5548 |
| Enzyme 54 Name |
Acyl-CoA desaturase |
| Enzyme 54 Synonyms |
- Delta(9)-desaturase
- Fatty acid desaturase
- Stearoyl-CoA desaturase
|
| Enzyme 54 Gene Name |
SCD |
| Enzyme 54 Protein Sequence |
>Acyl-CoA desaturase
MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYK
DKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAH
RLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFS
HVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGE
TFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNY
HHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG
|
| Enzyme 54 Number of Residues |
359 |
| Enzyme 54 Molecular Weight |
41522.3 |
| Enzyme 54 Theoretical pI |
9.28 |
| Enzyme 54 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
- stearoyl-CoA 9-desaturase activity
- transition metal ion binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- lipid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
- primary metabolic process
|
| Component |
- cell part
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane
- membrane-bounded organelle
- organelle
|
|
| Enzyme 54 General Function |
Involved in oxidoreductase activity |
| Enzyme 54 Specific Function |
Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA |
| Enzyme 54 Pathways |
Not Available |
| Enzyme 54 Reactions |
- stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O [RN:R02222]
|
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
- 76-96
98-118
223-243
315-335
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
7415721  |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
O00767  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
ACOD_HUMAN  |
| Enzyme 54 PDB ID |
Not Available |
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>1080 bp
ATGCCGGCCCACTTGCTGCAGGACGATATCTCTAGCTCCTATACCACCACCACCACCATT
ACAGCGCCTCCCTCCAGGGTCCTGCAGAATGGAGGAGATAAGTTGGAGACGATGCCCCTC
TACTTGGAAGACGACATTCGCCCTGATATAAAAGATGATATATATGACCCCACCTACAAG
GATAAGGAAGGCCCAAGCCCCAAGGTTGAATATGTCTGGAGAAACATCATCCTTATGTCT
CTGCTACACTTGGGAGCCCTGTATGGGATCACTTTGATTCCTACCTGCAAGTTCTACACC
TGGCTTTGGGGGGTATTCTACTATTTTGTCAGTGCCCTGGGCATAACAGCAGGAGCTCAT
CGTCTGTGGAGCCACCGCTCTTACAAAGCTCGGCTGCCCCTACGGCTCTTTCTGATCATT
GCCAACACAATGGCATTCCAGAATGATGTCTATGAATGGGCTCGTGACCACCGTGCCCAC
CACAAGTTTTCAGAAACACATGCTGATCCTCATAATTCCCGACGTGGCTTTTTCTTCTCT
CACGTGGGTTGGCTGCTTGTGCGCAAACACCCAGCTGTCAAAGAGAAGGGGAGTACGCTA
GACTTGTCTGACCTAGAAGCTGAGAAACTGGTGATGTTCCAGAGGAGGTACTACAAACCT
GGCTTGCTGCTGATGTGCTTCATCCTGCCCACGCTTGTGCCCTGGTATTTCTGGGGTGAA
ACTTTTCAAAACAGTGTGTTCGTTGCCACTTTCTTGCGATATGCTGTGGTGCTTAATGCC
ACCTGGCTGGTGAACAGTGCTGCCCACCTCTTCGGATATCGTCCTTATGACAAGAACATT
AGCCCCCGGGAGAATATCCTGGTTTCACTTGGAGCTGTGGGTGAGGGCTTCCACAACTAC
CACCACTCCTTTCCCTATGACTACTCTGCCAGTGAGTACCGCTGGCACATCAACTTCACC
ACATTCTTCATTGATTGCATGGCCGCCCTCGGTCTGGCCTATGACCGGAAGAAAGTCTCC
AAGGCCGCCATCTTGGCCAGGATTAAAAGAACCGGAGATGGAAACTACAAGAGTGGCTGA
|
| Enzyme 54 GenBank Gene ID |
AB032261  |
| Enzyme 54 GeneCard ID |
SCD  |
| Enzyme 54 GenAtlas ID |
SCD  |
| Enzyme 54 HGNC ID |
HGNC:10571  |
| Enzyme 54 Chromosome Location |
1 |
| Enzyme 54 Locus |
10q24.31 |
| Enzyme 54 SNPs |
SNPJam Report  |
| Enzyme 54 General References |
- Zhang L, Ge L, Parimoo S, Stenn K, Prouty SM: Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites. Biochem J. 1999 May 15;340 ( Pt 1):255-64. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang L, Ge L, Tran T, Stenn K, Prouty SM: Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element. Biochem J. 2001 Jul 1;357(Pt 1):183-93. [PubMed
]
- Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [PubMed
]
- Li J, Ding SF, Habib NA, Fermor BF, Wood CB, Gilmour RS: Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues. Int J Cancer. 1994 May 1;57(3):348-52. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
|
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
5626 |
| Enzyme 55 Name |
Trifunctional enzyme subunit alpha, mitochondrial |
| Enzyme 55 Synonyms |
- 78 kDa gastrin-binding protein
- TP-alpha
- Long-chain enoyl-CoA hydratase
- Long chain 3-hydroxyacyl-CoA dehydrogenase
|
| Enzyme 55 Gene Name |
HADHA |
| Enzyme 55 Protein Sequence |
>Trifunctional enzyme subunit alpha, mitochondrial
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
|
| Enzyme 55 Number of Residues |
763 |
| Enzyme 55 Molecular Weight |
82999.0 |
| Enzyme 55 Theoretical pI |
9.52 |
| Enzyme 55 GO Classification |
| Function |
- 3-hydroxyacyl-CoA dehydrogenase activity
- binding
- carbon-oxygen lyase activity
- catalytic activity
- coenzyme binding
- cofactor binding
- enoyl-CoA hydratase activity
- hydro-lyase activity
- lyase activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- fatty acid beta-oxidation multienzyme complex
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- mitochondrion
- organelle
- protein complex
|
|
| Enzyme 55 General Function |
Involved in oxidoreductase activity |
| Enzyme 55 Specific Function |
Bifunctional subunit |
| Enzyme 55 Pathways |
|
| Enzyme 55 Reactions |
- (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O [RN:R02685 R07314]
|
| Enzyme 55 Pfam Domain Function |
|
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
189053609  |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
P40939  |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
ECHA_HUMAN  |
| Enzyme 55 PDB ID |
Not Available |
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
>2292 bp
ATGGTGGCCTGCCGGGCGATTGGCATCCTCAGCCGCTTTTCTGCCTTCAGGATCCTCCGC
TCCCGAGGTTATATATGCCGCAATTTTACAGGGTCTTCTGCTTTGCTGACCAGAACCCAT
ATTAACTATGGAGTCAAAGGGGATGTGGCAGTTGTTCGAATTAACTCTCCCAATTCAAAG
GTAAATACACTGAGTAAAGAGCTACATTCAGAGTTCTCAGAAGTTATGAATGAAATCTGG
GCTAGTGATCAAATCAGAAGTGCCGTCCTTATCTCATCAAAGCCAGGCTGCTTTATTGCA
GGTGCTGATATCAACATGTTAGCCGCTTGCAAGACCCTTCAAGAAGTAACACAGCTATCA
CAAGAAGCACAGAGAATAGTTGAGAAACTTGAAAAGTCCACAAAGCCTATTGTGGCTGCC
ATCAATGGATCCTGCCTGGGAGGAGGACTTGAGGTTGCCATTTCATGCCAATATAGAATA
GCAACAAAAGACAGAAAAACAGTATTAGGTACCCCTGAAGTTTTGCTGGGGGCCTTACCA
GGAGCAGGAGGCACACAAAGGCTGCCCAAAATGGTGGGTGTGCCTGCTGCTTTGGACATG
ATGCTGACTGGTAGAAGCATTCGTGCAGACAGGGCAAAGAAAATGGGACTGGTTGACCAA
CTGGTGGAACCCCTGGGACCAGGACTAAAACCTCCAGAGGAACGGACAATAGAATACCTA
GAAGAAGTTGCAATTACTTTTGCCAAAGGACTAGCTGATAAGAAGATCTCTCCAAAGAGA
GACAAGGGATTGGTGGAAAAATTGACAGCGTATGCCATGACTATTCCATTTGTCAGGCAA
CAGGTTTACAAAAAAGTGGAAGAAAAAGTGCGAAAGCAGACTAAAGGCCTTTATCCTGCA
CCTCTGAAAATAATTGATGTGGTAAAGACTGGAATTGAGCAAGGGAGTGATGCCGGTTAT
CTCTGTGAATCTCAGAAATTTGGAGAGCTTGTAATGACCAAAGAATCAAAGGCCTTGATG
GGACTCTACCATGGTCAGGTCCTGTGCAAGAAGAATAAATTTGGAGCTCCACAGAAGGAT
GTTAAGCATCTGGCTATTCTTGGTGCAGGGCTGATGGGAGCAGGCATCGCCCAAGTCTCC
GTGGATAAGGGGCTAAAGACTATACTTAAAGATGCCACCCTCACTGCGCTAGACCGAGGA
CAGCAACAAGTGTTCAAAGGATTGAATGACAAAGTGAAGAAGAAAGCTCTAACATCATTT
GAAAGGGATTCCATCTTCAGCAACTTGACTGGGCAGCTTGATTACCAAGGTTTTGAAAAG
GCCGACATGGTGATTGAAGCTGTGTTTGAGGACCTTAGTCTTAAGCACAGAGTGCTAAAG
GAAGTAGAAGCGGTGATTCCAGATCACTGTATCTTTGCCAGTAACACATCTGCTCTCCCA
ATCAGTGAAATCGCTGCTGTCAGCAAAAGACCTGAGAAGGTGATTGGCATGCACTACTTC
TCTCCCGTGGACAAGATGCAGCTGCTGGAGATTATCACGACCGAGAAAACTTCCAAAGAC
ACCAGTGCTTCAGCTGTAGCAGTTGGTCTCAAGCAGGGGAAGGTCATCATTGTGGTTAAG
GATGGACCTGGCTTCTATACTACCAGGTGTCTTGCGCCCATGATGTCTGAAGTCATCCGA
ATCCTCCAGGAAGGAGTTGACCCGAAGAAGCTGGATTCCCTGACCACAAGCTTTGGCTTT
CCTGTGGGTGCCGCCACACTGGTGGATGAAGTTGGTGTGGATGTAGCGAAACATGTGGCG
GAAGATCTGGGCAAAGTCTTTGGGGAGCGGTTTGGAGGTGGAAACCCAGAACTGCTGACA
CAGATGGTGTCCAAGGGCTTCCTAGGTCGTAAATCTGGGAAGGGCTTTTACATCTATCAG
GAGGGTGTGAAGAGGAAGGATTTGAATTCTGACATGGATAGTATTTTAGCGAGTCTGAAG
CTGCCTCCTAAGTCTGAAGTCTCATCAGACGAAGACATCCAGTTCCGCCTGGTGACAAGA
TTTGTGAATGAGGCAGTCATGTGCCTGCAAGAGGGGATCTTGGCCACACCTGCAGAGGGA
GACATCGGAGCCGTCTTTGGGCTTGGCTTCCCGCCTTGTCTGGGAGGGCCTTTCCGCTTT
GTGGATCTGTATGGCGCCCAGAAGATAGTGGACCGGCTCAAGAAATATGAAGCTGCCTAT
GGAAAACAGTTCACCCCATGCCAGCTGCTAGCTGACCATGCTAACAGCCCTAACAAGAAG
TTCTACCAGTGA
|
| Enzyme 55 GenBank Gene ID |
AK313027  |
| Enzyme 55 GeneCard ID |
HADHA  |
| Enzyme 55 GenAtlas ID |
HADHA  |
| Enzyme 55 HGNC ID |
HGNC:4801  |
| Enzyme 55 Chromosome Location |
2 |
| Enzyme 55 Locus |
2p23 |
| Enzyme 55 SNPs |
SNPJam Report  |
| Enzyme 55 General References |
- Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed
]
- Zhang QX, Baldwin GS: Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene. Biochim Biophys Acta. 1994 Oct 18;1219(2):567-75. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kamijo T, Wanders RJ, Saudubray JM, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest. 1994 Apr;93(4):1740-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- IJlst L, Wanders RJ, Ushikubo S, Kamijo T, Hashimoto T: Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein. Biochim Biophys Acta. 1994 Dec 8;1215(3):347-50. [PubMed
]
- Sims HF, Brackett JC, Powell CK, Treem WR, Hale DE, Bennett MJ, Gibson B, Shapiro S, Strauss AW: The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):841-5. [PubMed
]
- IJlst L, Ruiter JP, Hoovers JM, Jakobs ME, Wanders RJ: Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene. J Clin Invest. 1996 Aug 15;98(4):1028-33. [PubMed
]
- IJlst L, Oostheim W, Ruiter JP, Wanders RJ: Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of two new mutations. J Inherit Metab Dis. 1997 Jul;20(3):420-2. [PubMed
]
- Ibdah JA, Tein I, Dionisi-Vici C, Bennett MJ, IJlst L, Gibson B, Wanders RJ, Strauss AW: Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation. J Clin Invest. 1998 Sep 15;102(6):1193-9. [PubMed
]
|
| Enzyme 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
5746 |
| Enzyme 56 Name |
Sterol O-acyltransferase 2 |
| Enzyme 56 Synonyms |
- Acyl-coenzyme A:cholesterol acyltransferase 2
- ACAT-2
- Cholesterol acyltransferase 2
|
| Enzyme 56 Gene Name |
SOAT2 |
| Enzyme 56 Protein Sequence |
>Sterol O-acyltransferase 2
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQL
RELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHF
RTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLA
PYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFL
MKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKN
FAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLH
CWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARG
VAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTM
LFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT
|
| Enzyme 56 Number of Residues |
522 |
| Enzyme 56 Molecular Weight |
59895.7 |
| Enzyme 56 Theoretical pI |
8.71 |
| Enzyme 56 GO Classification |
Not Available |
| Enzyme 56 General Function |
Involved in acyl-CoA binding |
| Enzyme 56 Specific Function |
Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa |
| Enzyme 56 Pathways |
|
| Enzyme 56 Reactions |
- acyl-CoA + cholesterol = CoA + cholesterol ester [RN:R01461]
|
| Enzyme 56 Pfam Domain Function |
|
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
- 124-144
155-175
200-220
262-282
304-324
344-366
437-457
472-492
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
Not Available |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
O75908  |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
SOAT2_HUMAN  |
| Enzyme 56 PDB ID |
Not Available |
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 Gene Sequence |
>1569 bp
ATGGAGCCAGGCGGGGCCCGTCTGCGTCTGCAGAGGACAGAAGGGCTGGGAGGGGAGCGG
GAGCGCCAACCCTGTGGAGATGGAAACACTGAGACGCACAGAGCCCCGGACTTGGTACAA
TGGACCCGACACATGGAGGCTGTGAAGGCACAATTGCTGGAGCAAGCGCAGGGACAACTG
AGGGAGCTGCTGGATCGGGCCATGCGGGAGGCTATACAATCCTACCCATCACAAGACAAA
CCTCTGCCCCCACCTCCCCCAGGTTCCTTGAGCAGGACCCAGGAGCCATCCCTGGGGAAA
CAGAAAGTTTTCATCATCCGCAAGTCCCTGCTTGATGAGCTGATGGAGGTGCAGCATTTC
CGCACCATCTACCACATGTTCATCGCTGGCCTGTGTGTCTTCATCATCAGCACCCTGGCC
ATCGACTTCATTGATGAGGGCAGGCTGCTGCTGGAGTTTGACCTACTGATCTTCAGCTTC
GGACAGCTGCCATTGGCGCTGGTGACCTGGGTGCCCATGTTTCTGTCCACCCTGTTGGCG
CCGTACCAGGCCCTACGGCTGTGGGCCAGGGGCACCTGGACGCAGGCGACGGGCCTGGGC
TGTGCGCTGCTAGCCGCCCACGCCGTGGTGCTCTGCGCGCTGCCGGTCCACGTGGCCGTG
GAGCATCAGCTCCCGCCGGCCTCCCGTTGTGTCCTGGTCTTCGAGCAGGTTAGGTTCCTG
ATGAAAAGCTACTCCTTCCTGAGAGAGGCTGTGCCTGGGACCCTTCGTGCCAGACGAGGT
GAGGGGATCCAGGCCCCCAGTTTCTCCAGCTACCTCTACTTCCTCTTCTGCCCAACACTC
ATCTACAGGGAGACTTACCCTAGGACGCCCTATGTCAGGTGGAATTATGTGGCCAAGAAC
TTTGCCCAGGCCCTGGGATGTGTGCTCTATGCCTGCTTCATCCTGGGCCGCCTCTGTGTT
CCTGTCTTTGCCAACATGAGCCGAGAGCCCTTCAGCACCCGTGCCCTGGTGCTCTCTATC
CTGCATGCCACGTTGCCAGGCATCTTCATGCTGCTGCTCATCTTCTTTGCCTTCCTCCAT
TGCTGGCTCAACGCCTTTGCCGAGATGCTACGATTTGGAGACAGGATGTTCTACCGGGAC
TGGTGGAACTCAACGTCCTTCTCCAACTACTACCGCACTTGGAACGTGGTGGTCCATGAC
TGGCTGTACAGCTACGTGTATCAGGATGGGCTGCGGCTCCTTGGTGCCCGGGCCCGAGGG
GTAGCCATGCTGGGTGTGTTCCTGGTCTCCGCAGTGGCCCATGAGTATATCTTCTGCTTC
GTCCTGGGGTTCTTCTATCCCGTCATGCTGATACTCTTCCTTGTCATTGGAGGAATGTTG
AACTTCATGATGCATGACCAGCGCACCGGCCCGGCATGGAACGTGCTGATGTGGACCATG
CTGTTTCTAGGCCAGGGAATCCAGGTCAGCCTGTACTGCCAGGAGTGGTACGCACGGCGG
CACTGCCCCTTACCCCAGGCAACTTTCTGGGGGCTGGTGACACCTCGATCTTGGTCCTGC
CATACCTAG
|
| Enzyme 56 GenBank Gene ID |
AF059203  |
| Enzyme 56 GeneCard ID |
SOAT2  |
| Enzyme 56 GenAtlas ID |
SOAT2  |
| Enzyme 56 HGNC ID |
HGNC:11178  |
| Enzyme 56 Chromosome Location |
1 |
| Enzyme 56 Locus |
12q13.13 |
| Enzyme 56 SNPs |
SNPJam Report  |
| Enzyme 56 General References |
- Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [PubMed
]
- Chang CC, Sakashita N, Ornvold K, Lee O, Chang ET, Dong R, Lin S, Lee CY, Strom SC, Kashyap R, Fung JJ, Farese RV Jr, Patoiseau JF, Delhon A, Chang TY: Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine. J Biol Chem. 2000 Sep 8;275(36):28083-92. [PubMed
]
- Katsuren K, Tamura T, Arashiro R, Takata K, Matsuura T, Niikawa N, Ohta T: Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2) gene and its relation to dyslipidemia. Biochim Biophys Acta. 2001 Apr 30;1531(3):230-40. [PubMed
]
- Song BL, Qi W, Yang XY, Chang CC, Zhu JQ, Chang TY, Li BL: Organization of human ACAT-2 gene and its cell-type-specific promoter activity. Biochem Biophys Res Commun. 2001 Mar 30;282(2):580-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
5751 |
| Enzyme 57 Name |
Sterol O-acyltransferase 1 |
| Enzyme 57 Synonyms |
- Acyl-coenzyme A:cholesterol acyltransferase 1
- ACAT-1
- Cholesterol acyltransferase 1
|
| Enzyme 57 Gene Name |
SOAT1 |
| Enzyme 57 Protein Sequence |
>Sterol O-acyltransferase 1
MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEE
LKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGK
IFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGK
FPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPT
YVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYF
LFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSAR
VLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTW
NVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFM
FFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVR
PRSWTCRYVF
|
| Enzyme 57 Number of Residues |
550 |
| Enzyme 57 Molecular Weight |
64734.0 |
| Enzyme 57 Theoretical pI |
9.18 |
| Enzyme 57 GO Classification |
Not Available |
| Enzyme 57 General Function |
Involved in acyl-CoA binding |
| Enzyme 57 Specific Function |
Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase |
| Enzyme 57 Pathways |
|
| Enzyme 57 Reactions |
- acyl-CoA + cholesterol = CoA + cholesterol ester [RN:R01461]
|
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
- 141-159
320-341
361-382
470-490
498-518
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
55959989  |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
P35610  |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
SOAT1_HUMAN  |
| Enzyme 57 PDB ID |
Not Available |
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>1653 bp
ATGGTGGGTGAAGAGAAGATGTCTCTAAGAAACCGGCTGTCAAAGTCCAGGGAAAATCCT
GAGGAAGATGAAGACCAGAGAAACCCTGCAAAGGAGTCCCTAGAGACACCTAGTAATGGT
CGAATTGACATAAAACAGTTGATAGCAAAGAAGATAAAGTTGACAGCAGAGGCAGAGGAA
TTGAAGCCATTTTTTATGAAGGAAGTTGGCAGTCACTTTGATGATTTTGTGACCAATCTC
ATTGAAAAGTCAGCATCATTAGATAATGGTGGGTGCGCTCTCACAACCTTTTCTGTTCTT
GAAGGAGAGAAAAACAACCATAGAGCGAAGGATTTGAGAGCACCTCCAGAACAAGGAAAG
ATTTTTATTGCAAGGCGCTCTCTCTTAGATGAACTGCTTGAAGTGGACCACATCAGAACA
ATATATCACATGTTTATTGCCCTCCTCATTCTCTTTATCCTCAGCACACTTGTAGTAGAT
TACATTGATGAAGGAAGGCTGGTGCTTGAGTTCAGCCTCCTGTCTTATGCTTTTGGCAAA
TTTCCTACCGTTGTTTGGACCTGGTGGATCATGTTCCTGTCTACATTTTCAGTTCCCTAT
TTTCTGTTTCAACATTGGGCCACTGGCTATAGCAAGAGTTCTCATCCGCTGATCCGTTCT
CTCTTCCATGGCTTTCTTTTCATGATCTTCCAGATTGGAGTTCTAGGTTTTGGACCAACA
TATGTTGTGTTAGCATATACACTGCCACCAGCTTCCCGGTTCATCATTATATTCGAGCAG
ATTCGTTTTGTAATGAAGGCCCACTCATTTGTCAGAGAGAACGTGCCTCGGGTACTAAAT
TCAGCTAAGGAGAAATCAAGCACTGTTCCAATACCTACAGTCAACCAGTATTTGTACTTC
TTATTTGCTCCTACCCTTATCTACCGTGACAGCTATCCCAGGAATCCCACTGTAAGATGG
GGTTATGTCGCTATGAAGTTTGCACAGGTCTTTGGTTGCTTTTTCTATGTGTACTACATC
TTTGAAAGGCTTTGTGCCCCCTTGTTTCGGAATATCAAACAGGAGCCCTTCAGCGCTCGT
GTTCTGGTCCTATGTGTATTTAACTCCATCTTGCCAGGTGTGCTGATTCTCTTCCTTACT
TTTTTTGCCTTTTTGCACTGCTGGCTCAATGCCTTTGCTGAGATGTTACGCTTTGGTGAC
AGGATGTTCTATAAGGATTGGTGGAACTCCACGTCATACTCCAACTATTATAGAACCTGG
AATGTGGTGGTCCATGACTGGCTATATTACTATGCTTACAAGGACTTTCTCTGGTTTTTC
TCCAAGAGATTCAAATCTGCTGCCATGTTAGCTGTCTTTGCTGTATCTGCTGTAGTACAC
GAATATGCCTTGGCTGTTTGCTTGAGCTTTTTCTATCCCGTGCTCTTCGTGCTCTTCATG
TTCTTTGGAATGGCTTTCAACTTCATTGTCAATGATAGTCGGAAAAAGCCGATTTGGAAT
GTTCTGATGTGGACTTCTCTTTTCTTGGGCAATGGAGTCTTACTCTGCTTTTATTCTCAA
GAATGGTATGCACGTCAGCACTGTCCTCTGAAAAATCCCACATTTTTGGATTATGTCCGG
CCACGTTCCTGGACTTGTCGTTACGTGTTTTAG
|
| Enzyme 57 GenBank Gene ID |
AL451075  |
| Enzyme 57 GeneCard ID |
SOAT1  |
| Enzyme 57 GenAtlas ID |
SOAT1  |
| Enzyme 57 HGNC ID |
HGNC:11177  |
| Enzyme 57 Chromosome Location |
1 |
| Enzyme 57 Locus |
1q25 |
| Enzyme 57 SNPs |
SNPJam Report  |
| Enzyme 57 General References |
- Chang CC, Huh HY, Cadigan KM, Chang TY: Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells. J Biol Chem. 1993 Oct 5;268(28):20747-55. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lin S, Cheng D, Liu MS, Chen J, Chang TY: Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains. J Biol Chem. 1999 Aug 13;274(33):23276-85. [PubMed
]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
5762 |
| Enzyme 58 Name |
N-acetylglutamate synthase, mitochondrial |
| Enzyme 58 Synonyms |
- Amino-acid acetyltransferase
- N-acetylglutamate synthase long form
- N-acetylglutamate synthase short form
- N-acetylglutamate synthase conserved domain form
|
| Enzyme 58 Gene Name |
NAGS |
| Enzyme 58 Protein Sequence |
>N-acetylglutamate synthase, mitochondrial
MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPP
EEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEA
RHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAP
TAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVS
VETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLR
DSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTE
LFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYV
SEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNP
INPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS
|
| Enzyme 58 Number of Residues |
534 |
| Enzyme 58 Molecular Weight |
58155.8 |
| Enzyme 58 Theoretical pI |
9.12 |
| Enzyme 58 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- arginine biosynthetic process
- arginine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid biosynthetic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 58 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 58 Specific Function |
Plays a role in the regulation of ureagenesis by producing variable amounts of N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPSI) activity |
| Enzyme 58 Pathways |
Not Available |
| Enzyme 58 Reactions |
- acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate [RN:R00259]
|
| Enzyme 58 Pfam Domain Function |
|
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
22651771  |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
Q8N159  |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
NAGS_HUMAN  |
| Enzyme 58 PDB ID |
Not Available |
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
>1605 bp
ATGGCGACGGCGCTGATGGCTGTGGTTCTGCGGGCAGCTGCTGTAGCCCCGAGGCTGAGA
GGCCGGGGAGGCACTGGGGGCGCCCGAAGGCTGAGCTGTGGCGCGCGGCGGCGGGCGGCG
AGGGGCACCAGCCCGGGGCGCCGGCTCAGCACCGCCTGGTCGCAGCCCCAGCCCCCGCCC
GAGGAGTACGCGGGCGCGGACGACGTCTCCCAGTCGCCCGTCGCCGAGGAGCCGTCGTGG
GTGCCGAGTCCCAGGCCCCCGGTGCCCCACGAGTCCCCAGAGCCTCCTTCGGGCCGCTCG
CTGGTGCAGCGGGACATCCAGGCCTTCCTGAACCAGTGCGGGGCCAGCCCTGGGGAGGCG
CGCCACTGGCTCACGCAGTTCCAGACCTGCCATCACTCCGCGGACAAGCCCTTCGCCGTC
ATCGAGGTGGACGAGGAGGTGCTCAAGTGCCAGCAGGGCGTATCCAGTCTGGCCTTTGCC
CTGGCCTTCTTGCAGCGCATGGACATGAAGCCGCTGGTGGTCCTGGGGCTGCCGGCCCCT
ACGGCTCCCTCGGGCTGTCTTTCCTTCTGGGAGGCCAAGGCGCAGCTGGCCAAGAGCTGC
AAGGTGCTGGTAGACGCGCTTCGACACAACGCCGCCGCTGCTGTGCCATTTTTTGGCGGC
GGGTCTGTGCTACGCGCTGCCGAGCCGGCTCCCCATGCCAGCTACGGCGGCATCGTCTCG
GTGGAGACAGACCTGCTGCAGTGGTGCCTGGAGTCGGGCAGCATCCCCATCCTGTGCCCC
ATCGGGGAGACGGCCGCGCGCCGCTCCGTGCTTCTCGACTCCCTGGAGGTGACCGCGTCG
CTGGCCAAGGCGCTGCGGCCCACCAAAATCATCTTCCTCAATAACACAGGCGGCCTGCGC
GACAGCAGTCATAAGGTCCTGAGTAACGTGAACCTGCCCGCCGACCTGGACCTGGTGTGC
AACGCCGAGTGGGTGAGCACAAAAGAACGGCAGCAGATGCGGCTCATCGTGGACGTGCTC
AGCCGCCTGCCCCACCACTCCTCGGCCGTCATCACCGCCGCTAGCACGCTGCTCACTGAG
CTCTTTAGCAACAAGGGGTCCGGGACCCTGTTCAAGAACGCCGAGCGAATGCTACGGGTG
CGCAGCCTGGACAAGCTGGACCAGGGCCGTCTAGTGGACCTGGTCAACGCCAGCTTCGGC
AAGAAGCTCAGGGACGACTACCTGGCCTCGCTGCGCCCGCGGCTGCACTCCATCTACGTC
TCCGAGGGGTACAACGCCGCCGCCATTCTGACCATGGAGCCCGTCCTGGGGGGCACCCCG
TACCTGGACAAATTTGTGGTGAGCTCCAGCCGCCAGGGCCAAGGCTCCGGCCAGATGCTG
TGGGAGTGCCTGCGGCGGGACCTTCAGACACTTTTCTGGCGCTCCCGGGTCACCAACCCC
ATCAATCCCTGGTACTTCAAACACAGTGATGGCAGCTTCTCCAACAAGCAGTGGATCTTC
TTCTGGTTTGGCCTGGCTGATATCCGGGACTCCTATGAGTTGGTCAACCACGCCAAGGGA
CTGCCAGACTCCTTTCACAAGCCAGCTTCTGACCCAGGCAGCTGA
|
| Enzyme 58 GenBank Gene ID |
AY116538  |
| Enzyme 58 GeneCard ID |
NAGS  |
| Enzyme 58 GenAtlas ID |
NAGS  |
| Enzyme 58 HGNC ID |
HGNC:17996  |
| Enzyme 58 Chromosome Location |
1 |
| Enzyme 58 Locus |
17q21.31 |
| Enzyme 58 SNPs |
SNPJam Report  |
| Enzyme 58 General References |
- Haberle J, Schmidt E, Pauli S, Kreuder JG, Plecko B, Galler A, Wermuth B, Harms E, Koch HG: Mutation analysis in patients with N-acetylglutamate synthase deficiency. Hum Mutat. 2003 Jun;21(6):593-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Caldovic L, Morizono H, Gracia Panglao M, Gallegos R, Yu X, Shi D, Malamy MH, Allewell NM, Tuchman M: Cloning and expression of the human N-acetylglutamate synthase gene. Biochem Biophys Res Commun. 2002 Dec 13;299(4):581-6. [PubMed
]
- Schmidt E, Nuoffer JM, Haberle J, Pauli S, Guffon N, Vianey-Saban C, Wermuth B, Koch HG: Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies. Biochim Biophys Acta. 2005 Apr 15;1740(1):54-9. Epub 2005 Feb 24. [PubMed
]
|
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
5821 |
| Enzyme 59 Name |
Bile acid-CoA:amino acid N-acyltransferase |
| Enzyme 59 Synonyms |
- BACAT
- BAT
- Glycine N-choloyltransferase
- Long-chain fatty-acyl-CoA hydrolase
|
| Enzyme 59 Gene Name |
BAAT |
| Enzyme 59 Protein Sequence |
>Bile acid-CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
|
| Enzyme 59 Number of Residues |
418 |
| Enzyme 59 Molecular Weight |
46298.9 |
| Enzyme 59 Theoretical pI |
7.00 |
| Enzyme 59 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 59 General Function |
Involved in thiolester hydrolase activity |
| Enzyme 59 Specific Function |
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs |
| Enzyme 59 Pathways |
- Bile Acid Biosynthesis (map00120
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 59 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
Not Available |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
Q14032  |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
BAAT_HUMAN  |
| Enzyme 59 PDB ID |
Not Available |
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
|
| Enzyme 59 GenBank Gene ID |
L34081  |
| Enzyme 59 GeneCard ID |
BAAT  |
| Enzyme 59 GenAtlas ID |
BAAT  |
| Enzyme 59 HGNC ID |
HGNC:932  |
| Enzyme 59 Chromosome Location |
9 |
| Enzyme 59 Locus |
9q22.3 |
| Enzyme 59 SNPs |
SNPJam Report  |
| Enzyme 59 General References |
- Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Johnson MR, Barnes S, Kwakye JB, Diasio RB: Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J Biol Chem. 1991 Jun 5;266(16):10227-33. [PubMed
]
- Sfakianos MK, Wilson L, Sakalian M, Falany CN, Barnes S: Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. J Biol Chem. 2002 Dec 6;277(49):47270-5. Epub 2002 Sep 17. [PubMed
]
- O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE: The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J Biol Chem. 2003 Sep 5;278(36):34237-44. Epub 2003 Jun 16. [PubMed
]
- Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed
]
|
| Enzyme 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
5842 |
| Enzyme 60 Name |
Long-chain-fatty-acid--CoA ligase 4 |
| Enzyme 60 Synonyms |
- Long-chain acyl-CoA synthetase 4
- LACS 4
|
| Enzyme 60 Gene Name |
ACSL4 |
| Enzyme 60 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 4
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
|
| Enzyme 60 Number of Residues |
711 |
| Enzyme 60 Molecular Weight |
79187.4 |
| Enzyme 60 Theoretical pI |
8.51 |
| Enzyme 60 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 60 General Function |
Involved in catalytic activity |
| Enzyme 60 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates |
| Enzyme 60 Pathways |
|
| Enzyme 60 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
12669909  |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
O60488  |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
ACSL4_HUMAN  |
| Enzyme 60 PDB ID |
Not Available |
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>2136 bp
ATGAAACTTAAGCTAAATGTGCTCACCATTATTTTGCTGCCTGTCCACTTGTTAATAACA
ATATACAGTGCCCTTATATTTATTCCATGGTATTTTCTTACCAATGCCAAGAAGAAAAAC
GCTATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGC
TCTGTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGAT
AAATTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAA
ATCCTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTT
GGGAATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGT
GGACTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGG
GCCGAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTA
TATGCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTAT
CTGATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGT
TGTGTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAA
GGATTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTG
GGCATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGT
TCTACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACA
GGCCAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCT
TTGGCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATT
GGATATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAA
GGAGACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGA
ATTTATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTC
AAGATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGC
AATCTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTG
TCTGGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGC
CCAATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTA
ACTGACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAA
GACTGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTA
ATTGGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGAT
TATTCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCAT
CCCGATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGA
GAGTATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAAC
ATCTGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAG
AAAAGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGC
AATAATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATG
AAATTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCT
GAAACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTAC
CTCAAAGACATTGAACGAATGTATGGGGGCAAATAA
|
| Enzyme 60 GenBank Gene ID |
NM_022977.2  |
| Enzyme 60 GeneCard ID |
ACSL4  |
| Enzyme 60 GenAtlas ID |
ACSL4  |
| Enzyme 60 HGNC ID |
HGNC:3571  |
| Enzyme 60 Chromosome Location |
Not Available |
| Enzyme 60 Locus |
Not Available |
| Enzyme 60 SNPs |
SNPJam Report  |
| Enzyme 60 General References |
- Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed
]
- Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
5849 |
| Enzyme 61 Name |
Long-chain-fatty-acid--CoA ligase 1 |
| Enzyme 61 Synonyms |
- Acyl-CoA synthetase 1
- ACS1
- Long-chain acyl-CoA synthetase 1
- LACS 1
- Long-chain acyl-CoA synthetase 2
- LACS 2
- Long-chain fatty acid-CoA ligase 2
- Palmitoyl-CoA ligase 1
- Palmitoyl-CoA ligase 2
|
| Enzyme 61 Gene Name |
ACSL1 |
| Enzyme 61 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 1
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
|
| Enzyme 61 Number of Residues |
698 |
| Enzyme 61 Molecular Weight |
77942.7 |
| Enzyme 61 Theoretical pI |
7.16 |
| Enzyme 61 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 61 General Function |
Involved in catalytic activity |
| Enzyme 61 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate |
| Enzyme 61 Pathways |
|
| Enzyme 61 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
Not Available |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
P33121  |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
ACSL1_HUMAN  |
| Enzyme 61 PDB ID |
Not Available |
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>2097 bp
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
|
| Enzyme 61 GenBank Gene ID |
D10040  |
| Enzyme 61 GeneCard ID |
ACSL1  |
| Enzyme 61 GenAtlas ID |
ACSL1  |
| Enzyme 61 HGNC ID |
HGNC:3569  |
| Enzyme 61 Chromosome Location |
4 |
| Enzyme 61 Locus |
4q35 |
| Enzyme 61 SNPs |
SNPJam Report  |
| Enzyme 61 General References |
- Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed
]
- Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed
]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
5894 |
| Enzyme 62 Name |
Long-chain-fatty-acid--CoA ligase 6 |
| Enzyme 62 Synonyms |
- Long-chain acyl-CoA synthetase 6
- LACS 6
|
| Enzyme 62 Gene Name |
ACSL6 |
| Enzyme 62 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 6
MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
|
| Enzyme 62 Number of Residues |
697 |
| Enzyme 62 Molecular Weight |
77751.3 |
| Enzyme 62 Theoretical pI |
7.46 |
| Enzyme 62 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 62 General Function |
Involved in catalytic activity |
| Enzyme 62 Specific Function |
Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid |
| Enzyme 62 Pathways |
|
| Enzyme 62 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
5702202  |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
Q9UKU0  |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
ACSL6_HUMAN  |
| Enzyme 62 PDB ID |
Not Available |
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>2094 bp
ATGCAGACACAGGAGATCCTGAGGATACTGCGACTGCCTGAGCTAGGTGACTTGGAACAG
TTTTTCCGCAGCCTCTCGGCCACCACCCTCGTGAGTATGGGTGCCCTGGCTGCCATCCTT
GCCTACTGGTTCACTCAGCGGCCAAAGGCCTTGCAGCCGCCATGCAACCTCCTGATGCAG
TCAGAAGAAGTAGAGGACAGTGGCGGGGCACGGCGATCTGTGATTGGGTCTGGCCCTCAG
CTACTTACCCACTACTATGATGATGCCCGGACCATGTACCAGGTGTTCCGCCGTGGGCTT
AGCATCTCAGGGAATGGGCCCTGTCTTGGTTTCAGGAAGCCTAAGCAGCCTTACCAGTGG
CTGTCCTACCAGGAGGTGGCCGACAGGGCTGAATTTCTGGGGTCCGGACTTCTCCAGCAC
AATTGTAAAGCATGCACTGATCAGTTTATTGGTGTTTTTGCACAAAATCGGCCAGAGTGG
ATCATTGTGGAGCTGGCCTGCTACACATATTCCATGGTGGTGGTCCCGCTCTATGACACC
CTGGGCCCTGGGGCTATCCGCTACATCATCAATACAGCGGACATCAGCACCGTGATTGTG
GACAAACCTCAGAAGGCTGTGCTTCTGCTAGAGCATGTGGAGAGGAAGGAGACTCCAGGC
CTCAAGCTGATCATCCTCATGGACCCATTCGAAGAAGCCCTGAAAGAGAGAGGGCAGAAG
TGCGGGGTGGTCATTAAGTCCATGCAGGCCGTGGAGGACTGTGGCCAAGAGAATCACCAG
GCTCCTGTGCCCCCGCAGCCTGATGACCTCTCCATTGTGTGTTTCACAAGCGGCACGACA
GGGAACCCAAAAGGTGCGATGCTCACCCATGGGAACGTGGTGGCTGATTTCTCAGGCTTT
CTGAAAGTGACAGAGAGTCAGTGGGCTCCCACTTGTGCGGATGTGCACATTTCCTATTTG
CCTTTAGCACACATGTTTGAGCGAATGGTGCAGTCTGTCGTCTATTGCCACGGAGGGCGT
GTTGGCTTCTTCCAGGGAGATATCCGCCTTCTCTCAGATGACATGAAGGCTCTATGCCCC
ACCATCTTCCCTGTGGTCCCACGACTGCTGAACCGGATGTACGACAAGATCTTCAGCCAG
GCAAACACACCATTAAAGCGCTGGCTCCTGGAGTTTGCAGCAAAGCGTAAGCAAGCCGAG
GTCCGGAGTGGAATCATCAGGAATGATAGTATCTGGGATGAACTCTTCTTTAATAAGATT
CAGGCCAGTCTTGGTGGGTGTGTGCGGATGATTGTTACTGGAGCAGCCCCAGCATCACCA
ACAGTTCTGGGATTTCTCCGGGCAGCTCTAGGGTGCCAGGTTTATGAAGGTTATGGCCAA
ACTGAGTGCACAGCTGGATGTACCTTCACCACTCCTGGCGACTGGACCTCAGGGCACGTA
GGGGCGCCACTTCCCTGCAATCATATCAAGCTCGTTGATGTTGAGGAACTGAACTACTGG
GCCTGCAAAGGAGAGGGAGAGATATGTGTGAGAGGACCAAATGTGTTCAAAGGCTACTTG
AAAGATCCAGACAGGACGAAGGAGGCCCTGGACAGCGATGGCTGGCTTCACACTGGAGAC
ATCGGAAAATGGCTGCCGGCAGGAACTCTTAAAATTATTGATCGGAAAAAGCATATATTT
AAACTTGCTCAGGGAGAATATGTTGCACCCGAGAAGATTGAGAACATCTACATCCGGAGC
CAACCTGTGGCGCAAATCTATGTCCATGGGGACAGCTTAAAGGCCTTTTTGGTAGGCATT
GTTGTGCCTGACCCTGAAGTTATGCCCTCCTGGGCCCAGAAGAGAGGAATTGAAGGAACA
TATGCAGATCTCTGCACAAATAAGGATCTGAAGAAAGCCATTTTGGAAGATATGGTGAGG
TTAGGAAAAGAAAGTGGACTCCATTCTTTTGAGCAGGTTAAAGCCATTCACATCCATTCT
GACATGTTCTCAGTTCAAAATGGCTTGCTGACCCCAACACTAAAAGCTAAGAGACCTGAG
CTGAGAGAGTACTTCAAAAAACAAATAGAAGAGCTTTACTCAATCCCCATGTGA
|
| Enzyme 62 GenBank Gene ID |
AF129166  |
| Enzyme 62 GeneCard ID |
ACSL6  |
| Enzyme 62 GenAtlas ID |
ACSL6  |
| Enzyme 62 HGNC ID |
HGNC:16496  |
| Enzyme 62 Chromosome Location |
5 |
| Enzyme 62 Locus |
5q31 |
| Enzyme 62 SNPs |
SNPJam Report  |
| Enzyme 62 General References |
- Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed
]
- Yagasaki F, Jinnai I, Yoshida S, Yokoyama Y, Matsuda A, Kusumoto S, Kobayashi H, Terasaki H, Ohyashiki K, Asou N, Murohashi I, Bessho M, Hirashima K: Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). Genes Chromosomes Cancer. 1999 Nov;26(3):192-202. [PubMed
]
- Soupene E, Kuypers FA: Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains. BMC Mol Biol. 2006 Jul 11;7:21. [PubMed
]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed
]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
5916 |
| Enzyme 63 Name |
Long-chain-fatty-acid--CoA ligase 5 |
| Enzyme 63 Synonyms |
- Long-chain acyl-CoA synthetase 5
- LACS 5
|
| Enzyme 63 Gene Name |
ACSL5 |
| Enzyme 63 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 5
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD
|
| Enzyme 63 Number of Residues |
683 |
| Enzyme 63 Molecular Weight |
75990.1 |
| Enzyme 63 Theoretical pI |
6.91 |
| Enzyme 63 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 63 General Function |
Involved in catalytic activity |
| Enzyme 63 Specific Function |
Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. It was suggested that it may also stimulate fatty acid oxidation. At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells |
| Enzyme 63 Pathways |
|
| Enzyme 63 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
6174680  |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
Q9ULC5  |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
ACSL5_HUMAN  |
| Enzyme 63 PDB ID |
Not Available |
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>2052 bp
ATGCTTTTTATCTTTAACTTTTTGTTTTCCCCACTTCCGACCCCGGCGTTGATCTGCATC
CTGACATTTGGAGCTGCCATCTTCTTGTGGCTGATCACCAGACCTCAACCCGTCTTACCT
CTTCTTGACCTGAACAATCAGTCTGTGGGAATTGAGGGAGGAGCACGGAAGGGGGTTTCC
CAGAAGAACAATGACCTAACAAGTTGCTGCTTCTCAGATGCCAAGACTATGTATGAGGTT
TTCCAAAGAGGACTCGCTGTGTCTGACAATGGGCCCTGCTTGGGATATAGAAAACCAAAC
CAGCCCTACAGATGGCTATCTTACAAACAGGTGTCTGATAGAGCAGAGTACCTGGGTTCC
TGTCTCTTGCATAAAGGTTATAAATCATCACCAGACCAGTTTGTCGGCATCTTTGCTCAG
AATAGGCCAGAGTGGATCATCTCCGAATTGGCTTGTTACACGTACTCTATGGTAGCTGTA
CCTCTGTATGACACCTTGGGACCAGAAGCCATCGTACATATTGTCAACAAGGCTGATATC
GCCATGGTGATCTGTGACACACCCCAAAAGGCATTGGTGCTGATAGGGAATGTAGAGAAA
GGCTTCACCCCGAGCCTGAAGGTGATCATCCTTATGGACCCCTTTGATGATGACCTGAAG
CAAAGAGGGGAGAAGAGTGGAATTGAGATCTTATCCCTATATGATGCTGAGAACCTAGGC
AAAGAGCACTTCAGAAAACCTGTGCCTCCTAGCCCAGAAGACCTGAGCGTCATCTGCTTC
ACCAGTGGGACCACAGGTGACCCCAAAGGAGCCATGATAACCCATCAAAATATTGTTTCA
AATGCTGCTGCCTTTCTCAAATGTGTGGAGCATGCTTATGAGCCCACTCCTGATGATGTG
GCCATATCCTACCTCCCTCTGGCTCATATGTTTGAGAGGATTGTACAGGCTGTTGTGTAC
AGCTGTGGAGCCAGAGTTGGATTCTTCCAAGGGGATATTCGGTTGCTGGCTGACGACATG
AAGACTTTGAAGCCCACATTGTTTCCCGCGGTGCCTCGACTCCTTAACAGGATCTACGAT
AAGGTACAAAATGAGGCCAAGACACCCTTGAAGAAGTTCTTGTTGAAGCTGGCTGTTTCC
AGTAAATTCAAAGAGCTTCAAAAGGGTATCATCAGGCATGATAGTTTCTGGGACAAGCTC
ATCTTTGCAAAGATCCAGGACAGCCTGGGCGGAAGGGTTCGTGTAATTGTCACTGGAGCT
GCCCCCATGTCCACTTCAGTCATGACATTCTTCCGGGCAGCAATGGGATGTCAGGTGTAT
GAAGCTTATGGTCAAACAGAATGCACAGGTGGCTGTACATTTACATTACCTGGGGACTGG
ACATCAGGTCACGTTGGGGTGCCCCTGGCTTGCAATTACGTGAAGCTGGAAGATGTGGCT
GACATGAACTACTTTACAGTGAATAATGAAGGAGAGGTCTGCATCAAGGGTACAAACGTG
TTCAAAGGATACCTGAAGGACCCTGAGAAGACACAGGAAGCCCTGGACAGTGATGGCTGG
CTTCACACAGGAGACATTGGTCGCTGGCTCCCGAATGGAACTCTGAAGATCATCGACCGT
AAAAAGAACATTTTCAAGCTGGCCCAAGGAGAATACATTGCACCAGAGAAGATAGAAAAT
ATCTACAACAGGAGTCAACCAGTGTTACAAATTTTTGTACACGGGGAGAGCTTACGGTCA
TCCTTAGTAGGAGTGGTGGTTCCTGACACAGATGTACTTCCCTCATTTGCAGCCAAGCTT
GGGGTGAAGGGCTCCTTTGAGGAACTGTGCCAAAACCAAGTTGTAAGGGAAGCCATTTTA
GAAGACTTGCAGAAAATTGGGAAAGAAAGTGGCCTTAAAACTTTTGAACAGGTCAAAGCC
ATTTTTCTTCATCCAGAGCCATTTTCCATTGAAAATGGGCTCTTGACACCAACATTGAAA
GCAAAGCGAGGAGAGCTTTCCAAATACTTTCGGACCCAAATTGACAGCCTGTATGAGCAC
ATCCAGGATTAG
|
| Enzyme 63 GenBank Gene ID |
AB033899  |
| Enzyme 63 GeneCard ID |
ACSL5  |
| Enzyme 63 GenAtlas ID |
ACSL5  |
| Enzyme 63 HGNC ID |
HGNC:16526  |
| Enzyme 63 Chromosome Location |
1 |
| Enzyme 63 Locus |
10q25.1-q25.2 |
| Enzyme 63 SNPs |
SNPJam Report  |
| Enzyme 63 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gassler N, Roth W, Funke B, Schneider A, Herzog F, Tischendorf JJ, Grund K, Penzel R, Bravo IG, Mariadason J, Ehemann V, Sykora J, Haas TL, Walczak H, Ganten T, Zentgraf H, Erb P, Alonso A, Autschbach F, Schirmacher P, Knuchel R, Kopitz J: Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing. Gastroenterology. 2007 Aug;133(2):587-98. Epub 2007 Jun 8. [PubMed
]
- Mashima T, Sato S, Okabe S, Miyata S, Matsuura M, Sugimoto Y, Tsuruo T, Seimiya H: Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide. Cancer Sci. 2009 Aug;100(8):1556-62. Epub 2009 May 13. [PubMed
]
- Mashima T, Sato S, Sugimoto Y, Tsuruo T, Seimiya H: Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions. Oncogene. 2009 Jan 8;28(1):9-19. Epub 2008 Sep 22. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
5919 |
| Enzyme 64 Name |
Long-chain-fatty-acid--CoA ligase 3 |
| Enzyme 64 Synonyms |
- Long-chain acyl-CoA synthetase 3
- LACS 3
|
| Enzyme 64 Gene Name |
ACSL3 |
| Enzyme 64 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 3
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
|
| Enzyme 64 Number of Residues |
720 |
| Enzyme 64 Molecular Weight |
80419.4 |
| Enzyme 64 Theoretical pI |
8.51 |
| Enzyme 64 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 64 General Function |
Involved in catalytic activity |
| Enzyme 64 Specific Function |
Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) |
| Enzyme 64 Pathways |
|
| Enzyme 64 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
17026088  |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
O95573  |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
ACSL3_HUMAN  |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>2163 bp
ATGAATAACCACGTGTCTTCAAAACCATCTACCATGAAGCTAAAACATACCATCAACCCT
ATTCTTTTATATTTTATACATTTTCTAATATCACTTTATACTATTTTAACATACATTCCG
TTTTATTTTTTCTCCGAGTCAAGACAAGAAAAATCAAACCGAATTAAAGCAAAGCCTGTA
AATTCAAAACCTGATTCTGCATACAGATCTGTTAATAGTTTGGATGGTTTGGCTTCAGTA
TTATACCCTGGATGTGATACTTTAGATAAAGTTTTTACATATGCAAAAAACAAATTTAAG
AACAAAAGACTCTTGGGAACACGTGAAGTTTTAAATGAGGAAGATGAAGTACAACCAAAT
GGAAAAATTTTTAAAAAGGTTATTCTTGGACAGTATAATTGGCTTTCCTATGAAGATGTC
TTTGTTCGAGCCTTTAATTTTGGAAATGGATTACAGATGTTGGGTCAGAAACCAAAGACC
AACATCGCCATCTTCTGTGAGACCAGGGCCGAGTGGATGATAGCTGCACAGGCGTGTTTT
ATGTATAATTTTCAGCTTGTTACATTATATGCCACTCTAGGAGGTCCAGCCATTGTTCAT
GCATTAAATGAAACAGAGGTGACCAACATCATTACTAGTAAAGAACTCTTACAAACAAAG
TTGAAGGATATAGTTTCTTTGGTCCCACGCCTGCGGCACATCATCACTGTTGATGGAAAG
CCACCGACCTGGTCCGACTTCCCCAAGGGCATCATTGTGCATACCATGGCTGCAGTGGAG
GCCCTGGGAGCCAAGGCCAGCATGGAAAACCAACCTCATAGCAAACCATTGCCCTCAGAT
ATTGCAGTAATCATGTACACAAGTGGATCCACAGGACTTCCAAAGGGAGTCATGATCTCA
CATAGTAACATTATTGCTGGTATAACTGGGATGGCAGAAAGGATTCCAGAACTAGGAGAG
GAAGATGTCTACATTGGATATTTGCCTCTGGCCCATGTTCTAGAATTAAGTGCTGAGCTT
GTCTGTCTTTCTCACGGATGCCGCATTGGTTACTCTTCACCACAGACTTTAGCAGATCAG
TCTTCAAAAATTAAAAAAGGAAGCAAAGGGGATACATCCATGTTGAAACCAACACTGATG
GCAGCAGTTCCGGAAATCATGGATCGGATCTACAAAAATGTCATGAATAAAGTCAGTGAA
ATGAGTAGTTTTCAACGTAATCTGTTTATTCTGGCCTATAATTACAAAATGGAACAGATT
TCAAAAGGACGTAATACTCCACTGTGCGACAGCTTTGTTTTCCGGAAAGTTCGAAGCTTG
CTAGGGGGAAATATTCGTCTCCTGTTGTGTGGTGGCGCTCCACTTTCTGCAACCACGCAG
CGATTCATGAACATCTGTTTCTGCTGTCCTGTTGGTCAGGGATACGGGCTCACTGAATCT
GCTGGGGCTGGAACAATTTCCGAAGTGTGGGACTACAATACTGGCAGAGTGGGAGCACCA
TTAGTTTGCTGTGAAATCAAATTAAAAAACTGGGAGGAAGGTGGATACTTTAATACTGAT
AAGCCACACCCCAGGGGTGAAATTCTTATTGGGGGCCAAAGTGTGACAATGGGGTACTAC
AAAAATGAAGCAAAAACAAAAGCTGATTTCTCTGAAGATGAAAATGGACAAAGGTGGCTC
TGTACTGGGGATATTGGAGAGTTTGAACCCGATGGATGCTTAAAGATTATTGATCGTAAA
AAGGACCTTGTAAAACTACAGGCAGGGGAATATGTTTCTCTTGGGAAAGTAGAGGCAGCT
TTGAAGAATCTTCCACTAGTAGATAACATTTGTGCATATGCAAACAGTTATCATTCTTAT
GTCATTGGATTTGTTGTGCCAAATCAAAAGGAACTAACTGAACTAGCTCGAAAGAAAGGA
CTTAAAGGGACTTGGGAGGAGCTGTGTAACAGTTGTGAAATGGAAAATGAGGTACTTAAA
GTGCTTTCCGAAGCTGCTATTTCAGCAAGTCTGGAAAAGTTTGAAATTCCAGTAAAAATT
CGTTTGAGTCCTGAACCGTGGACCCCTGAAACTGGTCTGGTGACAGATGCCTTCAAGCTG
AAACGCAAAGAGCTTAAAACACATTACCAGGCGGACATTGAGCGAATGTATGGAAGAAAA
TAA
|
| Enzyme 64 GenBank Gene ID |
AB061436  |
| Enzyme 64 GeneCard ID |
ACSL3  |
| Enzyme 64 GenAtlas ID |
ACSL3  |
| Enzyme 64 HGNC ID |
HGNC:3570  |
| Enzyme 64 Chromosome Location |
2 |
| Enzyme 64 Locus |
2q34-q35 |
| Enzyme 64 SNPs |
SNPJam Report  |
| Enzyme 64 General References |
- Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT: Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. Genomics. 1997 May 15;42(1):180-1. [PubMed
]
- Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT: Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 2001 Oct 31;278(1-2):185-92. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Yao H, Ye J: Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells. J Biol Chem. 2008 Jan 11;283(2):849-54. Epub 2007 Nov 14. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
6119 |
| Enzyme 65 Name |
Glycerol-3-phosphate acyltransferase 1, mitochondrial |
| Enzyme 65 Synonyms |
- GPAT-1
|
| Enzyme 65 Gene Name |
GPAM |
| Enzyme 65 Protein Sequence |
>Glycerol-3-phosphate acyltransferase 1, mitochondrial
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKR
PFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDV
HKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVAT
VSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLT
FILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHI
VELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRII
EGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSA
LLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSC
AIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLL
GNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLG
GPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAE
HDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITF
LQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVK
NAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
|
| Enzyme 65 Number of Residues |
828 |
| Enzyme 65 Molecular Weight |
93793.9 |
| Enzyme 65 Theoretical pI |
7.78 |
| Enzyme 65 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 65 General Function |
Involved in acyltransferase activity |
| Enzyme 65 Specific Function |
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis |
| Enzyme 65 Pathways |
|
| Enzyme 65 Reactions |
- acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
|
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
190358539  |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
Q9HCL2  |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
GPAT1_HUMAN  |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>2487 bp
ATGGATGAATCTGCACTGACCCTTGGTACAATAGATGTTTCTTATCTGCCACATTCATCA
GAATACAGTGTTGGTCGATGTAAGCACACAAGTGAGGAATGGGGTGAGTGTGGCTTTAGA
CCCACCATCTTCAGATCTGCAACTTTAAAATGGAAAGAAAGCCTAATGAGTCGGAAAAGG
CCATTTGTTGGAAGATGTTGTTACTCCTGCACTCCCCAGAGCTGGGACAAATTTTTCAAC
CCCAGTATCCCGTCTTTGGGTTTGCGGAATGTTATTTATATCAATGAAACTCACACAAGA
CACCGCGGATGGCTTGCAAGACGCCTTTCTTACGTTCTTTTTATTCAAGAGCGAGATGTG
CATAAGGGCATGTTTGCCACCAATGTGACTGAAAATGTGCTGAACAGCAGTAGAGTACAA
GAGGCAATTGCAGAAGTGGCTGCTGAATTAAACCCTGATGGTTCTGCCCAGCAGCAATCA
AAAGCCGTTAACAAAGTGAAAAAGAAAGCTAAAAGGATTCTTCAAGAAATGGTTGCCACT
GTCTCACCGGCAATGATCAGACTGACTGGGTGGGTGCTGCTAAAACTGTTCAACAGCTTC
TTTTGGAACATTCAAATTCACAAAGGTCAACTTGAGATGGTTAAAGCTGCAACTGAGACG
AATTTGCCGCTTCTGTTTCTACCAGTTCATAGATCCCATATTGACTATCTGCTGCTCACT
TTCATTCTCTTCTGCCATAACATCAAAGCACCATACATTGCTTCAGGCAATAATCTCAAC
ATCCCAATCTTCAGTACCTTGATCCATAAGCTTGGGGGCTTCTTCATACGACGAAGGCTC
GATGAAACACCAGATGGACGGAAAGATGTTCTCTATAGAGCTTTGCTCCATGGGCATATA
GTTGAATTACTTCGACAGCAGCAATTCTTGGAGATCTTCCTGGAAGGCACACGTTCTAGG
AGTGGAAAAACCTCTTGTGCTCGGGCAGGACTTTTGTCAGTTGTGGTAGATACTCTGTCT
ACCAATGTCATCCCAGACATCTTGATAATACCTGTTGGAATCTCCTATGATCGCATTATC
GAAGGTCACTACAATGGTGAACAACTGGGCAAACCTAAGAAGAATGAGAGCCTGTGGAGT
GTAGCAAGAGGTGTTATTAGAATGTTACGAAAAAACTATGGTTGTGTCCGAGTGGATTTT
GCACAGCCATTTTCCTTAAAGGAATATTTAGAAAGCCAAAGTCAGAAACCGGTGTCTGCT
CTACTTTCCCTGGAGCAAGCGTTGTTACCAGCTATACTTCCTTCAAGACCCAGTGATGCT
GCTGATGAAGGTAGAGACACGTCCATTAATGAGTCCAGAAATGCAACAGATGAATCCCTA
CGAAGGAGGTTGATTGCAAATCTGGCTGAGCATATTCTATTCACTGCTAGCAAGTCCTGT
GCCATTATGTCCACACACATTGTGGCTTGCCTGCTCCTCTACAGACACAGGCAGGGAATT
GATCTCTCCACATTGGTCGAAGACTTCTTTGTGATGAAAGAGGAAGTCCTGGCTCGTGAT
TTTGACCTGGGGTTCTCAGGAAATTCAGAAGATGTAGTAATGCATGCCATACAGCTGCTG
GGAAATTGTGTCACAATCACCCACACTAGCAGGAACGATGAGTTTTTTATCACCCCCAGC
ACAACTGTCCCATCAGTCTTCGAACTCAACTTCTACAGCAATGGGGTACTTCATGTCTTT
ATCATGGAGGCCATCATAGCTTGCAGCCTTTATGCAGTTCTGAACAAGAGGGGACTGGGG
GGTCCCACTAGCACCCCACCTAACCTGATCAGCCAGGAGCAGCTGGTGCGGAAGGCGGCC
AGCCTGTGCTACCTTCTCTCCAATGAAGGCACCATCTCACTGCCTTGCCAGACATTTTAC
CAAGTCTGCCATGAAACAGTAGGAAAGTTTATCCAGTATGGCATTCTTACAGTGGCAGAG
CACGATGACCAGGAAGATATCAGTCCTAGTCTTGCTGAGCAGCAGTGGGACAAGAAGCTT
CCAGAACCTTTGTCTTGGAGAAGTGATGAAGAAGATGAAGACAGTGACTTTGGGGAGGAA
CAGCGAGATTGCTACCTGAAGGTGAGCCAATCCAAGGAGCACCAGCAGTTTATCACCTTC
TTACAGAGACTCCTTGGGCCTTTGCTGGAGGCCTACAGCTCTGCTGCCATCTTTGTTCAC
AACTTCAGTGGTCCTGTTCCAGAACCTGAGTATCTGCAAAAGTTGCACAAATACCTAATA
ACCAGAACAGAAAGAAATGTTGCAGTATATGCTGAGAGTGCCACATATTGTCTTGTGAAG
AATGCTGTGAAAATGTTTAAGGATATTGGGGTTTTCAAGGAGACCAAACAAAAGAGAGTG
TCTGTTTTAGAACTGAGCAGCACTTTTCTACCTCAATGCAACCGACAAAAACTTCTAGAA
TATATTCTGAGTTTTGTGGTGCTGTAG
|
| Enzyme 65 GenBank Gene ID |
NM_020918.4  |
| Enzyme 65 GeneCard ID |
GPAM  |
| Enzyme 65 GenAtlas ID |
GPAM  |
| Enzyme 65 HGNC ID |
HGNC:24865  |
| Enzyme 65 Chromosome Location |
1 |
| Enzyme 65 Locus |
10q25.2 |
| Enzyme 65 SNPs |
SNPJam Report  |
| Enzyme 65 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G: AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase. J Biol Chem. 2008 Apr 11;283(15):10048-57. Epub 2008 Jan 31. [PubMed
]
- Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed
]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
6298 |
| Enzyme 66 Name |
Trans-2-enoyl-CoA reductase, mitochondrial |
| Enzyme 66 Synonyms |
- Nuclear receptor-binding factor 1
- HsNrbf-1
- NRBF-1
|
| Enzyme 66 Gene Name |
MECR |
| Enzyme 66 Protein Sequence |
>Trans-2-enoyl-CoA reductase, mitochondrial
MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVEL
KNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGLLPELPAVGGNEGVAQVVAVGSNVT
GLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ
LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEE
ELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLL
IFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS
MKPFISSKQILTM
|
| Enzyme 66 Number of Residues |
373 |
| Enzyme 66 Molecular Weight |
40427.4 |
| Enzyme 66 Theoretical pI |
9.01 |
| Enzyme 66 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- oxidoreductase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 66 General Function |
Involved in zinc ion binding |
| Enzyme 66 Specific Function |
Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids |
| Enzyme 66 Pathways |
Not Available |
| Enzyme 66 Reactions |
- acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
|
| Enzyme 66 Pfam Domain Function |
|
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
4929595  |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q9BV79  |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
MECR_HUMAN  |
| Enzyme 66 PDB ID |
Not Available |
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>1122 bp
ATGTGGGTCTGCAGTACCCTGTGGCGGGTGCGAACCCCGCCCGGCAGTGGCGGGGGCCTG
CTCCCAGCTTCTGGCTGTCACGGACCTGCCGCCTCCTCCTACTCCGCATCCGCCGAGCCT
GCCCGGGTCCGCGGCGTTGTCTATGGGCACCACGGGGATCCAGCCAAGGTCGTCGAACTC
AAGAACCTGGAGCTAGCTGCTGTGAGAGGATCAGATGTCCGTGTGAAGATGCTGGCGGCC
CCTATCAATCCATCTGACATAAATATGATCCAAGGAAACTACGGACTCCTTCCTGAACTG
CCTGCTGTTGGAGGGAACGAAGGTGTTGCACAGGTGGTAGCGGTGGGCAGCAATGTGACC
GGGCTGAAGCCAGGAGACTGGGTGATTCCAGCAAATGCTGGTTTAGGAACCTGGCGGACC
GAGGCTGTGTTCAGCGAGGAAGCACTGATCCAAGTTCCGAGTGACATCCCTCTTCAGAGC
GCTGCCACCCTGGGTGTCAATCCCTGCACAGCCTACAGGATGTTGATGGACTTCGAGCAA
CTGCAGCCAGGGGATTCTGTCATCCAGAATGCATCCAACAGCGGAGTGGGGCAAGCGGTC
ATCCAGATCGCCGCAGCCCTGGGCCTAAGAACCATCAATGTGGTCCGAGACAGACCTGAT
ATCCAGAAGCTGAGTGACAGACTGAAGAGTCTGGGGGCTGAGCATGTCATCACAGAAGAG
GAGCTAAGAAGGCCCGAAATGAAAAACTTCTTTAAGGACATGCCCCAGCCACGGCTTGCT
CTCAACTGTGTTGGTGGGAAAAGCTCCACAGAGCTGCTGCGCCAGTTAGCGCGTGGAGGA
ACCATGGTAACCTATGGGGGGATGGCCAAGCAGCCCGTCGTAGCCTCTGTGAGCCTGCTC
ATTTTTAAGGATCTCAAACTTCGAGGCTTTTGGTTGTCCCAGTGGAAGAAGGATCACAGT
CCAGACCAGTTCAAGGAGCTGATCCTCACACTGTGCGATCTCATCCGCCGAGGCCAGCTC
ACAGCCCCTGCCTGCTCCCAGGTCCCGCTGCAGGACTACCAGTCTGCCTTGGAAGCCTCC
ATGAAGCCCTTCATATCTTCAAAGCAGATTCTCACCATGTGA
|
| Enzyme 66 GenBank Gene ID |
AF151821  |
| Enzyme 66 GeneCard ID |
MECR  |
| Enzyme 66 GenAtlas ID |
MECR  |
| Enzyme 66 HGNC ID |
HGNC:19691  |
| Enzyme 66 Chromosome Location |
1 |
| Enzyme 66 Locus |
1p36.1-p35.1 |
| Enzyme 66 SNPs |
SNPJam Report  |
| Enzyme 66 General References |
- Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Miinalainen IJ, Chen ZJ, Torkko JM, Pirila PL, Sormunen RT, Bergmann U, Qin YM, Hiltunen JK: Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J Biol Chem. 2003 May 30;278(22):20154-61. Epub 2003 Mar 24. [PubMed
]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
6299 |
| Enzyme 67 Name |
Peroxisomal trans-2-enoyl-CoA reductase |
| Enzyme 67 Synonyms |
- TERP
- 2,4-dienoyl-CoA reductase-related protein
- DCR-RP
- HPDHase
- pVI-ARL
|
| Enzyme 67 Gene Name |
PECR |
| Enzyme 67 Protein Sequence |
>Peroxisomal trans-2-enoyl-CoA reductase
MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAD
ELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHIS
SKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYN
LTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVS
SVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEK
AKL
|
| Enzyme 67 Number of Residues |
303 |
| Enzyme 67 Molecular Weight |
32544.1 |
| Enzyme 67 Theoretical pI |
9.12 |
| Enzyme 67 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
|
| Process |
- biological regulation
- metabolic process
- oxidation reduction
- regulation of apoptosis
- regulation of biological process
- regulation of cell death
- regulation of cellular process
- regulation of programmed cell death
|
| Component |
| — |
|
| Enzyme 67 General Function |
Involved in regulation of apoptosis |
| Enzyme 67 Specific Function |
Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity |
| Enzyme 67 Pathways |
Not Available |
| Enzyme 67 Reactions |
- acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
|
| Enzyme 67 Pfam Domain Function |
|
| Enzyme 67 Signals |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
Not Available |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
Q9BY49  |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
PECR_HUMAN  |
| Enzyme 67 PDB ID |
1YXM  |
| Enzyme 67 PDB File |
Show |
| Enzyme 67 3D Structure |
|
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>912 bp
ATGGCCTCCTGGGCTAAGGGCAGGAGCTACCTGGCGCCTGGTTTGCTGCAGGGCCAAGTG
GCCATCGTCACCGGCGGGGCCACGGGCATCGGAAAAGCCATCGTGAAGGAGCTCCTGGAG
CTGGGGAGTAATGTGGTCATTGCATCCCGTAAGTTGGAGAGATTGAAGTCTGCGGCAGAT
GAACTGCAGGCCAACCTACCTCCCACAAAGCAGGCACGAGTCATTCCCATACAATGCAAC
ATCCGGAATGAGGAGGAGGTGAATAATTTGGTCAAATCTACCTTAGATACTTTTGGTAAG
ATCAATTTCTTGGTGAACAATGGAGGAGGCCAGTTTCTTTCCCCTGCTGAACACATCAGT
TCTAAGGGATGGCACGCTGTGCTTGAGACCAACCTGACGGGTACCTTCTACATGTGCAAA
GCAGTTTACAGCTCCTGGATGAAAGAGCATGGAGGATCTATCGTCAATATCATTGTCCCT
ACTAAAGCTGGATTTCCATTAGCTGTGCATTCTGGAGCTGCAAGAGCAGGTGTTTACAAC
CTCACCAAATCTTTAGCTTTGGAATGGGCCTGCAGTGGAATACGGATCAATTGTGTTGCC
CCTGGAGTTATTTATTCCCAGACTGCTGTGGAGAACTATGGTTCCTGGGGACAAAGCTTC
TTTGAAGGGTCTTTTCAGAAAATCCCCGCTAAACGAATTGGTGTTCCTGAGGAGGTCTCC
TCTGTGGTCTGCTTCCTACTGTCTCCTGCAGCTTCCTTCATCACTGGACAGTCAGTGGAT
GTGGATGGGGGCCGGAGTCTCTATACTCACTCGTATGAGGTACCAGATCATGACAACTGG
CCCAAGGGAGCAGGGGACCTTTCTGTTGTCAAAAAGATGAAGGAGACCTTTAAGGAGAAA
GCTAAGCTCTGA
|
| Enzyme 67 GenBank Gene ID |
AF232009  |
| Enzyme 67 GeneCard ID |
PECR  |
| Enzyme 67 GenAtlas ID |
PECR  |
| Enzyme 67 HGNC ID |
HGNC:18281  |
| Enzyme 67 Chromosome Location |
2 |
| Enzyme 67 Locus |
2q35 |
| Enzyme 67 SNPs |
SNPJam Report  |
| Enzyme 67 General References |
- Das AK, Uhler MD, Hajra AK: Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J Biol Chem. 2000 Aug 11;275(32):24333-40. [PubMed
]
- Amery L, Mannaerts GP, Subramani S, Van Veldhoven PP, Fransen M: Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology. Comb Chem High Throughput Screen. 2001 Nov;4(7):545-52. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Braastad CD, Leguia M, Hendrickson EA: Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element. Nucleic Acids Res. 2002 Apr 15;30(8):1713-24. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
6335 |
| Enzyme 68 Name |
Cytosolic acyl coenzyme A thioester hydrolase |
| Enzyme 68 Synonyms |
- Acyl-CoA thioesterase 7
- Brain acyl-CoA hydrolase
- CTE-IIa
- CTE-II
- Long chain acyl-CoA thioester hydrolase
|
| Enzyme 68 Gene Name |
ACOT7 |
| Enzyme 68 Protein Sequence |
>Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
|
| Enzyme 68 Number of Residues |
380 |
| Enzyme 68 Molecular Weight |
41795.8 |
| Enzyme 68 Theoretical pI |
8.66 |
| Enzyme 68 GO Classification |
Not Available |
| Enzyme 68 General Function |
Lipid transport and metabolism |
| Enzyme 68 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA |
| Enzyme 68 Pathways |
Not Available |
| Enzyme 68 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
32528282  |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
O00154  |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
BACH_HUMAN  |
| Enzyme 68 PDB ID |
Not Available |
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>1143 bp
ATGAAGCTGCTTGCCAGGGCTCTCCGGCTCTGTGAGTTTGGGAGGCAGGCATCTTCCAGG
AGGCTGGTGGCTGGCCAGGGATGTGTGGGGCCCCGGCGAGGGTGCTGCGCTCCCGTCCAG
GTGGTTGGGCCCAGGGCTGATCTCCCACCCTGTGGAGCCTGCATTACTGGAAGGATCATG
CGGCCAGATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATC
GAGGAGGCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGT
GTGGCCGCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAG
GTGGCGCATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTC
AACGTGATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTG
TGGTATGTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTG
TATTCCCGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAG
CGCATGGAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCG
AACACTGTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACC
CTGCACGGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATC
GTGGCTGCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTT
CATGACAAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGC
AATAAGTCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAG
AAGCGCTACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGG
TCGCTGCCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAA
GGCAAAGGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCC
TAG
|
| Enzyme 68 GenBank Gene ID |
NM_181864.2  |
| Enzyme 68 GeneCard ID |
ACOT7  |
| Enzyme 68 GenAtlas ID |
ACOT7  |
| Enzyme 68 HGNC ID |
HGNC:24157  |
| Enzyme 68 Chromosome Location |
1 |
| Enzyme 68 Locus |
1p36 |
| Enzyme 68 SNPs |
SNPJam Report  |
| Enzyme 68 General References |
- Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed
]
- Yamada J, Kuramochi Y, Takagi M, Watanabe T, Suga T: Human brain acyl-CoA hydrolase isoforms encoded by a single gene. Biochem Biophys Res Commun. 2002 Nov 22;299(1):49-56. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
6336 |
| Enzyme 69 Name |
Acyl-coenzyme A thioesterase 2, mitochondrial |
| Enzyme 69 Synonyms |
- Acyl-CoA thioesterase 2
- Acyl-coenzyme A thioester hydrolase 2a
- CTE-Ia
- Long-chain acyl-CoA thioesterase 2
- ZAP128
|
| Enzyme 69 Gene Name |
ACOT2 |
| Enzyme 69 Protein Sequence |
>Acyl-coenzyme A thioesterase 2, mitochondrial
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIP
SKV
|
| Enzyme 69 Number of Residues |
483 |
| Enzyme 69 Molecular Weight |
53218.0 |
| Enzyme 69 Theoretical pI |
8.62 |
| Enzyme 69 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 69 General Function |
Involved in thiolester hydrolase activity |
| Enzyme 69 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs |
| Enzyme 69 Pathways |
Not Available |
| Enzyme 69 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
7023514  |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
P49753  |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
ACOT2_HUMAN  |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>1452 bp
ATGTCTAACAAGCTTCTTTCTCCCCACCCCCATTCAGTTGTTCTCAGGTCTGAATTCAAA
ATGGCCTCATCTCCTGCTGTCCTTCGAGCGTCCCGGCTGTACCAATGGAGCCTGAAGAGT
TCGGCGCAGTTCCTGGGGTCTCCACAGCTGAGGCAGGTTGGTCAGATCATTAGGGTTCCT
GCTCGGATGGCGGCGACGCTGATCCTGGAGCCTGCGGGCCGCTGCTGCTGGGACGAACCG
GTGCGAATCGCCGTGCGCGGCCTAGCCCCGGAGCAGCCGGTCACGCTGCGCGCGTCCCTG
CGCGACGAGAAGGGCGCGCTTTTCCAGGCCCACGCGCGCTACCGCGCCGACACTCTTGGC
GAGCTGGACCTGGAGCGCGCGCCCGCGCTGGGCGGCAGCTTCGCGGGGCTTGAGCCCATG
GGGCTGCTCTGGGCCTTGGAGCCCGAGAAACCTTTGGTGCGGCTGGTGAAGCGCGACGTG
CGAACGCCCTTGGCCGTGGTGCTGGAGGTGCTGGATGGCCACGACCCCGACCCCGGGCGG
CTGCTGTGCCAGACGCGGCACGAGCGCTACTTCCTCCCGCCCGGGGTGCGGCGCGAGCCG
GTGCGCGTGGGCCGGGTGCGAGGCACGCTCTTCCTGCCGCCAGAACCTGGGCCCTTTCCT
GGGATTGTGGACATGTTCGGAACTGGAGGTGGCCTGCTGGAGTATCGGGCTAGTCTGCTG
GCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTATTATAACTATGAAGACCTCCCCAAG
ACCATGGAGACGCTCCATCTGGAGTACTTTGAAGAAGCCATGAACTACTTGCTCAGTCAT
CCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGGAATTTCCAAAGGGGGTGAGCTCTGC
CTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGCTGCTGTCGTCATCAACGGCTCTGTG
GCCAATGTTGGGGGAACCTTACGCTACAAGGGCGAGACCCTGCCCCCTGTGGGCGTCAAC
AGAAATCGCATCAAGGTGACCAAAGATGGCTATGCAGACATTGTGGATGTCCTGAACAGC
CCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCCTGTGGAAAGGGCAGAGAGCACCTTC
CTGTTCCTGGTAGGTCAGGATGACCACAACTGGAAGAGTGAGTTCTATGCTAATGAGGCC
TGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCCCCAGATCATCTGTTACCCAGAGACA
GGGCACTATATTGAGCCTCCTTACTTCCCCCTGTGTCGGGCTTCCCTGCATGCCTTGGTG
GGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGCTCATGCCATGGCTCAGGTGGATGCT
TGGAAACAACTCCAGACTTTCTTCCACAAACACTTGGGTGGCCGCGAGGGGACAATCCCA
TCAAAAGTGTAA
|
| Enzyme 69 GenBank Gene ID |
AK001939  |
| Enzyme 69 GeneCard ID |
ACOT2  |
| Enzyme 69 GenAtlas ID |
ACOT2  |
| Enzyme 69 HGNC ID |
HGNC:18431  |
| Enzyme 69 Chromosome Location |
1 |
| Enzyme 69 Locus |
14q24.3 |
| Enzyme 69 SNPs |
SNPJam Report  |
| Enzyme 69 General References |
- Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed
]
- Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
6337 |
| Enzyme 70 Name |
Acyl-coenzyme A thioesterase 4 |
| Enzyme 70 Synonyms |
- Acyl-CoA thioesterase 4
- PTE-2b
- Peroxisomal acyl coenzyme A thioester hydrolase Ib
- Peroxisomal long-chain acyl-CoA thioesterase Ib
- PTE-Ib
|
| Enzyme 70 Gene Name |
ACOT4 |
| Enzyme 70 Protein Sequence |
>Acyl-coenzyme A thioesterase 4
MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADARGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLL
CQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAG
HGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLS
MASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALV
GGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGH
YIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPK
L
|
| Enzyme 70 Number of Residues |
421 |
| Enzyme 70 Molecular Weight |
46326.1 |
| Enzyme 70 Theoretical pI |
8.16 |
| Enzyme 70 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 70 General Function |
Involved in thiolester hydrolase activity |
| Enzyme 70 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs |
| Enzyme 70 Pathways |
Not Available |
| Enzyme 70 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
187761341  |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q8N9L9  |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
ACOT4_HUMAN  |
| Enzyme 70 PDB ID |
Not Available |
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
>1266 bp
ATGTCAGCAACGCTGATCCTGGAGCCCCCAGGCCGCTGCTGCTGGAACGAGCCGGTGCGC
ATTGCCGTGCGCGGCCTGGCCCCGGAGCAGCGGGTTACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTCTTCCGGGCCCACGCGCGCTACTGCGCCGACGCCCGCGGCGAGCTG
GACCTGGAGCGCGCACCCGCGCTGGGCGGCAGCTTCGCGGGACTCGAGCCCATGGGGCTG
CTCTGGGCCCTGGAACCCGAGAAGCCTTTTTGGCGCTTCCTGAAGCGGGACGTACAGATT
CCTTTTGTCGTGGAGTTGGAGGTGCTGGACGGCCACGACCCCGAGCCTGGACGGCTGCTG
TGCCAGGCGCAGCACGAGCGCCACTTCCTCCCGCCAGGGGTGCGGCGCCAGTCGGTGCGA
GCGGGCCGGGTGCGCGCCACGCTCTTCCTGCCGCCAGGACCTGGACCCTTCCCAGGGATC
ATTGACATCTTTGGTATTGGAGGGGGCCTCTTGGAATATCGAGCCAGCCTCCTTGCTGGC
CATGGCTTTGCCACGTTGGCTCTAGCTTATTATAACTTTGAAGATCTCCCCAATAACATG
GACAACATATCCCTGGAGTACTTCGAAGAAGCCGTATGCTACATGCTTCAACATCCCCAG
GTAAAAGGCCCAGGCATTGGGCTTTTGGGCATTTCTCTAGGAGCTGATATTTGTCTCTCA
ATGGCCTCATTCTTGAAGAATGTCTCAGCCACAGTTTCCATCAATGGATCTGGGATCAGT
GGGAACACAGCCATCAACTATAAGCACAGTAGCATTCCACCATTGGGCTATGACCTGAGG
AGAATCAAGGTAGCTTTCTCAGGCCTCGTGGACATTGTGGATATAAGGAATGCTCTCGTA
GGAGGGTACAAGAACCCCAGCATGATTCCAATAGAGAAGGCCCAGGGGCCCATCCTGCTC
ATTGTTGGTCAGGATGACCATAACTGGAGAAGTGAGTTGTATGCCCAAACAGTCTCTGAA
CGGTTACAGGCCCATGGAAAGGAAAAACCCCAGATCATCTGTTACCCTGGGACTGGGCAT
TACATCGAGCCTCCTTACTTCCCCCTGTGCCCAGCTTCCCTTCACAGATTACTGAACAAA
CATGTTATATGGGGTGGGGAGCCCAGGGCTCATTCTAAGGCCCAGGAAGATGCCTGGAAG
CAAATTCTAGCCTTCTTCTGCAAACACCTGGGAGGTACCCAGAAAACAGCTGTCCCTAAA
TTGTAA
|
| Enzyme 70 GenBank Gene ID |
NM_152331.3  |
| Enzyme 70 GeneCard ID |
ACOT4  |
| Enzyme 70 GenAtlas ID |
ACOT4  |
| Enzyme 70 HGNC ID |
HGNC:19748  |
| Enzyme 70 Chromosome Location |
1 |
| Enzyme 70 Locus |
14q24.3 |
| Enzyme 70 SNPs |
SNPJam Report  |
| Enzyme 70 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed
]
|
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
6338 |
| Enzyme 71 Name |
Acyl-coenzyme A thioesterase 8 |
| Enzyme 71 Synonyms |
- Acyl-CoA thioesterase 8
- Choloyl-coenzyme A thioesterase
- HIV-Nef-associated acyl-CoA thioesterase
- PTE-2
- Peroxisomal acyl-coenzyme A thioester hydrolase 1
- PTE-1
- Peroxisomal long-chain acyl-CoA thioesterase 1
- Thioesterase II
- hACTE-III
- hACTEIII
- hTE
|
| Enzyme 71 Gene Name |
ACOT8 |
| Enzyme 71 Protein Sequence |
>Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
|
| Enzyme 71 Number of Residues |
319 |
| Enzyme 71 Molecular Weight |
35914.0 |
| Enzyme 71 Theoretical pI |
7.60 |
| Enzyme 71 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 71 General Function |
Involved in acyl-CoA thioesterase activity |
| Enzyme 71 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation |
| Enzyme 71 Pathways |
Not Available |
| Enzyme 71 Reactions |
- choloyl-CoA + H2O = cholate + CoA [RN:R07296]
|
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
Not Available |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
O14734  |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
ACOT8_HUMAN  |
| Enzyme 71 PDB ID |
Not Available |
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
|
| Enzyme 71 GenBank Gene ID |
AF014404  |
| Enzyme 71 GeneCard ID |
ACOT8  |
| Enzyme 71 GenAtlas ID |
ACOT8  |
| Enzyme 71 HGNC ID |
HGNC:15919  |
| Enzyme 71 Chromosome Location |
2 |
| Enzyme 71 Locus |
20q13.12 |
| Enzyme 71 SNPs |
SNPJam Report  |
| Enzyme 71 General References |
- Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed
]
- Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed
]
- Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ishizuka M, Toyama Y, Watanabe H, Fujiki Y, Takeuchi A, Yamasaki S, Yuasa S, Miyazaki M, Nakajima N, Taki S, Saito T: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp Cell Res. 2004 Jul 1;297(1):127-41. [PubMed
]
- Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
6839 |
| Enzyme 72 Name |
Dihydroxyacetone phosphate acyltransferase |
| Enzyme 72 Synonyms |
- DAP-AT
- DHAP-AT
- Acyl-CoA:dihydroxyacetonephosphateacyltransferase
- Glycerone-phosphate O-acyltransferase
|
| Enzyme 72 Gene Name |
GNPAT |
| Enzyme 72 Protein Sequence |
>Dihydroxyacetone phosphate acyltransferase
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVY
KGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIR
FCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDL
PVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEF
FLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGV
PKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSE
DMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFG
GFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSA
YRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGC
YLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQY
LAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATT
KLEEMLGCKTPIGKPATAKL
|
| Enzyme 72 Number of Residues |
680 |
| Enzyme 72 Molecular Weight |
77187.2 |
| Enzyme 72 Theoretical pI |
6.52 |
| Enzyme 72 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 72 General Function |
Lipid transport and metabolism |
| Enzyme 72 Specific Function |
Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate |
| Enzyme 72 Pathways |
|
| Enzyme 72 Reactions |
- acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate [RN:R01013]
|
| Enzyme 72 Pfam Domain Function |
|
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
3258645  |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
O15228  |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
GNPAT_HUMAN  |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
>2043 bp
ATGGAGTCTTCCAGTTCATCTAACTCTTATTTCTCCGTTGGCCCAACCAGTCCCAGCGCT
GTCGTGCTCCTCTACTCGAAGGAGCTCAAAAAGTGGGATGAGTTTGAAGATATTTTAGAA
GAGAGGAGGCATGTCAGTGACTTGAAATTTGCAATGAAATGCTACACACCTCTTGTCTAT
AAGGGAATTACTCCATGTAAACCAATTGATATTAAATGTAGTGTTCTCAATTCTGAGGAG
ATTCATTATGTCATTAAACAGCTTTCCAAGGAATCCCTTCAATCTGTGGATGTCCTCCGA
GAGGAAGTGAGTGAGATCTTAGATGAAATGAGTCACAAACTGCGTCTTGGAGCCATTCGG
TTTTGTGCCTTCACCCTGAGCAAAGTATTTAAACAAATTTTCTCGAAGGTGTGTGTAAAT
GAAGAAGGTATTCAGAAACTACAAAGAGCCATCCAGGAGCATCCTGTTGTTCTGCTGCCT
AGTCATCGAAGTTACATTGACTTCCTCATGTTGTCTTTTCTTCTATACAATTATGATTTG
CCTGTGCCAGTTATAGCAGCAGGAATGGACTTCCTGGGAATGAAAATGGTTGGTGAGCTG
CTACGAATGTCGGGTGCCTTTTTCATGCGGCGTACCTTTGGTGGCAATAAACTCTACTGG
GCTGTATTCTCTGAATATGTAAAAACTATGTTACGGAATGGTTATGCTCCTGTTGAATTT
TTCCTCGAAGGGACAAGAAGCCGCTCTGCCAAGACATTGACTCCTAAATTTGGTCTTCTG
AATATTGTGATGGAGCCATTTTTTAAAAGAGAAGTTTTTGATACCTACCTTGTCCCAATT
AGTATCAGTTATGATAAGATCTTGGAAGAAACTCTTTATGTGTATGAGCTTCTAGGGGTT
CCTAAACCAAAAGAATCTACAACTGGGTTGCTGAAAGCCAGAAAGATTCTCTCTGAAAAT
TTTGGAAGCATCCATGTGTACTTTGGAGATCCTGTGTCACTTCGATCTTTGGCAGCTGGG
AGGATGAGTCGGAGCTCATATAACTTGGTTCCAAGATACATTCCTCAGAAACAGTCTGAG
GACATGCATGCCTTTGTCACTGAAGTTGCCTACAAAATGGAGCTTCTGCAAATTGAAAAC
ATGGTTTTGAGCCCCTGGACCCTAATAGTTGCTGTTCTGCTTCAGAACCGGCCATCCATG
GACTTTGATGCTCTGGTGGAAAAGACTTTATGGCTAAAAGGCTTAACCCAGGCATTTGGA
GGGTTTCTCATTTGGCCTGATAATAAACCTGCTGAAGAAGTTGTCCCGGCCAGCATTCTT
CTGCATTCCAACATTGCCAGCCTTGTCAAAGACCAGGTGATTCTGAAAGTGGACTCCGGA
GACTCGGAAGTGGTCGATGGGCTTATGCTCCAGCACATCACTCTCCTCATGTGCTCAGCT
TATAGGAACCAGCTGCTCAACATTTTTGTGCGCCCATCCTTAGTAGCAGTAGCATTGCAG
ATGACACCAGGGTTCAGGAAAGAGGATGTCTACAGTTGCTTTCGCTTCCTACGTGATGTT
TTTGCAGATGAGTTCATCTTCCTTCCAGGAAACACACTAAAGGACTTTGAAGAAGGCTGT
TACCTGCTTTGTAAAAGTGAAGCCATACAAGTGACTACGAAAGACATCCTAGTTACAGAG
AAAGGAAATACTGTGTTAGAATTTTTAGTAGGACTCTTTAAACCTTTTGTGGAAAGCTAT
CAGATAATTTGCAAGTACCTTTTGAGTGAAGAAGAGGACCACTTCAGTGAGGAACAGTAC
TTGGCTGCAGTCAGAAAATTCACAAGTCAGCTTCTCGATCAAGGTACCTCTCAATGTTAT
GATGTATTATCTTCTGATGTGCAGAAAAACGCCTTAGCAGCCTGTGTGAGGCTCGGAGTA
GTGGAGAAGAAGAAGATAAATAATAACTGTATATTTAATGTGAATGAACCTGCCACAACC
AAATTAGAAGAAATGCTTGGTTGTAAGACACCAATAGGAAAACCAGCCACTGCAAAACTT
TAA
|
| Enzyme 72 GenBank Gene ID |
AF043937  |
| Enzyme 72 GeneCard ID |
GNPAT  |
| Enzyme 72 GenAtlas ID |
Not Available |
| Enzyme 72 HGNC ID |
Not Available |
| Enzyme 72 Chromosome Location |
1 |
| Enzyme 72 Locus |
1q42 |
| Enzyme 72 SNPs |
SNPJam Report  |
| Enzyme 72 General References |
- Thai TP, Heid H, Rackwitz HR, Hunziker A, Gorgas K, Just WW: Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase. FEBS Lett. 1997 Dec 29;420(2-3):205-11. [PubMed
]
- Ofman R, Hettema EH, Hogenhout EM, Caruso U, Muijsers AO, Wanders RJ: Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2. Hum Mol Genet. 1998 May;7(5):847-53. [PubMed
]
- Ofman R, Lajmir S, Wanders RJ: Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations. Biochem Biophys Res Commun. 2001 Mar 2;281(3):754-60. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Thai TP, Rodemer C, Jauch A, Hunziker A, Moser A, Gorgas K, Just WW: Impaired membrane traffic in defective ether lipid biosynthesis. Hum Mol Genet. 2001 Jan 15;10(2):127-36. [PubMed
]
|
| Enzyme 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
6873 |
| Enzyme 73 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma |
| Enzyme 73 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 3
- 1-AGP acyltransferase 3
- 1-AGPAT 3
- Lysophosphatidic acid acyltransferase gamma
- LPAAT-gamma
|
| Enzyme 73 Gene Name |
AGPAT3 |
| Enzyme 73 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
|
| Enzyme 73 Number of Residues |
376 |
| Enzyme 73 Molecular Weight |
43380.6 |
| Enzyme 73 Theoretical pI |
8.91 |
| Enzyme 73 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 73 General Function |
Involved in acyltransferase activity |
| Enzyme 73 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 73 Pathways |
|
| Enzyme 73 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
|
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
- 11-31
124-144
308-330
335-357
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
11611541  |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
Q9NRZ7  |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
PLCC_HUMAN  |
| Enzyme 73 PDB ID |
Not Available |
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>1131 bp
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCCTACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
|
| Enzyme 73 GenBank Gene ID |
AB040138  |
| Enzyme 73 GeneCard ID |
AGPAT3  |
| Enzyme 73 GenAtlas ID |
AGPAT3  |
| Enzyme 73 HGNC ID |
HGNC:326  |
| Enzyme 73 Chromosome Location |
2 |
| Enzyme 73 Locus |
21q22.3 |
| Enzyme 73 SNPs |
SNPJam Report  |
| Enzyme 73 General References |
- Leung DW: The structure and functions of human lysophosphatidic acid acyltransferases. Front Biosci. 2001 Aug 1;6:D944-53. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
|
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
6875 |
| Enzyme 74 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase beta |
| Enzyme 74 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 2
- 1-AGP acyltransferase 2
- 1-AGPAT 2
- Lysophosphatidic acid acyltransferase beta
- LPAAT-beta
|
| Enzyme 74 Gene Name |
AGPAT2 |
| Enzyme 74 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase beta
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
|
| Enzyme 74 Number of Residues |
278 |
| Enzyme 74 Molecular Weight |
30914.1 |
| Enzyme 74 Theoretical pI |
9.22 |
| Enzyme 74 GO Classification |
| Function |
- 1-acylglycerol-3-phosphate O-acyltransferase activity
- O-acyltransferase activity
- acylglycerol O-acyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 74 General Function |
Lipid transport and metabolism |
| Enzyme 74 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 74 Pathways |
|
| Enzyme 74 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
|
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
2282590  |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
O15120  |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
PLCB_HUMAN  |
| Enzyme 74 PDB ID |
Not Available |
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>837 bp
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
|
| Enzyme 74 GenBank Gene ID |
AF000237  |
| Enzyme 74 GeneCard ID |
AGPAT2  |
| Enzyme 74 GenAtlas ID |
Not Available |
| Enzyme 74 HGNC ID |
Not Available |
| Enzyme 74 Chromosome Location |
9 |
| Enzyme 74 Locus |
9q34.3 |
| Enzyme 74 SNPs |
SNPJam Report  |
| Enzyme 74 General References |
- Eberhardt C, Gray PW, Tjoelker LW: Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3. J Biol Chem. 1997 Aug 8;272(32):20299-305. [PubMed
]
- Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed
]
- West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Garg A: Acquired and inherited lipodystrophies. N Engl J Med. 2004 Mar 18;350(12):1220-34. [PubMed
]
- Agarwal AK, Arioglu E, De Almeida S, Akkoc N, Taylor SI, Bowcock AM, Barnes RI, Garg A: AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nat Genet. 2002 May;31(1):21-3. Epub 2002 Apr 22. [PubMed
]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
6877 |
| Enzyme 75 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha |
| Enzyme 75 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 1
- 1-AGP acyltransferase 1
- 1-AGPAT 1
- Lysophosphatidic acid acyltransferase alpha
- LPAAT-alpha
- Protein G15
|
| Enzyme 75 Gene Name |
AGPAT1 |
| Enzyme 75 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
|
| Enzyme 75 Number of Residues |
283 |
| Enzyme 75 Molecular Weight |
31716.3 |
| Enzyme 75 Theoretical pI |
9.75 |
| Enzyme 75 GO Classification |
| Function |
- 1-acylglycerol-3-phosphate O-acyltransferase activity
- O-acyltransferase activity
- acylglycerol O-acyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 75 General Function |
Involved in acyltransferase activity |
| Enzyme 75 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 75 Pathways |
|
| Enzyme 75 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
|
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
55961399  |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
Q99943  |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
PLCA_HUMAN  |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>852 bp
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
|
| Enzyme 75 GenBank Gene ID |
AL662828  |
| Enzyme 75 GeneCard ID |
AGPAT1  |
| Enzyme 75 GenAtlas ID |
AGPAT1  |
| Enzyme 75 HGNC ID |
HGNC:324  |
| Enzyme 75 Chromosome Location |
6 |
| Enzyme 75 Locus |
6p21.3 |
| Enzyme 75 SNPs |
SNPJam Report  |
| Enzyme 75 General References |
- West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed
]
- Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed
]
- Aguado B, Campbell RD: Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex. J Biol Chem. 1998 Feb 13;273(7):4096-105. [PubMed
]
- Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 2003 Dec;13(12):2621-36. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
6936 |
| Enzyme 76 Name |
Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 76 Synonyms |
- SBCAD
- 2-methyl branched chain acyl-CoA dehydrogenase
- 2-MEBCAD
- 2-methylbutyryl-coenzyme A dehydrogenase
- 2-methylbutyryl-CoA dehydrogenase
|
| Enzyme 76 Gene Name |
ACADSB |
| Enzyme 76 Protein Sequence |
>Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDE
EMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLS
TVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAG
AGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRD
TPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQ
MLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAG
KPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ
LNTIAKHIDAEY
|
| Enzyme 76 Number of Residues |
432 |
| Enzyme 76 Molecular Weight |
47485.0 |
| Enzyme 76 Theoretical pI |
7.00 |
| Enzyme 76 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 76 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 76 Specific Function |
Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent |
| Enzyme 76 Pathways |
Not Available |
| Enzyme 76 Reactions |
Not Available |
| Enzyme 76 Pfam Domain Function |
|
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
Not Available |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
P45954  |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
ACDSB_HUMAN  |
| Enzyme 76 PDB ID |
Not Available |
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>1299 bp
ATGGAGGGCCTGGCAGTGCGGTTGCTGCGCGGCAGCAGGCTGCTAAGAAGAAATTTCCTG
ACTTGTTTGTCTTCTTGGAAGATTCCTCCTCATGTCTCAAAATCTTCCCAGTCAGAAGCT
CTACTCAATATAACAAATAATGGAATACACTTTGCTCCCCTGCAAACATTTACAGATGAG
GAAATGATGATAAAGAGTTCAGTTAAAAAATTTGCTCAGGAACAAATTGCACCTTTGGTT
TCAACCATGGATGAAAATTCGAAAATGGAGAAATCAGTAATACAAGGATTATTTCAACAA
GGGTTGATGGGTATTGAAGTTGACCCAGAATATGGAGGCACAGGAGCTTCTTTTTTATCC
ACTGTGCTCGTGATAGAGGAATTAGCCAAAGTTGATGCATCTGTGGCTGTCTTTTGTGAG
ATCCAGAACACATTAATTAACACACTGATTAGAAAACATGGAACAGAAGAACAAAAGGCC
ACCTATTTGCCTCAGCTCACTACAGAAAAAGTAGGAAGTTTCTGCCTTTCAGAGGCTGGA
GCAGGTAGTGACTCATTTGCTTTGAAGACCAGAGCTGATAAAGAGGGAGATTATTATGTC
CTCAATGGATCAAAGATGTGGATCAGCAGTGCTGAGCATGCAGGGCTCTTTCTGGTGATG
GCAAATGTAGACCCTACCATTGGATATAAGGGAATTACCTCCTTCTTAGTAGATCGTGAT
ACTCCGGGCCTTCATATAGGGAAACCTGAAAACAAATTGGGGCTCAGAGCTTCTTCCACC
TGCCCGTTAACATTCGAAAATGTCAAGGTTCCAGAAGCCAATATCTTGGGACAAATTGGA
CATGGCTATAAGTATGCCATAGGGAGTCTCAATGAAGGTAGAATAGGAATTGCTGCACAG
ATGCTGGGACTGGCGCAAGGATGTTTTGACTACACTATTCCATATATTAAAGAAAGGATA
CAATTTGGCAAAAGACTATTTGATTTTCAGGGCCTCCAACACCAAGTGGCTCACGTGGCC
ACCCAGCTGGAAGCTGCAAGATTACTAACATACAATGCTGCTAGGCTTTTAGAAGCTGGA
AAGCCATTCATAAAAGAAGCGTCAATGGCCAAATACTATGCATCAGAGATTGCAGGACAA
ACAACGAGTAAATGTATCGAGTGGATGGGGGGAGTAGGCTACACCAAAGATTACCCTGTG
GAGAAATACTTCCGAGATGCAAAGATTGGTACGATATATGAAGGAGCTTCCAACATCCAG
TTGAACACCATTGCAAAGCATATCGATGCAGAATACTGA
|
| Enzyme 76 GenBank Gene ID |
U12778  |
| Enzyme 76 GeneCard ID |
ACADSB  |
| Enzyme 76 GenAtlas ID |
ACADSB  |
| Enzyme 76 HGNC ID |
HGNC:91  |
| Enzyme 76 Chromosome Location |
1 |
| Enzyme 76 Locus |
10q26.13 |
| Enzyme 76 SNPs |
SNPJam Report  |
| Enzyme 76 General References |
- Rozen R, Vockley J, Zhou L, Milos R, Willard J, Fu K, Vicanek C, Low-Nang L, Torban E, Fournier B: Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics. 1994 Nov 15;24(2):280-7. [PubMed
]
- Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Gibson KM, Burlingame TG, Hogema B, Jakobs C, Schutgens RB, Millington D, Roe CR, Roe DS, Sweetman L, Steiner RD, Linck L, Pohowalla P, Sacks M, Kiss D, Rinaldo P, Vockley J: 2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism. Pediatr Res. 2000 Jun;47(6):830-3. [PubMed
]
- Madsen PP, Kibaek M, Roca X, Sachidanandam R, Krainer AR, Christensen E, Steiner RD, Gibson KM, Corydon TJ, Knudsen I, Wanders RJ, Ruiter JP, Gregersen N, Andresen BS: Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping. Hum Genet. 2006 Feb;118(6):680-90. Epub 2005 Nov 30. [PubMed
]
|
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
7358 |
| Enzyme 77 Name |
Very long-chain acyl-CoA synthetase |
| Enzyme 77 Synonyms |
- VLACS
- VLCS
- Fatty acid transport protein 2
- FATP-2
- Fatty-acid-coenzyme A ligase, very long-chain 1
- Long-chain-fatty-acid--CoA ligase
- Solute carrier family 27 member 2
- THCA-CoA ligase
- Very long-chain-fatty-acid-CoA ligase
|
| Enzyme 77 Gene Name |
SLC27A2 |
| Enzyme 77 Protein Sequence |
>Very long-chain acyl-CoA synthetase
MLSAIYTVLAGLLFLPLLVNLCCPYFFQDIGYFLKVAAVGRRVRSYGKRRPARTILRAFL
EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWL
WLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIY
YVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQ
RIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDD
CRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYE
FYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKG
EVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDR
VGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGK
KLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAK
MYVPMTEDIYNAISAKTLKL
|
| Enzyme 77 Number of Residues |
620 |
| Enzyme 77 Molecular Weight |
70311.7 |
| Enzyme 77 Theoretical pI |
8.65 |
| Enzyme 77 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 77 General Function |
Involved in catalytic activity |
| Enzyme 77 Specific Function |
Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes |
| Enzyme 77 Pathways |
|
| Enzyme 77 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 77 Pfam Domain Function |
|
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
227499619  |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
O14975  |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
S27A2_HUMAN  |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>1863 bp
ATGCTTTCCGCCATCTACACAGTCCTGGCGGGACTGCTGTTCCTGCCGCTCCTGGTGAAC
CTCTGCTGCCCATACTTCTTCCAGGACATAGGCTACTTCTTGAAGGTGGCCGCCGTGGGC
CGGAGGGTGCGCAGCTACGGGAAGCGGCGGCCGGCGCGCACCATCCTGCGGGCGTTCCTG
GAGAAAGCGCGCCAGACGCCACACAAGCCTTTTCTGCTCTTCCGCGACGAGACTCTCACC
TACGCGCAGGTGGACCGGCGCAGCAATCAAGTGGCCCGGGCGCTGCACGACCACCTCGGC
CTGCGCCAGGGAGACTGCGTGGCGCTCCTTATGGGTAACGAGCCGGCCTACGTGTGGCTG
TGGCTGGGGCTGGTGAAGCTGGGCTGTGCCATGGCGTGCCTCAATTACAACATCCGCGCG
AAGTCCCTGCTGCACTGCTTCCAGTGCTGCGGGGCGAAGGTGCTGCTGGTGTCGCCAGAA
CTACAAGCAGCTGTCGAAGAGATACTGCCAAGCCTTAAAAAAGATGATGTGTCCATCTAT
TATGTGAGCAGAACTTCTAACACAGATGGGATTGACTCTTTCCTGGACAAAGTGGATGAA
GTATCAACTGAACCTATCCCAGAGTCATGGAGGTCTGAAGTCACTTTTTCCACTCCTGCC
TTATACATTTATACTTCTGGAACCACAGGTCTTCCAAAAGCAGCCATGATCACTCATCAG
CGCATATGGTATGGAACTGGCCTCACTTTTGTAAGCGGATTGAAGGCAGATGATGTCATC
TATATCACTCTGCCCTTTTACCACAGTGCTGCACTACTGATTGGCATTCACGGATGTATT
GTGGCTGGTGCTACTCTTGCCTTGCGGACTAAATTTTCAGCCAGCCAGTTTTGGGATGAC
TGCAGAAAATACAACGTCACTGTCATTCAGTATATCGGTGAACTGCTTCGGTATTTATGC
AACTCACCACAGAAACCAAATGACCGTGATCATAAAGTGAGACTGGCACTGGGAAATGGC
TTACGAGGAGATGTGTGGAGACAATTTGTCAAGAGATTTGGGGACATATGCATCTATGAG
TTCTATGCTGCCACTGAAGGCAATATTGGATTTATGAATTATGCGAGAAAAGTTGGTGCT
GTTGGAAGAGTAAACTACCTACAGAAAAAAATCATAACTTATGACCTGATTAAATATGAT
GTGGAGAAAGATGAACCTGTCCGTGATGAAAATGGATATTGCGTCAGAGTTCCCAAAGGT
GAAGTTGGACTTCTGGTTTGCAAAATCACACAACTTACACCATTTAATGGCTATGCTGGA
GCAAAGGCTCAGACAGAGAAGAAAAAACTGAGAGATGTCTTTAAGAAAGGAGACCTCTAT
TTCAACAGTGGAGATCTCTTAATGGTTGACCATGAAAATTTCATCTATTTCCACGACAGA
GTTGGAGATACATTCCGGTGGAAAGGGGAAAATGTGGCCACCACTGAAGTTGCTGATACA
GTTGGACTGGTTGATTTTGTCCAAGAAGTAAATGTTTATGGAGTGCATGTGCCAGATCAT
GAGGGTCGCATTGGCATGGCCTCCATCAAAATGAAAGAAAACCATGAATTTGATGGAAAG
AAACTCTTTCAGCACATTGCTGATTACCTACCTAGTTATGCAAGGCCCCGGTTTCTAAGA
ATACAGGACACCATTGAGATCACTGGAACTTTTAAACACCGCAAAATGACCCTGGTGGAG
GAGGGCTTTAACCCTGCTGTCATCAAAGATGCCTTGTATTTCTTGGATGACACAGCAAAA
ATGTATGTGCCTATGACTGAGGACATCTATAATGCCATAAGTGCTAAAACCCTGAAACTC
TGA
|
| Enzyme 77 GenBank Gene ID |
NM_003645.3  |
| Enzyme 77 GeneCard ID |
SLC27A2  |
| Enzyme 77 GenAtlas ID |
SLC27A2  |
| Enzyme 77 HGNC ID |
HGNC:10996  |
| Enzyme 77 Chromosome Location |
1 |
| Enzyme 77 Locus |
15q21.2 |
| Enzyme 77 SNPs |
SNPJam Report  |
| Enzyme 77 General References |
- Steinberg SJ, Wang SJ, Kim DG, Mihalik SJ, Watkins PA: Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism. Biochem Biophys Res Commun. 1999 Apr 13;257(2):615-21. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA: Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. J Biol Chem. 2002 Jul 5;277(27):24771-9. Epub 2002 Apr 29. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
7657 |
| Enzyme 78 Name |
Peroxisome proliferator-activated receptor gamma |
| Enzyme 78 Synonyms |
- PPAR-gamma
- Nuclear receptor subfamily 1 group C member 3
|
| Enzyme 78 Gene Name |
PPARG |
| Enzyme 78 Protein Sequence |
>Peroxisome proliferator-activated receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC
RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR
ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE
QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS
LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII
LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL
LQVIKKTETDMSLHPLLQEIYKDLY
|
| Enzyme 78 Number of Residues |
505 |
| Enzyme 78 Molecular Weight |
57619.6 |
| Enzyme 78 Theoretical pI |
5.77 |
| Enzyme 78 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 78 General Function |
Involved in DNA binding |
| Enzyme 78 Specific Function |
Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis |
| Enzyme 78 Pathways |
Not Available |
| Enzyme 78 Reactions |
Not Available |
| Enzyme 78 Pfam Domain Function |
|
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
Not Available |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
P37231  |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
PPARG_HUMAN  |
| Enzyme 78 PDB ID |
1I7I  |
| Enzyme 78 PDB File |
Show |
| Enzyme 78 3D Structure |
|
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>1518 bp
ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA
CTGTCTGCAAACATATCACAAGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCC
ACCAACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTT
GATATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGAC
ATTCCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAA
GAGTACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACT
CAGCTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGT
GTCTGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAG
GGTTTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGT
CGGATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCA
GTGGGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAG
CTGTTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGG
GCCCTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAG
GCGAGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATG
AATTCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAG
CAGAGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCT
GTGCAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAAC
GACCAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCC
TTGATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTT
CTAAAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTG
AAGTTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATT
CTCAGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAAC
CTGCTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTT
GCCAAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTA
CTGCAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATC
TACAAGGACTTGTACTAG
|
| Enzyme 78 GenBank Gene ID |
U79012  |
| Enzyme 78 GeneCard ID |
PPARG  |
| Enzyme 78 GenAtlas ID |
PPARG  |
| Enzyme 78 HGNC ID |
HGNC:9236  |
| Enzyme 78 Chromosome Location |
3 |
| Enzyme 78 Locus |
3p25 |
| Enzyme 78 SNPs |
SNPJam Report  |
| Enzyme 78 General References |
- Mukherjee R, Jow L, Croston GE, Paterniti JR Jr: Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2 versus PPARgamma1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem. 1997 Mar 21;272(12):8071-6. [PubMed
]
- Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz M, Moller DE, Berger J: Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2. Biochem Biophys Res Commun. 1996 Jul 16;224(2):431-7. [PubMed
]
- Yanase T, Yashiro T, Takitani K, Kato S, Taniguchi S, Takayanagi R, Nawata H: Differential expression of PPAR gamma1 and gamma2 isoforms in human adipose tissue. Biochem Biophys Res Commun. 1997 Apr 17;233(2):320-4. [PubMed
]
- Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD: Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping. Gene Expr. 1995;4(4-5):281-99. [PubMed
]
- Okazawa H, Mori H, Tamori Y, Araki S, Niki T, Masugi J, Kawanishi M, Kubota T, Shinoda H, Kasuga M: No coding mutations are detected in the peroxisome proliferator-activated receptor-gamma gene in Japanese patients with lipoatrophic diabetes. Diabetes. 1997 Nov;46(11):1904-6. [PubMed
]
- Lambe KG, Tugwood JD: A human peroxisome-proliferator-activated receptor-gamma is activated by inducers of adipogenesis, including thiazolidinedione drugs. Eur J Biochem. 1996 Jul 1;239(1):1-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed
]
- Zhou XP, Smith WM, Gimm O, Mueller E, Gao X, Sarraf P, Prior TW, Plass C, von Deimling A, Black PM, Yates AJ, Eng C: Over-representation of PPARgamma sequence variants in sporadic cases of glioblastoma multiforme: preliminary evidence for common low penetrance modifiers for brain tumour risk in the general population. J Med Genet. 2000 Jun;37(6):410-4. [PubMed
]
- Shao W, Halachmi S, Brown M: ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol Cell Biol. 2002 May;22(10):3358-72. [PubMed
]
- Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ: ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor. Biochem Biophys Res Commun. 2004 Apr 23;317(1):54-9. [PubMed
]
- Drori S, Girnun GD, Tou L, Szwaya JD, Mueller E, Xia K, Shivdasani RA, Spiegelman BM: Hic-5 regulates an epithelial program mediated by PPARgamma. Genes Dev. 2005 Feb 1;19(3):362-75. [PubMed
]
- Uppenberg J, Svensson C, Jaki M, Bertilsson G, Jendeberg L, Berkenstam A: Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma. J Biol Chem. 1998 Nov 20;273(47):31108-12. [PubMed
]
- Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998 Sep 10;395(6698):137-43. [PubMed
]
- Gampe RT Jr, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE: Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55. [PubMed
]
- Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed
]
- Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure. 2001 Aug;9(8):699-706. [PubMed
]
- Ebdrup S, Pettersson I, Rasmussen HB, Deussen HJ, Frost Jensen A, Mortensen SB, Fleckner J, Pridal L, Nygaard L, Sauerberg P: Synthesis and biological and structural characterization of the dual-acting peroxisome proliferator-activated receptor alpha/gamma agonist ragaglitazar. J Med Chem. 2003 Apr 10;46(8):1306-17. [PubMed
]
- Ostberg T, Svensson S, Selen G, Uppenberg J, Thor M, Sundbom M, Sydow-Backman M, Gustavsson AL, Jendeberg L: A new class of peroxisome proliferator-activated receptor agonists with a novel binding epitope shows antidiabetic effects. J Biol Chem. 2004 Sep 24;279(39):41124-30. Epub 2004 Jul 15. [PubMed
]
- Haffner CD, Lenhard JM, Miller AB, McDougald DL, Dwornik K, Ittoop OR, Gampe RT Jr, Xu HE, Blanchard S, Montana VG, Consler TG, Bledsoe RK, Ayscue A, Croom D: Structure-based design of potent retinoid X receptor alpha agonists. J Med Chem. 2004 Apr 8;47(8):2010-29. [PubMed
]
- Shi GQ, Dropinski JF, McKeever BM, Xu S, Becker JW, Berger JP, MacNaul KL, Elbrecht A, Zhou G, Doebber TW, Wang P, Chao YS, Forrest M, Heck JV, Moller DE, Jones AB: Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic and lipid modulating activity. J Med Chem. 2005 Jun 30;48(13):4457-68. [PubMed
]
- Li Y, Choi M, Suino K, Kovach A, Daugherty J, Kliewer SA, Xu HE: Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner. Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9505-10. Epub 2005 Jun 23. [PubMed
]
- Hopkins CR, O'neil SV, Laufersweiler MC, Wang Y, Pokross M, Mekel M, Evdokimov A, Walter R, Kontoyianni M, Petrey ME, Sabatakos G, Roesgen JT, Richardson E, Demuth TP Jr: Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent PPAR-gamma binding agents with potential application to the treatment of osteoporosis. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5659-63. Epub 2006 Aug 21. [PubMed
]
- Mahindroo N, Wang CC, Liao CC, Huang CF, Lu IL, Lien TW, Peng YH, Huang WJ, Lin YT, Hsu MC, Lin CH, Tsai CH, Hsu JT, Chen X, Lyu PC, Chao YS, Wu SY, Hsieh HP: Indol-1-yl acetic acids as peroxisome proliferator-activated receptor agonists: design, synthesis, structural biology, and molecular docking studies. J Med Chem. 2006 Feb 9;49(3):1212-6. [PubMed
]
- Lu IL, Huang CF, Peng YH, Lin YT, Hsieh HP, Chen CT, Lien TW, Lee HJ, Mahindroo N, Prakash E, Yueh A, Chen HY, Goparaju CM, Chen X, Liao CC, Chao YS, Hsu JT, Wu SY: Structure-based drug design of a novel family of PPARgamma partial agonists: virtual screening, X-ray crystallography, and in vitro/in vivo biological activities. J Med Chem. 2006 May 4;49(9):2703-12. [PubMed
]
- Yen CJ, Beamer BA, Negri C, Silver K, Brown KA, Yarnall DP, Burns DK, Roth J, Shuldiner AR: Molecular scanning of the human peroxisome proliferator activated receptor gamma (hPPAR gamma) gene in diabetic Caucasians: identification of a Pro12Ala PPAR gamma 2 missense mutation. Biochem Biophys Res Commun. 1997 Dec 18;241(2):270-4. [PubMed
]
- Ristow M, Muller-Wieland D, Pfeiffer A, Krone W, Kahn CR: Obesity associated with a mutation in a genetic regulator of adipocyte differentiation. N Engl J Med. 1998 Oct 1;339(14):953-9. [PubMed
]
- Deeb SS, Fajas L, Nemoto M, Pihlajamaki J, Mykkanen L, Kuusisto J, Laakso M, Fujimoto W, Auwerx J: A Pro12Ala substitution in PPARgamma2 associated with decreased receptor activity, lower body mass index and improved insulin sensitivity. Nat Genet. 1998 Nov;20(3):284-7. [PubMed
]
- Hamann A, Munzberg H, Buttron P, Busing B, Hinney A, Mayer H, Siegfried W, Hebebrand J, Greten H: Missense variants in the human peroxisome proliferator-activated receptor-gamma2 gene in lean and obese subjects. Eur J Endocrinol. 1999 Jul;141(1):90-2. [PubMed
]
- Valve R, Sivenius K, Miettinen R, Pihlajamaki J, Rissanen A, Deeb SS, Auwerx J, Uusitupa M, Laakso M: Two polymorphisms in the peroxisome proliferator-activated receptor-gamma gene are associated with severe overweight among obese women. J Clin Endocrinol Metab. 1999 Oct;84(10):3708-12. [PubMed
]
- Sarraf P, Mueller E, Smith WM, Wright HM, Kum JB, Aaltonen LA, de la Chapelle A, Spiegelman BM, Eng C: Loss-of-function mutations in PPAR gamma associated with human colon cancer. Mol Cell. 1999 Jun;3(6):799-804. [PubMed
]
- Barroso I, Gurnell M, Crowley VE, Agostini M, Schwabe JW, Soos MA, Maslen GL, Williams TD, Lewis H, Schafer AJ, Chatterjee VK, O'Rahilly S: Dominant negative mutations in human PPARgamma associated with severe insulin resistance, diabetes mellitus and hypertension. Nature. 1999 Dec 23-30;402(6764):880-3. [PubMed
]
- Hegele RA, Cao H, Frankowski C, Mathews ST, Leff T: PPARG F388L, a transactivation-deficient mutant, in familial partial lipodystrophy. Diabetes. 2002 Dec;51(12):3586-90. [PubMed
]
- Agarwal AK, Garg A: A novel heterozygous mutation in peroxisome proliferator-activated receptor-gamma gene in a patient with familial partial lipodystrophy. J Clin Endocrinol Metab. 2002 Jan;87(1):408-11. [PubMed
]
- Masud S, Ye S: Effect of the peroxisome proliferator activated receptor-gamma gene Pro12Ala variant on body mass index: a meta-analysis. J Med Genet. 2003 Oct;40(10):773-80. [PubMed
]
- Temelkova-Kurktschiev T, Hanefeld M, Chinetti G, Zawadzki C, Haulon S, Kubaszek A, Koehler C, Leonhardt W, Staels B, Laakso M: Ala12Ala genotype of the peroxisome proliferator-activated receptor gamma2 protects against atherosclerosis. J Clin Endocrinol Metab. 2004 Sep;89(9):4238-42. [PubMed
]
- Kim KS, Choi SM, Shin SU, Yang HS, Yoon Y: Effects of peroxisome proliferator-activated receptor-gamma 2 Pro12Ala polymorphism on body fat distribution in female Korean subjects. Metabolism. 2004 Dec;53(12):1538-43. [PubMed
]
|
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
7694 |
| Enzyme 79 Name |
Peroxisome proliferator-activated receptor alpha |
| Enzyme 79 Synonyms |
- PPAR-alpha
- Nuclear receptor subfamily 1 group C member 1
|
| Enzyme 79 Gene Name |
PPARA |
| Enzyme 79 Protein Sequence |
>Peroxisome proliferator-activated receptor alpha
MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSC
PGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACE
GCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSE
KAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFV
IHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANL
DLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFD
FAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDI
FLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY
|
| Enzyme 79 Number of Residues |
468 |
| Enzyme 79 Molecular Weight |
52224.6 |
| Enzyme 79 Theoretical pI |
6.20 |
| Enzyme 79 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 79 General Function |
Involved in DNA binding |
| Enzyme 79 Specific Function |
Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl- 2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene |
| Enzyme 79 Pathways |
Not Available |
| Enzyme 79 Reactions |
Not Available |
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
216409688  |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
Q07869  |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
PPARA_HUMAN  |
| Enzyme 79 PDB ID |
1K7L  |
| Enzyme 79 PDB File |
Show |
| Enzyme 79 3D Structure |
|
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
>1407 bp
ATGGTGGACACGGAAAGCCCACTCTGCCCCCTCTCCCCACTCGAGGCCGGCGATCTAGAG
AGCCCGTTATCTGAAGAGTTCCTGCAAGAAATGGGAAACATCCAAGAGATTTCGCAATCC
ATCGGCGAGGATAGTTCTGGAAGCTTTGGCTTTACGGAATACCAGTATTTAGGAAGCTGT
CCTGGCTCAGATGGCTCGGTCATCACGGACACGCTTTCACCAGCTTCGAGCCCCTCCTCG
GTGACTTATCCTGTGGTCCCCGGCAGCGTGGACGAGTCTCCCAGTGGAGCATTGAACATC
GAATGTAGAATCTGCGGGGACAAGGCCTCAGGCTATCATTACGGAGTCCACGCGTGTGAA
GGCTGCAAGGGCTTCTTTCGGCGAACGATTCGACTCAAGCTGGTGTATGACAAGTGCGAC
CGCAGCTGCAAGATCCAGAAAAAGAACAGAAACAAATGCCAGTATTGTCGATTTCACAAG
TGCCTTTCTGTCGGGATGTCACACAACGCGATTCGTTTTGGACGAATGCCAAGATCTGAG
AAAGCAAAACTGAAAGCAGAAATTCTTACCTGTGAACATGACATAGAAGATTCTGAAACT
GCAGATCTCAAATCTCTGGCCAAGAGAATCTACGAGGCCTACTTGAAGAACTTCAACATG
AACAAGGTCAAAGCCCGGGTCATCCTCTCAGGAAAGGCCAGTAACAATCCACCTTTTGTC
ATACATGATATGGAGACACTGTGTATGGCTGAGAAGACGCTGGTGGCCAAGCTGGTGGCC
AATGGCATCCAGAACAAGGAGGCGGAGGTCCGCATCTTTCACTGCTGCCAGTGCACGTCA
GTGGAGACCGTCACGGAGCTCACGGAATTCGCCAAGGCCATCCCAGGCTTCGCAAACTTG
GACCTGAACGATCAAGTGACATTGCTAAAATACGGAGTTTATGAGGCCATATTCGCCATG
CTGTCTTCTGTGATGAACAAAGACGGGATGCTGGTAGCGTATGGAAATGGGTTTATAACT
CGTGAATTCCTAAAAAGCCTAAGGAAACCGTTCTGTGATATCATGGAACCCAAGTTTGAT
TTTGCCATGAAGTTCAATGCACTGGAACTGGATGACAGTGATATCTCCCTTTTTGTGGCT
GCTATCATTTGCTGTGGAGATCGTCCTGGCCTTCTAAACGTAGGACACATTGAAAAAATG
CAGGAGGGTATTGTACATGTGCTCAGACTCCACCTGCAGAGCAACCACCCGGACGATATC
TTTCTCTTCCCCAAACTTCTTCAAAAAATGGCAGACCTCCGGCAGCTGGTGACGGAGCAT
GCGCAGCTGGTGCAGATCATCAAGAAGACGGAGTCGGATGCTGCGCTGCACCCGCTACTG
CAGGAGATCTACAGGGACATGTACTGA
|
| Enzyme 79 GenBank Gene ID |
AB307690  |
| Enzyme 79 GeneCard ID |
PPARA  |
| Enzyme 79 GenAtlas ID |
PPARA  |
| Enzyme 79 HGNC ID |
HGNC:9232  |
| Enzyme 79 Chromosome Location |
2 |
| Enzyme 79 Locus |
22q12-q13.1|22q13.31 |
| Enzyme 79 SNPs |
SNPJam Report  |
| Enzyme 79 General References |
- Sher T, Yi HF, McBride OW, Gonzalez FJ: cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry. 1993 Jun 1;32(21):5598-604. [PubMed
]
- Mukherjee R, Jow L, Noonan D, McDonnell DP: Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators. J Steroid Biochem Mol Biol. 1994 Nov;51(3-4):157-66. [PubMed
]
- Tugwood JD, Aldridge TC, Lambe KG, Macdonald N, Woodyatt NJ: Peroxisome proliferator-activated receptors: structures and function. Ann N Y Acad Sci. 1996 Dec 27;804:252-65. [PubMed
]
- Kobayashi T, Kodani Y, Nozawa A, Endo Y, Sawasaki T: DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system. FEBS Lett. 2008 Aug 6;582(18):2737-44. Epub 2008 Jul 11. [PubMed
]
- Cho MC, Lee S, Choi HS, Yang Y, Tae Hong J, Kim SJ, Yoon DY: Optimization of an enzyme-linked immunosorbent assay to screen ligand of Peroxisome proliferator-activated receptor alpha. Immunopharmacol Immunotoxicol. 2009;31(3):459-67. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8479-84. [PubMed
]
- Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed
]
- Fu J, Gaetani S, Oveisi F, Lo Verme J, Serrano A, Rodriguez De Fonseca F, Rosengarth A, Luecke H, Di Giacomo B, Tarzia G, Piomelli D: Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-alpha. Nature. 2003 Sep 4;425(6953):90-3. [PubMed
]
- Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed
]
- Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure. 2001 Aug;9(8):699-706. [PubMed
]
- Xu HE, Stanley TB, Montana VG, Lambert MH, Shearer BG, Cobb JE, McKee DD, Galardi CM, Plunket KD, Nolte RT, Parks DJ, Moore JT, Kliewer SA, Willson TM, Stimmel JB: Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha. Nature. 2002 Feb 14;415(6873):813-7. [PubMed
]
- Oon Han H, Kim SH, Kim KH, Hur GC, Joo Yim H, Chung HK, Ho Woo S, Dong Koo K, Lee CS, Sung Koh J, Kim GT: Design and synthesis of oxime ethers of alpha-acyl-beta-phenylpropanoic acids as PPAR dual agonists. Bioorg Med Chem Lett. 2007 Feb 15;17(4):937-41. Epub 2006 Nov 18. [PubMed
]
- Sierra ML, Beneton V, Boullay AB, Boyer T, Brewster AG, Donche F, Forest MC, Fouchet MH, Gellibert FJ, Grillot DA, Lambert MH, Laroze A, Le Grumelec C, Linget JM, Montana VG, Nguyen VL, Nicodeme E, Patel V, Penfornis A, Pineau O, Pohin D, Potvain F, Poulain G, Ruault CB, Saunders M, Toum J, Xu HE, Xu RX, Pianetti PM: Substituted 2-[(4-aminomethyl)phenoxy]-2-methylpropionic acid PPARalpha agonists. 1. Discovery of a novel series of potent HDLc raising agents. J Med Chem. 2007 Feb 22;50(4):685-95. Epub 2007 Jan 23. [PubMed
]
- Oyama T, Toyota K, Waku T, Hirakawa Y, Nagasawa N, Kasuga JI, Hashimoto Y, Miyachi H, Morikawa K: Adaptability and selectivity of human peroxisome proliferator-activated receptor (PPAR) pan agonists revealed from crystal structures. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):786-95. Epub 2009 Jul 10. [PubMed
]
- Benardeau A, Benz J, Binggeli A, Blum D, Boehringer M, Grether U, Hilpert H, Kuhn B, Marki HP, Meyer M, Puntener K, Raab S, Ruf A, Schlatter D, Mohr P: Aleglitazar, a new, potent, and balanced dual PPARalpha/gamma agonist for the treatment of type II diabetes. Bioorg Med Chem Lett. 2009 May 1;19(9):2468-73. Epub 2009 Mar 14. [PubMed
]
- Artis DR, Lin JJ, Zhang C, Wang W, Mehra U, Perreault M, Erbe D, Krupka HI, England BP, Arnold J, Plotnikov AN, Marimuthu A, Nguyen H, Will S, Signaevsky M, Kral J, Cantwell J, Settachatgull C, Yan DS, Fong D, Oh A, Shi S, Womack P, Powell B, Habets G, West BL, Zhang KY, Milburn MV, Vlasuk GP, Hirth KP, Nolop K, Bollag G, Ibrahim PN, Tobin JF: Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent. Proc Natl Acad Sci U S A. 2009 Jan 6;106(1):262-7. Epub 2008 Dec 30. [PubMed
]
|
| Enzyme 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
7848 |
| Enzyme 80 Name |
Peroxisome proliferator-activated receptor delta |
| Enzyme 80 Synonyms |
- PPAR-delta
- NUCI
- Nuclear hormone receptor 1
- NUC1
- Nuclear receptor subfamily 1 group C member 2
- Peroxisome proliferator-activated receptor beta
- PPAR-beta
|
| Enzyme 80 Gene Name |
PPARD |
| Enzyme 80 Protein Sequence |
>Peroxisome proliferator-activated receptor delta
MEQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYTDLSRSSSPPSLLDQLQM
GCDGASCGSLNMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCERSCKIQKK
NRNKCQYCRFQKCLALGMSHNAIRFGRMPEAEKRKLVAGLTANEGSQYNPQVADLKAFSK
HIYNAYLKNFNMTKKKARSILTGKASHTAPFVIHDIETLWQAEKGLVWKQLVNGLPPYKE
ISVHVFYRCQCTTVETVRELTEFAKSIPSFSSLFLNDQVTLLKYGVHEAIFAMLASIVNK
DGLLVANGSGFVTREFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGD
RPGLMNVPRVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRI
KKTETETSLHPLLQEIYKDMY
|
| Enzyme 80 Number of Residues |
441 |
| Enzyme 80 Molecular Weight |
49903.0 |
| Enzyme 80 Theoretical pI |
7.65 |
| Enzyme 80 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 80 General Function |
Involved in DNA binding |
| Enzyme 80 Specific Function |
Ligand-activated transcription factor. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand |
| Enzyme 80 Pathways |
Not Available |
| Enzyme 80 Reactions |
Not Available |
| Enzyme 80 Pfam Domain Function |
|
| Enzyme 80 Signals |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
Not Available |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
Q03181  |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
PPARD_HUMAN  |
| Enzyme 80 PDB ID |
1Y0S  |
| Enzyme 80 PDB File |
Show |
| Enzyme 80 3D Structure |
|
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
>1326 bp
ATGGAGCAGCCACAGGAGGAAGCCCCTGAGGTCCGGGAAGAGGAGGAGAAAGAGGAAGTG
GCAGAGGCAGAAGGAGCCCCAGAGCTCAATGGGGGACCACAGCATGCACTTCCTTCCAGC
AGCTACACAGACCTCTCCCGGAGCTCCTCGCCACCCTCACTGCTGGACCAACTGCAGATG
GGCTGTGACGGGGCCTCATGCGGCAGCCTCAACATGGAGTGCCGGGTGTGCGGGGACAAG
GCATCGGGCTTCCACTACGGTGTTCATGCATGTGAGGGGTGCAAGGGCTTCTTCCGTCGT
ACGATCCGCATGAAGCTGGAGTACGAGAAGTGTGAGCGCAGCTGCAAGATTCAGAAGAAG
AACCGCAACAAGTGCCAGTACTGCCGCTTCCAGAAGTGCCTGGCACTGGGCATGTCACAC
AACGCTATCCGTTTTGGTCGGATGCCGGAGGCTGAGAAGAGGAAGCTGGTGGCAGGGCTG
ACTGCAAACGAGGGGAGCCAGTACAACCCACAGGTGGCCGACCTGAAGGCCTTCTCCAAG
CACATCTACAATGCCTACCTGAAAAACTTCAACATGACCAAAAAGAAGGCCCGCAGCATC
CTCACCGGCAAAGCCAGCCACACGGCGCCCTTTGTGATCCACGACATCGAGACATTGTGG
CAGGCAGAGAAGGGGCTGGTGTGGAAGCAGTTGGTGAATGGCCTGCCTCCCTACAAGGAG
ATCAGCGTGCACGTCTTCTACCGCTGCCAGTGCACCACAGTGGAGACCGTGCGGGAGCTC
ACTGAGTTCGCCAAGAGCATCCCCAGCTTCAGCAGCCTCTTCCTCAACGACCAGGTTACC
CTTCTCAAGTATGGCGTGCACGAGGCCATCTTCGCCATGCTGGCCTCTATCGTCAACAAG
GACGGGCTGCTGGTAGCCAACGGCAGTGGCTTTGTCACCCGTGAGTTCCTGCGCAGCCTC
CGCAAACCCTTCAGTGATATCATTGAGCCTAAGTTTGAATTTGCTGTCAAGTTCAACGCC
CTGGAACTTGATGACAGTGACCTGGCCCTATTCATTGCGGCCATCATTCTGTGTGGAGAC
CGGCCAGGCCTCATGAACGTTCCACGGGTGGAGGCTATCCAGGACACCATCCTGCGTGCC
CTCGAATTCCACCTGCAGGCCAACCACCCTGATGCCCAGTACCTCTTCCCCAAGCTGCTG
CAGAAGATGGCTGACCTGCGGCAACTGGTCACCGAGCACGCCCAGATGATGCAGCGGATC
AAGAAGACCGAAACCGAGACCTCGCTGCACCCTCTGCTCCAGGAGATCTACAAGGACATG
TACTAA
|
| Enzyme 80 GenBank Gene ID |
L07592  |
| Enzyme 80 GeneCard ID |
PPARD  |
| Enzyme 80 GenAtlas ID |
PPARD  |
| Enzyme 80 HGNC ID |
HGNC:9235  |
| Enzyme 80 Chromosome Location |
6 |
| Enzyme 80 Locus |
6p21.2 |
| Enzyme 80 SNPs |
SNPJam Report  |
| Enzyme 80 General References |
- Schmidt A, Endo N, Rutledge SJ, Vogel R, Shinar D, Rodan GA: Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids. Mol Endocrinol. 1992 Oct;6(10):1634-41. [PubMed
]
- Skogsberg J, Kannisto K, Roshani L, Gagne E, Hamsten A, Larsson C, Ehrenborg E: Characterization of the human peroxisome proliferator activated receptor delta gene and its expression. Int J Mol Med. 2000 Jul;6(1):73-81. [PubMed
]
- Kobayashi T, Kodani Y, Nozawa A, Endo Y, Sawasaki T: DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system. FEBS Lett. 2008 Aug 6;582(18):2737-44. Epub 2008 Jul 11. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- van der Veen JN, Kruit JK, Havinga R, Baller JF, Chimini G, Lestavel S, Staels B, Groot PH, Groen AK, Kuipers F: Reduced cholesterol absorption upon PPARdelta activation coincides with decreased intestinal expression of NPC1L1. J Lipid Res. 2005 Mar;46(3):526-34. Epub 2004 Dec 16. [PubMed
]
- Xu HE, Lambert MH, Montana VG, Parks DJ, Blanchard SG, Brown PJ, Sternbach DD, Lehmann JM, Wisely GB, Willson TM, Kliewer SA, Milburn MV: Molecular recognition of fatty acids by peroxisome proliferator-activated receptors. Mol Cell. 1999 Mar;3(3):397-403. [PubMed
]
- Takada I, Yu RT, Xu HE, Lambert MH, Montana VG, Kliewer SA, Evans RM, Umesono K: Alteration of a single amino acid in peroxisome proliferator-activated receptor-alpha (PPAR alpha) generates a PPAR delta phenotype. Mol Endocrinol. 2000 May;14(5):733-40. [PubMed
]
- Epple R, Azimioara M, Russo R, Xie Y, Wang X, Cow C, Wityak J, Karanewsky D, Bursulaya B, Kreusch A, Tuntland T, Gerken A, Iskandar M, Saez E, Martin Seidel H, Tian SS: 3,4,5-Trisubstituted isoxazoles as novel PPARdelta agonists. Part 2. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5488-92. Epub 2006 Aug 22. [PubMed
]
- Fyffe SA, Alphey MS, Buetow L, Smith TK, Ferguson MA, Sorensen MD, Bjorkling F, Hunter WN: Recombinant human PPAR-beta/delta ligand-binding domain is locked in an activated conformation by endogenous fatty acids. J Mol Biol. 2006 Mar 3;356(4):1005-13. Epub 2006 Jan 4. [PubMed
]
- Fyffe SA, Alphey MS, Buetow L, Smith TK, Ferguson MA, Sorensen MD, Bjorkling F, Hunter WN: Reevaluation of the PPAR-beta/delta ligand binding domain model reveals why it exhibits the activated form. Mol Cell. 2006 Jan 6;21(1):1-2. [PubMed
]
- Pettersson I, Ebdrup S, Havranek M, Pihera P, Korinek M, Mogensen JP, Jeppesen CB, Johansson E, Sauerberg P: Design of a partial PPARdelta agonist. Bioorg Med Chem Lett. 2007 Aug 15;17(16):4625-9. Epub 2007 May 27. [PubMed
]
- Shearer BG, Patel HS, Billin AN, Way JM, Winegar DA, Lambert MH, Xu RX, Leesnitzer LM, Merrihew RV, Huet S, Willson TM: Discovery of a novel class of PPARdelta partial agonists. Bioorg Med Chem Lett. 2008 Sep 15;18(18):5018-22. Epub 2008 Aug 9. [PubMed
]
- Oyama T, Toyota K, Waku T, Hirakawa Y, Nagasawa N, Kasuga JI, Hashimoto Y, Miyachi H, Morikawa K: Adaptability and selectivity of human peroxisome proliferator-activated receptor (PPAR) pan agonists revealed from crystal structures. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):786-95. Epub 2009 Jul 10. [PubMed
]
- Connors RV, Wang Z, Harrison M, Zhang A, Wanska M, Hiscock S, Fox B, Dore M, Labelle M, Sudom A, Johnstone S, Liu J, Walker NP, Chai A, Siegler K, Li Y, Coward P: Identification of a PPARdelta agonist with partial agonistic activity on PPARgamma. Bioorg Med Chem Lett. 2009 Jul 1;19(13):3550-4. Epub 2009 May 9. [PubMed
]
- Artis DR, Lin JJ, Zhang C, Wang W, Mehra U, Perreault M, Erbe D, Krupka HI, England BP, Arnold J, Plotnikov AN, Marimuthu A, Nguyen H, Will S, Signaevsky M, Kral J, Cantwell J, Settachatgull C, Yan DS, Fong D, Oh A, Shi S, Womack P, Powell B, Habets G, West BL, Zhang KY, Milburn MV, Vlasuk GP, Hirth KP, Nolop K, Bollag G, Ibrahim PN, Tobin JF: Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent. Proc Natl Acad Sci U S A. 2009 Jan 6;106(1):262-7. Epub 2008 Dec 30. [PubMed
]
|
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
7861 |
| Enzyme 81 Name |
Acyl-CoA-binding protein |
| Enzyme 81 Synonyms |
- ACBP
- Diazepam-binding inhibitor
- DBI
- Endozepine
- EP
|
| Enzyme 81 Gene Name |
DBI |
| Enzyme 81 Protein Sequence |
>Acyl-CoA-binding protein
MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWN
ELKGTSKEDAMKAYINKVEELKKKYGI
|
| Enzyme 81 Number of Residues |
87 |
| Enzyme 81 Molecular Weight |
10044.4 |
| Enzyme 81 Theoretical pI |
6.54 |
| Enzyme 81 GO Classification |
| Function |
- acyl-CoA binding
- binding
- fatty acid binding
- lipid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 81 General Function |
Involved in acyl-CoA binding |
| Enzyme 81 Specific Function |
Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor |
| Enzyme 81 Pathways |
Not Available |
| Enzyme 81 Reactions |
Not Available |
| Enzyme 81 Pfam Domain Function |
|
| Enzyme 81 Signals |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
73746603  |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
P07108  |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
ACBP_HUMAN  |
| Enzyme 81 PDB ID |
1NVL  |
| Enzyme 81 PDB File |
Show |
| Enzyme 81 3D Structure |
|
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
>252 bp
GCTGAGTTTGAGAAAGCTGCAGAGGAGGTTAGGCACCTTAAGACCAAGCCAGCAGATGAT
GAGATGCTGTTCATCTATGGCCGCTACAAACAAGCAACTGTGGGCGACATAAATACAGAA
CGGCCCGGGATGTTGGACTTCACAGGCAAGGCCAAGTGGGATGCCTGGAATGAGCTGAAA
GGGACTACCAAGGAAGATGCCATGAAAGCTTACATCAACAAAGTAGAAGAGCTAAAGAAA
AAATACGGGATA
|
| Enzyme 81 GenBank Gene ID |
DQ150443  |
| Enzyme 81 GeneCard ID |
DBI  |
| Enzyme 81 GenAtlas ID |
DBI  |
| Enzyme 81 HGNC ID |
HGNC:2690  |
| Enzyme 81 Chromosome Location |
2 |
| Enzyme 81 Locus |
2q12-q21 |
| Enzyme 81 SNPs |
SNPJam Report  |
| Enzyme 81 General References |
- Gray PW, Glaister D, Seeburg PH, Guidotti A, Costa E: Cloning and expression of cDNA for human diazepam binding inhibitor, a natural ligand of an allosteric regulatory site of the gamma-aminobutyric acid type A receptor. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7547-51. [PubMed
]
- Webb NR, Rose TM, Malik N, Marquardt H, Shoyab M, Todaro GJ, Lee DC: Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand. DNA. 1987 Feb;6(1):71-9. [PubMed
]
- Nitz I, Doring F, Schrezenmeir J, Burwinkel B: Identification of new acyl-CoA binding protein transcripts in human and mouse. Int J Biochem Cell Biol. 2005 Nov;37(11):2395-405. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Marquardt H, Todaro GJ, Shoyab M: Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor. J Biol Chem. 1986 Jul 25;261(21):9727-31. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Apfel R, Lottspeich F, Hoppe J, Behl C, Durr G, Bogdahn U: Purification and analysis of growth regulating proteins secreted by a human melanoma cell line. Melanoma Res. 1992 Dec;2(5-6):327-36. [PubMed
]
- Kolmer M, Rovio A, Alho H: The characterization of two diazepam binding inhibitor (DBI) transcripts in humans. Biochem J. 1995 Mar 1;306 ( Pt 2):327-30. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Taskinen JP, van Aalten DM, Knudsen J, Wierenga RK: High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand. Proteins. 2007 Jan 1;66(1):229-38. [PubMed
]
|
| Enzyme 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
8034 |
| Enzyme 82 Name |
Histone acetyltransferase KAT2A |
| Enzyme 82 Synonyms |
- General control of amino acid synthesis protein 5-like 2
- Histone acetyltransferase GCN5
- HsGCN5
- Lysine acetyltransferase 2A
- STAF97
|
| Enzyme 82 Gene Name |
KAT2A |
| Enzyme 82 Protein Sequence |
>Histone acetyltransferase KAT2A
MAEPSQAPTPAPAAQPRPLQSPAPAPTPTPAPSPASAPIPTPTPAPAPAPAAAPAGSTGT
GGPGVGSGGAGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKC
NGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVE
NLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQ
YKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQAEDVATYKVNYTRWLCYCH
VPQSCDSLPRYETTHVFGRSLLRSIFTVTRRQLLEKFRVEKDKLVPEKRTLILTHFPKFL
SMLEEEIYGANSPIWESGFTMPPSEGTQLVPRPASVSAAVVPSTPIFSPSMGGGSNSSLS
LDSAGAEPMPGEKRTLPENLTLEDAKRLRVMGDIPMELVNEVMLTITDPAAMLGPETSLL
SANAARDETARLEERRGIIEFHVIGNSLTPKANRRVLLWLVGLQNVFSHQLPRMPKEYIA
RLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKE
YHIKHNILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIP
YTELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGIRETGWKPLG
KEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTE
RLRSRYYVTRKLFVADLQRVIANCREYNPPDSEYCRCASALEKFFYFKLKEGGLIDK
|
| Enzyme 82 Number of Residues |
837 |
| Enzyme 82 Molecular Weight |
93924.7 |
| Enzyme 82 Theoretical pI |
9.39 |
| Enzyme 82 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- histone acetyltransferase activity
- lysine N-acetyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- covalent chromatin modification
- histone acetylation
- histone modification
- metabolic process
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 82 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 82 Specific Function |
Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 |
| Enzyme 82 Pathways |
Not Available |
| Enzyme 82 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 82 Pfam Domain Function |
|
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
3220164  |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
Q92830  |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
KAT2A_HUMAN  |
| Enzyme 82 PDB ID |
1Z4R  |
| Enzyme 82 PDB File |
Show |
| Enzyme 82 3D Structure |
|
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>2514 bp
ATGGCGGAACCTTCCCAGGCCCCGACCCCGGCCCCGGCTGCGCAGCCCCGGCCCCTTCAG
TCCCCAGCCCCTGCCCCAACTCCGACTCCTGCACCCAGCCCGGCTTCAGCCCCGATTCCG
ACTCCCACCCCGGCACCAGCCCCTGCCCCAGCTGCAGCCCCAGCCGGCAGCACAGGGACT
GGGGGGCCCGGGGTAGGAAGTGGGGGGGCCGGGAGCGGGGGGGATCCGGCTCGGCCTGGC
CTGAGCCAGCAGCAGCGCGCCAGTCAGAGGAAGGCGCAAGTCCGGGGGCTGCCCCGCGCC
AAGAAGCTTGAGAAGCTAGGGGTCTTCTCGGCTTGCAAGGCCAATGGAACCTGTAAGTGT
AATGGCTGGAAAAACCCCAAGCCCCCCACTGCACCCCGCATAGATCTGCAGCAGCCAGCT
GCCAACCTGAGTGAGCTGTGCCGCAGTTGTGAGCACCCCTTGGCTGACCACGTATCCCAC
TTGGAGAATGTGTCAGAGGATGAGATAAACCGACTGCTGGGGATGGTGGTGGATGTGGAG
AATCTCTTCATGTCTGTTCACAAGGAAGAGGACACAGACACCAAGCAGGTCTATTTCTAC
CTCTTCAAGCTACTGCGGAAATGCATCCTGCAGATGACCCGGCCTGTGGTGGAGGGGTCC
CTGGGCAGCCCTCCATTTGAGAAACCTAATATTGAGCAGGGTGTGCTGAACTTTGTGCAG
TACAAGTTTAGTCACCTGGCTCCCCGGGAGCGGCAGACGATGTTCGAGCTCTCAAAGATG
TTCTTGCTCTGCCTTAACTACTGGGAGCTTGAGACACCTGCCCAGTTTCGGCAGAGGTCT
CAGGCTGAGGACGTGGCTACCTACAAGGTCAATTACACCAGATGGCTCTGTTACTGCCAC
GTGCCCCAGAGCTGTGATAGCCTCCCCCGCTACGAAACCACTCATGTCTTTGGGCGAAGC
CTTCTCCGGTCCATTTTCACCGTTACCCGCCGGCAGCTGCTGGAAAAGTTCCGAGTGGAG
AAGGACAAATTGGTGCCCGAGAAGAGGACCCTCATCCTCACTCACTTCCCCAAATTCCTG
TCCATGCTGGAGGAGGAGATCTATGGGGCAAACTCTCCAATCTGGGAGTCAGGCTTCACC
ATGCCACCCTCAGAGGGGACACAGCTGGTTCCCCGGCCAGCTTCAGTCAGTGCAGCGGTT
GTTCCCAGCACCCCCATCTTCAGCCCCAGCATGGGTGGGGGCAGCAACAGCTCCCTGAGT
CTGGATTCTGCAGGGGCCGAGCCTATGCCAGGCGAGAAGAGGACGCTCCCAGAGAACCTG
ACCCTGGAGGATGCCAAGCGGCTCCGTGTGATGGGTGACATCCCCATGGAGCTGGTCAAT
GAGGTCATGCTGACCATCACTGACCCTGCTGCCATGCTGGGGCCTGAGACGAGCCTGCTT
TCGGCCAATGCGGCCCGGGATGAGACAGCCCGCCTGGAGGAGCGCCGCGGCATCATCGAG
TTCCATGTCATCGGCAACTCACTGACGCCCAAGGCCAACCGGCGGGTGTTGCTGTGGCTC
GTGGGGCTGCAGAATGTCTTTTCCCACCAGCTGCCGCGCATGCCTAAGGAGTATATCGCC
CGCCTCGTCTTTGACCCGAAGCACAAGACTCTGGCCTTGATCAAGGATGGGCGGGTCATC
GGTGGCATCTGCTTCCGCATGTTTCCCACCCAGGGCTTCACGGAGATTGTCTTCTGTGCT
GTCACCTCGAATGAGCAGGTCAAGGGTTATGGGACCCACCTGATGAACCACCTGAAGGAG
TATCACATCAAGCACAACATTCTCTACTTCCTCACCTACGCCGACGAGTACGCCATCGGC
TACTTCAAAAAGCAGGGTTTCTCCAAGGACATCAAGGTGCCCAAGAGCCGCTACCTGGGC
TACATCAAGGACTACGAGGGAGCGACGCTGATGGAGTGTGAGCTGAATCCCCGCATCCCC
TACACGGAGCTGTCCCACATCATCAAGAAGCAGAAAGAGATCATCAAGAAGCTGATTGAG
CGCAAACAGGCCCAGATCCGCAAGGTCTACCCGGGGCTCAGCTGCTTCAAGGAGGGCGTG
AGGCAGATCCCTGTGGAGAGCGTTCCTGGCATTCGAGAGACAGGCTGGAAGCCATTGGGG
AAGGAGAAGGGGAAGGAGCTGAAGGACCCCGACCAGCTCTACACAACCCTCAAAAACCTG
CTGGCCCAAATCAAGTCTCACCCCAGTGCCTGGCCCTTCATGGAGCCTGTGAAGAAGTCG
GAGGCCCCTGACTACTACGAGGTCATCCGCTTCCCCATTGACCTGAAGACCATGACTGAG
CGGCTGCGAAGCCGCTACTACGTGACCCGGAAGCTCTTTGTGGCCGACCTGCAGCGGGTC
ATCGCCAACTGTCGCGAGTACAACCCCCCGGACAGCGAGTACTGCCGCTGTGCCAGCGCC
CTGGAGAAGTTCTTCTACTTCAAGCTCAAGGAGGGAGGCCTCATTGACAAGTAG
|
| Enzyme 82 GenBank Gene ID |
AF029777  |
| Enzyme 82 GeneCard ID |
KAT2A  |
| Enzyme 82 GenAtlas ID |
KAT2A  |
| Enzyme 82 HGNC ID |
HGNC:4201  |
| Enzyme 82 Chromosome Location |
1 |
| Enzyme 82 Locus |
17q21 |
| Enzyme 82 SNPs |
SNPJam Report  |
| Enzyme 82 General References |
- Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, Berger SL: Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol Cell Biol. 1996 Feb;16(2):593-602. [PubMed
]
- Smith ER, Belote JM, Schiltz RL, Yang XJ, Moore PA, Berger SL, Nakatani Y, Allis CD: Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members. Nucleic Acids Res. 1998 Jun 15;26(12):2948-54. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 1996 Jul 25;382(6589):319-24. [PubMed
]
- Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG: Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol Cell Biol. 2001 Oct;21(20):6782-95. [PubMed
]
- Brand M, Yamamoto K, Staub A, Tora L: Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. J Biol Chem. 1999 Jun 25;274(26):18285-9. [PubMed
]
- McMahon SB, Wood MA, Cole MD: The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. Mol Cell Biol. 2000 Jan;20(2):556-62. [PubMed
]
- Col E, Caron C, Seigneurin-Berny D, Gracia J, Favier A, Khochbin S: The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat. J Biol Chem. 2001 Jul 27;276(30):28179-84. Epub 2001 May 30. [PubMed
]
- Gangloff YG, Pointud JC, Thuault S, Carre L, Romier C, Muratoglu S, Brand M, Tora L, Couderc JL, Davidson I: The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger. Mol Cell Biol. 2001 Aug;21(15):5109-21. [PubMed
]
- Gangisetty O, Lauffart B, Sondarva GV, Chelsea DM, Still IH: The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases. Oncogene. 2004 Apr 1;23(14):2559-63. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Zhao Y, Lang G, Ito S, Bonnet J, Metzger E, Sawatsubashi S, Suzuki E, Le Guezennec X, Stunnenberg HG, Krasnov A, Georgieva SG, Schule R, Takeyama K, Kato S, Tora L, Devys D: A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing. Mol Cell. 2008 Jan 18;29(1):92-101. [PubMed
]
- Guelman S, Kozuka K, Mao Y, Pham V, Solloway MJ, Wang J, Wu J, Lill JR, Zha J: The double-histone-acetyltransferase complex ATAC is essential for mammalian development. Mol Cell Biol. 2009 Mar;29(5):1176-88. Epub 2008 Dec 22. [PubMed
]
- Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE: Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J Mol Biol. 2000 Dec 1;304(3):355-70. [PubMed
]
|
| Enzyme 82 Metabolite References |
Not Available |
|
Enzyme 83
[top]
|
| Enzyme 83 ID |
8205 |
| Enzyme 83 Name |
Fatty acid-binding protein, heart |
| Enzyme 83 Synonyms |
- Fatty acid-binding protein 3
- Heart-type fatty acid-binding protein
- H-FABP
- Mammary-derived growth inhibitor
- MDGI
- Muscle fatty acid-binding protein
- M-FABP
|
| Enzyme 83 Gene Name |
FABP3 |
| Enzyme 83 Protein Sequence |
>Fatty acid-binding protein, heart
MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKN
TEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTH
GTAVCTRTYEKEA
|
| Enzyme 83 Number of Residues |
133 |
| Enzyme 83 Molecular Weight |
14857.9 |
| Enzyme 83 Theoretical pI |
6.80 |
| Enzyme 83 GO Classification |
| Function |
- binding
- lipid binding
- transporter activity
|
| Process |
- establishment of localization
- transport
|
| Component |
| — |
|
| Enzyme 83 General Function |
Involved in negative regulation of cell proliferation |
| Enzyme 83 Specific Function |
FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters |
| Enzyme 83 Pathways |
Not Available |
| Enzyme 83 Reactions |
Not Available |
| Enzyme 83 Pfam Domain Function |
|
| Enzyme 83 Signals |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
189054293  |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
P05413  |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
FABPH_HUMAN  |
| Enzyme 83 PDB ID |
1G5W  |
| Enzyme 83 PDB File |
Show |
| Enzyme 83 3D Structure |
|
| Enzyme 83 Cellular Location |
Not Available |
| Enzyme 83 Gene Sequence |
>402 bp
ATGGTGGACGCTTTCCTGGGCACCTGGAAGCTAGTGGACAGCAAGAATTTCGATGACTAC
ATGAAGTCACTCGGTGTGGGTTTTGCTACCAGGCAGGTGGCCAGCATGACCAAGCCTACC
ACAATCATCGAAAAGAATGGGGACATTCTCACCCTAAAAACACACAGCACCTTCAAGAAC
ACAGAGATCAGCTTTAAGTTGGGGGTGGAGTTCGATGAGACAACAGCAGATGACAGGAAG
GTCAAGTCCATTGTGACACTGGATGGAGGGAAACTTGTTCACCTGCAGAAATGGGACGGG
CAAGAGACCACACTTGTGCGGGAGCTAATTGATGGAAAACTCATCCTGACACTCACCCAC
GGCACTGCAGTTTGCACTCGCACTTACGAGAAAGAGGCATGA
|
| Enzyme 83 GenBank Gene ID |
AK314122  |
| Enzyme 83 GeneCard ID |
FABP3  |
| Enzyme 83 GenAtlas ID |
Not Available |
| Enzyme 83 HGNC ID |
Not Available |
| Enzyme 83 Chromosome Location |
1 |
| Enzyme 83 Locus |
1p33-p32 |
| Enzyme 83 SNPs |
SNPJam Report  |
| Enzyme 83 General References |
- Peeters RA, Veerkamp JH, Geurts van Kessel A, Kanda T, Ono T: Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding protein, its peptide sequence and chromosomal localization. Biochem J. 1991 May 15;276 ( Pt 1):203-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Offner GD, Brecher P, Sawlivich WB, Costello CE, Troxler RF: Characterization and amino acid sequence of a fatty acid-binding protein from human heart. Biochem J. 1988 May 15;252(1):191-8. [PubMed
]
- Borchers T, Hojrup P, Nielsen SU, Roepstorff P, Spener F, Knudsen J: Revision of the amino acid sequence of human heart fatty acid-binding protein. Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):127-33. [PubMed
]
- Troxler RF, Offner GD, Jiang JW, Wu BL, Skare JC, Milunsky A, Wyandt HE: Localization of the gene for human heart fatty acid binding protein to chromosome 1p32-1p33. Hum Genet. 1993 Dec;92(6):563-6. [PubMed
]
- Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [PubMed
]
- Zanotti G, Scapin G, Spadon P, Veerkamp JH, Sacchettini JC: Three-dimensional structure of recombinant human muscle fatty acid-binding protein. J Biol Chem. 1992 Sep 15;267(26):18541-50. [PubMed
]
- Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC: Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids. Structure. 1994 Jun 15;2(6):523-34. [PubMed
]
- Lucke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Ruterjans H: Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP). Biochem J. 2001 Mar 1;354(Pt 2):259-66. [PubMed
]
|
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
8524 |
| Enzyme 84 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon |
| Enzyme 84 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 5
- 1-AGP acyltransferase 5
- 1-AGPAT 5
- Lysophosphatidic acid acyltransferase epsilon
- LPAAT-epsilon
|
| Enzyme 84 Gene Name |
AGPAT5 |
| Enzyme 84 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQS
MVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLK
EGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPE
QTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQ
RRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPD
PERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWV
TIKA
|
| Enzyme 84 Number of Residues |
364 |
| Enzyme 84 Molecular Weight |
42071.8 |
| Enzyme 84 Theoretical pI |
9.41 |
| Enzyme 84 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 84 General Function |
Involved in acyltransferase activity |
| Enzyme 84 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 84 Pathways |
|
| Enzyme 84 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
|
| Enzyme 84 Pfam Domain Function |
|
| Enzyme 84 Signals |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
14161585  |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
Q9NUQ2  |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
PLCE_HUMAN  |
| Enzyme 84 PDB ID |
Not Available |
| Enzyme 84 Cellular Location |
Not Available |
| Enzyme 84 Gene Sequence |
>1095 bp
ATGCTGCTGTCCCTGGTGCTCCACACGTACTCCATGCGCTACCTGCTGCCCAGCGTCGTG
CTCCTGGGCACGGCGCCCACCTACGTGTTGGCCTGGGGGGTCTGGCGGCTGCTCTCCGCC
TTCCTGCCCGCCCGCTTCTACCAAGCGCTGGACGACCGGCTCTACTGCGTCTACCAGAGC
ATGGTGCTCTTCTTCTTCGAGAATTACACCGGGGTCCAGATATTGCTATATGGAGATTTG
CCAAAAAATAAAGAAAATATAATATATTTAGCAAATCATCAAAGCACAGTTGACTGGATT
GTTGCTGACATCTTGGCCATCAGGCAGAATGCGCTAGGACATGTGCGCTACGTGCTGAAA
GAAGGGTTAAAATGGCTGCCATTGTATGGGTGTTACTTTGCTCAGCATGGAGGAATCTAT
GTAAAGCGCAGTGCCAAATTTAACGAGAAAGAGATGCGAAACAAGTTGCAGAGCTACGTG
GACGCAGGAACTCCAATGTATCTTGTGATTTTTCCAGAAGGTACAAGGTATAATCCAGAG
CAAACAAAAGTCCTTTCAGCTAGTCAGGCATTTGCTGCCCAACGTGGCCTTGCAGTATTA
AAACATGTGCTAACACCACGAATAAAGGCAACTCACGTTGCTTTTGATTGCATGAAGAAT
TATTTAGATGCAATTTATGATGTTACGGTGGTTTATGAAGGGAAAGACGATGGAGGGCAG
CGAAGAGAGTCACCGACCATGACGGAATTTCTCTGCAAAGAATGTCCAAAAATTCATATT
CACATTGATCGTATCGACAAAAAAGATGTCCCAGAAGAACAAGAACATATGAGAAGATGG
CTGCATGAACGTTTCGAAATCAAAGATAAGATGCTTATAGAATTTTATGAGTCACCAGAT
CCAGAAAGAAGAAAAAGATTTCCTGGGAAAAGTGTTAATTCCAAATTAAGTATCAAGAAG
ACTTTACCATCAATGTTGATCTTAAGTGGTTTGACTGCAGGCATGCTTATGACCGATGCT
GGAAGGAAGCTGTATGTGAACACCTGGATATATGGAACCCTACTTGGCTGCCTGTGGGTT
ACTATTAAAGCATAG
|
| Enzyme 84 GenBank Gene ID |
AF375789  |
| Enzyme 84 GeneCard ID |
AGPAT5  |
| Enzyme 84 GenAtlas ID |
AGPAT5  |
| Enzyme 84 HGNC ID |
HGNC:20886  |
| Enzyme 84 Chromosome Location |
8 |
| Enzyme 84 Locus |
8p23.1 |
| Enzyme 84 SNPs |
SNPJam Report  |
| Enzyme 84 General References |
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
8564 |
| Enzyme 85 Name |
Acetyl-coenzyme A transporter 1 |
| Enzyme 85 Synonyms |
- AT-1
- Acetyl-CoA transporter 1
- Solute carrier family 33 member 1
|
| Enzyme 85 Gene Name |
SLC33A1 |
| Enzyme 85 Protein Sequence |
>Acetyl-coenzyme A transporter 1
MSPTISHKDSSRQRRPGNFSHSLDMKSGPLPPGGWDDSHLDSAGREGDREALLGDTGTGD
FLKAPQSFRAELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFS
LKLLWAPLVDAVYVKNFGRRKSWLVPTQYILGLFMIYLSTQVDRLLGNTDDRTPDVIALT
VAFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADF
CNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENEVSVVKEETQGITDTYKL
LFAIIKMPAVLTFCLLILTAKIGFSAADAVTGLKLVEEGVPKEHLALLAVPMVPLQIILP
LIISKYTAGPQPLNTFYKAMPYRLLLGLEYALLVWWTPKVEHQGGFPIYYYIVVLLSYAL
HQVTVYSMYVSIMAFNAKVSDPLIGGTYMTLLNTVSNLGGNWPSTVALWLVDPLTVKECV
GASNQNCRTPDAVELCKKLGGSCVTALDGYYVESIICVFIGFGWWFFLGPKFKKLQDEGS
SSWKCKRNN
|
| Enzyme 85 Number of Residues |
549 |
| Enzyme 85 Molecular Weight |
60908.4 |
| Enzyme 85 Theoretical pI |
7.37 |
| Enzyme 85 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 85 General Function |
Carbohydrate transport and metabolism |
| Enzyme 85 Specific Function |
Probable acetyl-CoA transporter necessary for O- acetylation of gangliosides |
| Enzyme 85 Pathways |
Not Available |
| Enzyme 85 Reactions |
Not Available |
| Enzyme 85 Pfam Domain Function |
Not Available |
| Enzyme 85 Signals |
|
| Enzyme 85 Transmembrane Regions |
- 75-95
114-134
142-162
176-196
218-238
257-277
300-320
344-364
379-398
405-425
509-529
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
189053393  |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
O00400  |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
ACATN_HUMAN  |
| Enzyme 85 PDB ID |
Not Available |
| Enzyme 85 Cellular Location |
Not Available |
| Enzyme 85 Gene Sequence |
>1650 bp
ATGTCACCCACCATCTCCCACAAGGACAGCAGCCGGCAACGGCGGCCAGGGAATTTCAGT
CACTCTCTGGATATGAAGAGCGGTCCCCTGCCGCCAGGCGGTTGGGATGACAGTCATTTG
GACTCAGCGGGCCGGGAAGGGGACAGAGAAGCTCTTCTGGGGGATACCGGCACTGGCGAC
TTCTTAAAAGCCCCACAGAGCTTCCGGGCCGAACTAAGCAGCATTTTGCTACTACTCTTT
CTTTACGTGCTTCAGGGTATTCCCCTGGGCTTGGCGGGAAGCATCCCACTCATTTTGCAA
AGCAAAAATGTTAGCTATACAGACCAAGCTTTCTTCAGTTTTGTCTTTTGGCCCTTCAGT
CTCAAATTACTCTGGGCCCCGTTGGTTGATGCGGTCTACGTTAAGAACTTCGGTCGTCGC
AAATCTTGGCTTGTCCCGACACAGTATATACTAGGACTCTTCATGATCTATTTATCCACT
CAGGTGGACCGTTTGCTTGGGAATACCGATGACAGAACACCCGACGTGATTGCTCTCACT
GTGGCGTTCTTTTTGTTTGAATTCTTGGCCGCCACTCAGGACATTGCCGTCGATGGTTGG
GCGTTAACTATGTTATCCAGGGAAAATGTGGGTTATGCTTCTACTTGCAATTCGGTGGGC
CAAACAGCGGGTTACTTTTTGGGCAATGTTTTGTTTTTGGCCCTTGAATCTGCCGACTTT
TGTAACAAATATTTGCGGTTTCAGCCTCAACCCAGAGGAATCGTTACTCTTTCAGATTTC
CTTTTTTTCTGGGGAACTGTATTTTTAATAACAACAACATTGGTTGCCCTTCTGAAAAAA
GAAAACGAAGTATCAGTAGTAAAAGAAGAAACACAAGGGATCACAGATACTTACAAGCTG
CTTTTTGCAATTATAAAAATGCCAGCAGTTCTGACATTTTGCCTTCTGATTCTAACTGCA
AAGATTGGTTTTTCAGCAGCAGATGCTGTAACAGGACTGAAATTGGTAGAAGAGGGAGTA
CCCAAAGAACATTTAGCCTTATTGGCAGTTCCAATGGTTCCTTTGCAGATAATACTGCCT
CTGATTATCAGCAAATACACTGCAGGTCCCCAGCCATTAAACACATTTTACAAAGCCATG
CCCTACAGATTATTGCTTGGGTTAGAATATGCCCTACTGGTTTGGTGGACTCCTAAAGTA
GAACATCAAGGGGGATTCCCTATATATTACTATATCGTAGTCCTGCTGAGTTATGCTTTA
CATCAGGTTACAGTGTACAGCATGTATGTTTCTATAATGGCTTTCAATGCAAAGGTTAGT
GATCCACTTATTGGAGGAACATACATGACCCTTTTAAATACCGTGTCCAATCTGGGAGGA
AACTGGCCTTCTACAGTAGCTCTTTGGCTTGTAGATCCCCTCACAGTAAAAGAGTGTGTA
GGAGCATCAAACCAGAATTGTCGAACACCTGATGCTGTTGAGCTTTGCAAAAAACTGGGT
GGCTCATGTGTTACAGCCCTGGATGGTTATTATGTGGAGTCCATTATTTGTGTTTTCATT
GGATTTGGTTGGTGGTTCTTTCTTGGTCCAAAATTTAAAAAGTTACAGGATGAAGGATCA
TCTTCGTGGAAATGCAAAAGGAACAATTAA
|
| Enzyme 85 GenBank Gene ID |
AK312268  |
| Enzyme 85 GeneCard ID |
SLC33A1  |
| Enzyme 85 GenAtlas ID |
SLC33A1  |
| Enzyme 85 HGNC ID |
HGNC:95  |
| Enzyme 85 Chromosome Location |
3 |
| Enzyme 85 Locus |
3q25.31 |
| Enzyme 85 SNPs |
SNPJam Report  |
| Enzyme 85 General References |
- Kanamori A, Nakayama J, Fukuda MN, Stallcup WB, Sasaki K, Fukuda M, Hirabayashi Y: Expression cloning and characterization of a cDNA encoding a novel membrane protein required for the formation of O-acetylated ganglioside: a putative acetyl-CoA transporter. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2897-902. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
- Lin P, Li J, Liu Q, Mao F, Li J, Qiu R, Hu H, Song Y, Yang Y, Gao G, Yan C, Yang W, Shao C, Gong Y: A missense mutation in SLC33A1, which encodes the acetyl-CoA transporter, causes autosomal-dominant spastic paraplegia (SPG42). Am J Hum Genet. 2008 Dec;83(6):752-9. [PubMed
]
|
| Enzyme 85 Metabolite References |
Not Available |
|
Enzyme 86
[top]
|
| Enzyme 86 ID |
8587 |
| Enzyme 86 Name |
Bile acyl-CoA synthetase |
| Enzyme 86 Synonyms |
- BACS
- Bile acid-CoA ligase
- BA-CoA ligase
- BAL
- Cholate--CoA ligase
- Fatty acid transport protein 5
- FATP-5
- Fatty-acid-coenzyme A ligase, very long-chain 3
- Solute carrier family 27 member 5
- Very long-chain acyl-CoA synthetase homolog 2
- VLCS-H2
- VLCSH2
- Very long-chain acyl-CoA synthetase-related protein
- VLACS-related
- VLACSR
|
| Enzyme 86 Gene Name |
SLC27A5 |
| Enzyme 86 Protein Sequence |
>Bile acyl-CoA synthetase
MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWV
PHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAF
ERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVL
ASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILP
KLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTG
LPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP
KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ
QRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDN
QGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMD
REGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQ
LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVD
PLFVLDNRAQSFRPLTAEMYQAVCEGTWRL
|
| Enzyme 86 Number of Residues |
690 |
| Enzyme 86 Molecular Weight |
75384.4 |
| Enzyme 86 Theoretical pI |
7.70 |
| Enzyme 86 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 86 General Function |
Involved in catalytic activity |
| Enzyme 86 Specific Function |
Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol |
| Enzyme 86 Pathways |
|
| Enzyme 86 Reactions |
- (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN:R02794]
- (2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN:R04580]
|
| Enzyme 86 Pfam Domain Function |
|
| Enzyme 86 Signals |
|
| Enzyme 86 Transmembrane Regions |
|
| Enzyme 86 Essentiality |
Not Available |
| Enzyme 86 GenBank ID Protein |
4768277  |
| Enzyme 86 UniProtKB/Swiss-Prot ID |
Q9Y2P5  |
| Enzyme 86 UniProtKB/Swiss-Prot Entry Name |
S27A5_HUMAN  |
| Enzyme 86 PDB ID |
Not Available |
| Enzyme 86 Cellular Location |
Not Available |
| Enzyme 86 Gene Sequence |
>2073 bp
ATGGGTGTCAGGCAACAGTTGGCCTTGCTGCTGCTGCTGCTGCTCCTGCTCTGGGGCCTG
GGGCAGCCAGTGTGGCCAGTCGCTGTGGCCTTGACCCTGCGCTGGCTCCTGGGGGATCCC
ACATGTTGCGTGCTACTTGGGCTGGCCATGTTAGCACGGCCCTGGCTCGGCCCCTGGGTG
CCCCATGGGCTGAGCCTGGCAGCTGCGGCCCTGGCACTAACCCTCCTGCCAGCACGGCTG
CCCCCAGGACTACGCTGGCTGCCGGCTGATGTGATCTTCTTGGCCAAGATCCTCCACCTG
GGCCTGAAGATCAGGGGATGCTTGAGCCGGCAGCCGCCTGACACCTTTGTAGATGCCTTC
GAGCGGCGAGCACGAGCGCAGCCTGGCAGGGCACTCTTGGTGTGGACGGGGCCTGGGGCC
GGCTCAGTCACCTTTGGTGAGCTGGATGCCCGGGCCTGCCAGGCGGCATGGGCCCTGAAG
GCTGAGCTGGGTGACCCTGCGAGCCTGTGTGCCGGGGAGCCTACTGCCCTCCTTGTGCTG
GCTTCCCAGGCCGTTCCAGCCCTGTGTATGTGGCTGGGGCTGGCCAAGCTGGGCTGCCCA
ACAGCCTGGATCAACCCGCATGGCCGGGGGATGCCCCTGGCGCACTCTGTGCTGAGCTCT
GGGGCCCGGGTGCTGGTGGTGGACCCAGACCTCCGGGAGAGCCTGGAGGAGATCCTTCCC
AAGCTGCAGGCTGAGAACATCCGCTGCTTCTACCTCAGCCATACCTCCCCTACACCAGGG
GTGGGGGCTCTGGGGGCTGCCCTGGATGCAGCGCCCTCCCACCCAGTGCCTGCTGACCTG
CGTGCTGGGATCACATGGAGAAGCCCTGCCCTCTTCATCTATACCTCGGGGACCACTGGC
CTCCCGAAGCCAGCCATCCTCACGCATGAGCGGGTACTGCAGATGAGCAAGATGCTGTCC
TTATCTGGGGCCACAGCTGATGATGTGGTTTACACGGTCCTGCCTCTGTACCACGTGATG
GGACTTGTCGTTGGGATCCTCGGCTGCTTAGATCTCGGAGCCACCTGTGTTCTGGCCCCC
AAGTTCTCTACTTCCTGCTTCTGGGATGACTGTCGGCAGCATGGCGTGACAGTGATCCTG
TATGTGGGCGAGCTCCTGCGGTACTTGTGTAACATTCCCCAGCAACCAGAGGACCGGACA
CATACAGTCCGCCTGGCAATGGGCAATGGACTACGGGCTGATGTGTGGGAGACCTTCCAG
CAGCGCTTCGGTCCTATTCGGATCTGGGAAGTCTACGGCTCCACAGAAGGCAACATGGGC
TTAGTCAACTATGTGGGGCGCTGCGGGGCCCTGGGCAAGATGAGCTGCCTCCTCCGAATG
CTGTCCCCCTTTGAGCTGGTGCAGTTCGACATGGAGGCGGCGGAGCCTGTGAGGGACAAT
CAGGGCTTCTGCATCCCTGTAGGGCTAGGGGAGCCGGGGCTGCTGCTGACCAAGGTGGTA
AGCCAGCAACCCTTCGTGGGCTACCGCGGCCCCCGAGAGCTGTCGGAACGGAAGCTGGTG
CGCAACGTGCGGCAATCGGGCGACGTTTACTACAACACCGGGGACGTACTGGCCATGGAC
CGCGAAGGCTTCCTCTACTTCCGCGACCGCCTCGGGGACACCTTCCGATGGAAGGGCGAG
AACGTGTCCACGCACGAGGTGGAGGGCGTGTTGTCGCAGGTGGACTTCTTGCAACAGGTT
AACGTGTATGGCGTGTGCGTGCCAGGTTGTGAGGGTAAGGTGGGCATGGCTGCTGTGCAG
CTAGCCCCCGGCCAGACTTTCGACGGGGAGAAGTTGTACCAGCACGTTCGCGCTTGGCTC
CCTGCCTACGCTACCCCCCATTTCATCCGCATCCAGGACGCCATGGAGGTCACCAGCACG
TTCAAACTGATGAAGACCCGGTTGGTGCGTGAGGGCTTCAATGTGGGGATCGTGGTTGAC
CCTCTGTTTGTACTGGACAACCGGGCCCAGTCCTTCCGGCCCCTGACGGCAGAAATGTAC
CAGGCTGTGTGTGAGGGAACCTGGAGGCTCTGA
|
| Enzyme 86 GenBank Gene ID |
AF064255  |
| Enzyme 86 GeneCard ID |
SLC27A5  |
| Enzyme 86 GenAtlas ID |
SLC27A5  |
| Enzyme 86 HGNC ID |
HGNC:10999  |
| Enzyme 86 Chromosome Location |
1 |
| Enzyme 86 Locus |
19q13.43 |
| Enzyme 86 SNPs |
SNPJam Report  |
| Enzyme 86 General References |
- Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA: Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. Mol Genet Metab. 1999 Sep;68(1):32-42. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Steinberg SJ, Mihalik SJ, Kim DG, Cuebas DA, Watkins PA: The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase. J Biol Chem. 2000 May 26;275(21):15605-8. [PubMed
]
- Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA: Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. J Biol Chem. 2002 Jul 5;277(27):24771-9. Epub 2002 Apr 29. [PubMed
]
|
| Enzyme 86 Metabolite References |
Not Available |
|
Enzyme 87
[top]
|
| Enzyme 87 ID |
8614 |
| Enzyme 87 Name |
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial |
| Enzyme 87 Synonyms |
- Branched-chain alpha-keto acid dehydrogenase complex component E2
- BCKAD-E2
- BCKADE2
- Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
- Dihydrolipoamide branched chain transacylase
- Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
|
| Enzyme 87 Gene Name |
DBT |
| Enzyme 87 Protein Sequence |
>Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAAL
RGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKK
LYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRL
AMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPIL
VSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFA
RGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVK
NVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAI
GALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD
LK
|
| Enzyme 87 Number of Residues |
482 |
| Enzyme 87 Molecular Weight |
53486.6 |
| Enzyme 87 Theoretical pI |
8.75 |
| Enzyme 87 GO Classification |
| Function |
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- fatty-acyl-CoA biosynthetic process
- fatty-acyl-CoA metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 87 General Function |
Involved in acyltransferase activity |
| Enzyme 87 Specific Function |
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 87 Pathways |
Not Available |
| Enzyme 87 Reactions |
- 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine [RN:R02662]
|
| Enzyme 87 Pfam Domain Function |
|
| Enzyme 87 Signals |
|
| Enzyme 87 Transmembrane Regions |
|
| Enzyme 87 Essentiality |
Not Available |
| Enzyme 87 GenBank ID Protein |
189053756  |
| Enzyme 87 UniProtKB/Swiss-Prot ID |
P11182  |
| Enzyme 87 UniProtKB/Swiss-Prot Entry Name |
ODB2_HUMAN  |
| Enzyme 87 PDB ID |
1K8O  |
| Enzyme 87 PDB File |
Show |
| Enzyme 87 3D Structure |
|
| Enzyme 87 Cellular Location |
Not Available |
| Enzyme 87 Gene Sequence |
>1449 bp
ATGGCTGCAGTCCGTATGCTGAGAACCTGGAGCAGGAATGCGGGGAAGCTGATTTGTGTT
CGCTATTTTCAAACATGTGGTAATGTTCATGTTTTGAAGCCAAATTATGTGTGTTTCTTT
GGTTATCCTTCATTCAAGTATAGTCATCCACATCACTTCCTGAAAACAACTGCTGCTCTC
CGTGGACAGGTTGTTCAGTTCAAGCTCTCAGACATTGGAGAAGGGATTAGAGAAGTAACT
GTTAAAGAATGGTATGTAAAAGAAGGAGATACAGTGTCTCAGTTTGATAGCATCTGTGAA
GTTCAAAGTGATAAAGCTTCTGTTACCATCACTAGTCGTTATGATGGAGTCATTAAAAAA
CTCTATTATAATCTAGACGATATTGCCTATGTGGGGAAGCCATTAGTAGACATAGAAACG
GAAGCTTTAAAAGATTCAGAAGAAGATGTTGTTGAAACTCCTGCAGTGTCTCATGATGAA
CATACACACCAAGAGATAAAGGGCCGAAAAACACTGGCAACTCCTGCAGTTCGCCGTCTG
GCAATGGAAAACAATATTAAGCTGAGTGAAGTTGTTGGCTCAGGAAAAGATGGCAGAATA
CTTAAAGAAGATATCCTCAACTATTTGGAAAAGCAGACAGGAGCTATATTGCCTCCTTCA
CCCAAAGTTGAAATTATGCCACCTCCACCAAAGCCAAAAGACATGACTGTTCCTATACTA
GTATCAAAACCTCCGGTATTCACAGGCAAAGACAAAACAGAACCCATAAAAGGCTTTCAA
AAAGCAATGGTCAAGACTATGTCTGCAGCCCTGAAGATACCTCATTTTGGTTATTGTGAT
GAGATTGACCTTACTGAACTGGTTAAGCTCCGAGAAGAATTAAAACCCATTGCATTTGCT
CGTGGAATTAAACTCTCCTTTATGCCTTTCTTCTTAAAGGCTGCTTCCTTGGGATTACTA
CAGTTTCCTATCCTTAACGCTTCTGTGGATGAAAACTGCCAGAATATAACATATAAGGCT
TCTCATAACATTGGGATAGCAATGGATACTGAGCAGGGTTTGATTGTCCCTAATGTGAAA
AATGTTCAGATCTGCTCTATATTTGACATCGCCACTGAACTGAACCGCCTCCAGAAATTG
GGCTCTGTGGGTCAGCTCAGCACCACTGATCTTACAGGAGGAACATTTACTCTTTCCAAC
ATTGGATCAATTGGTGGTACCTTTGCCAAACCAGTGATAATGCCACCTGAAGTAGCCATT
GGGGCCCTTGGATCAATTAAGGCCATTCCCCGATTTAACCAGAAAGGAGAAGTATATAAG
GCACAGATAATGAATGTGAGCTGGTCAGCTGATCACAGAGTTATTGATGGTGCTACAATG
TCACGCTTCTCCAATTTGTGGAAATCCTATTTAGAAAACCCAGCTTTTATGCTACTAGAT
CTGAAATGA
|
| Enzyme 87 GenBank Gene ID |
AK313191  |
| Enzyme 87 GeneCard ID |
DBT  |
| Enzyme 87 GenAtlas ID |
DBT  |
| Enzyme 87 HGNC ID |
HGNC:2698  |
| Enzyme 87 Chromosome Location |
1 |
| Enzyme 87 Locus |
1p31 |
| Enzyme 87 SNPs |
SNPJam Report  |
| Enzyme 87 General References |
- Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT: The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex. Biochim Biophys Acta. 1992 Oct 20;1132(3):319-21. [PubMed
]
- Hummel KB, Litwer S, Bradford AP, Aitken A, Danner DJ, Yeaman SJ: Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure. J Biol Chem. 1988 May 5;263(13):6165-8. [PubMed
]
- Danner DJ, Litwer S, Herring WJ, Pruckler J: Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase. J Biol Chem. 1989 May 5;264(13):7742-6. [PubMed
]
- Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I: Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex. Biochem Biophys Res Commun. 1989 Jun 30;161(3):1035-41. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lau KS, Griffin TA, Hu CW, Chuang DT: Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry. 1988 Mar 22;27(6):1972-81. [PubMed
]
- Lau KS, Herring WJ, Chuang JL, McKean M, Danner DJ, Cox RP, Chuang DT: Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene. J Biol Chem. 1992 Nov 25;267(33):24090-6. [PubMed
]
- Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Chang CF, Chou HT, Chuang JL, Chuang DT, Huang TH: Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. J Biol Chem. 2002 May 3;277(18):15865-73. Epub 2002 Feb 11. [PubMed
]
- Fisher CW, Lau KS, Fisher CR, Wynn RM, Cox RP, Chuang DT: A 17-bp insertion and a Phe215----Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34. Biochem Biophys Res Commun. 1991 Jan 31;174(2):804-9. [PubMed
]
- Tsuruta M, Mitsubuchi H, Mardy S, Miura Y, Hayashida Y, Kinugasa A, Ishitsu T, Matsuda I, Indo Y: Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex. J Hum Genet. 1998;43(2):91-100. [PubMed
]
|
| Enzyme 87 Metabolite References |
Not Available |
|
Enzyme 88
[top]
|
| Enzyme 88 ID |
8626 |
| Enzyme 88 Name |
2-acylglycerol O-acyltransferase 2 |
| Enzyme 88 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 2
- MGAT2
- hMGAT2
- Diacylglycerol O-acyltransferase candidate 5
- hDC5
- Diacylglycerol acyltransferase 2-like protein 5
- Monoacylglycerol O-acyltransferase 2
|
| Enzyme 88 Gene Name |
MOGAT2 |
| Enzyme 88 Protein Sequence |
>2-acylglycerol O-acyltransferase 2
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
|
| Enzyme 88 Number of Residues |
334 |
| Enzyme 88 Molecular Weight |
38195.3 |
| Enzyme 88 Theoretical pI |
9.77 |
| Enzyme 88 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 88 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 88 Specific Function |
Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity |
| Enzyme 88 Pathways |
|
| Enzyme 88 Reactions |
- acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
|
| Enzyme 88 Pfam Domain Function |
|
| Enzyme 88 Signals |
|
| Enzyme 88 Transmembrane Regions |
|
| Enzyme 88 Essentiality |
Not Available |
| Enzyme 88 GenBank ID Protein |
37537527  |
| Enzyme 88 UniProtKB/Swiss-Prot ID |
Q3SYC2  |
| Enzyme 88 UniProtKB/Swiss-Prot Entry Name |
MOGT2_HUMAN  |
| Enzyme 88 PDB ID |
Not Available |
| Enzyme 88 Cellular Location |
Not Available |
| Enzyme 88 Gene Sequence |
>1005 bp
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
|
| Enzyme 88 GenBank Gene ID |
NM_025098.2  |
| Enzyme 88 GeneCard ID |
MOGAT2  |
| Enzyme 88 GenAtlas ID |
MOGAT2  |
| Enzyme 88 HGNC ID |
HGNC:23248  |
| Enzyme 88 Chromosome Location |
1 |
| Enzyme 88 Locus |
11q13.5 |
| Enzyme 88 SNPs |
SNPJam Report  |
| Enzyme 88 General References |
- Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lockwood JF, Cao J, Burn P, Shi Y: Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E927-37. Epub 2003 Jun 24. [PubMed
]
|
| Enzyme 88 Metabolite References |
Not Available |
|
Enzyme 89
[top]
|
| Enzyme 89 ID |
8676 |
| Enzyme 89 Name |
Long-chain fatty acid transport protein 3 |
| Enzyme 89 Synonyms |
- FATP-3
- Fatty acid transport protein 3
- Solute carrier family 27 member 3
- Very long-chain acyl-CoA synthetase homolog 3
- VLCS-3
|
| Enzyme 89 Gene Name |
SLC27A3 |
| Enzyme 89 Protein Sequence |
>Long-chain fatty acid transport protein 3
MGVCQRTRAPWKEKSQLERAALGFRKGGSGMFASGWNQTVPIEEAGSMAALLLLPLLLLL
PLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEGPEGGCSLAWRLAE
LAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGGDSGEGSAGEGERA
APGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEFLWLWFGLAKAGLR
TAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAG
ISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQ
LCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQ
YIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVA
TINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVS
QQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGE
NVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENL
PPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQAVGAYLPLTTARY
SALLAGNLRI
|
| Enzyme 89 Number of Residues |
730 |
| Enzyme 89 Molecular Weight |
78643.4 |
| Enzyme 89 Theoretical pI |
7.53 |
| Enzyme 89 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 89 General Function |
Involved in catalytic activity |
| Enzyme 89 Specific Function |
Has acyl-CoA ligase activity for long-chain and very- long-chain fatty acids. Does not exhibit fatty acid transport activity |
| Enzyme 89 Pathways |
Not Available |
| Enzyme 89 Reactions |
Not Available |
| Enzyme 89 Pfam Domain Function |
|
| Enzyme 89 Signals |
|
| Enzyme 89 Transmembrane Regions |
|
| Enzyme 89 Essentiality |
Not Available |
| Enzyme 89 GenBank ID Protein |
13236579  |
| Enzyme 89 UniProtKB/Swiss-Prot ID |
Q5K4L6  |
| Enzyme 89 UniProtKB/Swiss-Prot Entry Name |
S27A3_HUMAN  |
| Enzyme 89 PDB ID |
Not Available |
| Enzyme 89 Cellular Location |
Not Available |
| Enzyme 89 Gene Sequence |
>2193 bp
ATGGGCGTGTGCCAGCGCACGCGCGCTCCCTGGAAGGAGAAGTCTCAGCTAGAACGAGCG
GCCCTAGGTTTTCGGAAGGGAGGATCAGGGATGTTTGCGAGCGGCTGGAACCAGACGGTG
CCGATAGAGGAAGCGGGCTCCATGGCTGCCCTCCTGCTGCTGCCCCTGCTGCTGTTGCTA
CCGCTGCTGCTGCTGAAGCTACACCTCTGGCCGCAGTTGCGCTGGCTTCCGGCGGACTTG
GCCTTTGCGGTGCGAGCTCTGTGCTGCAAAAGGGCTCTTCGAGCTCGCGCCCTGGCCGCG
GCTGCCGCCGACCCGGAAGGTCCCGAGGGGGGCTGCAGCCTGGCCTGGCGCCTCGCGGAA
CTGGCCCAGCAGCGCGCCGCGCACACCTTTCTCATTCACGGCTCGCGGCGCTTTAGCTAC
TCAGAGGCGGAGCGCGAGAGTAACAGGGCTGCACGCGCCTTCCTACGTGCGCTAGGCTGG
GACTGGGGACCCGACGGCGGCGACAGCGGCGAGGGGAGCGCTGGAGAAGGCGAGCGGGCA
GCGCCGGGAGCCGGAGATGCAGCGGCCGGAAGCGGCGCGGAGTTTGCCGGAGGGGACGGT
GCCGCCAGAGGTGGAGGAGCCGCCGCCCCTCTGTCACCTGGAGCAACTGTGGCGCTGCTC
CTCCCCGCTGGCCCAGAGTTTCTGTGGCTCTGGTTCGGGCTGGCCAAGGCCGGCCTGCGC
ACTGCCTTTGTGCCCACCGCCCTGCGCCGGGGCCCCCTGCTGCACTGCCTCCGCAGCTGC
GGCGCGCGCGCGCTGGTGCTGGCGCCAGAGTTTCTGGAGTCCCTGGAGCCGGACCTGCCC
GCCCTGAGAGCCATGGGGCTCCACCTGTGGGCTGCAGGCCCAGGAACCCACCCTGCTGGA
ATTAGCGATTTGCTGGCTGAAGTGTCCGCTGAAGTGGATGGGCCAGTGCCAGGATACCTC
TCTTCCCCCCAGAGCATAACAGACACGTGCCTGTACATCTTCACCTCTGGCACCACGGGC
CTCCCCAAGGCTGCTCGGATCAGTCATCTGAAGATCCTGCAATGCCAGGGCTTCTATCAG
CTGTGTGGTGTCCACCAGGAAGATGTGATCTACCTCGCCCTCCCACTCTACCACATGTCC
GGTTCCCTGCTGGGCATCGTGGGCTGCATGGGCATTGGGGCCACAGTGGTGCTGAAATCC
AAGTTCTCGGCTGGTCAGTTCTGGGAAGATTGCCAGCAGCACAGGGTGACGGTGTTCCAG
TACATTGGGGAGCTGTGCCGATACCTTGTCAACCAGCCCCCGAGCAAGGCAGAACGTGGC
CATAAGGTCCGGCTGGCAGTGGGCAGCGGGCTGCGCCCAGATACCTGGGAGCGTTTTGTG
CGGCGCTTCGGGCCCCTGCAGGTGCTGGAGACATATGGACTGACAGAGGGCAACGTGGCC
ACCATCAACTACACAGGACAGCGGGGCGCTGTGGGGCGTGCTTCCTGGCTTTACAAGCAT
ATCTTCCCCTTCTCCTTGATTCGCTATGATGTCACCACAGGAGAGCCAATTCGGGACCCC
CAGGGGCACTGTATGGCCACATCTCCAGGTGAGCCAGGGCTGCTGGTGGCCCCGGTAAGC
CAGCAGTCCCCATTCCTGGGCTATGCTGGCGGGCCAGAGCTGGCCCAGGGGAAGTTGCTA
AAGGATGTCTTCCGGCCTGGGGATGTTTTCTTCAACACTGGGGACCTGCTGGTCTGCGAT
GACCAAGGTTTTCTCCGCTTCCATGATCGTACTGGAGACACCTTCAGGTGGAAGGGGGAG
AATGTGGCCACAACCGAGGTGGCAGAGGTCTTCGAGGCCCTAGATTTTCTTCAGGAGGTG
AACGTCTATGGAGTCACTGTGCCAGGGCATGAAGGCAGGGCTGGAATGGCAGCCCTAGTT
CTGCGTCCCCCCCACGCTTTGGACCTTATGCAGCTCTACACCCACGTGTCTGAGAACTTG
CCACCTTATGCCCGGCCCCGATTCCTCAGGCTCCAGGAGTCTTTGGCCACCACAGAGACC
TTCAAACAGCAGAAAGTTCGGATGGCAAATGAGGGCTTCGACCCCAGCACCCTGTCTGAC
CCACTGTACGTTCTGGACCAGGCTGTAGGTGCCTACCTGCCCCTCACAACTGCCCGGTAC
AGCGCCCTCCTGGCAGGAAACCTTCGAATCTGA
|
| Enzyme 89 GenBank Gene ID |
NM_024330.1  |
| Enzyme 89 GeneCard ID |
SLC27A3  |
| Enzyme 89 GenAtlas ID |
SLC27A3  |
| Enzyme 89 HGNC ID |
HGNC:10997  |
| Enzyme 89 Chromosome Location |
1 |
| Enzyme 89 Locus |
1q21.3 |
| Enzyme 89 SNPs |
SNPJam Report  |
| Enzyme 89 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 89 Metabolite References |
Not Available |
|
Enzyme 90
[top]
|
| Enzyme 90 ID |
8735 |
| Enzyme 90 Name |
Long-chain fatty acid transport protein 1 |
| Enzyme 90 Synonyms |
- FATP-1
- Fatty acid transport protein 1
- Solute carrier family 27 member 1
|
| Enzyme 90 Gene Name |
SLC27A1 |
| Enzyme 90 Protein Sequence |
>Long-chain fatty acid transport protein 1
MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSV
LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLF
RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI
FGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGM
DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIG
VGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL
AVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR
LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSV
FSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY
GVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ
KTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL
|
| Enzyme 90 Number of Residues |
646 |
| Enzyme 90 Molecular Weight |
71107.5 |
| Enzyme 90 Theoretical pI |
8.63 |
| Enzyme 90 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 90 General Function |
Lipid transport and metabolism |
| Enzyme 90 Specific Function |
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids |
| Enzyme 90 Pathways |
Not Available |
| Enzyme 90 Reactions |
Not Available |
| Enzyme 90 Pfam Domain Function |
|
| Enzyme 90 Signals |
|
| Enzyme 90 Transmembrane Regions |
|
| Enzyme 90 Essentiality |
Not Available |
| Enzyme 90 GenBank ID Protein |
38524616  |
| Enzyme 90 UniProtKB/Swiss-Prot ID |
Q6PCB7  |
| Enzyme 90 UniProtKB/Swiss-Prot Entry Name |
S27A1_HUMAN  |
| Enzyme 90 PDB ID |
Not Available |
| Enzyme 90 Cellular Location |
Not Available |
| Enzyme 90 Gene Sequence |
>1941 bp
ATGCGGGCTCCGGGTGCGGGCGCGGCCTCGGTGGTCTCGCTGGCGCTGTTGTGGCTGCTG
GGGCTGCCGTGGACCTGGAGCGCGGCAGCGGCGCTCGGCGTGTACGTGGGCAGCGGCGGC
TGGCGCTTCCTGCGCATCGTCTGCAAGACCGCGAGGCGAGACCTCTTCGGTCTCTCTGTG
CTGATCCGCGTGCGCCTGGAGCTGCGGCGGCACCAGCGTGCCGGCCACACCATCCCGCGC
ATCTTTCAGGCGGTAGTGCAGCGACAGCCCGAGCGCCTGGCGCTGGTGGATGCCGGGACC
GGCGAGTGCTGGACCTTTGCGCAGCTGGACGCCTACTCCAATGCGGTAGCCAACCTCTTC
CGCCAGCTGGGCTTCGCGCCGGGCGACGTGGTGGCCATCTTCCTGGAGGGCCGGCCGGAG
TTCGTGGGGCTGTGGCTGGGCCTGGCCAAGGCGGGCATGGAGGCCGCGCTGCTCAACGTG
AACCTGCGGCGCGAGCCCCTGGCCTTCTGCCTGGGCACCTCGGGCGCTAAGGCCCTGATC
TTTGGAGGAGAAATGGTGGCGGCGGTGGCCGAAGTGAGCGGGCATCTGGGGAAAAGTTTG
ATCAAGTTCTGCTCTGGAGACTTGGGGCCCGAGGGCATCTTGCCGGACACCCACCTCCTG
GACCCGCTGCTGAAGGAGGCCTCTACTGCCCCCTTGGCACAGATCCCCAGCAAGGGCATG
GACGATCGTCTTTTCTACATCTACACGTCGGGGACCACCGGGCTGCCCAAGGCTGCCATT
GTCGTGCACAGCAGGTACTACCGCATGGCAGCCTTCGGCCACCACGCCTACCGCATGCAG
GCGGCTGACGTGCTCTATGACTGCCTGCCCCTGTACCACTCGGCAGGAAACATCATCGGC
GTGGGGCAGTGTCTCATCTATGGGCTGACAGTCGTCCTCCGCAAGAAATTCTCGGCCAGC
CGCTTCTGGGACGACTGCATCAAGTACAACTGCACGGTGGTTCAGTACATCGGGGAGATC
TGCCGCTACCTGCTGAAGCAGCCGGTGCGCGAGGCGGAGAGGCGACACCGCGTGCGCCTG
GCGGTGGGGAACGGGCTGCGTCCTGCCATCTGGGAGGAGTTCACGGAGCGCTTCGGCGTA
CGCCAAATCGGGGAGTTCTACGGCGCCACCGAGTGCAACTGCAGCATTGCCAACATGGAC
GGCAAGGTCGGCTCCTGTGGTTTCAACAGCCGCATCCTGCCCCACGTGTACCCCATCCGG
CTGGTGAAGGTCAATGAGGACACAATGGAGCTGCTGCGGGATGCCCAGGGCCTCTGCATC
CCCTGCCAGGCCGGGGAGCCTGGCCTCCTTGTGGGTCAGATCAACCAACAGGACCCGCTG
CGCCGCTTCGATGGCTATGTCAGCGAGAGCGCCACCAGCAAGAAGATCGCCCACAGCGTC
TTCAGCAAGGGCGACAGCGCCTACCTCTCAGGTGACGTGCTAGTGATGGATGAGCTGGGC
TACATGTACTTCCGGGACCGTAGCGGGGACACCTTCCGCTGGCGAGGGGAGAACGTCTCC
ACCACCGAGGTGGAGGGCGTGCTGAGCCGCCTGCTGGGCCAGACAGACGTGGCCGTCTAT
GGGGTGGCTGTTCCAGGAGTGGAGGGTAAGGCAGGGATGGCGGCCGTCGCAGACCCCCAC
AGCCTGCTGGACCCCAACGCGATATACCAGGAGCTGCAGAAGGTGCTGGCACCCTATGCC
CGGCCCATCTTCCTGCGCCTCCTGCCCCAGGTGGACACCACAGGCACCTTCAAGATCCAG
AAGACGAGGCTGCAGCGAGAGGGCTTTGACCCACGCCAGACCTCAGACCGGCTCTTCTTC
CTGGACCTGAAGCAGGGCCACTACCTGCCCTTAAATGAGGCAGTCTACACTCGCATCTGC
TCGGGCGCCTTCGCCCTCTGA
|
| Enzyme 90 GenBank Gene ID |
NM_198580.1  |
| Enzyme 90 GeneCard ID |
SLC27A1  |
| Enzyme 90 GenAtlas ID |
Not Available |
| Enzyme 90 HGNC ID |
Not Available |
| Enzyme 90 Chromosome Location |
1 |
| Enzyme 90 Locus |
19p13.11 |
| Enzyme 90 SNPs |
SNPJam Report  |
| Enzyme 90 General References |
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Martin G, Nemoto M, Gelman L, Geffroy S, Najib J, Fruchart JC, Roevens P, de Martinville B, Deeb S, Auwerx J: The human fatty acid transport protein-1 (SLC27A1; FATP-1) cDNA and gene: organization, chromosomal localization, and expression. Genomics. 2000 Jun 15;66(3):296-304. [PubMed
]
- Hatch GM, Smith AJ, Xu FY, Hall AM, Bernlohr DA: FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells. J Lipid Res. 2002 Sep;43(9):1380-9. [PubMed
]
|
| Enzyme 90 Metabolite References |
Not Available |
|
Enzyme 91
[top]
|
| Enzyme 91 ID |
8802 |
| Enzyme 91 Name |
Acyl-CoA dehydrogenase family member 10 |
| Enzyme 91 Synonyms |
- ACAD-10
|
| Enzyme 91 Gene Name |
ACAD10 |
| Enzyme 91 Protein Sequence |
>Acyl-CoA dehydrogenase family member 10
MCVRSCFQSPRLQWVWRTAFLKHTQRRHQGSHRWTHLGGSTYRAVIFDMGGVLIPSPGRV
AAEWEVQNRIPSGTILKALMEGGENGPWMRFMRAEITAEGFLREFGRLCSEMLKTSVPVD
SFFSLLTSERVAKQFPVMTEAITQIRAKGLQTAVLSNNFYLPNQKSFLPLDRKQFDVIVE
SCMEGICKPDPRIYKLCLEQLGLQPSESIFLDDLGTNLKEAARLGIHTIKVNDPETAVKE
LEALLGFTLRVGVPNTRPVKKTMEIPKDSLQKYLKDLLGIQTTGPLELLQFDHGQSNPTY
YIRLANRDLVLRKKPPGTLLPSAHAIEREFRIMKALANAGVPVPNVLDLCEDSSVIGTPF
YVMEYCPGLIYKDPSLPGLEPSHRRAIYTAMNTVLCKIHSVDLQAVGLEDYGKQGDYIPR
QVRTWVKQYRASETSTIPAMERLIEWLPLHLPRQQRTTVVHGDFRLDNLVFHPEEPEVLA
VLDWELSTLGDPLADVAYSCLAHYLPSSFPVLRGINDCDLTQLGIPAAEEYFRMYCLQMG
LPPTENWNFYMAFSFFRVAAILQGVYKRSLTGQASSTYAEQTGKLTEFVSNLAWDFAVKE
GFRVFKEMPFTNPLTRSYHTWARPQSQWCPTGSRSYSSVPEASPAHTSRGGLVISPESLS
PPVRELYHRLKHFMEQRVYPAEPELQSHQASAARWSPSPLIEDLKEKAKAEGLWNLFLPL
EADPEKKYGAGLTNVEYAHLCELMGTSLYAPEVCNCSAPDTGNMELLVRYGTEAQKARWL
IPLLEGKARSCFAMTEPQVASSDATNIEASIREEDSFYVINGHKWWITGILDPRCQLCVF
MGKTDPHAPRHRQQSVLLVPMDTPGIKIIRPLTVYGLEDAPGGHGEVRFEHVRVPKENMV
LGPGRGFEIAQGRLGPGRIHHCMRLIGFSERALALMKARVKSRLAFGKPLVEQGTVLADI
AQSRVEIEQARLLVLRAAHLMDLAGNKAAALDIAMIKMVAPSMASRVIDRAIQAFGAAGL
SSDYPLAQFFTWARALRFADGPDEVHRATVAKLELKHRI
|
| Enzyme 91 Number of Residues |
1059 |
| Enzyme 91 Molecular Weight |
118833.0 |
| Enzyme 91 Theoretical pI |
8.13 |
| Enzyme 91 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- hydrolase activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 91 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 91 Specific Function |
May function as oxidoreductase |
| Enzyme 91 Pathways |
Not Available |
| Enzyme 91 Reactions |
Not Available |
| Enzyme 91 Pfam Domain Function |
|
| Enzyme 91 Signals |
|
| Enzyme 91 Transmembrane Regions |
|
| Enzyme 91 Essentiality |
Not Available |
| Enzyme 91 GenBank ID Protein |
48976061  |
| Enzyme 91 UniProtKB/Swiss-Prot ID |
Q6JQN1  |
| Enzyme 91 UniProtKB/Swiss-Prot Entry Name |
ACD10_HUMAN  |
| Enzyme 91 PDB ID |
Not Available |
| Enzyme 91 Cellular Location |
Not Available |
| Enzyme 91 Gene Sequence |
>3180 bp
ATGTGTGTCAGGAGCTGTTTCCAGTCCCCCCGTCTCCAGTGGGTGTGGAGAACAGCCTTC
CTGAAACACACCCAGCGCAGGCACCAGGGGTCCCACCGATGGACACACCTTGGAGGCAGC
ACCTACAGAGCGGTGATTTTCGACATGGGCGGAGTTCTCATTCCTTCTCCAGGGAGAGTC
GCTGCAGAATGGGAGGTACAGAATCGTATCCCTTCTGGAACTATATTAAAGGCCTTGATG
GAAGGTGGTGAAAATGGGCCCTGGATGAGATTTATGAGAGCAGAAATAACAGCAGAGGGT
TTTTTACGAGAATTTGGGAGACTTTGCTCTGAAATGTTAAAGACCTCCGTGCCTGTGGAC
TCATTTTTCTCTCTGTTGACCAGTGAGCGAGTGGCAAAGCAGTTCCCAGTGATGACTGAG
GCCATAACTCAAATTCGGGCAAAAGGTCTTCAGACTGCAGTCTTGAGCAATAATTTTTAT
CTTCCCAACCAGAAAAGCTTTTTGCCCCTGGACCGGAAACAGTTTGATGTGATTGTGGAG
TCCTGCATGGAAGGGATCTGTAAGCCAGACCCTAGGATCTACAAGCTGTGCTTGGAGCAG
CTCGGCCTGCAGCCCTCTGAGTCCATCTTTCTTGATGACCTTGGAACAAATCTAAAAGAA
GCTGCCAGACTTGGTATTCACACCATTAAGGTTAATGACCCAGAGACTGCAGTAAAGGAA
TTAGAAGCTCTCTTGGGTTTTACATTGAGAGTAGGTGTTCCAAACACTCGGCCTGTGAAA
AAGACGATGGAAATTCCGAAAGATTCCTTGCAGAAGTACCTCAAAGACTTACTGGGTATC
CAGACCACAGGCCCATTGGAACTACTTCAGTTTGATCACGGGCAGTCAAATCCAACTTAC
TACATCAGGCTGGCTAATCGTGATCTAGTTCTGAGGAAGAAGCCCCCAGGGACACTCCTT
CCATCTGCCCATGCCATAGAGAGGGAGTTCAGGATTATGAAAGCCCTTGCAAATGCTGGA
GTACCTGTCCCTAACGTTCTTGATCTCTGTGAAGATTCAAGTGTCATTGGCACCCCCTTC
TATGTGATGGAGTACTGCCCAGGTCTCATCTACAAAGACCCTTCCCTGCCAGGCTTGGAG
CCCAGCCACAGACGAGCCATATACACTGCCATGAACACAGTCCTGTGCAAAATTCACAGT
GTGGATCTGCAGGCTGTGGGACTTGAAGACTATGGGAAGCAAGGGGACTATATTCCACGC
CAGGTACGAACCTGGGTTAAGCAGTATCGAGCTTCCGAAACTAGCACCATCCCAGCCATG
GAGAGGCTGATCGAATGGCTGCCCCTCCATCTTCCCCGTCAGCAGAGGACCACAGTGGTG
CACGGGGACTTCAGGCTCGACAACCTGGTGTTTCATCCAGAAGAGCCAGAGGTGCTTGCT
GTCCTTGACTGGGAACTTTCTACCTTGGGCGACCCCCTTGCTGATGTGGCCTACAGCTGC
CTGGCTCATTACCTGCCATCCAGTTTTCCCGTGCTGAGAGGTATTAATGACTGTGACTTG
ACACAGCTGGGAATCCCTGCTGCAGAGGAGTATTTCAGGATGTACTGTCTCCAAATGGGG
CTCCCTCCCACTGAGAACTGGAACTTCTATATGGCTTTTTCCTTTTTCCGTGTGGCTGCA
ATCCTACAGGGAGTCTACAAGCGATCACTCACAGGGCAAGCAAGCTCCACATATGCGGAA
CAAACTGGAAAGCTGACCGAATTTGTGTCTAACCTGGCGTGGGATTTCGCAGTCAAAGAA
GGGTTCCGGGTTTTCAAAGAGATGCCCTTCACAAATCCGTTAACAAGGTCCTACCACACG
TGGGCCAGGCCCCAGTCCCAGTGGTGCCCCACAGGCAGCAGGAGTTATAGCTCCGTTCCA
GAAGCTTCCCCAGCTCATACCTCAAGGGGAGGTCTGGTTATCTCTCCAGAGAGCCTCTCT
CCACCTGTCAGAGAGCTGTATCACCGGCTGAAGCACTTCATGGAGCAACGTGTGTACCCT
GCAGAGCCAGAGCTGCAGAGTCACCAGGCCTCAGCAGCCAGGTGGAGCCCCTCCCCACTG
ATCGAAGACCTCAAGGAGAAAGCCAAAGCTGAAGGACTTTGGAACCTTTTCCTACCCTTA
GAGGCTGATCCCGAGAAAAAATACGGAGCAGGACTGACCAATGTGGAATATGCACATCTG
TGTGAGCTCATGGGCACGTCCCTGTATGCCCCCGAGGTATGTAACTGCTCTGCGCCTGAC
ACGGGCAACATGGAGCTGCTGGTGAGGTATGGCACCGAAGCGCAGAAGGCTCGCTGGCTG
ATTCCTCTGCTGGAGGGGAAAGCCCGCTCCTGTTTTGCTATGACCGAGCCCCAGGTTGCC
TCTTCAGATGCCACCAACATTGAGGCTTCCATCAGAGAGGAGGACAGCTTCTATGTCATA
AACGGTCACAAATGGTGGATCACAGGCATCCTGGATCCTCGTTGCCAACTCTGTGTGTTT
ATGGGAAAAACAGACCCACATGCACCAAGACACCGGCAGCAGTCTGTGCTCTTGGTTCCC
ATGGATACCCCAGGGATAAAAATCATCCGGCCTCTGACGGTGTATGGACTGGAAGATGCA
CCAGGTGGCCATGGTGAAGTCCGATTTGAGCACGTGCGTGTGCCCAAAGAGAACATGGTC
CTGGGCCCTGGCCGAGGCTTTGAGATCGCCCAGGGCAGACTGGGCCCCGGCAGGATCCAT
CACTGCATGAGGCTGATCGGGTTCTCAGAGAGGGCCCTGGCACTCATGAAGGCCCGCGTG
AAGTCCCGCTTGGCTTTTGGGAAGCCCCTGGTGGAGCAGGGCACAGTGCTGGCGGACATC
GCGCAGTCGCGCGTGGAGATTGAGCAGGCACGGCTGCTGGTGCTGAGAGCTGCCCACCTC
ATGGACCTGGCAGGAAACAAGGCTGCAGCCTTGGATATAGCCATGATTAAAATGGTCGCC
CCGTCCATGGCCTCCCGAGTGATTGATCGTGCGATTCAGGCCTTTGGAGCAGCAGGCCTG
AGCAGCGACTACCCACTGGCTCAGTTCTTCACCTGGGCCCGAGCCCTGCGCTTTGCCGAC
GGCCCTGACGAGGTGCACCGGGCCACGGTGGCCAAGCTAGAGCTGAAGCACCGCATTTAG
|
| Enzyme 91 GenBank Gene ID |
NM_025247.5  |
| Enzyme 91 GeneCard ID |
ACAD10  |
| Enzyme 91 GenAtlas ID |
ACAD10  |
| Enzyme 91 HGNC ID |
HGNC:21597  |
| Enzyme 91 Chromosome Location |
1 |
| Enzyme 91 Locus |
12q24.12 |
| Enzyme 91 SNPs |
SNPJam Report  |
| Enzyme 91 General References |
- Ye X, Ji C, Zhou C, Zeng L, Gu S, Ying K, Xie Y, Mao Y: Cloning and characterization of a human cDNA ACAD10 mapped to chromosome 12q24.1. Mol Biol Rep. 2004 Sep;31(3):191-5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 91 Metabolite References |
Not Available |
|
Enzyme 92
[top]
|
| Enzyme 92 ID |
8816 |
| Enzyme 92 Name |
Acyl-CoA dehydrogenase family member 11 |
| Enzyme 92 Synonyms |
- ACAD-11
|
| Enzyme 92 Gene Name |
ACAD11 |
| Enzyme 92 Protein Sequence |
>Acyl-CoA dehydrogenase family member 11
MKPGATGESDLAEVLPQHKFDSKSLEAYLNQHLSGFGAEREATLTIAQYRAGKSNPTFYL
QKGFQTYVLRKKPPGSLLPKAHQIDREFKVQKALFSIGFPVPKPILYCSDTSVIGTEFYV
MEHVQGRIFRDLTIPGLSPAERSAIYVATVETLAQLRSLNIQSLQLEGYGIGAGYCKRQV
STWTKQYQAAAHQDIPAMQQLSEWLMKNLPDNDNEENLIHGDFRLDNIVFHPKECRVIAV
LDWELSTIGHPLSDLAHFSLFYFWPRTVPMINQGSYSENSGIPSMEELISIYCRCRGINS
ILPNWNFFLALSYFKMAGIAQGVYSRYLLGNNSSEDSFLFANIVQPLAETGLQLSKRTFS
TVLPQIDTTGQLFVQTRKGQEVLIKVKHFMKQHILPAEKEVTEFYVQNENSVDKWGKPLV
IDKLKEMAKVEGLWNLFLPAVSGLSHVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLH
LYGSEEQKKQWLEPLLQGNITSCFCMTEPDVASSDATNIECSIQRDEDSYVINGKKWWSS
GAGNPKCKIAIVLGRTQNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNFHGGHFE
IHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAF
KKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAMIKVAAPRAVSK
IVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELRDQAKRLTAKI
|
| Enzyme 92 Number of Residues |
780 |
| Enzyme 92 Molecular Weight |
87282.7 |
| Enzyme 92 Theoretical pI |
8.21 |
| Enzyme 92 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 92 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 92 Specific Function |
May function as oxidoreductase (Probable) |
| Enzyme 92 Pathways |
Not Available |
| Enzyme 92 Reactions |
Not Available |
| Enzyme 92 Pfam Domain Function |
|
| Enzyme 92 Signals |
|
| Enzyme 92 Transmembrane Regions |
|
| Enzyme 92 Essentiality |
Not Available |
| Enzyme 92 GenBank ID Protein |
38490142  |
| Enzyme 92 UniProtKB/Swiss-Prot ID |
Q709F0  |
| Enzyme 92 UniProtKB/Swiss-Prot Entry Name |
ACD11_HUMAN  |
| Enzyme 92 PDB ID |
Not Available |
| Enzyme 92 Cellular Location |
Not Available |
| Enzyme 92 Gene Sequence |
>2343 bp
ATGAAGCCAGGTGCTACTGGCGAGTCCGATTTGGCCGAAGTGCTGCCCCAGCACAAGTTC
GACAGCAAGTCCCTGGAGGCCTACCTAAACCAGCACTTGTCTGGCTTTGGGGCCGAACGT
GAGGCTACGCTGACCATTGCCCAGTACAGAGCAGGAAAGTCCAATCCAACCTTTTATCTC
CAGAAGGGCTTTCAAACATATGTGCTCAGGAAAAAACCACCAGGTTCACTTCTTCCTAAA
GCACATCAGATTGATAGAGAATTTAAAGTCCAGAAAGCCTTGTTTTCAATTGGATTCCCC
GTTCCCAAGCCTATACTGTACTGCAGTGATACTTCTGTCATTGGAACAGAATTTTACGTA
ATGGAACATGTGCAGGGTCGAATCTTCCGTGATTTAACAATTCCTGGACTTAGCCCAGCA
GAACGTTCAGCCATATATGTGGCCACGGTAGAAACATTGGCTCAGTTACATTCCTTGAAT
ATACAGTCACTGCAGCTGGAAGGATATGGTATAGGTGCTGGGTACTGCAAAAGACAGGTA
TCAACCTGGACAAAGCAATATCAAGCTGCAGCTCATCAGGACATCCCTGCCATGCAACAG
CTATCGGAGTGGCTAATGAAGAACTTGCCCGATAATGACAATGAAGAGAATTTGATTCAT
GGAGATTTCAGACTAGATAACATAGTTTTCCACCCTAAAGAGTGTCGAGTTATAGCAGTG
CTGGATTGGGAGCTGTCAACCATTGGTCATCCTTTGTCAGACTTAGCTCATTTTTCCCTG
TTCTACTTTTGGCCAAGGACAGTTCCAATGATAAATCAAGGTTCTTATAGTGAAAACTCA
GGGATACCATCAATGGAAGAACTGATTTCAATATATTGCCGCTGCAGGGGAATTAATTCT
ATTCTTCCTAACTGGAATTTCTTTCTTGCCCTTTCATATTTTAAGATGGCTGGAATAGCA
CAGGGAGTATATAGCAGATATCTTCTGGGAAATAATTCATCTGAGGATAGCTTTTTATTT
GCCAATATTGTGCAACCTCTGGCAGAAACTGGACTACAACTCTCCAAACGAACTTTCAGT
ACTGTACTACCACAGATTGATACTACTGGACAGTTGTTTGTACAGACTCGGAAAGGTCAG
GAAGTTCTTATTAAGGTGAAGCATTTCATGAAACAACACATTCTTCCAGCTGAAAAGGAG
GTAACTGAGTTCTATGTTCAAAATGAAAATTCAGTGGACAAGTGGGGAAAACCTTTAGTG
ATTGATAAACTCAAGGAAATGGCCAAAGTCGAGGGTCTCTGGAACTTGTTTTTGCCAGCT
GTCAGCGGACTCAGCCACGTGGACTATGCCTTGATTGCTGAAGAAACAGGAAAATGCTTT
TTTGCTCCAGATGTCTTTAACTGCCAAGCACCAGACACAGGGAATATGGAGGTTCTGCAC
CTGTATGGAAGTGAGGAACAGAAGAAACAGTGGCTTGAGCCTCTTCTTCAAGGGAACATT
ACCTCTTGCTTCTGTATGACAGAACCTGATGTAGCTTCAAGTGATGCCACGAATATTGAA
TGCAGCATCCAACGAGATGAAGATAGCTATGTAATTAACGGCAAAAAATGGTGGAGCAGT
GGAGCTGGGAATCCCAAGTGCAAAGTTGCAATTGTTTTGGGAAGAACTCAAAATACTTCT
CTCTCCAGACACAAACAGCACAGCATGATTCTTGTTCCCATGAACACACCTGGAGTAAAA
ATAATAAGGCCTTTGTCAGTTTTTGGCTACACAGATAATTTTCATGGAGGACATTTTGAG
ATCCATTTTAATCAAGTGCGAGTTCCTGCCACAAATCTAATACTAGGTGAAGGTAGGGGA
TTTGAAATTTCCCAAGGCCGCCTTGGACCTGGCAGAATCCACCACTGTATGAGAACAGTA
GGTTTGGCGGAACGCGCTTTGCAGATCATGTGTGAGCGGGCAACACAAAGGATAGCTTTC
AAGAAGAAGTTGTATGCACATGAGGTTGTGGCTCACTGGATTGCTGAAAGCCGCATTGCC
ATTGAGAAGATCCGCTTGTTGACTCTGAAAGCTGCTCACAGCATGGACACTCTGGGCAGT
GCTGGCGCTAAGAAAGAGATTGCAATGATCAAAGTGGCTGCCCCACGGGCTGTCAGCAAA
ATCGTTGACTGGGCCATCCAGGTGTGCGGAGGTGCTGGTGTTTCCCAGGATTACCCTCTG
GCTAACATGTATGCTATAACCCGAGTTTTGCGTTTAGCAGATGGACCTGACGAAGTTCAT
CTTTCAGCAATCGCAACAATGGAGCTGCGGGACCAAGCCAAAAGACTGACAGCCAAGATA
TAA
|
| Enzyme 92 GenBank Gene ID |
AJ608287  |
| Enzyme 92 GeneCard ID |
ACAD11  |
| Enzyme 92 GenAtlas ID |
ACAD11  |
| Enzyme 92 HGNC ID |
HGNC:30211  |
| Enzyme 92 Chromosome Location |
3 |
| Enzyme 92 Locus |
3q22.1 |
| Enzyme 92 SNPs |
SNPJam Report  |
| Enzyme 92 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 92 Metabolite References |
Not Available |
|
Enzyme 93
[top]
|
| Enzyme 93 ID |
8871 |
| Enzyme 93 Name |
Glycerol-3-phosphate acyltransferase 4 |
| Enzyme 93 Synonyms |
- GPAT4
- 1-acylglycerol-3-phosphate O-acyltransferase 6
- 1-AGP acyltransferase 6
- 1-AGPAT 6
- Acyl-CoA:glycerol-3-phosphate acyltransferase 4
- Lysophosphatidic acid acyltransferase zeta
- LPAAT-zeta
|
| Enzyme 93 Gene Name |
AGPAT6 |
| Enzyme 93 Protein Sequence |
>Glycerol-3-phosphate acyltransferase 4
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
|
| Enzyme 93 Number of Residues |
456 |
| Enzyme 93 Molecular Weight |
52070.6 |
| Enzyme 93 Theoretical pI |
9.56 |
| Enzyme 93 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 93 General Function |
Involved in acyltransferase activity |
| Enzyme 93 Specific Function |
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long- chain fatty acyl-CoAs |
| Enzyme 93 Pathways |
|
| Enzyme 93 Reactions |
- acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
|
| Enzyme 93 Pfam Domain Function |
|
| Enzyme 93 Signals |
|
| Enzyme 93 Transmembrane Regions |
|
| Enzyme 93 Essentiality |
Not Available |
| Enzyme 93 GenBank ID Protein |
30142570  |
| Enzyme 93 UniProtKB/Swiss-Prot ID |
Q86UL3  |
| Enzyme 93 UniProtKB/Swiss-Prot Entry Name |
GPAT4_HUMAN  |
| Enzyme 93 PDB ID |
Not Available |
| Enzyme 93 Cellular Location |
Not Available |
| Enzyme 93 Gene Sequence |
>1371 bp
ATGTTCCTGTTGCTGCCTTTTGATAGCCTGATTGTCAACCTTCTGGGCATCTCCCTGACT
GTCCTCTTCACCCTCCTTCTCGTTTTCATCATAGTGCCAGCCATTTTTGGAGTCTCCTTT
GGTATCCGCAAACTCTACATGAAAAGTCTGTTAAAAATCTTTGCGTGGGCTACCTTGAGA
ATGGAGCGAGGAGCCAAGGAGAAGAACCACCAGCTTTACAAGCCCTACACCAACGGAATC
ATTGCAAAGGATCCCACTTCACTAGAAGAAGAGATCAAAGAGATTCGTCGAAGTGGTAGT
AGTAAGGCTCTGGACAACACTCCAGAGTTCGAGCTCTCTGACATTTTCTACTTTTGCCGG
AAAGGAATGGAGACCATTATGGATGATGAGGTGACAAAGAGATTCTCAGCAGAAGAACTG
GAGTCCTGGAACCTGCTGAGCAGAACCAATTATAACTTCCAGTACATCAGCCTTCGGCTC
ACGGTCCTGTGGGGGTTAGGAGTGCTGATTCGGTACTGCTTTCTGCTGCCGCTCAGGATA
GCACTGGCTTTCACAGGGATTAGCCTTCTGGTGGTGGGCACAACTGTGGTGGGATACTTG
CCAAATGGGAGGTTTAAGGAGTTCATGAGTAAACATGTTCACTTAATGTGTTACCGGATC
TGCGTGCGAGCGCTGACAGCCATCATCACCTACCATGACAGGGAAAACAGACCAAGAAAT
GGTGGCATCTGTGTGGCCAATCATACCTCACCGATCGATGTGATCATCTTGGCCAGCGAT
GGCTATTATGCCATGGTGGGTCAAGTGCACGGGGGACTCATGGGTGTGATTCAGAGAGCC
ATGGTGAAGGCCTGCCCACACGTCTGGTTTGAGCGCTCGGAAGTGAAGGATCGCCACCTG
GTGGCTAAGAGACTGACTGAACATGTGCAAGATAAAAGCAAGCTGCCTATCCTCATCTTC
CCAGAAGGAACCTGCATCAATAATACATCGGTGATGATGTTCAAAAAGGGAAGTTTTGAA
ATTGGAGCCACAGTTTACCCTGTTGCTATCAAGTATGACCCTCAATTTGGCGATGCCTTC
TGGAACAGCAGCAAATACGGGATGGTGACGTACCTGCTGCGAATGATGACCAGCTGGGCC
ATTGTCTGCAGCGTGTGGTACCTGCCTCCCATGACTAGAGAGGCAGATGAAGATGCTGTC
CAGTTTGCGAATAGGGTGAAATCTGCCATTGCCAGGCAGGGAGGACTTGTGGACCTGCTG
TGGGATGGGGGCCTGAAGAGGGAGAAGGTGAAGGACACGTTCAAGGAGGAGCAGCAGAAG
CTGTACAGCAAGATGATCGTGGGGAACCACAAGGACAGGAGCCGCTCCTGA
|
| Enzyme 93 GenBank Gene ID |
AF406612  |
| Enzyme 93 GeneCard ID |
AGPAT6  |
| Enzyme 93 GenAtlas ID |
AGPAT6  |
| Enzyme 93 HGNC ID |
HGNC:20880  |
| Enzyme 93 Chromosome Location |
8 |
| Enzyme 93 Locus |
8p11.21 |
| Enzyme 93 SNPs |
SNPJam Report  |
| Enzyme 93 General References |
- Li D, Yu L, Wu H, Shan Y, Guo J, Dang Y, Wei Y, Zhao S: Cloning and identification of the human LPAAT-zeta gene, a novel member of the lysophosphatidic acid acyltransferase family. J Hum Genet. 2003;48(8):438-42. Epub 2003 Aug 19. [PubMed
]
- Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G: AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase. J Biol Chem. 2008 Apr 11;283(15):10048-57. Epub 2008 Jan 31. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
|
| Enzyme 93 Metabolite References |
Not Available |
|
Enzyme 94
[top]
|
| Enzyme 94 ID |
9777 |
| Enzyme 94 Name |
Acyl-coenzyme A synthetase ACSM1, mitochondrial |
| Enzyme 94 Synonyms |
- Acyl-CoA synthetase medium-chain family member 1
- Butyrate--CoA ligase 1
- Butyryl-coenzyme A synthetase 1
- Lipoate-activating enzyme
- Middle-chain acyl-CoA synthetase 1
|
| Enzyme 94 Gene Name |
ACSM1 |
| Enzyme 94 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM1, mitochondrial
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM
|
| Enzyme 94 Number of Residues |
577 |
| Enzyme 94 Molecular Weight |
65272.7 |
| Enzyme 94 Theoretical pI |
8.40 |
| Enzyme 94 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 94 General Function |
Involved in catalytic activity |
| Enzyme 94 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). Functions as GTP-dependent lipoate- activating enzyme that generates the substrate for lipoyltransferase |
| Enzyme 94 Pathways |
|
| Enzyme 94 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 94 Pfam Domain Function |
|
| Enzyme 94 Signals |
|
| Enzyme 94 Transmembrane Regions |
|
| Enzyme 94 Essentiality |
Not Available |
| Enzyme 94 GenBank ID Protein |
15487302  |
| Enzyme 94 UniProtKB/Swiss-Prot ID |
Q08AH1  |
| Enzyme 94 UniProtKB/Swiss-Prot Entry Name |
ACSM1_HUMAN  |
| Enzyme 94 PDB ID |
Not Available |
| Enzyme 94 Cellular Location |
Not Available |
| Enzyme 94 Gene Sequence |
>1734 bp
ATGCAGTGGCTAATGAGGTTCCGGACCCTCTGGGGCATCCACAAATCCTTCCACAACATC
CACCCTGCCCCTTCACAGCTGCGCTGCCGGTCTTTATCAGAATTTGGAGCCCCAAGATGG
AATGACTATGAAGTACCGGAGGAATTTAACTTTGCAAGTTATGTACTGGACTACTGGGCT
CAAAAGGAGAAGGAGGGCAAGAGAGGTCCAAATCCAGCTTTTTGGTGGGTGAATGGCCAA
GGGGATGAAGTAAAGTGGAGCTTCAGAGAGATGGGAGACCTAACCCGCCGTGTAGCCAAC
GTCTTCACACAGACCTGTGGCCTACAACAGGGAGACCATCTGGCCTTGATGCTGCCTCGA
GTTCCTGAGTGGTGGCTGGTGGCTGTGGGCTGCATGCGAACAGGGATCATCTTCATTCCT
GCGACCATCCTGTTGAAGGCCAAAGACATTCTCTATCGACTACAGTTGTCTAAAGCCAAG
GGCATTGTGACCATAGATGCCCTTGCCTCAGAGGTGGACTCCATAGCTTCTCAGTGCCCC
TCTCTGAAAACCAAGCTCCTGGTGTCTGATCACAGCCGTGAAGGGTGGCTGGACTTCCGA
TCGCTGGTTAAATCAGCATCCCCAGAACACACCTGTGTTAAGTCAAAGACCTTGGACCCA
ATGGTCATCTTCTTCACCAGTGGGACCACAGGCTTCCCCAAGATGGCAAAACACTCCCAT
GGGTTGGCCTTACAACCCTCCTTCCCAGGAAGTAGGAAATTACGGAGCCTGAAGACATCT
GATGTCTCCTGGTGCCTGTCGGACTCAGGATGGATTGTGGCTACCATTTGGACCCTGGTA
GAACCATGGACAGCGGGTTGTACAGTCTTTATCCACCATCTGCCACAGTTTGACACCAAG
GTCATCATACAGACATTGTTGAAATACCCCATTAACCACTTTTGGGGGGTATCATCTATA
TATCGAATGATTCTGCAGCAGGATTTCACCAGCATCAGGTTCCCTGCCCTGGAGCACTGC
TATACTGGCGGGGAGGTCGTGTTGCCCAAGGATCAGGAGGAGTGGAAAAGACGGACGGGC
CTTCTGCTCTACGAGAACTATGGGCAGTCGGAAACGGGACTAATTTGTGCCACCTACTGG
GGAATGAAGATCAAGCCGGGTTTCATGGGGAAGGCCACTCCACCCTATGACGTCCAGGTC
ATTGATGACAAGGGCAGCATCCTGCCACCTAACACAGAAGGAAACATTGGCATCAGAATC
AAACCTGTCAGGCCTGTGAGCCTCTTCATGTGCTATGAGGGTGACCCAGAGAAGACAGCT
AAAGTGGAATGTGGGGACTTCTACAACACTGGGGACAGAGGAAAGATGGATGAAGAGGGC
TACATTTGTTTCCTGGGGAGGAGTGATGACATCATTAATGCCTCTGGGTATCGCATCGGG
CCTGCAGAGGTTGAAAGCGCTTTGGTGGAGCACCCAGCGGTGGCGGAGTCAGCCGTGGTG
GGCAGCCCAGACCCGATTCGAGGGGAGGTGGTGAAGGCCTTTATTGTCCTGACCCCACAG
TTCCTGTCCCATGACAAGGATCAGCTGACCAAGGAACTGCAGCAGCATGTCAAGTCAGTG
ACAGCCCCATACAAGTACCCAAGGAACGTGGAGTTTGTCTCAGAGCTGCCAAAAACCATC
ACTGGCAAGATTGAACGGAAGGAACTTCGGAAAAAGGAGACTGGTCAGATGTAA
|
| Enzyme 94 GenBank Gene ID |
AB059429  |
| Enzyme 94 GeneCard ID |
ACSM1  |
| Enzyme 94 GenAtlas ID |
ACSM1  |
| Enzyme 94 HGNC ID |
HGNC:18049  |
| Enzyme 94 Chromosome Location |
1 |
| Enzyme 94 Locus |
16p12.3 |
| Enzyme 94 SNPs |
SNPJam Report  |
| Enzyme 94 General References |
- Fujino T, Takei YA, Sone H, Ioka RX, Kamataki A, Magoori K, Takahashi S, Sakai J, Yamamoto TT: Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol Chem. 2001 Sep 21;276(38):35961-6. Epub 2001 Jul 24. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 94 Metabolite References |
Not Available |
|
Enzyme 95
[top]
|
| Enzyme 95 ID |
10076 |
| Enzyme 95 Name |
Diacylglycerol O-acyltransferase 2 |
| Enzyme 95 Synonyms |
- Diglyceride acyltransferase 2
|
| Enzyme 95 Gene Name |
DGAT2 |
| Enzyme 95 Protein Sequence |
>Diacylglycerol O-acyltransferase 2
MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLN
RSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKG
GRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATE
VSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGG
AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQ
KKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHT
MYMEALVKLFDKHKTKFGLPETEVLEVN
|
| Enzyme 95 Number of Residues |
388 |
| Enzyme 95 Molecular Weight |
43830.5 |
| Enzyme 95 Theoretical pI |
9.80 |
| Enzyme 95 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 95 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 95 Specific Function |
Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation |
| Enzyme 95 Pathways |
|
| Enzyme 95 Reactions |
- acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
|
| Enzyme 95 Pfam Domain Function |
|
| Enzyme 95 Signals |
|
| Enzyme 95 Transmembrane Regions |
|
| Enzyme 95 Essentiality |
Not Available |
| Enzyme 95 GenBank ID Protein |
22506631  |
| Enzyme 95 UniProtKB/Swiss-Prot ID |
Q96PD7  |
| Enzyme 95 UniProtKB/Swiss-Prot Entry Name |
DGAT2_HUMAN  |
| Enzyme 95 PDB ID |
Not Available |
| Enzyme 95 Cellular Location |
Not Available |
| Enzyme 95 Gene Sequence |
>1167 bp
ATGAAGACCCTCATAGCCGCCTACTCCGGGGTCCTGCGCGGCGAGCGTCAGGCCGAGGCT
GACCGGAGCCAGCGCTCTCACGGAGGACCTGCGCTGTCGCGCGAGGGGTCTGGGAGATGG
GGCACTGGATCCAGCATCCTCTCCGCCCTCCAGGACCTCTTCTCTGTCACCTGGCTCAAT
AGGTCCAAGGTGGAAAAGCAGCTACAGGTCATCTCAGTGCTCCAGTGGGTCCTGTCCTTC
CTTGTACTGGGAGTGGCCTGCAGTGCCATCCTCATGTACATATTCTGCACTGATTGCTGG
CTCATCGCTGTGCTCTACTTCACTTGGCTGGTGTTTGACTGGAACACACCCAAGAAAGGT
GGCAGGAGGTCACAGTGGGTCCGAAACTGGGCTGTGTGGCGCTACTTTCGAGACTACTTT
CCCATCCAGCTGGTGAAGACACACAACCTGCTGACCACCAGGAACTATATCTTTGGATAC
CACCCCCATGGTATCATGGGCCTGGGTGCCTTCTGCAACTTCAGCACAGAGGCCACAGAA
GTGAGCAAGAAGTTCCCAGGCATACGGCCTTACCTGGCTACACTGGCAGGCAACTTCCGA
ATGCCTGTGTTGAGGGAGTACCTGATGTCTGGAGGTATCTGCCCTGTCAGCCGGGACACC
ATAGACTATTTGCTTTCAAAGAATGGGAGTGGCAATGCTATCATCATCGTGGTCGGGGGT
GCGGCTGAGTCTCTGAGCTCCATGCCTGGCAAGAATGCAGTCACCCTGCGGAACCGCAAG
GGCTTTGTGAAACTGGCCCTGCGTCATGGAGCTGACCTGGTTCCCATCTACTCCTTTGGA
GAGAATGAAGTGTACAAGCAGGTGATCTTCGAGGAGGGCTCCTGGGGCCGATGGGTCCAG
AAGAAGTTCCAGAAATACATTGGTTTCGCCCCATGCATCTTCCATGGTCGAGGCCTCTTC
TCCTCCGACACCTGGGGGCTGGTGCCCTACTCCAAGCCCATCACCACTGTTGTGGGAGAG
CCCATCACCATCCCCAAGCTGGAGCACCCAACCCAGCAAGACATCGACCTGTACCACACC
ATGTACATGGAGGCCCTGGTGAAGCTCTTCGACAAGCACAAGACCAAGTTCGGCCTCCCG
GAGACTGAGGTCCTGGAGGTGAACTGA
|
| Enzyme 95 GenBank Gene ID |
AB048286  |
| Enzyme 95 GeneCard ID |
DGAT2  |
| Enzyme 95 GenAtlas ID |
DGAT2  |
| Enzyme 95 HGNC ID |
HGNC:16940  |
| Enzyme 95 Chromosome Location |
1 |
| Enzyme 95 Locus |
11q13.5 |
| Enzyme 95 SNPs |
SNPJam Report  |
| Enzyme 95 General References |
- Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [PubMed
]
- Wakimoto K, Chiba H, Michibata H, Seishima M, Kawasaki S, Okubo K, Mitsui H, Torii H, Imai Y: A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice. Biochem Biophys Res Commun. 2003 Oct 17;310(2):296-302. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed
]
|
| Enzyme 95 Metabolite References |
Not Available |
|
Enzyme 96
[top]
|
| Enzyme 96 ID |
10119 |
| Enzyme 96 Name |
1-acyl-sn-glycerol-3-phosphate acyltransferase delta |
| Enzyme 96 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 4
- 1-AGP acyltransferase 4
- 1-AGPAT 4
- Lysophosphatidic acid acyltransferase delta
- LPAAT-delta
|
| Enzyme 96 Gene Name |
AGPAT4 |
| Enzyme 96 Protein Sequence |
>1-acyl-sn-glycerol-3-phosphate acyltransferase delta
MDLAGLLKSQFLCHLVFCYVFIASGLIINTIQLFTLLLWPINKQLFRKINCRLSYCISSQ
LVMLLEWWSGTECTIFTDPRAYLKYGKENAIVVLNHKFEIDFLCGWSLSERFGLLGGSKV
LAKKELAYVPIIGWMWYFTEMVFCSRKWEQDRKTVATSLQHLRDYPEKYFFLIHCEGTRF
TEKKHEISMQVARAKGLPRLKHHLLPRTKGFAITVRSLRNVVSAVYDCTLNFRNNENPTL
LGVLNGKKYHADLYVRRIPLEDIPEDDDECSAWLHKLYQEKDAFQEEYYRTGTFPETPMV
PPRRPWTLVNWLFWASLVLYPFFQFLVSMIRSGSSLTLASFILVFFVASVGVRWMIGVTE
IDKGSAYGNSDSKQKLND
|
| Enzyme 96 Number of Residues |
378 |
| Enzyme 96 Molecular Weight |
44020.9 |
| Enzyme 96 Theoretical pI |
8.90 |
| Enzyme 96 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 96 General Function |
Involved in acyltransferase activity |
| Enzyme 96 Specific Function |
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone |
| Enzyme 96 Pathways |
|
| Enzyme 96 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
|
| Enzyme 96 Pfam Domain Function |
|
| Enzyme 96 Signals |
|
| Enzyme 96 Transmembrane Regions |
- 11-31
125-145
307-327
338-358
|
| Enzyme 96 Essentiality |
Not Available |
| Enzyme 96 GenBank ID Protein |
8886005  |
| Enzyme 96 UniProtKB/Swiss-Prot ID |
Q9NRZ5  |
| Enzyme 96 UniProtKB/Swiss-Prot Entry Name |
PLCD_HUMAN  |
| Enzyme 96 PDB ID |
Not Available |
| Enzyme 96 Cellular Location |
Not Available |
| Enzyme 96 Gene Sequence |
>1137 bp
ATGGACCTCGCGGGACTGCTGAAGTCTCAGTTCCTGTGCCACCTGGTCTTCTGCTACGTC
TTTATTGCCTCAGGGCTAATCATCAACACCATTCAGCTCTTCACTCTCCTCCTCTGGCCC
ATTAACAAGCAGCTCTTCCGGAAGATCAACTGCAGACTGTCCTATTGCATCTCAAGCCAG
CTGGTGATGCTGCTGGAGTGGTGGTCGGGCACGGAATGCACCATCTTCACGGACCCGCGC
GCCTACCTCAAGTATGGGAAGGAAAATGCCATCGTGGTTCTCAACCACAAGTTTGAAATT
GACTTTCTGTGTGGCTGGAGCCTGTCCGAACGCTTTGGGCTGTTAGGGGGCTCCAAGGTC
CTGGCCAAGAAAGAGCTGGCCTATGTCCCAATTATCGGCTGGATGTGGTACTTCACCGAG
ATGGTCTTCTGTTCGCGCAAGTGGGAGCAGGATCGCAAGACGGTTGCCACCAGTTTGCAG
CACCTCCGGGACTACCCCGAGAAGTATTTTTTCCTGATTCACTGTGAGGGCACACGGTTC
ACGGAGAAGAAGCATGAGATCAGCATGCAGGTGGCCCGGGCCAAGGGGCTGCCTCGCCTC
AAGCATCACCTGTTGCCACGAACCAAGGGCTTCGCCATCACCGTGAGGAGCTTGAGAAAT
GTAGTTTCAGCTGTATATGACTGTACACTCAATTTCAGAAATAATGAAAATCCAACACTG
CTGGGAGTCCTAAACGGAAAGAAATACCATGCAGATTTGTATGTTAGGAGGATCCCACTG
GAAGACATCCCTGAAGACGATGACGAGTGCTCGGCCTGGCTGCACAAGCTCTACCAGGAG
AAGGATGCCTTTCAGGAGGAGTACTACAGGACGGGCACCTTCCCAGAGACGCCCATGGTG
CCCCCCCGGCGGCCCTGGACCCTCGTGAACTGGCTGTTTTGGGCCTCGCTGGTGCTCTAC
CCTTTCTTCCAGTTCCTGGTCAGCATGATCAGGAGCGGGTCTTCCCTGACGCTGGCCAGC
TTCATCCTCGTCTTCTTTGTGGCCTCCGTGGGAGTTCGATGGATGATTGGTGTGACGGAA
ATTGACAAGGGCTCTGCCTACGGCAACTCTGACAGCAAGCAGAAACTGAATGACTGA
|
| Enzyme 96 GenBank Gene ID |
AF156776  |
| Enzyme 96 GeneCard ID |
AGPAT4  |
| Enzyme 96 GenAtlas ID |
AGPAT4  |
| Enzyme 96 HGNC ID |
HGNC:20885  |
| Enzyme 96 Chromosome Location |
6 |
| Enzyme 96 Locus |
6q26 |
| Enzyme 96 SNPs |
SNPJam Report  |
| Enzyme 96 General References |
- Leung DW: The structure and functions of human lysophosphatidic acid acyltransferases. Front Biosci. 2001 Aug 1;6:D944-53. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 96 Metabolite References |
Not Available |
|
Enzyme 97
[top]
|
| Enzyme 97 ID |
10239 |
| Enzyme 97 Name |
2-acylglycerol O-acyltransferase 1 |
| Enzyme 97 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 1
- MGAT1
- Diacylglycerol O-acyltransferase candidate 2
- hDC2
- Diacylglycerol acyltransferase 2-like protein 1
- Monoacylglycerol O-acyltransferase 1
|
| Enzyme 97 Gene Name |
MOGAT1 |
| Enzyme 97 Protein Sequence |
>2-acylglycerol O-acyltransferase 1
MKVEFAPLNIQLARRLQTVAVLQWVLKYLLLGPMSIGITVMLIIHNYLFLYIPYLMWLYF
DWHTPERGGRRSSWIKNWTLWKHFKDYFPIHLIKTQDLDPSHNYIFGFHPHGIMAVGAFG
NFSVNYSDFKDLFPGFTSYLHVLPLWFWCPVFREYVMSVGLVSVSKKSVSYMVSKEGGGN
ISVIVLGGAKESLDAHPGKFTLFIRQRKGFVKIALTHGASLVPVVSFGENELFKQTDNPE
GSWIRTVQNKLQKIMGFALPLFHARGVFQYNFGLMTYRKAIHTVVGRPIPVRQTLNPTQE
QIEELHQTYMEELRKLFEEHKGKYGIPEHETLVLK
|
| Enzyme 97 Number of Residues |
335 |
| Enzyme 97 Molecular Weight |
38812.2 |
| Enzyme 97 Theoretical pI |
9.96 |
| Enzyme 97 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 97 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 97 Specific Function |
Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine |
| Enzyme 97 Pathways |
|
| Enzyme 97 Reactions |
- acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
|
| Enzyme 97 Pfam Domain Function |
|
| Enzyme 97 Signals |
|
| Enzyme 97 Transmembrane Regions |
|
| Enzyme 97 Essentiality |
Not Available |
| Enzyme 97 GenBank ID Protein |
148746191  |
| Enzyme 97 UniProtKB/Swiss-Prot ID |
Q96PD6  |
| Enzyme 97 UniProtKB/Swiss-Prot Entry Name |
MOGT1_HUMAN  |
| Enzyme 97 PDB ID |
Not Available |
| Enzyme 97 Cellular Location |
Not Available |
| Enzyme 97 Gene Sequence |
>1008 bp
ATGAAGGTAGAGTTTGCACCGCTCAACATCCAGCTGGCGCGGCGGCTGCAGACGGTGGCC
GTGCTGCAGTGGGTCCTGAAATACCTGCTGCTCGGGCCGATGTCCATTGGAATCACTGTG
ATGCTGATCATACACAACTATTTGTTCCTTTACATCCCTTATTTGATGTGGCTTTACTTT
GACTGGCATACCCCAGAGCGAGGAGGCAGGAGATCCAGCTGGATCAAAAATTGGACTCTT
TGGAAACACTTTAAGGACTATTTTCCAATTCATCTTATCAAAACTCAAGATTTGGATCCA
AGTCACAACTATATATTTGGGTTTCACCCCCATGGAATAATGGCAGTTGGAGCCTTTGGG
AATTTTTCTGTAAATTATTCTGACTTCAAGGACCTGTTTCCTGGCTTTACTTCATATCTT
CACGTGCTGCCACTTTGGTTCTGGTGTCCTGTCTTTCGAGAATATGTGATGAGTGTTGGG
CTGGTTTCAGTTTCCAAGAAAAGTGTGTCCTACATGGTAAGCAAGGAGGGAGGTGGAAAC
ATCTCTGTCATTGTCCTTGGGGGTGCAAAAGAATCACTGGATGCTCATCCTGGAAAGTTC
ACTCTGTTCATCCGCCAGCGGAAAGGATTTGTTAAAATTGCTTTGACCCATGGCGCCTCT
CTGGTCCCAGTGGTTTCTTTTGGTGAAAATGAACTGTTTAAACAAACTGACAACCCTGAA
GGATCATGGATTAGAACTGTTCAGAATAAACTGCAGAAGATCATGGGGTTTGCTTTGCCC
CTGTTTCATGCCAGGGGAGTTTTTCAGTACAATTTTGGCCTAATGACCTATAGGAAAGCC
ATCCACACTGTTGTTGGCCGCCCGATCCCTGTTCGTCAGACTCTGAACCCGACCCAGGAG
CAGATTGAGGAGTTACATCAGACCTATATGGAGGAACTTAGGAAATTGTTTGAGGAACAC
AAAGGAAAGTATGGCATTCCAGAGCACGAGACTCTTGTTTTAAAATGA
|
| Enzyme 97 GenBank Gene ID |
NM_058165.2  |
| Enzyme 97 GeneCard ID |
MOGAT1  |
| Enzyme 97 GenAtlas ID |
MOGAT1  |
| Enzyme 97 HGNC ID |
HGNC:18210  |
| Enzyme 97 Chromosome Location |
2 |
| Enzyme 97 Locus |
2q36.1 |
| Enzyme 97 SNPs |
SNPJam Report  |
| Enzyme 97 General References |
- Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
|
| Enzyme 97 Metabolite References |
Not Available |
|
Enzyme 98
[top]
|
| Enzyme 98 ID |
10872 |
| Enzyme 98 Name |
Isobutyryl-CoA dehydrogenase, mitochondrial |
| Enzyme 98 Synonyms |
- Activator-recruited cofactor 42 kDa component
- ARC42
- Acyl-CoA dehydrogenase family member 8
- ACAD-8
|
| Enzyme 98 Gene Name |
ACAD8 |
| Enzyme 98 Protein Sequence |
>Isobutyryl-CoA dehydrogenase, mitochondrial
MLWSGCRRFGARLGCLPGGLRVLVQTGHRSLTSCIDPSMGLNEEQKEFQKVAFDFAAREM
APNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT
AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQG
DHYILNGSKAFISGAGESDIYVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNS
QPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAAHASVILTRDHLN
VRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD
ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE
|
| Enzyme 98 Number of Residues |
415 |
| Enzyme 98 Molecular Weight |
45069.4 |
| Enzyme 98 Theoretical pI |
7.91 |
| Enzyme 98 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 98 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 98 Specific Function |
Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex |
| Enzyme 98 Pathways |
Not Available |
| Enzyme 98 Reactions |
Not Available |
| Enzyme 98 Pfam Domain Function |
|
| Enzyme 98 Signals |
|
| Enzyme 98 Transmembrane Regions |
|
| Enzyme 98 Essentiality |
Not Available |
| Enzyme 98 GenBank ID Protein |
Not Available |
| Enzyme 98 UniProtKB/Swiss-Prot ID |
Q9UKU7  |
| Enzyme 98 UniProtKB/Swiss-Prot Entry Name |
ACAD8_HUMAN  |
| Enzyme 98 PDB ID |
1RX0  |
| Enzyme 98 PDB File |
Show |
| Enzyme 98 3D Structure |
|
| Enzyme 98 Cellular Location |
Not Available |
| Enzyme 98 Gene Sequence |
>1248 bp
ATGCTGTGGAGCGGCTGCCGGCGTTTCGGGGCGCGCCTCGGCTGCCTGCCCGGCGGTCTC
CGGGTCCTCGTCCAGACCGGCCACCGGAGCTTGACCTCCTGCATCGACCCTTCCATGGGA
CTTAATGAAGAGCAGAAAGAATTTCAAAAAGTGGCCTTTGACTTTGCTGCCCGAGAGATG
GCTCCAAATATGGCAGAGTGGGACCAGAAGGAGCTGTTCCCAGTGGATGTGATGCGGAAG
GCAGCCCAGCTAGGCTTCGGAGGGGTCTACATACAAACAGATGTGGGCGGGTCTGGGCTG
TCACGTCTTGATACCTCTGTCATTTTTGAAGCCTTGGCTACAGGCTGCACCAGCACCACA
GCCTATATAAGCATCCACAACATGTGTGCCTGGATGATTGATAGCTTCGGAAATGAGGAA
CAGAGGCACAAATTTTGCCCACCGCTCTGTACCATGGAGAAGTTTGCTTCCTACTGCCTC
ACTGAACCAGGAAGTGGGAGTGATGCTGCCTCTCTTCTGACCTCCGCTAAGAAACAGGGA
GATCATTACATCCTCAATGGCTCCAAGGCCTTCATCAGTGGTGCTGGTGAGTCAGACATC
TATGTGGTCATGTGCCGAACAGGAGGACCAGGCCCCAAGGGCATCTCATGCATAGTTGTT
GAGAAGGGGACCCCTGGCCTCAGCTTTGGCAAGAAGGAGAAAAAGGTGGGGTGGAACTCC
CAGCCAACACGAGCTGTGATCTTCGAAGACTGTGCTGTCCCTGTGGCCAACAGAATTGGG
AGCGAGGGGCAGGGCTTCCTCATTGCCGTGAGAGGACTGAACGGAGGGAGGATCAATATT
GCTTCCTGCTCCCTGGGGGCTGCCCACGCCTCTGTCATCCTCACCCGAGACCACCTCAAT
GTCCGGAAGCAGTTTGGAGAGCCTCTGGCCAGTAACCAGTACTTGCAATTCACACTGGCT
GATATGGCAACAAGGCTGGTGGCCGCGCGGCTGATGGTCCGCAATGCAGCAGTGGCTCTG
CAGGAGGAGAGGAAGGATGCAGTGGCCTTGTGCTCCATGGCCAAGCTCTTTGCTACAGAT
GAATGCTTTGCCATCTGCAACCAGGCCTTGCAGATGCACGGGGGCTACGGCTACCTGAAG
GATTACGCTGTTCAGCAGTACGTGCGGGACTCCAGGGTCCACCAGATTCTAGAAGGTAGC
AATGAAGTGATGAGGATACTGATCTCTAGAAGCCTGCTTCAGGAGTAG
|
| Enzyme 98 GenBank Gene ID |
AF126245  |
| Enzyme 98 GeneCard ID |
ACAD8  |
| Enzyme 98 GenAtlas ID |
ACAD8  |
| Enzyme 98 HGNC ID |
HGNC:87  |
| Enzyme 98 Chromosome Location |
1 |
| Enzyme 98 Locus |
11q25 |
| Enzyme 98 SNPs |
SNPJam Report  |
| Enzyme 98 General References |
- Telford EA, Moynihan LM, Markham AF, Lench NJ: Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family. Biochim Biophys Acta. 1999 Sep 3;1446(3):371-6. [PubMed
]
- Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Naar AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R: Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature. 1999 Apr 29;398(6730):828-32. [PubMed
]
- Battaile KP, Nguyen TV, Vockley J, Kim JJ: Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases. J Biol Chem. 2004 Apr 16;279(16):16526-34. Epub 2004 Jan 28. [PubMed
]
- Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J: Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. Mol Genet Metab. 2002 Sep-Oct;77(1-2):68-79. [PubMed
]
- Sass JO, Sander S, Zschocke J: Isobutyryl-CoA dehydrogenase deficiency: isobutyrylglycinuria and ACAD8 gene mutations in two infants. J Inherit Metab Dis. 2004;27(6):741-5. [PubMed
]
- Pedersen CB, Bischoff C, Christensen E, Simonsen H, Lund AM, Young SP, Koeberl DD, Millington DS, Roe CR, Roe DS, Wanders RJ, Ruiter JP, Keppen LD, Stein Q, Knudsen I, Gregersen N, Andresen BS: Variations in IBD (ACAD8) in children with elevated C4-carnitine detected by tandem mass spectrometry newborn screening. Pediatr Res. 2006 Sep;60(3):315-20. Epub 2006 Jul 20. [PubMed
]
|
| Enzyme 98 Metabolite References |
Not Available |
|
Enzyme 99
[top]
|
| Enzyme 99 ID |
10874 |
| Enzyme 99 Name |
Acyl-CoA dehydrogenase family member 9, mitochondrial |
| Enzyme 99 Synonyms |
- ACAD-9
|
| Enzyme 99 Gene Name |
ACAD9 |
| Enzyme 99 Protein Sequence |
>Acyl-CoA dehydrogenase family member 9, mitochondrial
MSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVRAFAKELFLGKIKKKEVFPFPEVS
QDELNEINQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGF
SNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCL
TEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKD
KITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNIL
NSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMT
YLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTR
ILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVD
LGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINL
YGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKK
VSQQILEKRAYICAHPLDRTC
|
| Enzyme 99 Number of Residues |
621 |
| Enzyme 99 Molecular Weight |
68759.7 |
| Enzyme 99 Theoretical pI |
8.05 |
| Enzyme 99 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 99 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 99 Specific Function |
Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA then on stearoyl-CoA. Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0) |
| Enzyme 99 Pathways |
Not Available |
| Enzyme 99 Reactions |
Not Available |
| Enzyme 99 Pfam Domain Function |
|
| Enzyme 99 Signals |
|
| Enzyme 99 Transmembrane Regions |
|
| Enzyme 99 Essentiality |
Not Available |
| Enzyme 99 GenBank ID Protein |
18028283  |
| Enzyme 99 UniProtKB/Swiss-Prot ID |
Q9H845  |
| Enzyme 99 UniProtKB/Swiss-Prot Entry Name |
ACAD9_HUMAN  |
| Enzyme 99 PDB ID |
Not Available |
| Enzyme 99 Cellular Location |
Not Available |
| Enzyme 99 Gene Sequence |
>1866 bp
ATGAGCGGCTGCGGGCTCTTCCTGCGCACCACGGCTGCGGCTCGTGCCTGCCGGGGTCTG
GTGGTCTCTACCGCGAACCGGCGGCTACTGCGCACCAGCCCGCCTGTACGAGCTTTCGCC
AAAGAGCTTTTCCTAGGCAAAATCAAGAAGAAAGAAGTTTTCCCATTTCCAGAAGTTAGC
CAAGATGAACTTAATGAAATCAATCAGTTCTTGGGACCCGTGGAAAAATTCTTCACTGAA
GAGGTGGACTCCCGAAAAATTGACCAGGAAGGGAAAATCCCAGATGAAACTTTGGAGAAA
TTGAAGAGCCTAGGGCTTTTTGGGCTGCAAGTCCCAGAAGAATATGGTGGCCTGGGCTTC
TCCAACACCATGTACTCAAGACTAGGGGAGATCATCAGCATGGATGGGTCCATCACTGTG
ACCCTGGCAGCGCACCAGGCTATTGGCCTCAAGGGGATCATCTTGGCTGGCACTGAGGAG
CAGAAAGCCAAATACTTGCCTAAACTGGCGTCCGGGGAGCACATTGCAGCCTTCTGCCTC
ACGGAGCCAGCCAGTGGGAGCGATGCAGCCTCAATCCGGAGCAGAGCCACACTAAGTGAA
GACAAGAAGCACTACATCCTCAATGGCTCCAAGGTCTGGATTACTAATGGAGGACTGGCC
AATATTTTTACTGTGTTTGCAAAGACTGAGGTCGTTGATTCTGATGGATCAGTGAAAGAC
AAAATCACAGCATTCATAGTAGAAAGAGACTTTGGTGGAGTCACTAATGGGAAACCCGAA
GATAAATTAGGCATTCGGGGCTCCAACACTTGTGAAGTCCATTTTGAAAACACCAAGATA
CCTGTGGAAAACATCCTTGGAGAGGTCGGAGATGGGTTTAAGGTGGCCATGAACATCCTC
AACAGCGGCCGGTTCAGCATGGGCAGCGTCGTGGCTGGGCTGCTCAAGAGATTGATTGAA
ATGACTGCTGAGTACGCCTGCACAAGGAAACAGTTTAACAAGAGGCTCAGTGAATTTGGA
TTGATTCAGGAGAAATTTGCACTGATGGCTCAGAAGGCTTACGTCATGGAGAGTATGACC
TACCTCACAGCAGGGATGCTGGACCAACCTGGCTTTCCCGACTGCTCCATCGAGGCAGCC
ATGGTGAAGGTGTTCAGCTCCGAGGCCGCCTGGCAGTGTGTGAGTGAGGTGCTGCAGATC
CTCGGGGGCTTGGGCTACACAAGGGACTATCCGTACGAGCGCATATTGCGTGACACCCGC
ATCCTCCTCATCTTCGAGGGAACCAATGAGATTCTCCGGATGTACATCGCCCTGACGGGT
CTGCAGCATGCCGGCCGCATCCTGACTACCAGGATCCATGAGCTTAAACAGGCCAAAGTG
AGCACAGTCATGGATACCGTTGGCCGGAGGCTTCGGGACTCGCTGGGCCGAACTGTGGAC
CTGGGGCTGACAGGCAACCATGGAGTTGTGCACCCCAGTCTTGCGGACAGTGCCAACAAG
TTTGAGGAGAACACCTACTGCTTCGGCCGGACCGTGGAGACACTGCTGCTCCGCTTTGGC
AAGACCATCATGGAGGAGCAGCTGGTACTGAAGCGGGTGGCCAACATCCTCATCAACCTG
TATGGCATGACGGCCGTGCTGTCGCGGGCCAGCCGCTCCATCCGCATTGGGCTCCGCAAC
CACGACCACGAGGTTCTCTTGGCCAACACCTTCTGCGTGGAAGCTTACTTGCAGAATCTC
TTCAGCCTCTCTCAGCTGGACAAGTATGCTCCAGAAAACCTAGATGAGCAGATTAAGAAA
GTGTCCCAGCAGATCCTTGAGAAGCGAGCCTATATCTGTGCCCACCCTCTGGACAGGACA
TGCTGA
|
| Enzyme 99 GenBank Gene ID |
AF327351  |
| Enzyme 99 GeneCard ID |
ACAD9  |
| Enzyme 99 GenAtlas ID |
ACAD9  |
| Enzyme 99 HGNC ID |
HGNC:21497  |
| Enzyme 99 Chromosome Location |
3 |
| Enzyme 99 Locus |
3q21.3 |
| Enzyme 99 SNPs |
SNPJam Report  |
| Enzyme 99 General References |
- Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X: Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1033-42. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- He M, Rutledge SL, Kelly DR, Palmer CA, Murdoch G, Majumder N, Nicholls RD, Pei Z, Watkins PA, Vockley J: A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency. Am J Hum Genet. 2007 Jul;81(1):87-103. Epub 2007 Jun 4. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 99 Metabolite References |
Not Available |
|
Enzyme 100
[top]
|
| Enzyme 100 ID |
12492 |
| Enzyme 100 Name |
Long-chain fatty acid transport protein 4 |
| Enzyme 100 Synonyms |
- FATP-4
- Fatty acid transport protein 4
- Solute carrier family 27 member 4
|
| Enzyme 100 Gene Name |
SLC27A4 |
| Enzyme 100 Protein Sequence |
>Long-chain fatty acid transport protein 4
MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLL
KVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQA
RGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFG
SEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDK
LFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQ
CLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALG
NGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVR
VNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKK
GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE
VPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTE
LRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
|
| Enzyme 100 Number of Residues |
643 |
| Enzyme 100 Molecular Weight |
72063.6 |
| Enzyme 100 Theoretical pI |
8.58 |
| Enzyme 100 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 100 General Function |
Involved in catalytic activity |
| Enzyme 100 Specific Function |
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids |
| Enzyme 100 Pathways |
Not Available |
| Enzyme 100 Reactions |
Not Available |
| Enzyme 100 Pfam Domain Function |
|
| Enzyme 100 Signals |
|
| Enzyme 100 Transmembrane Regions |
|
| Enzyme 100 Essentiality |
Not Available |
| Enzyme 100 GenBank ID Protein |
40807357  |
| Enzyme 100 UniProtKB/Swiss-Prot ID |
Q6P1M0  |
| Enzyme 100 UniProtKB/Swiss-Prot Entry Name |
S27A4_HUMAN  |
| Enzyme 100 PDB ID |
Not Available |
| Enzyme 100 Cellular Location |
Not Available |
| Enzyme 100 Gene Sequence |
>1932 bp
ATGCTGCTTGGAGCCTCTCTGGTGGGGGTGCTGCTGTTCTCCAAGCTGGTGCTGAAACTG
CCCTGGACCCAGGTGGGATTCTCCCTGTTGTTCCTCTACTTGGGATCTGGCGGCTGGCGC
TTCATCCGGGTCTTCATCAAGACCATCAGGCGCGATATCTTTGGCGGCCTGGTCCTCCTG
AAGGTGAAGGCAAAGGTGCGACAGTGCCTGCAGGAGCGGCGGACAGTGCCCATTTTGTTT
GCCTCTACCGTTCGGCGCCACCCCGACAAGACGGCCCTGATCTTCGAGGGCACAGATACC
CACTGGACCTTCCGCCAGCTGGATGAGTACTCAAGCAGTGTAGCCAACTTCCTGCAGGCC
CGGGGCCTGGCCTCGGGCGATGTGGCTGCCATCTTCATGGAGAACCGCAATGAGTTCGTG
GGCCTATGGCTGGGCATGGCCAAGCTCGGTGTGGAGGCAGCCCTCATCAACACCAACCTG
CGGCGGGATGCTCTGCTCCACTGCCTCACCACCTCGCGCGCACGGGCCCTTGTCTTTGGC
AGCGAAATGGCCTCAGCCATCTGTGAGGTCCATGCCAGCCTGGACCCCTCGCTCAGCCTC
TTCTGCTCTGGCTCCTGGGAGCCCGGTGCGGTGCCTCCAAGCACAGAACACCTGGACCCT
CTGCTGAAAGATGCTCCCAAGCACCTTCCCAGTTGCCCTGACAAGGGCTTCACAGATAAA
CTGTTCTACATCTACACATCCGGCACCACAGGGCTGCCCAAGGCCGCCATCGTGGTGCAC
AGCAGGTATTACCGCATGGCTGCCCTGGTGTACTATGGATTCCGCATGCGGCCCAACGAC
ATCGTCTATGACTGCCTCCCCCTCTACCACTCAGCAGGAAACATCGTGGGAATCGGCCAG
TGCCTGCTGCATGGCATGACGGTGGTGATTCGGAAGAAGTTCTCAGCCTCCCGGTTCTGG
GACGATTGTATCAAGTACAACTGCACGATTGTGCAGTACATTGGTGAACTGTGCCGCTAC
CTCCTGAACCAGCCACCGCGGGAGGCAGAAAACCAGCACCAGGTTCGCATGGCACTAGGC
AATGGCCTCCGGCAGTCCATCTGGACCAACTTTTCCAGCCGCTTCCACATACCCCAGGTG
GCTGAGTTCTACGGGGCCACAGAGTGCAACTGTAGCCTGGGCAACTTCGACAGCCAGGTG
GGGGCCTGTGGTTTCAATAGCCGCATCCTGTCCTTCGTGTACCCCATCCGGTTGGTACGT
GTCAACGAGGACACCATGGAGCTGATCCGGGGGCCCGACGGCGTCTGCATTCCCTGCCAG
CCAGGTGAGCCGGGCCAGCTGGTGGGCCGCATCATCCAGAAAGACCCCCTGCGCCGCTTC
GATGGCTACCTCAACCAGGGCGCCAACAACAAGAAGATTGCCAAGGATGTCTTCAAGAAG
GGGGACCAGGCCTACCTTACTGGTGATGTGCTGGTGATGGACGAGCTGGGCTACCTGTAC
TTCCGAGACCGCACTGGGGACACGTTCCGCTGGAAAGGTGAGAACGTGTCCACCACCGAG
GTGGAAGGCACACTCAGCCGCCTGCTGGACATGGCTGACGTGGCCGTGTATGGTGTCGAG
GTGCCAGGAACCGAGGGCCGGGCCGGAATGGCTGCTGTGGCCAGCCCCACTGGCAACTGT
GACCTGGAGCGCTTTGCTCAGGTCTTGGAGAAGGAACTGCCCCTGTATGCGCGCCCCATC
TTCCTGCGCCTCCTGCCTGAGCTGCACAAAACAGGAACCTACAAGTTCCAGAAGACAGAG
CTACGGAAGGAGGGCTTTGACCCGGCTATTGTGAAAGACCCGCTGTTCTATCTAGATGCC
CAGAAGGGCCGCTACGTCCCGCTGGACCAAGAGGCCTACAGCCGCATCCAGGCAGGCGAG
GAGAAGCTGTGA
|
| Enzyme 100 GenBank Gene ID |
NM_005094.3  |
| Enzyme 100 GeneCard ID |
SLC27A4  |
| Enzyme 100 GenAtlas ID |
SLC27A4  |
| Enzyme 100 HGNC ID |
HGNC:10998  |
| Enzyme 100 Chromosome Location |
9 |
| Enzyme 100 Locus |
9q34.11 |
| Enzyme 100 SNPs |
SNPJam Report  |
| Enzyme 100 General References |
- Fitscher BA, Riedel HD, Young KC, Stremmel W: Tissue distribution and cDNA cloning of a human fatty acid transport protein (hsFATP4). Biochim Biophys Acta. 1998 Dec 22;1443(3):381-5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gertow K, Bellanda M, Eriksson P, Boquist S, Hamsten A, Sunnerhagen M, Fisher RM: Genetic and structural evaluation of fatty acid transport protein-4 in relation to markers of the insulin resistance syndrome. J Clin Endocrinol Metab. 2004 Jan;89(1):392-9. [PubMed
]
- Klar J, Schweiger M, Zimmerman R, Zechner R, Li H, Torma H, Vahlquist A, Bouadjar B, Dahl N, Fischer J: Mutations in the fatty acid transport protein 4 gene cause the ichthyosis prematurity syndrome. Am J Hum Genet. 2009 Aug;85(2):248-53. Epub 2009 Jul 23. [PubMed
]
|
| Enzyme 100 Metabolite References |
Not Available |
|
Enzyme 101
[top]
|
| Enzyme 101 ID |
12889 |
| Enzyme 101 Name |
Fatty acyl-CoA reductase 1 |
| Enzyme 101 Synonyms |
- Male sterility domain-containing protein 2
|
| Enzyme 101 Gene Name |
FAR1 |
| Enzyme 101 Protein Sequence |
>Fatty acyl-CoA reductase 1
MVSIPEYYEGKNVLLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEVL
SGKLFDRLRDENPDFREKIIAINSELTQPKLALSEEDKEVIIDSTNIIFHCAATVRFNEN
LRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDS
LEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPF
PGWIDNFNGPSGLFIAAGKGILRTIRASNNALADLVPVDVVVNMSLAAAWYSGVNRPRNI
MVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAP
AFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTENVNMLMNQLNPEDKKT
FNIDVRQLHWAEYIENYCLGTKKYVLNEEMSGLPAARKHLNKLRNIRYGFNTILVILIWR
IFIARSQMARNIWYFVVSLCYKFLSYFRASSTMRY
|
| Enzyme 101 Number of Residues |
515 |
| Enzyme 101 Molecular Weight |
59356.3 |
| Enzyme 101 Theoretical pI |
9.52 |
| Enzyme 101 GO Classification |
| Function |
- binding
- catalytic activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 101 General Function |
Involved in catalytic activity |
| Enzyme 101 Specific Function |
Catalyzes the reduction of saturated fatty acyl-CoA with chain length C16 or C18 to fatty alcohols |
| Enzyme 101 Pathways |
Not Available |
| Enzyme 101 Reactions |
Not Available |
| Enzyme 101 Pfam Domain Function |
|
| Enzyme 101 Signals |
|
| Enzyme 101 Transmembrane Regions |
|
| Enzyme 101 Essentiality |
Not Available |
| Enzyme 101 GenBank ID Protein |
37182687  |
| Enzyme 101 UniProtKB/Swiss-Prot ID |
Q8WVX9  |
| Enzyme 101 UniProtKB/Swiss-Prot Entry Name |
FACR1_HUMAN  |
| Enzyme 101 PDB ID |
Not Available |
| Enzyme 101 Cellular Location |
Not Available |
| Enzyme 101 Gene Sequence |
>1548 bp
ATGGTTTCAATCCCAGAATACTATGAAGGCAAGAACGTCCTCCTCACAGGAGCTACCGGT
TTTCTAGGGAAGGTGCTTCTGGAAAAGTTGCTGAGGTCTTGTCCTAAGGTGAATTCAGTA
TATGTTTTGGTGAGGCAGAAAGCTGGACAGACACCACAAGAGCGAGTGGAAGAAGTCCTT
AGTGGCAAGCTTTTTGACAGATTGAGAGATGAAAATCCAGATTTTAGAGAGAAAATTATA
GCAATCAACAGCGAACTCACCCAACCTAAACTGGCTCTCAGTGAAGAAGATAAAGAGGTG
ATCATAGATTCTACCAATATTATATTCCACTGTGCAGCTACAGTAAGGTTTAATGAAAAT
TTAAGAGATGCTGTTCAGTTAAATGTGATTGCAACGCGACAGCTTATTCTCCTTGCACAA
CAAATGAAGAATCTGGAAGTGTTCATGCATGTATCAACAGCATATGCCTACTGTAATCGC
AAGCATATTGATGAAGTAGTCTATCCACCACCTGTGGATCCCAAGAAGCTGATTGATTCT
TTAGAGTGGATGGATGATGGCCTAGTAAATGATATCACGCCAAAATTGATAGGAGACAGA
CCTAATACATACATATACACAAAAGCATTGGCAGAATATGTTGTACAACAAGAAGGAGCA
AAACTAAATGTGGCAATTGTAAGGCCATCGATTGTTGGTGCCAGTTGGAAAGAACCTTTT
CCAGGATGGATTGATAACTTTAATGGACCAAGTGGTCTCTTTATTGCGGCAGGGAAAGGA
ATTCTTCGAACAATACGTGCCTCCAACAATGCCCTTGCAGATCTTGTTCCTGTAGATGTA
GTTGTCAACATGAGTCTTGCGGCAGCCTGGTATTCCGGAGTTAATAGACCAAGAAACATC
ATGGTGTATAATTGTACAACAGGCAGCACTAATCCTTTCCACTGGGGTGAAGTTGAGTAC
CATGTAATTTCCACTTTCAAGAGGAATCCTCTCGAACAGGCCTTCAGACGGCCCAATGTA
AATCTAACCTCCAATCATCTTTTATATCATTACTGGATTGCTGTAAGCCATAAGGCCCCA
GCATTCCTGTATGATATCTACCTCAGGATGACTGGAAGAAGCCCAAGGATGATGAAAACA
ATAACTCGTCTTCACAAAGCTATGGTGTTTCTTGAATATTTCACAAGTAATTCTTGGGTT
TGGAATACTGAGAATGTCAATATGTTAATGAATCAACTAAACCCTGAAGATAAAAAGACC
TTCAATATTGATGTACGGCAGTTACATTGGGCAGAATATATAGAGAACTACTGCTTGGGA
ACTAAGAAGTACGTATTGAATGAAGAAATGTCTGGCCTCCCTGCAGCCAGAAAACATCTG
AACAAGTTGCGGAATATACGTTATGGTTTTAATACTATCCTTGTGATCCTCATCTGGCGC
ATTTTTATTGCAAGATCACAAATGGCAAGAAATATCTGGTACTTTGTGGTTAGTCTGTGT
TACAAGTTTTTGTCATACTTCCGAGCATCCAGCACTATGAGATACTGA
|
| Enzyme 101 GenBank Gene ID |
AY358784  |
| Enzyme 101 GeneCard ID |
FAR1  |
| Enzyme 101 GenAtlas ID |
FAR1  |
| Enzyme 101 HGNC ID |
HGNC:26222  |
| Enzyme 101 Chromosome Location |
1 |
| Enzyme 101 Locus |
11p15.2 |
| Enzyme 101 SNPs |
SNPJam Report  |
| Enzyme 101 General References |
- Cheng JB, Russell DW: Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J Biol Chem. 2004 Sep 3;279(36):37789-97. Epub 2004 Jun 27. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 101 Metabolite References |
Not Available |
|
Enzyme 102
[top]
|
| Enzyme 102 ID |
12890 |
| Enzyme 102 Name |
Fatty acyl-CoA reductase 2 |
| Enzyme 102 Synonyms |
- Male sterility domain-containing protein 1
|
| Enzyme 102 Gene Name |
FAR2 |
| Enzyme 102 Protein Sequence |
>Fatty acyl-CoA reductase 2
MSTIAAFYGGKSILITGATGFLGKVLMEKLFRTSPDLKVIYILVRPKAGQTLQQRVFQIL
DSKLFEKVKEVCPNVHEKIRAIYADLNQNDFAISKEDMQELLSCTNIIFHCAATVRFDDT
LRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKIIDS
LEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPF
PGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKST
LVYHITSGNMNPCNWHKMGVQVLATFEKIPFERPFRRPNANFTSNSFTSQYWNAVSHRAP
AIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRV
FNFDVRQLNWLEYIENYVLGVKKYLLKEDMAGIPKAKQRLKRLRNIHYLFNTALFLIAWR
LLIARSQMARNVWFFIVSFCYKFLSYFRASSTLKV
|
| Enzyme 102 Number of Residues |
515 |
| Enzyme 102 Molecular Weight |
59437.9 |
| Enzyme 102 Theoretical pI |
9.79 |
| Enzyme 102 GO Classification |
| Function |
- binding
- catalytic activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 102 General Function |
Involved in catalytic activity |
| Enzyme 102 Specific Function |
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 but low activity can be observed with C10-C14 substrates |
| Enzyme 102 Pathways |
Not Available |
| Enzyme 102 Reactions |
Not Available |
| Enzyme 102 Pfam Domain Function |
|
| Enzyme 102 Signals |
|
| Enzyme 102 Transmembrane Regions |
|
| Enzyme 102 Essentiality |
Not Available |
| Enzyme 102 GenBank ID Protein |
7022510  |
| Enzyme 102 UniProtKB/Swiss-Prot ID |
Q96K12  |
| Enzyme 102 UniProtKB/Swiss-Prot Entry Name |
FACR2_HUMAN  |
| Enzyme 102 PDB ID |
Not Available |
| Enzyme 102 Cellular Location |
Not Available |
| Enzyme 102 Gene Sequence |
>1548 bp
ATGTCCACAATTGCAGCTTTCTATGGCGGCAAGTCCATCCTCATCACGGGGGCCACAGGC
TTTCTGGGCAAAGTGCTAATGGAGAAGCTGTTTCGCACCAGCCCAGACCTGAAAGTCATT
TACATCCTTGTGAGGCCCAAGGCTGGCCAGACACTGCAGCAGAGGGTTTTCCAGATCCTA
GACAGTAAGCTATTTGAGAAAGTCAAAGAAGTTTGTCCAAATGTGCATGAGAAGATCAGA
GCTATTTATGCAGATCTCAATCAGAATGACTTTGCCATCAGCAAAGAGGACATGCAGGAG
CTTCTCTCCTGTACAAACATAATATTTCACTGTGCAGCCACTGTACGCTTTGACGACACT
CTCAGACATGCTGTGCAACTTAACGTCACTGCCACCCGGCAGCTCTTGCTTATGGCTAGT
CAGATGCCAAAGCTGGAAGCCTTTATACATATCTCTACTGCCTATTCAAATTGTAACCTG
AAGCACATCGATGAAGTTACCTATCCGTGCCCTGTGGAGCCAAAAAAAATCATTGATTCC
CTTGAGTGGTTAGACGATGCTATTATTGACGAGATTACACCCAAGCTGATCAGAGATTGG
CCCAATATTTATACCTACACCAAGGCCTTGGGAGAAATGGTGGTGCAGCAAGAGAGCAGG
AACCTGAACATTGCCATCATAAGGCCCTCCATTGTGGGAGCAACTTGGCAGGAGCCTTTC
CCAGGTTGGGTTGATAATATAAATGGACCTAATGGAATCATTATTGCGACTGGGAAAGGG
TTTCTTCGGGCCATAAAAGCTACTCCAATGGCTGTGGCAGACGTAATTCCAGTTGATACA
GTCGTCAATCTCATGCTAGCTGTAGGATGGTATACTGCAGTTCACAGACCTAAGTCAACA
TTAGTCTACCACATTACATCTGGTAACATGAATCCCTGCAATTGGCACAAAATGGGAGTC
CAAGTCTTGGCAACCTTTGAAAAAATCCCATTTGAGAGACCTTTCAGGAGGCCAAATGCT
AATTTTACCAGCAACAGCTTCACATCACAGTACTGGAATGCGGTCAGCCACCGGGCCCCT
GCCATTATCTATGACTGCTATCTGCGGCTCACTGGAAGGAAGCCCAGGATGACAAAGCTC
ATGAATCGGCTTTTAAGAACTGTTTCCATGTTGGAGTATTTCATCAACCGGAGTTGGGAA
TGGAGCACGTACAATACAGAAATGCTGATGTCTGAGCTGAGTCCTGAAGACCAGAGGGTA
TTCAACTTTGACGTGCGCCAGTTGAACTGGTTGGAATACATTGAAAATTATGTTTTGGGA
GTTAAAAAATACTTATTGAAAGAGGATATGGCTGGGATCCCAAAGGCAAAGCAACGCTTA
AAAAGGCTCCGAAATATTCACTACCTCTTTAATACTGCCCTCTTCCTTATCGCCTGGCGC
CTTCTCATTGCAAGATCTCAGATGGCTCGGAATGTCTGGTTCTTCATTGTAAGCTTCTGT
TATAAATTCCTCTCCTACTTTAGAGCATCCAGCACGCTCAAAGTTTAA
|
| Enzyme 102 GenBank Gene ID |
AK001324  |
| Enzyme 102 GeneCard ID |
FAR2  |
| Enzyme 102 GenAtlas ID |
FAR2  |
| Enzyme 102 HGNC ID |
HGNC:25531  |
| Enzyme 102 Chromosome Location |
1 |
| Enzyme 102 Locus |
12p11.22 |
| Enzyme 102 SNPs |
SNPJam Report  |
| Enzyme 102 General References |
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cheng JB, Russell DW: Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J Biol Chem. 2004 Sep 3;279(36):37789-97. Epub 2004 Jun 27. [PubMed
]
|
| Enzyme 102 Metabolite References |
Not Available |
|
Enzyme 103
[top]
|
| Enzyme 103 ID |
12897 |
| Enzyme 103 Name |
Acyl-CoA wax alcohol acyltransferase 1 |
| Enzyme 103 Synonyms |
- Diacylglycerol O-acyltransferase 2-like protein 3
- Diacylglycerol acyltransferase 2
- Long-chain-alcohol O-fatty-acyltransferase 1
|
| Enzyme 103 Gene Name |
AWAT1 |
| Enzyme 103 Protein Sequence |
>Acyl-CoA wax alcohol acyltransferase 1
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPE
RGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEA
TGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVG
GVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKF
QSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHA
LYMDALHKLFDQHKTHYGCSETQKLFFL
|
| Enzyme 103 Number of Residues |
328 |
| Enzyme 103 Molecular Weight |
37758.8 |
| Enzyme 103 Theoretical pI |
9.02 |
| Enzyme 103 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 103 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 103 Specific Function |
Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20) |
| Enzyme 103 Pathways |
Not Available |
| Enzyme 103 Reactions |
- acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
|
| Enzyme 103 Pfam Domain Function |
|
| Enzyme 103 Signals |
|
| Enzyme 103 Transmembrane Regions |
|
| Enzyme 103 Essentiality |
Not Available |
| Enzyme 103 GenBank ID Protein |
123227401  |
| Enzyme 103 UniProtKB/Swiss-Prot ID |
Q58HT5  |
| Enzyme 103 UniProtKB/Swiss-Prot Entry Name |
AWAT1_HUMAN  |
| Enzyme 103 PDB ID |
Not Available |
| Enzyme 103 Cellular Location |
Not Available |
| Enzyme 103 Gene Sequence |
>987 bp
ATGGCTCATTCCAAGCAGCCTAGTCACTTCCAGAGTCTGATGCTTCTGCAGTGGCCTTTG
AGCTACCTTGCCATCTTTTGGATCTTGCAGCCATTGTTCGTCTACCTGCTGTTTACATCC
TTGTGGCCGCTACCAGTGCTTTACTTTGCCTGGTTGTTCCTGGACTGGAAGACCCCAGAG
CGAGGTGGCAGGCGTTCGGCCTGGGTAAGGAACTGGTGTGTCTGGACCCACATCAGGGAC
TATTTCCCCATTACGATCCTGAAGACAAAGGACCTATCACCTGAGCACAACTACCTCATG
GGGGTTCACCCCCATGGCCTCCTGACCTTTGGCGCCTTCTGCAACTTCTGCACTGAGGCC
ACAGGCTTCTCGAAGACCTTCCCAGGCATCACTCCTCACTTGGCCACGCTGTCCTGGTTC
TTCAAGATCCCCTTTGTTAGGGAGTACCTCATGGCCAAAGGTGTGTGCTCTGTGAGCCAG
CCAGCCATCAACTATCTGCTGAGCCATGGCACTGGCAACCTCGTGGGCATTGTAGTGGGA
GGTGTGGGTGAGGCCCTGCAAAGTGTGCCCAACACCACCACCCTCATCCTCCAGAAGCGC
AAGGGGTTCGTGCGCACAGCCCTCCAGCATGGGGCTCATCTGGTCCCCACCTTCACTTTT
GGGGAAACTGAGGTGTATGATCAGGTGCTGTTCCATAAGGATAGCAGGATGTACAAGTTC
CAGAGCTGCTTCCGCCGTATCTTTGGTTTCTACTGTTGTGTCTTCTATGGACAAAGCTTC
TGTCAAGGCTCCACTGGGCTCCTGCCATACTCCAGGCCTATTGTCACTGTGGTTGGGGAG
CCTCTGCCACTGCCCCAAATTGAAAAGCCAAGCCAGGAGATGGTGGACAAATACCATGCA
CTTTATATGGATGCTCTGCACAAACTGTTCGACCAGCATAAGACCCACTATGGCTGCTCA
GAGACCCAAAAGCTGTTTTTCCTGTGA
|
| Enzyme 103 GenBank Gene ID |
AL357752  |
| Enzyme 103 GeneCard ID |
AWAT1  |
| Enzyme 103 GenAtlas ID |
AWAT1  |
| Enzyme 103 HGNC ID |
HGNC:23252  |
| Enzyme 103 Chromosome Location |
Not Available |
| Enzyme 103 Locus |
Not Available |
| Enzyme 103 SNPs |
SNPJam Report  |
| Enzyme 103 General References |
- Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
|
| Enzyme 103 Metabolite References |
Not Available |
|
Enzyme 104
[top]
|
| Enzyme 104 ID |
12898 |
| Enzyme 104 Name |
Acyl-CoA wax alcohol acyltransferase 2 |
| Enzyme 104 Synonyms |
- Diacylglycerol O-acyltransferase 2-like protein 4
- Diacylglycerol O-acyltransferase candidate 4
- hDC4
- Long-chain-alcohol O-fatty-acyltransferase 2
- Multifunctional O-acyltransferase
- Wax synthase
- hWS
|
| Enzyme 104 Gene Name |
AWAT2 |
| Enzyme 104 Protein Sequence |
>Acyl-CoA wax alcohol acyltransferase 2
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII
|
| Enzyme 104 Number of Residues |
333 |
| Enzyme 104 Molecular Weight |
38093.2 |
| Enzyme 104 Theoretical pI |
9.69 |
| Enzyme 104 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 104 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 104 Specific Function |
Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo |
| Enzyme 104 Pathways |
Not Available |
| Enzyme 104 Reactions |
- acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
|
| Enzyme 104 Pfam Domain Function |
|
| Enzyme 104 Signals |
|
| Enzyme 104 Transmembrane Regions |
|
| Enzyme 104 Essentiality |
Not Available |
| Enzyme 104 GenBank ID Protein |
49854214  |
| Enzyme 104 UniProtKB/Swiss-Prot ID |
Q6E213  |
| Enzyme 104 UniProtKB/Swiss-Prot Entry Name |
AWAT2_HUMAN  |
| Enzyme 104 PDB ID |
Not Available |
| Enzyme 104 Cellular Location |
Not Available |
| Enzyme 104 Gene Sequence |
>1002 bp
ATGCTCTTGCCCTCTAAGAAGGACCTCAAGACTGCCCTGGATGTCTTTGCTGTTTTCCAG
TGGTCCTTCAGTGCCTTGCTTATCACAACCACTGTGATTGCTGTCAACCTCTACCTGGTG
GTGTTCACACCATACTGGCCTGTCACTGTGCTTATTCTTACCTGGCTGGCTTTTGACTGG
AAGACCCCTCAGCGAGGCGGCCGCCGGTTTACCTGTGTGAGGCACTGGCGCCTGTGGAAA
CACTACAGCGATTATTTCCCTCTCAAGCTTCTGAAGACTCATGACATCTGCCCCAGCCGC
AACTACATCCTCGTCTGCCACCCTCATGGGCTCTTTGCCCATGGATGGTTTGGCCACTTT
GCCACAGAGGCCTCAGGCTTCTCCAAGATATTTCCTGGCATCACCCCTTACATACTCACA
CTGGGAGCCTTTTTCTGGATGCCTTTCCTCAGAGAATATGTAATGTCTACAGGGGCCTGC
TCTGTGAGTCGATCCTCCATTGACTTTCTGCTGACTCATAAAGGCACAGGCAACATGGTC
ATTGTGGTGATTGGTGGACTGGCTGAGTGCAGATACAGCCTGCCAGGTTCTTCTACCCTG
GTGTTGAAGAACCGGTCTGGCTTTGTGCGCATGGCCCTTCAGCATGGGGTGCCTCTAATA
CCTGCCTATGCCTTTGGGGAGACGGACCTCTATGATCAGCACATTTTCACTCCTGGTGGC
TTTGTCAACCGCTTCCAGAAGTGGTTCCAGAGCATGGTACACATCTACCCTTGTGCTTTC
TATGGACGTGGCTTCACCAAGAACTCCTGGGGCCTTCTGCCCTATAGTCGGCCTGTAACC
ACCATCGTCGGGGAGCCTCTACCAATGCCCAAGATTGAGAATCCAAGCCAGGAGATCGTG
GCTAAATATCACACACTCTATATTGATGCCCTACGTAAACTGTTTGACCAGCATAAGACC
AAGTTTGGTATCTCAGAGACCCAGGAGCTGGAGATAATTTGA
|
| Enzyme 104 GenBank Gene ID |
AY605053  |
| Enzyme 104 GeneCard ID |
AWAT2  |
| Enzyme 104 GenAtlas ID |
AWAT2  |
| Enzyme 104 HGNC ID |
HGNC:23251  |
| Enzyme 104 Chromosome Location |
Not Available |
| Enzyme 104 Locus |
Not Available |
| Enzyme 104 SNPs |
SNPJam Report  |
| Enzyme 104 General References |
- Cheng JB, Russell DW: Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. J Biol Chem. 2004 Sep 3;279(36):37798-807. Epub 2004 Jun 27. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
- Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed
]
- Yen CL, Brown CH 4th, Monetti M, Farese RV Jr: A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. J Lipid Res. 2005 Nov;46(11):2388-97. Epub 2005 Aug 16. [PubMed
]
|
| Enzyme 104 Metabolite References |
Not Available |
|
Enzyme 105
[top]
|
| Enzyme 105 ID |
12899 |
| Enzyme 105 Name |
Diacylglycerol O-acyltransferase 2-like protein 6 |
| Enzyme 105 Synonyms |
- Diacylglycerol O-acyltransferase candidate 3
- hDC3
|
| Enzyme 105 Gene Name |
DGAT2L6 |
| Enzyme 105 Protein Sequence |
>Diacylglycerol O-acyltransferase 2-like protein 6
MAFFSRLNLQEGLQTFFVLQWIPVYIFLGAIPILLIPYFLLFSKFWPLAVLSLAWLTYDW
NTHSQGGRRSAWVRNWTLWKYFRNYFPVKLVKTHDLSPKHNYIIANHPHGILSFGVFINF
ATEATGIARIFPSITPFVGTLERIFWIPIVREYVMSMGVCPVSSSALKYLLTQKGSGNAV
VIVVGGAAEALLCRPGASTLFLKQRKGFVKMALQTGAYLVPSYSFGENEVFNQETFPEGT
WLRLFQKTFQDTFKKILGLNFCTFHGRGFTRGSWGFLPFNRPITTVVGEPLPIPRIKRPN
QKTVDKYHALYISALRKLFDQHKVEYGLPETQELTIT
|
| Enzyme 105 Number of Residues |
337 |
| Enzyme 105 Molecular Weight |
38592.9 |
| Enzyme 105 Theoretical pI |
10.34 |
| Enzyme 105 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 105 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 105 Specific Function |
Probable acyltransferase uses fatty acyl-CoA as substrate. Has no wax synthase activity to produce wax esters |
| Enzyme 105 Pathways |
Not Available |
| Enzyme 105 Reactions |
Not Available |
| Enzyme 105 Pfam Domain Function |
|
| Enzyme 105 Signals |
|
| Enzyme 105 Transmembrane Regions |
|
| Enzyme 105 Essentiality |
Not Available |
| Enzyme 105 GenBank ID Protein |
34526048  |
| Enzyme 105 UniProtKB/Swiss-Prot ID |
Q6ZPD8  |
| Enzyme 105 UniProtKB/Swiss-Prot Entry Name |
DG2L6_HUMAN  |
| Enzyme 105 PDB ID |
Not Available |
| Enzyme 105 Cellular Location |
Not Available |
| Enzyme 105 Gene Sequence |
>1014 bp
ATGGCTTTCTTCTCCCGACTGAATCTCCAGGAGGGCCTCCAAACCTTCTTTGTTTTGCAA
TGGATCCCAGTCTATATATTTTTAGGAGCTATTCCCATTCTCCTTATACCCTACTTTCTG
TTATTCAGTAAGTTCTGGCCCTTGGCTGTGCTCTCCTTAGCCTGGCTCACCTATGATTGG
AACACCCACAGTCAAGGTGGCAGGCGTTCAGCTTGGGTACGAAACTGGACCCTATGGAAG
TATTTCCGAAATTACTTCCCAGTAAAGCTGGTGAAGACTCATGATCTTTCTCCCAAACAC
AACTACATCATTGCCAATCACCCCCATGGCATTCTCTCTTTTGGTGTCTTCATCAACTTT
GCCACTGAGGCCACTGGCATTGCTCGGATTTTCCCATCCATCACTCCCTTTGTAGGGACC
TTAGAAAGGATATTTTGGATCCCAATTGTGCGAGAATATGTGATGTCAATGGGTGTGTGC
CCTGTGAGTAGCTCAGCCTTGAAGTACTTGCTGACCCAGAAAGGCTCAGGCAATGCCGTG
GTTATTGTGGTGGGTGGAGCTGCTGAAGCTCTCTTGTGCCGACCAGGAGCCTCCACTCTC
TTCCTCAAGCAGCGTAAAGGTTTTGTGAAGATGGCACTGCAAACAGGGGCATACCTTGTC
CCTTCATATTCCTTTGGTGAGAACGAAGTTTTCAATCAGGAGACCTTCCCTGAGGGCACG
TGGTTAAGGTTGTTCCAAAAAACCTTCCAGGACACATTCAAAAAAATCCTGGGACTAAAT
TTCTGTACCTTCCATGGCCGGGGCTTCACTCGCGGATCCTGGGGCTTCCTGCCTTTCAAT
CGGCCCATTACCACTGTTGTTGGGGAACCCCTTCCAATTCCCAGGATTAAGAGGCCAAAC
CAGAAGACAGTAGACAAGTATCACGCACTCTACATCAGTGCCCTGCGCAAGCTCTTTGAC
CAACACAAAGTTGAATATGGCCTCCCTGAGACCCAAGAGCTGACAATTACATAA
|
| Enzyme 105 GenBank Gene ID |
AK129500  |
| Enzyme 105 GeneCard ID |
DGAT2L6  |
| Enzyme 105 GenAtlas ID |
DGAT2L6  |
| Enzyme 105 HGNC ID |
HGNC:23250  |
| Enzyme 105 Chromosome Location |
Not Available |
| Enzyme 105 Locus |
Not Available |
| Enzyme 105 SNPs |
SNPJam Report  |
| Enzyme 105 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
- Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed
]
|
| Enzyme 105 Metabolite References |
Not Available |
|
Enzyme 106
[top]
|
| Enzyme 106 ID |
12900 |
| Enzyme 106 Name |
Putative diacylglycerol O-acyltransferase 2-like protein 7 |
| Enzyme 106 Synonyms |
Not Available |
| Enzyme 106 Gene Name |
DGAT2L7 |
| Enzyme 106 Protein Sequence |
>Putative diacylglycerol O-acyltransferase 2-like protein 7
MLAVLYLLVKTAKLGTSWNYLFDFHPHRVLVVGAFANFCTEPTGCSCLFPKLPPHLLMLP
CWFHLLFFQDYIMSGASALPPGLVSFVKAPLPQWWPGGCPGVGGPLQALEAKPGQLSLPI
RNQKRLVKSALELGENELFQQFPNPQSSWVQRTQEALRPLLSVALQLFLGRRGLPLPFRA
PIRTVVGSAIPVQQSPPPSPAQVDTLQARYVGRLTQLFEEHQARYGVPADRHLVLTEARP
TAWPRLSAG
|
| Enzyme 106 Number of Residues |
249 |
| Enzyme 106 Molecular Weight |
27571.0 |
| Enzyme 106 Theoretical pI |
9.99 |
| Enzyme 106 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 106 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 106 Specific Function |
Probable acyltransferase uses fatty acyl-CoA as substrate |
| Enzyme 106 Pathways |
Not Available |
| Enzyme 106 Reactions |
Not Available |
| Enzyme 106 Pfam Domain Function |
|
| Enzyme 106 Signals |
|
| Enzyme 106 Transmembrane Regions |
|
| Enzyme 106 Essentiality |
Not Available |
| Enzyme 106 GenBank ID Protein |
Not Available |
| Enzyme 106 UniProtKB/Swiss-Prot ID |
Q6IED9  |
| Enzyme 106 UniProtKB/Swiss-Prot Entry Name |
DG2L7_HUMAN  |
| Enzyme 106 PDB ID |
Not Available |
| Enzyme 106 Cellular Location |
Not Available |
| Enzyme 106 Gene Sequence |
Not Available |
| Enzyme 106 GenBank Gene ID |
Not Available |
| Enzyme 106 GeneCard ID |
DGAT2L7  |
| Enzyme 106 GenAtlas ID |
Not Available |
| Enzyme 106 HGNC ID |
Not Available |
| Enzyme 106 Chromosome Location |
7 |
| Enzyme 106 Locus |
7q22.1 |
| Enzyme 106 SNPs |
SNPJam Report  |
| Enzyme 106 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed
]
|
| Enzyme 106 Metabolite References |
Not Available |
|
Enzyme 107
[top]
|
| Enzyme 107 ID |
12903 |
| Enzyme 107 Name |
2-acylglycerol O-acyltransferase 3 |
| Enzyme 107 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 3
- MGAT3
- Diacylglycerol O-acyltransferase candidate 7
- hDC7
- Diacylglycerol acyltransferase 2-like protein 7
- Monoacylglycerol O-acyltransferase 3
|
| Enzyme 107 Gene Name |
MOGAT3 |
| Enzyme 107 Protein Sequence |
>2-acylglycerol O-acyltransferase 3
MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYL
VWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMC
TGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQ
PQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRL
KAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQR
LHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI
|
| Enzyme 107 Number of Residues |
341 |
| Enzyme 107 Molecular Weight |
38729.8 |
| Enzyme 107 Theoretical pI |
8.70 |
| Enzyme 107 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 107 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 107 Specific Function |
Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes |
| Enzyme 107 Pathways |
|
| Enzyme 107 Reactions |
- acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
|
| Enzyme 107 Pfam Domain Function |
|
| Enzyme 107 Signals |
|
| Enzyme 107 Transmembrane Regions |
|
| Enzyme 107 Essentiality |
Not Available |
| Enzyme 107 GenBank ID Protein |
29124967  |
| Enzyme 107 UniProtKB/Swiss-Prot ID |
Q86VF5  |
| Enzyme 107 UniProtKB/Swiss-Prot Entry Name |
MOGT3_HUMAN  |
| Enzyme 107 PDB ID |
Not Available |
| Enzyme 107 Cellular Location |
Not Available |
| Enzyme 107 Gene Sequence |
>1026 bp
ATGGGAGTTGCCACAACCCTGCAGCCCCCAACCACTTCCAAAACCTTGCAGAAGCAGCAT
CTAGAAGCAGTGGGCGCCTACCAATATGTGCTCACTTTCCTCTTCATGGGCCCTTTCTTC
TCCCTTCTTGTCTTTGTCCTCCTCTTCACGTCACTCTGGCCCTTCTCTGTTTTTTACTTG
GTGTGGCTCTATGTGGACTGGGACACACCCAACCAAGGTGGAAGGCGTTCGGAGTGGATA
AGGAACCGGGCAATTTGGAGACAACTAAGGGATTATTATCCTGTCAAGCTGGTGAAAACA
GCAGAGCTGCCCCCGGATCGGAACTACGTGCTGGGCGCCCACCCTCATGGGATCATGTGT
ACAGGCTTCCTCTGTAATTTCTCCACCGAGAGCAATGGCTTCTCCCAGCTCTTCCCGGGG
CTCCGGCCCTGGTTAGCCGTGCTGGCTGGCCTCTTCTACCTCCCGGTCTATCGCGACTAC
ATCATGTCCTTTGGACTCTGTCCGGTGAGCCGCCAGAGCCTGGACTTCATCCTGTCCCAG
CCCCAGCTCGGGCAGGCCGTGGTCATCATGGTGGGGGGTGCGCACGAGGCCCTGTATTCA
GTCCCCGGGGAGCACTGCCTTACGCTCCAGAAGCGCAAAGGCTTCGTGCGCCTGGCGCTG
AGGCACGGGGCGTCCCTGGTGCCCGTGTACTCCTTTGGGGAGAATGACATCTTTAGACTT
AAGGCTTTTGCCACAGGCTCCTGGCAGCATTGGTGCCAGCTCACCTTCAAGAAGCTCATG
GGCTTCTCTCCTTGCATCTTCTGGGGTCGCGGTCTCTTCTCAGCCACCTCCTGGGGCCTG
CTGCCCTTTGCTGTGCCCATCACCACTGTGGTGGGCCGCCCCATCCCCGTCCCCCAGCGC
CTCCACCCCACCGAGGAGGAAGTCAATCACTATCACGCCCTCTACATGACGGCCCTGGAG
CAGCTCTTCGAGGAGCACAAGGAAAGCTGTGGGGTCCCCGCTTCCACCTGCCTCACCTTC
ATCTAG
|
| Enzyme 107 GenBank Gene ID |
AY229854  |
| Enzyme 107 GeneCard ID |
MOGAT3  |
| Enzyme 107 GenAtlas ID |
MOGAT3  |
| Enzyme 107 HGNC ID |
HGNC:23249  |
| Enzyme 107 Chromosome Location |
7 |
| Enzyme 107 Locus |
7q22.1 |
| Enzyme 107 SNPs |
SNPJam Report  |
| Enzyme 107 General References |
- Cheng D, Nelson TC, Chen J, Walker SG, Wardwell-Swanson J, Meegalla R, Taub R, Billheimer JT, Ramaker M, Feder JN: Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption. J Biol Chem. 2003 Apr 18;278(16):13611-4. Epub 2003 Mar 3. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 107 Metabolite References |
Not Available |
|
Enzyme 108
[top]
|
| Enzyme 108 ID |
12907 |
| Enzyme 108 Name |
Lysophospholipid acyltransferase 5 |
| Enzyme 108 Synonyms |
- LPLAT 5
- 1-acylglycerophosphocholine O-acyltransferase
- 1-acylglycerophosphoserine O-acyltransferase
- Lysophosphatidylcholine acyltransferase
- LPCAT
- Lyso-PC acyltransferase
- Lysophosphatidylcholine acyltransferase 3
- Lyso-PC acyltransferase 3
- Lysophosphatidylserine acyltransferase
- LPSAT
- Lyso-PS acyltransferase
- Membrane-bound O-acyltransferase domain-containing protein 5
- O-acyltransferase domain-containing protein 5
|
| Enzyme 108 Gene Name |
LPCAT3 |
| Enzyme 108 Protein Sequence |
>Lysophospholipid acyltransferase 5
MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRH
YLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCF
QMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRG
VPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFY
LVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGL
GFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKE
LSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFY
YLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRK
EKLKKME
|
| Enzyme 108 Number of Residues |
487 |
| Enzyme 108 Molecular Weight |
56034.5 |
| Enzyme 108 Theoretical pI |
8.87 |
| Enzyme 108 GO Classification |
Not Available |
| Enzyme 108 General Function |
Involved in 1-acylglycerophosphocholine O-acyltransfera |
| Enzyme 108 Specific Function |
Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3- phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero- 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn- glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle |
| Enzyme 108 Pathways |
Not Available |
| Enzyme 108 Reactions |
- acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318]
|
| Enzyme 108 Pfam Domain Function |
|
| Enzyme 108 Signals |
|
| Enzyme 108 Transmembrane Regions |
- 44-64
84-104
111-131
180-200
227-247
285-305
364-384
422-442
453-473
|
| Enzyme 108 Essentiality |
Not Available |
| Enzyme 108 GenBank ID Protein |
42542394  |
| Enzyme 108 UniProtKB/Swiss-Prot ID |
Q6P1A2  |
| Enzyme 108 UniProtKB/Swiss-Prot Entry Name |
MBOA5_HUMAN  |
| Enzyme 108 PDB ID |
Not Available |
| Enzyme 108 Cellular Location |
Not Available |
| Enzyme 108 Gene Sequence |
>1464 bp
ATGGCGTCCTCAGCGGAGGGGGACGAGGGGACTGTGGTGGCGCTGGCGGGGGTTCTGCAG
TCGGGTTTCCAGGAGCTGAGCCTTAACAAGTTGGCGACGTCCCTGGGCGCGTCAGAACAG
GCGCTGCGGCTGATCATCTCCATCTTCCTGGGTTACCCCTTTGCTTTGTTTTATCGGCAT
TACCTTTTCTACAAGGAGACCTACCTCATCCACCTCTTCCATACCTTTACAGGCCTCTCA
ATTGCTTATTTTAACTTTGGAAACCAGCTCTACCACTCCCTGCTGTGTATTGTGCTTCAG
TTCCTCATCCTTCGACTAATGGGCCGCACCATCACTGCCGTCCTCACTACCTTTTGCTTC
CAGATGGCCTACCTTCTGGCTGGATACTATTACACTGCCACCGGCAACTACGATATCAAG
TGGACAATGCCACATTGTGTTCTGACTTTGAAGCTGATTGGTTTGGCTGTTGACTACTTT
GACGGAGGGAAAGATCAGAATTCCTTGTCCTCTGAGCAACAGAAATATGCCATACGTGGT
GTTCCTTCCCTGCTGGAAGTTGCTGGTTTCTCCTACTTCTATGGGGCCTTCTTGGTAGGG
CCCCAGTTCTCAATGAATCACTACATGAAGCTGGTGCAGGGAGAGCTGATTGACATACCA
GGAAAGATACCAAACAGCATCATTCCTGCTCTCAAGCGCCTGAGTCTGGGCCTTTTCTAC
CTAGTGGGCTACACACTGCTCAGCCCCCACATCACAGAAGACTATCTCCTCACTGAAGAC
TATGACAACCACCCCTTCTGGTTCCGCTGCATGTACATGCTGATCTGGGGCAAGTTTGTG
CTGTACAAATATGTCACCTGTTGGCTGGTCACAGAAGGAGTATGCATTTTGACGGGCCTG
GGCTTCAATGGCTTTGAAGAAAAGGGCAAGGCAAAGTGGGATGCCTGTGCCAACATGAAG
GTGTGGCTCTTTGAAACAAACCCCCGCTTCACTGGCACCATTGCCTCATTCAACATCAAC
ACCAACGCCTGGGTGGCCCGCTACATCTTCAAACGACTCAAGTTCCTTGGAAATAAAGAA
CTCTCTCAGGGTCTCTCGTTGCTATTCCTGGCCCTCTGGCACGGCCTGCACTCAGGATAC
CTGGTCTGCTTCCAGATGGAATTCCTCATTGTTATTGTGGAAAGACAGGCTGCCAGGCTC
ATTCAAGAGAGCCCCACCCTGAGCAAGCTGGCCGCCATTACTGTCCTCCAGCCCTTCTAC
TATTTGGTGCAACAGACCATCCACTGGCTCTTCATGGGTTACTCCATGACTGCCTTCTGC
CTCTTCACGTGGGACAAATGGCTTAAGGTGTATAAATCCATCTATTTCCTTGGCCACATC
TTCTTCCTGAGCCTACTATTCATATTGCCTTATATTCACAAAGCAATGGTGCCAAGGAAA
GAGAAGTTAAAGAAGATGGAATAA
|
| Enzyme 108 GenBank Gene ID |
NM_005768.5  |
| Enzyme 108 GeneCard ID |
LPCAT3  |
| Enzyme 108 GenAtlas ID |
LPCAT3  |
| Enzyme 108 HGNC ID |
HGNC:30244  |
| Enzyme 108 Chromosome Location |
1 |
| Enzyme 108 Locus |
12p13 |
| Enzyme 108 SNPs |
SNPJam Report  |
| Enzyme 108 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zhao Y, Chen YQ, Bonacci TM, Bredt DS, Li S, Bensch WR, Moller DE, Kowala M, Konrad RJ, Cao G: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J Biol Chem. 2008 Mar 28;283(13):8258-65. Epub 2008 Jan 14. [PubMed
]
- Gijon MA, Riekhof WR, Zarini S, Murphy RC, Voelker DR: Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils. J Biol Chem. 2008 Oct 31;283(44):30235-45. Epub 2008 Sep 3. [PubMed
]
|
| Enzyme 108 Metabolite References |
Not Available |
|
Enzyme 109
[top]
|
| Enzyme 109 ID |
12909 |
| Enzyme 109 Name |
Lysophosphatidylcholine acyltransferase 1 |
| Enzyme 109 Synonyms |
- LPC acyltransferase 1
- LPCAT-1
- LysoPC acyltransferase 1
- 1-acylglycerophosphocholine O-acyltransferase
- 1-alkylglycerophosphocholine O-acetyltransferase
- Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
- Acetyl-CoA:lyso-PAF acetyltransferase
- Lyso-PAF acetyltransferase
- LysoPAFAT
- Acyltransferase-like 2
- Phosphonoformate immuno-associated protein 3
|
| Enzyme 109 Gene Name |
LPCAT1 |
| Enzyme 109 Protein Sequence |
>Lysophosphatidylcholine acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
|
| Enzyme 109 Number of Residues |
534 |
| Enzyme 109 Molecular Weight |
59150.7 |
| Enzyme 109 Theoretical pI |
5.82 |
| Enzyme 109 GO Classification |
| Function |
- acyltransferase activity
- binding
- calcium ion binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 109 General Function |
Involved in acyltransferase activity |
| Enzyme 109 Specific Function |
Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology |
| Enzyme 109 Pathways |
|
| Enzyme 109 Reactions |
- acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
|
| Enzyme 109 Pfam Domain Function |
|
| Enzyme 109 Signals |
|
| Enzyme 109 Transmembrane Regions |
|
| Enzyme 109 Essentiality |
Not Available |
| Enzyme 109 GenBank ID Protein |
100811832  |
| Enzyme 109 UniProtKB/Swiss-Prot ID |
Q8NF37  |
| Enzyme 109 UniProtKB/Swiss-Prot Entry Name |
PCAT1_HUMAN  |
| Enzyme 109 PDB ID |
Not Available |
| Enzyme 109 Cellular Location |
Not Available |
| Enzyme 109 Gene Sequence |
>1605 bp
ATGAGGCTGCGGGGATGCGGACCCCGGGCCGCCCCTGCCTCCAGCGCAGGGGCCAGCGAC
GCTCGGCTGCTGGCGCCCCCGGGGCGGAACCCCTTCGTGCACGAGCTGCGCCTCAGCGCC
CTGCAGAAGGCCCAGGTGGCCCTCATGACACTGACGCTCTTCCCGGTCCGGCTCCTGGTT
GCCGCTGCCATGATGCTGCTGGCCTGGCCCCTCGCACTTGTCGCATCCCTGGGCTCTGCG
GAGAAGGAACCCGAGCAGCCCCCGGCCCTGTGGAGGAAGGTTGTGGACTTCCTGCTGAAG
GCCATCATGCGCACCATGTGGTTCGCCGGCGGCTTCCACCGGGTGGCCGTGAAGGGGCGG
CAGGCGCTGCCCACCGAGGCGGCCATCCTCACGCTCGCGCCTCACTCGTCCTACTTCGAC
GCCATCCCTGTGACCATGACGATGTCCTCCATCGTGATGAAGGCAGAGAGCAGAGACATC
CCGATCTGGGGAACTCTGATCCAGTATATACGGCCTGTGTTCGTGTCCCGGTCAGACCAG
GATTCTCGCAGGAAAACAGTAGAAGAAATCAAGAGACGGGCGCAGTCCAACGGAAAGTGG
CCACAGATAATGATTTTTCCAGAAGGAACTTGTACAAACAGGACCTGCCTAATTACCTTC
AAACCTGGTGCATTCATCCCTGGAGCGCCCGTCCAGCCTGTGGTTTTACGATATCCAAAT
AAACTGGACACCATCACATGGACGTGGCAAGGACCTGGAGCGCTGGAAATCCTGTGGCTC
ACGCTGTGTCAGTTTCACAACCAAGTGGAAATCGAGTTCCTTCCTGTGTACAGCCCTTCT
GAGGAGGAGAAGAGGAACCCCGCGCTGTATGCCAGCAACGTGCGGCGAGTCATGGCCGAG
GCCTTGGGTGTCTCCGTGACTGACTACACGTTCGAGGACTGCCAGCTGGCCCTGGCGGAA
GGACAGCTCCGTCTCCCCGCTGACACTTGCCTTTTAGAATTTGCCAGGCTCGTGCGGGGC
CTCGGGCTAAAACCAGAAAAGCTTGAAAAAGATCTGGACAGATACTCAGAAAGAGCCAGG
ATGAAGGGAGGAGAGAAGATAGGTATTGCGGAGTTTGCCGCCTCCCTGGAAGTCCCCGTT
TCTGACTTGCTGGAAGACATGTTTTCACTGTTCGACGAGAGCGGCAGCGGCGAGGTGGAC
CTGCGAGAGTGTGTGGTTGCCCTGTCTGTCGTCTGCCGGCCGGCCCGGACCCTGGACACC
ATCCAGCTGGCTTTCAAGATGTACGGAGCGCAAGAGGACGGCAGCGTCGGCGAAGGTGAC
CTGTCCTGCATCCTCAAGACGGCCCTGGGGGTGGCAGAGCTCACCGTGACCGACCTATTC
CGAGCCATTGACCAAGAGGAGAAGGGGAAGATCACATTCGCTGACTTCCACAGGTTTGCA
GAAATGTACCCTGCCTTCGCAGAGGAATACCTGTACCCGGATCAGACACATTTCGAAAGC
TGTGCAGAGACCTCACCTGCGCCAATCCCAAACGGCTTCTGTGCCGATTTCAGCCCGGAA
AACTCAGACGCTGGGCGGAAGCCTGTTCGCAAGAAGCTGGATTAG
|
| Enzyme 109 GenBank Gene ID |
AB244719  |
| Enzyme 109 GeneCard ID |
LPCAT1  |
| Enzyme 109 GenAtlas ID |
LPCAT1  |
| Enzyme 109 HGNC ID |
HGNC:25718  |
| Enzyme 109 Chromosome Location |
5 |
| Enzyme 109 Locus |
5p15.33 |
| Enzyme 109 SNPs |
SNPJam Report  |
| Enzyme 109 General References |
- Nakanishi H, Shindou H, Hishikawa D, Harayama T, Ogasawara R, Suwabe A, Taguchi R, Shimizu T: Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production. J Biol Chem. 2006 Jul 21;281(29):20140-7. Epub 2006 May 16. [PubMed
]
- Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Chen X, Hyatt BA, Mucenski ML, Mason RJ, Shannon JM: Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11724-9. Epub 2006 Jul 24. [PubMed
]
|
| Enzyme 109 Metabolite References |
Not Available |
|
Enzyme 110
[top]
|
| Enzyme 110 ID |
12931 |
| Enzyme 110 Name |
Lysocardiolipin acyltransferase 1 |
| Enzyme 110 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 8
- 1-AGP acyltransferase 8
- 1-AGPAT 8
- Acyl-CoA:lysocardiolipin acyltransferase 1
|
| Enzyme 110 Gene Name |
LCLAT1 |
| Enzyme 110 Protein Sequence |
>Lysocardiolipin acyltransferase 1
MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSI
FMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVII
MNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKS
HFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTF
VVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDL
QLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAM
CLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
|
| Enzyme 110 Number of Residues |
414 |
| Enzyme 110 Molecular Weight |
48919.8 |
| Enzyme 110 Theoretical pI |
8.80 |
| Enzyme 110 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 110 General Function |
Involved in acyltransferase activity |
| Enzyme 110 Specific Function |
Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages |
| Enzyme 110 Pathways |
|
| Enzyme 110 Reactions |
- acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
|
| Enzyme 110 Pfam Domain Function |
|
| Enzyme 110 Signals |
|
| Enzyme 110 Transmembrane Regions |
- 47-67
86-106
340-360
362-382
|
| Enzyme 110 Essentiality |
Not Available |
| Enzyme 110 GenBank ID Protein |
42558246  |
| Enzyme 110 UniProtKB/Swiss-Prot ID |
Q6UWP7  |
| Enzyme 110 UniProtKB/Swiss-Prot Entry Name |
LCLT1_HUMAN  |
| Enzyme 110 PDB ID |
Not Available |
| Enzyme 110 Cellular Location |
Not Available |
| Enzyme 110 Gene Sequence |
>1245 bp
ATGCATTCCAGGGGAAGGGAAATTGTGGTGCTTCTGAACCCATGGTCAATTAACGAGGCA
GTTTCTAGCTACTGCACGTACTTCATAAAGCAGGACTCTAAAAGCTTTGGAATCATGGTG
TCATGGAAAGGGATTTACTTTATACTGACTCTGTTTTGGGGAAGCTTTTTTGGAAGCATT
TTCATGCTGAGTCCCTTTTTACCTTTGATGTTTGTAAACCCATCTTGGTATCGCTGGATC
AACAACCGCCTTGTGGCAACATGGCTCACCCTACCTGTGGCATTATTGGAGACCATGTTT
GGTGTAAAAGTGATTATAACTGGGGATGCATTTGTTCCTGGAGAAAGAAGTGTCATTATC
ATGAACCATCGGACAAGAATGGACTGGATGTTCCTGTGGAATTGCCTGATGCGATATAGC
TACCTCAGATTGGAGAAAATTTGCCTCAAAGCGAGTCTCAAAGGTGTTCCTGGATTTGGT
TGGGCCATGCAGGCTGCTGCCTATATCTTCATTCATAGGAAATGGAAGGATGACAAGAGC
CATTTCGAAGACATGATTGATTACTTTTGTGATATTCACGAACCACTTCAACTCCTCATA
TTCCCAGAAGGGACTGATCTCACAGAAAACAGCAAGTCTCGAAGTAATGCATTTGCTGAA
AAAAATGGACTTCAGAAATATGAATATGTTTTACATCCAAGAACTACAGGCTTTACTTTT
GTGGTAGACCGTCTAAGAGAAGGTAAGAACCTTGATGCTGTCCATGATATCACTGTGGCG
TATCCTCACAACATTCCTCAATCAGAGAAGCACCTCCTCCAAGGAGACTTTCCCAGGGAA
ATCCACTTTCACGTCCACCGGTATCCAATAGACACCCTCCCCACATCCAAGGAGGACCTT
CAACTCTGGTGCCACAAACGGTGGGAAGAGAAAGAAGAGAGGCTGCGTTCCTTCTATCAA
GGGGAGAAGAATTTTTATTTTACCGGACAGAGTGTCATTCCACCTTGCAAGTCTGAACTC
AGGGTCCTTGTGGTCAAATTGCTCTCTATACTGTATTGGACCCTGTTCAGCCCTGCAATG
TGCCTACTCATATATTTGTACAGTCTTGTTAAGTGGTATTTTATAATCACCATTGTAATC
TTTGTGCTGCAAGAGAGAATATTTGGTGGACTGGAGATCATAGAACTTGCATGTTACCGA
CTTTTACACAAACAGCCACATTTAAATTCAAAGAAAAATGAGTAA
|
| Enzyme 110 GenBank Gene ID |
NM_182551.3  |
| Enzyme 110 GeneCard ID |
LCLAT1  |
| Enzyme 110 GenAtlas ID |
LCLAT1  |
| Enzyme 110 HGNC ID |
HGNC:26756  |
| Enzyme 110 Chromosome Location |
2 |
| Enzyme 110 Locus |
2p23.1 |
| Enzyme 110 SNPs |
SNPJam Report  |
| Enzyme 110 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Agarwal AK, Barnes RI, Garg A: Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity. Arch Biochem Biophys. 2006 May 15;449(1-2):64-76. Epub 2006 Mar 29. [PubMed
]
- Zhao Y, Chen YQ, Li S, Konrad RJ, Cao G: The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids. J Lipid Res. 2009 May;50(5):945-56. Epub 2008 Dec 15. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 110 Metabolite References |
Not Available |
|
Enzyme 111
[top]
|
| Enzyme 111 ID |
12935 |
| Enzyme 111 Name |
Lysophospholipid acyltransferase LPCAT4 |
| Enzyme 111 Synonyms |
- 1-acylglycerol-3-phosphate O-acyltransferase 7
- 1-AGP acyltransferase 7
- 1-AGPAT 7
- Acyltransferase-like 3
- Lysophosphatidylcholine acyltransferase 4
- Lysophosphatidylethanolamine acyltransferase 2
|
| Enzyme 111 Gene Name |
LPCAT4 |
| Enzyme 111 Protein Sequence |
>Lysophospholipid acyltransferase LPCAT4
MSQGSPGDWAPLDPTPGPPASPNPFVHELHLSRLQRVKFCLLGALLAPIRVLLAFIVLFL
LWPFAWLQVAGLSEEQLQEPITGWRKTVCHNGVLGLSRLLFFLLGFLRIRVRGQRASRLQ
APVLVAAPHSTFFDPIVLLPCDLPKVVSRAENLSVPVIGALLRFNQAILVSRHDPASRRR
VVEEVRRRATSGGKWPQVLFFPEGTCSNKKALLKFKPGAFIAGVPVQPVLIRYPNSLDTT
SWAWRGPGVLKVLWLTASQPCSIVDVEFLPVYHPSPEESRDPTLYANNVQRVMAQALGIP
ATECEFVGSLPVIVVGRLKVALEPQLWELGKVLRKAGLSAGYVDAGAEPGRSRMISQEEF
ARQLQLSDPQTVAGAFGYFQQDTKGLVDFRDVALALAALDGGRSLEELTRLAFELFAEEQ
AEGPNRLLYKDGFSTILHLLLGSPHPAATALHAELCQAGSSQGLSLCQFQNFSLHDPLYG
KLFSTYLRPPHTSRGTSQTPNASSPGNPTALANGTVQAPKQKGD
|
| Enzyme 111 Number of Residues |
524 |
| Enzyme 111 Molecular Weight |
57218.6 |
| Enzyme 111 Theoretical pI |
9.24 |
| Enzyme 111 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 111 General Function |
Involved in acyltransferase activity |
| Enzyme 111 Specific Function |
Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1- alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl- phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors |
| Enzyme 111 Pathways |
|
| Enzyme 111 Reactions |
Not Available |
| Enzyme 111 Pfam Domain Function |
|
| Enzyme 111 Signals |
|
| Enzyme 111 Transmembrane Regions |
|
| Enzyme 111 Essentiality |
Not Available |
| Enzyme 111 GenBank ID Protein |
87116681  |
| Enzyme 111 UniProtKB/Swiss-Prot ID |
Q643R3  |
| Enzyme 111 UniProtKB/Swiss-Prot Entry Name |
LPCT4_HUMAN  |
| Enzyme 111 PDB ID |
Not Available |
| Enzyme 111 Cellular Location |
Not Available |
| Enzyme 111 Gene Sequence |
>1575 bp
ATGAGCCAGGGAAGTCCGGGGGACTGGGCCCCCCTAGATCCCACCCCCGGACCCCCAGCA
TCCCCCAACCCCTTCGTGCATGAGTTACATCTCTCTCGCCTCCAGAGGGTTAAGTTCTGC
CTCCTGGGGGCATTGCTGGCCCCCATCCGAGTGCTTCTGGCCTTTATCGTCCTCTTTCTC
CTCTGGCCCTTTGCCTGGCTTCAAGTGGCCGGTCTTAGTGAGGAGCAGCTTCAGGAGCCA
ATTACAGGATGGAGGAAGACTGTGTGCCACAACGGGGTGCTAGGCCTGAGCCGCCTGCTG
TTTTTCCTGCTGGGCTTCCTCCGGATTCGCGTTCGTGGCCAGCGAGCCTCTCGCCTTCAA
GCCCCTGTCCTTGTTGCTGCCCCACACTCCACTTTCTTTGACCCCATTGTTCTGCTGCCC
TGTGACCTGCCCAAAGTTGTGTCCCGAGCTGAGAACCTTTCCGTTCCTGTCATTGGAGCC
CTTCTTCGATTCAACCAAGCCATCCTGGTATCCCGGCATGACCCGGCTTCTCGACGCAGA
GTGGTGGAGGAGGTCCGAAGGCGGGCCACCTCAGGAGGCAAGTGGCCGCAGGTGCTATTC
TTTCCTGAGGGCACCTGTTCCAACAAGAAGGCTTTGCTTAAGTTCAAACCAGGAGCCTTC
ATCGCAGGGGTGCCTGTGCAGCCTGTCCTCATCCGCTACCCCAACAGTCTGGACACCACC
AGCTGGGCATGGAGGGGTCCTGGAGTACTCAAAGTCCTCTGGCTCACAGCCTCTCAGCCC
TGCAGCATTGTGGATGTGGAGTTCCTTCCTGTGTATCACCCCAGCCCTGAGGAGAGCAGG
GACCCCACCCTCTATGCCAACAATGTTCAGAGGGTCATGGCACAGGCTCTGGGCATTCCA
GCCACCGAATGTGAGTTTGTAGGGAGCTTACCTGTGATTGTGGTGGGCCGGCTGAAGGTG
GCGTTGGAACCACAGCTCTGGGAACTGGGAAAAGTGCTTCGGAAGGCTGGGCTGTCCGCT
GGCTATGTGGACGCTGGGGCAGAGCCAGGCCGGAGTCGAATGATCAGCCAGGAAGAGTTT
GCCAGGCAGCTACAGCTCTCTGATCCTCAGACGGTGGCTGGTGCCTTTGGCTACTTCCAG
CAGGATACCAAGGGTTTGGTGGACTTCCGAGATGTGGCCCTTGCACTAGCAGCTCTGGAT
GGGGGCAGGAGCCTGGAAGAGCTAACTCGTCTGGCCTTTGAGCTCTTTGCTGAAGAGCAA
GCAGAGGGTCCCAACCGCCTGCTGTACAAAGACGGCTTCAGCACCATCCTGCACCTGCTG
CTGGGTTCACCCCACCCTGCTGCCACAGCTTTGCATGCTGAGCTGTGCCAGGCAGGATCC
AGCCAAGGCCTCTCCCTCTGTCAGTTCCAGAACTTCTCCCTCCATGACCCACTCTATGGG
AAACTCTTCAGCACCTACCTGCGCCCCCCACACACCTCTCGAGGCACCTCCCAGACACCA
AATGCCTCATCCCCAGGCAACCCCACTGCTCTGGCCAATGGGACTGTGCAAGCACCCAAG
CAGAAGGGAGACTGA
|
| Enzyme 111 GenBank Gene ID |
NM_153613.2  |
| Enzyme 111 GeneCard ID |
LPCAT4  |
| Enzyme 111 GenAtlas ID |
LPCAT4  |
| Enzyme 111 HGNC ID |
HGNC:30059  |
| Enzyme 111 Chromosome Location |
1 |
| Enzyme 111 Locus |
15q14 |
| Enzyme 111 SNPs |
SNPJam Report  |
| Enzyme 111 General References |
- Ye GM, Chen C, Huang S, Han DD, Guo JH, Wan B, Yu L: Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7. DNA Seq. 2005 Oct;16(5):386-90. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cao J, Shan D, Revett T, Li D, Wu L, Liu W, Tobin JF, Gimeno RE: Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2. J Biol Chem. 2008 Jul 4;283(27):19049-57. Epub 2008 May 5. [PubMed
]
|
| Enzyme 111 Metabolite References |
Not Available |
|
Enzyme 112
[top]
|
| Enzyme 112 ID |
12936 |
| Enzyme 112 Name |
Glycerol-3-phosphate acyltransferase 3 |
| Enzyme 112 Synonyms |
- GPAT-3
- 1-acylglycerol-3-phosphate O-acyltransferase 9
- 1-AGP acyltransferase 9
- 1-AGPAT 9
- Acyl-CoA:glycerol-3-phosphate acyltransferase 3
- hGPAT3
- Lung cancer metastasis-associated protein 1
- Lysophosphatidic acid acyltransferase theta
- LPAAT-theta
- MAG-1
|
| Enzyme 112 Gene Name |
AGPAT9 |
| Enzyme 112 Protein Sequence |
>Glycerol-3-phosphate acyltransferase 3
MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKE
SILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEE
LVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQ
LPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTT
DGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILI
FPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSW
AIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQ
KNYSKMIVGNGSLS
|
| Enzyme 112 Number of Residues |
434 |
| Enzyme 112 Molecular Weight |
48704.8 |
| Enzyme 112 Theoretical pI |
9.15 |
| Enzyme 112 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 112 General Function |
Involved in acyltransferase activity |
| Enzyme 112 Specific Function |
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Overexpression activates the mTOR pathway |
| Enzyme 112 Pathways |
|
| Enzyme 112 Reactions |
- acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
|
| Enzyme 112 Pfam Domain Function |
|
| Enzyme 112 Signals |
|
| Enzyme 112 Transmembrane Regions |
|
| Enzyme 112 Essentiality |
Not Available |
| Enzyme 112 GenBank ID Protein |
21362092  |
| Enzyme 112 UniProtKB/Swiss-Prot ID |
Q53EU6  |
| Enzyme 112 UniProtKB/Swiss-Prot Entry Name |
GPAT3_HUMAN  |
| Enzyme 112 PDB ID |
Not Available |
| Enzyme 112 Cellular Location |
Not Available |
| Enzyme 112 Gene Sequence |
>1305 bp
ATGGAGGGCGCAGAGCTGGCCGGGAAGATCCTTTCCACCTGGCTGACGCTGGTTCTCGGC
TTCATCCTTTTACCTTCGGTCTTCGGAGTGTCTCTGGGCATCTCCGAGATCTACATGAAG
ATCCTAGTGAAAACTTTAGAGTGGGCCACAATACGAATTGAAAAAGGAACCCCAAAGGAG
TCGATTCTTAAAAACTCTGCTTCTGTTGGTATTATCCAAAGAGATGAGTCACCCATGGAA
AAAGGGCTCTCTGGTCTACGAGGAAGGGACTTTGAGCTGTCTGACGTGTTTTATTTCTCC
AAGAAGGGATTGGAAGCCATTGTAGAAGATGAAGTGACCCAGAGGTTTTCCTCAGAGGAG
CTAGTGTCATGGAATCTCCTCACAAGAACCAATGTAAATTTCCAGTACATCAGTCTGCGG
CTCACTATGGTGTGGGTGCTGGGCGTCATAGTGCGCTATTGTGTCCTACTGCCTCTGAGG
GTTACCTTGGCTTTCATTGGGATCAGTTTGCTGGTTATAGGAACTACACTGGTTGGGCAG
CTGCCAGACAGCAGCCTCAAAAACTGGCTGAGTGAACTGGTCCATCTGACTTGCTGCCGG
ATCTGTGTGCGAGCCCTCTCTGGTACCATTCATTATCATAACAAGCAGTACAGACCCCAG
AAGGGAGGCATTTGTGTTGCCAACCATACTTCCCCCATTGATGTTTTAATCTTGACAACG
GATGGATGTTATGCTATGGTTGGCCAGGTTCATGGCGGCTTGATGGGAATTATTCAGAGA
GCTATGGTCAAGGCTTGTCCTCATGTCTGGTTTGAACGCTCAGAAATGAAGGATCGACAC
CTGGTTACTAAGAGACTAAAAGAACATATTGCTGATAAGAAGAAACTACCCATACTAATT
TTTCCTGAAGGAACTTGCATCAACAATACTTCAGTCATGATGTTTAAAAAGGGGAGCTTT
GAAATTGGAGGAACCATACATCCAGTTGCAATTAAGTATAACCCTCAGTTCGGTGATGCA
TTTTGGAACAGTAGTAAATACAACATGGTGAGCTACCTGCTTCGAATGATGACCAGCTGG
GCCATCGTCTGTGACGTGTGGTACATGCCCCCCATGACCAGAGAGGAAGGAGAAGATGCA
GTCCAGTTTGCTAACAGGGTTAAGTCTGCTATTGCTATACAAGGAGGCCTGACTGAACTT
CCCTGGGATGGAGGACTAAAGAGAGCAAAGGTGAAGGACATCTTTAAGGAAGAGCAGCAG
AAAAATTACAGCAAGATGATTGTGGGCAATGGATCTCTCAGCTAA
|
| Enzyme 112 GenBank Gene ID |
NM_032717.3  |
| Enzyme 112 GeneCard ID |
AGPAT9  |
| Enzyme 112 GenAtlas ID |
AGPAT9  |
| Enzyme 112 HGNC ID |
HGNC:28157  |
| Enzyme 112 Chromosome Location |
4 |
| Enzyme 112 Locus |
4q21.23 |
| Enzyme 112 SNPs |
SNPJam Report  |
| Enzyme 112 General References |
- Tang W, Yuan J, Chen X, Gu X, Luo K, Li J, Wan B, Wang Y, Yu L: Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway. J Biochem Mol Biol. 2006 Sep 30;39(5):626-35. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed
]
- Cao J, Li JL, Li D, Tobin JF, Gimeno RE: Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis. Proc Natl Acad Sci U S A. 2006 Dec 26;103(52):19695-700. Epub 2006 Dec 14. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 112 Metabolite References |
Not Available |
|
Enzyme 113
[top]
|
| Enzyme 113 ID |
12971 |
| Enzyme 113 Name |
Glycine N-acyltransferase |
| Enzyme 113 Synonyms |
- Acyl-CoA:glycine N-acyltransferase
- AAc
- Aralkyl acyl-CoA N-acyltransferase
- Aralkyl acyl-CoA:amino acid N-acyltransferase
- HRP-1(CLP)
|
| Enzyme 113 Gene Name |
GLYAT |
| Enzyme 113 Protein Sequence |
>Glycine N-acyltransferase
MMLPLQGAQMLQMLEKSLRKSLPASLKVYGTVFHINHGNPFNLKAVVDKWPDFNTVVVCP
QEQDMTDDLDHYTNTYQIYSKDPQNCQEFLGSPELINWKQHLQIQSSQPSLNEAIQNLAA
IKSFKVKQTQRILYMAAETAKELTPFLLKSKILSPSGGKPKAINQEMFKLSSMDVTHAHL
VNKFWHFGGNERSQRFIERCIQTFPTCCLLGPEGTPVCWDLMDQTGEMRMAGTLPEYRLH
GLVTYVIYSHAQKLGKLGFPVYSHVDYSNEAMQKMSYTLQHVPIPRSWNQWNCVPL
|
| Enzyme 113 Number of Residues |
296 |
| Enzyme 113 Molecular Weight |
33897.0 |
| Enzyme 113 Theoretical pI |
8.28 |
| Enzyme 113 GO Classification |
| Function |
- N-acyltransferase activity
- acyltransferase activity
- catalytic activity
- glycine N-acyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 113 General Function |
Involved in glycine N-acyltransferase activity |
| Enzyme 113 Specific Function |
Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines |
| Enzyme 113 Pathways |
Not Available |
| Enzyme 113 Reactions |
- acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
|
| Enzyme 113 Pfam Domain Function |
|
| Enzyme 113 Signals |
|
| Enzyme 113 Transmembrane Regions |
|
| Enzyme 113 Essentiality |
Not Available |
| Enzyme 113 GenBank ID Protein |
111038137  |
| Enzyme 113 UniProtKB/Swiss-Prot ID |
Q6IB77  |
| Enzyme 113 UniProtKB/Swiss-Prot Entry Name |
GLYAT_HUMAN  |
| Enzyme 113 PDB ID |
Not Available |
| Enzyme 113 Cellular Location |
Not Available |
| Enzyme 113 Gene Sequence |
>891 bp
ATGATGTTACCATTGCAAGGTGCCCAGATGCTGCAGATGCTGGAGAAATCCTTGAGGAAG
AGCCTCCCAGCATCCTTAAAGGTTTATGGAACTGTCTTTCACATAAACCATGGAAATCCA
TTCAATCTGAAGGCTGTGGTGGACAAGTGGCCTGATTTTAATACAGTGGTTGTCTGCCCT
CAGGAGCAGGATATGACAGATGACCTTGATCACTATACCAATACTTACCAAATCTACTCC
AAAGATCCCCAAAACTGTCAGGAATTCCTTGGATCACCAGAACTCATCAACTGGAAACAG
CATTTACAGATTCAAAGTTCACAGCCTAGCCTGAATGAGGCTATACAAAATCTTGCAGCC
ATTAAGTCCTTCAAAGTCAAACAAACACAACGCATTCTCTATATGGCAGCTGAAACAGCC
AAGGAACTGACTCCTTTCCTGCTGAAATCAAAGATTTTATCTCCCAATGGTGGCAAACCC
AAGGCCATCAACCAAGAGATGTTTAAACTCTCATCCATGGATGTTACCCATGCTCACTTG
GTGAATAAATTCTGGCATTTTGGTGGTAATGAGAGGAGCCAGAGATTCATTGAGCGCTGC
ATTCAGACCTTTCCCACCTGCTGTCTCCTGGGGCCTGAGGGGACCCCTGTGTGCTGGGAT
CTAATGGACCAGACTGGAGAGATGAGAATGGCAGGCACCTTGCCGGAATACCGGCTCCAT
GGCCTTGTGACGTATGTCATCTATTCCCACGCCCAGAAATTGGGCAAACTTGGGTTTCCT
GTCTATTCTCATGTAGACTACAGCAATGAAGCTATGCAAAAAATGAGTTACACACTGCAA
CATGTTCCCATTCCCAGAAGCTGGAACCAGTGGAACTGTGTACCTCTGTGA
|
| Enzyme 113 GenBank Gene ID |
NM_201648.2  |
| Enzyme 113 GeneCard ID |
GLYAT  |
| Enzyme 113 GenAtlas ID |
GLYAT  |
| Enzyme 113 HGNC ID |
HGNC:13734  |
| Enzyme 113 Chromosome Location |
1 |
| Enzyme 113 Locus |
11q12.1 |
| Enzyme 113 SNPs |
SNPJam Report  |
| Enzyme 113 General References |
- van der Westhuizen FH, Pretorius PJ, Erasmus E: The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase. J Biochem Mol Toxicol. 2000;14(2):102-9. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mawal YR, Qureshi IA: Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver. Biochem Biophys Res Commun. 1994 Dec 15;205(2):1373-9. [PubMed
]
|
| Enzyme 113 Metabolite References |
Not Available |
|
Enzyme 114
[top]
|
| Enzyme 114 ID |
12972 |
| Enzyme 114 Name |
Glycine N-acyltransferase-like protein 1 |
| Enzyme 114 Synonyms |
- Acyl-CoA:glycine N-acyltransferase-like protein 1
|
| Enzyme 114 Gene Name |
GLYATL1 |
| Enzyme 114 Protein Sequence |
>Glycine N-acyltransferase-like protein 1
MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQ
KQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFS
KSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSG
LVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRR
TGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLV
PF
|
| Enzyme 114 Number of Residues |
302 |
| Enzyme 114 Molecular Weight |
35100.9 |
| Enzyme 114 Theoretical pI |
6.86 |
| Enzyme 114 GO Classification |
| Function |
- N-acyltransferase activity
- acyltransferase activity
- catalytic activity
- glycine N-acyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 114 General Function |
Involved in glycine N-acyltransferase activity |
| Enzyme 114 Specific Function |
Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines |
| Enzyme 114 Pathways |
Not Available |
| Enzyme 114 Reactions |
- acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
|
| Enzyme 114 Pfam Domain Function |
|
| Enzyme 114 Signals |
|
| Enzyme 114 Transmembrane Regions |
|
| Enzyme 114 Essentiality |
Not Available |
| Enzyme 114 GenBank ID Protein |
Not Available |
| Enzyme 114 UniProtKB/Swiss-Prot ID |
Q969I3  |
| Enzyme 114 UniProtKB/Swiss-Prot Entry Name |
GLYL1_HUMAN  |
| Enzyme 114 PDB ID |
Not Available |
| Enzyme 114 Cellular Location |
Not Available |
| Enzyme 114 Gene Sequence |
>909 bp
ATGATCCTACTGAATAACTCCCATAAGCTGCTGGCCCTATACAAATCCTTGGCCAGGAGC
ATCCCTGAGTCCCTGAAGGTGTATGGCTCTGTGTATCACATCAATCACGGGAACCCCTTC
AACATGGAGGTGCTGGTGGATTCCTGGCCTGAATATCAGATGGTTATTATCCGGCCTCAA
AAGCAGGAGATGACTGATGACATGGATTCATACACAAACGTATATCGTATGTTCTCCAAA
GAGCCTCAAAAATCAGAAGAAGTTTTGAAAAATTGTGAGATCGTAAACTGGAAACAGAGA
CTCCAAATCCAAGGTCTTCAAGAAAGTTTAGGTGAGGGGATAAGAGTGGCTACATTTTCA
AAGTCAGTGAAAGTAGAGCATTCGAGAGCACTCCTCTTGGTTACGGAAGATATTCTGAAG
CTCAATGCCTCCAGTAAAAGCAAGCTTGGAAGCTGGGCTGAGACAGGCCACCCAGATGAT
GAATTTGAAAGTGAAACTCCCAACTTTAAGTATGCCCAGCTGGATGTCTCTTATTCTGGG
CTGGTAAATGACAACTGGAAGCGAGGGAAGAATGAGAGGAGCCTGCATTACATCAAGCGC
TGCATAGAAGACCTGCCAGCAGCCTGTATGCTCGGCCCAGAGGGAGTCCCGGTCTCATGG
GTAACCATGGACCCTTCTTGTGAAGTAGGAATGGCCTACAGCATGGAAAAATACCGAAGG
ACAGGCAACATGGCACGAGTGATGGTGCGATACATGAAATATCTGCGTCAGAAGAATATT
CCATTTTACATCTCTGTGTTGGAAGAAAATGAAGACTCCCGCAGATTTGTGGGGCAGTTT
GGTTTCTTTGAGGCCTCCTGTGAGTGGCACCAATGGACTTGCTACCCACAGAATCTAGTT
CCATTTTAG
|
| Enzyme 114 GenBank Gene ID |
DQ084381  |
| Enzyme 114 GeneCard ID |
GLYATL1  |
| Enzyme 114 GenAtlas ID |
GLYATL1  |
| Enzyme 114 HGNC ID |
HGNC:30519  |
| Enzyme 114 Chromosome Location |
1 |
| Enzyme 114 Locus |
11q12.1 |
| Enzyme 114 SNPs |
SNPJam Report  |
| Enzyme 114 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 114 Metabolite References |
Not Available |
|
Enzyme 115
[top]
|
| Enzyme 115 ID |
12973 |
| Enzyme 115 Name |
Glycine N-acyltransferase-like protein 2 |
| Enzyme 115 Synonyms |
- Acyl-CoA:glycine N-acyltransferase-like protein 2
|
| Enzyme 115 Gene Name |
GLYATL2 |
| Enzyme 115 Protein Sequence |
>Glycine N-acyltransferase-like protein 2
MLVLHNSQKLQILYKSLEKSIPESIKVYGAIFNIKDKNPFNMEVLVDAWPDYQIVITRPQ
KQEMKDDQDHYTNTYHIFTKAPDKLEEVLSYSNVISWEQTLQIQGCQEGLDEAIRKVATS
KSVQVDYMKTILFIPELPKKHKTSSNDKMELFEVDDDNKEGNFSNMFLDASHAGLVNEHW
AFGKNERSLKYIERCLQDFLGFGVLGPEGQLVSWIVMEQSCELRMGYTVPKYRHQGNMLQ
IGYHLEKYLSQKEIPFYFHVADNNEKSLQALNNLGFKICPCGWHQWKCTPKKYC
|
| Enzyme 115 Number of Residues |
294 |
| Enzyme 115 Molecular Weight |
34277.1 |
| Enzyme 115 Theoretical pI |
6.67 |
| Enzyme 115 GO Classification |
| Function |
- N-acyltransferase activity
- acyltransferase activity
- catalytic activity
- glycine N-acyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 115 General Function |
Involved in glycine N-acyltransferase activity |
| Enzyme 115 Specific Function |
Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines |
| Enzyme 115 Pathways |
Not Available |
| Enzyme 115 Reactions |
- acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
|
| Enzyme 115 Pfam Domain Function |
|
| Enzyme 115 Signals |
|
| Enzyme 115 Transmembrane Regions |
|
| Enzyme 115 Essentiality |
Not Available |
| Enzyme 115 GenBank ID Protein |
29243559  |
| Enzyme 115 UniProtKB/Swiss-Prot ID |
Q8WU03  |
| Enzyme 115 UniProtKB/Swiss-Prot Entry Name |
GLYL2_HUMAN  |
| Enzyme 115 PDB ID |
Not Available |
| Enzyme 115 Cellular Location |
Not Available |
| Enzyme 115 Gene Sequence |
>885 bp
ATGCTTGTGCTTCATAACTCTCAGAAGCTGCAGATTCTGTATAAATCCTTAGAAAAGAGC
ATCCCTGAATCCATAAAGGTATATGGCGCCATTTTCAACATAAAAGATAAAAACCCTTTC
AACATGGAGGTGCTGGTAGATGCCTGGCCAGATTACCAGATCGTCATTACCCGGCCTCAG
AAACAGGAGATGAAAGATGACCAGGATCATTATACCAACACTTACCACATCTTCACCAAA
GCTCCTGACAAATTAGAGGAAGTCCTGTCATACTCCAATGTAATCAGCTGGGAGCAAACT
TTGCAGATCCAAGGTTGCCAAGAGGGCTTGGATGAAGCAATAAGAAAGGTTGCAACTTCA
AAATCAGTGCAGGTAGATTACATGAAAACCATCCTCTTTATACCGGAATTACCAAAGAAA
CACAAGACCTCAAGTAATGACAAGATGGAGTTATTTGAAGTGGATGATGATAACAAGAAA
GGAAACTTTTCAAACATGTTCTTAGATGCTTCACATGCAGGTCTTGTGAATGAACACTGG
GCCTTTGGGAAAAATGAGAGGAGCTTGAAATATATTGAACGCTGCCTCCAGGATTTTCTA
GGATTTGGCGTGCTGGGTCCAGAGGGCCAGCTTGTCTCTTGGATTGTGATGGAACGGTCC
TGTGAGTTGAGAATGGGTTATACTGTCCCCAAATACAGACACCAAGGCAACATGTTGCAA
ATTGGTTACCATCTTGAAAAGTATCTTTCTCAGAAAGAAATCCCATTTTATTTCCATGTG
GCAGATAATAATGAGAAAAGCCTACAGGCACTGAACAATTTGGGGTTTAAGATTTGTCCC
TGTGGCTGGCATCAGTGGAAATGCACCCCCAAGAAATGTTGTTGA
|
| Enzyme 115 GenBank Gene ID |
AF426250  |
| Enzyme 115 GeneCard ID |
GLYATL2  |
| Enzyme 115 GenAtlas ID |
GLYATL2  |
| Enzyme 115 HGNC ID |
HGNC:24178  |
| Enzyme 115 Chromosome Location |
1 |
| Enzyme 115 Locus |
11q12.1 |
| Enzyme 115 SNPs |
SNPJam Report  |
| Enzyme 115 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 115 Metabolite References |
Not Available |
|
Enzyme 116
[top]
|
| Enzyme 116 ID |
12978 |
| Enzyme 116 Name |
Dihydrolipoamide S-acetyltransferase |
| Enzyme 116 Synonyms |
- SubName: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex mitochondrial
- SubName: cDNA FLJ32737 fis, clone TESTI2001269, highly similar to Homo sapiens dihydrolipoamide S-acetyltransferase, mRNA
|
| Enzyme 116 Gene Name |
DLAT |
| Enzyme 116 Protein Sequence |
>Dihydrolipoamide S-acetyltransferase
MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCG
WTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKIN
EGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYT
LDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEK
KVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADI
SAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPL
AKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVF
TDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFI
IKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIAND
VVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPA
DNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL
|
| Enzyme 116 Number of Residues |
647 |
| Enzyme 116 Molecular Weight |
68996.0 |
| Enzyme 116 Theoretical pI |
7.94 |
| Enzyme 116 GO Classification |
| Function |
- S-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- dihydrolipoyllysine-residue acetyltransferase activity
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
- pyruvate metabolic process
|
| Component |
- macromolecular complex
- protein complex
- pyruvate dehydrogenase complex
|
|
| Enzyme 116 General Function |
Involved in acyltransferase activity |
| Enzyme 116 Specific Function |
Not Available |
| Enzyme 116 Pathways |
Not Available |
| Enzyme 116 Reactions |
Not Available |
| Enzyme 116 Pfam Domain Function |
|
| Enzyme 116 Signals |
|
| Enzyme 116 Transmembrane Regions |
|
| Enzyme 116 Essentiality |
Not Available |
| Enzyme 116 GenBank ID Protein |
193787077  |
| Enzyme 116 UniProtKB/Swiss-Prot ID |
Q86YI5  |
| Enzyme 116 UniProtKB/Swiss-Prot Entry Name |
Q86YI5_HUMAN  |
| Enzyme 116 PDB ID |
1FYC  |
| Enzyme 116 PDB File |
Show |
| Enzyme 116 3D Structure |
|
| Enzyme 116 Cellular Location |
Not Available |
| Enzyme 116 Gene Sequence |
>1944 bp
ATGTGGCGCGTCTGTGCGCGACGGGCTCAGAATGTAGCCCCATGGGCGGGACTCGAGGCT
CGGTGGACGGCCTTGCAGGAGGTACCCGGAACTCCACGAGTGACCTCGCGATCTGGCCCG
GCTCCCGCTCGTCGCAACAGCGTGACTACAGGGTATGGCGGGGTCCGGGCACTGTGCGGC
TGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGCTTACTGCTGCAGCTTTTGGGGTCG
CCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAGAAGGTTCCATTGCCTTCTCTTTCC
CCCACAATGCAGGCAGGCACCATAGCCCGTTGGGAAAAAAAAGAGGGGGACAAAATCAAT
GAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAAGCCACTGTTGGATTTGAGAGCCTG
GAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAAGGTACCAGGGATGTTCCCATCGGA
GCGATCATCTGTATCACAGTTGGCAAGCCTGAGGATATTGAGGCCTTTAAAAATTATACA
CTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCCCCAGCACCAACCCCTGCTGCCACT
GCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGTAGCTCATATCCCCCTCACATGCAG
GTACTTCTTCCTGCCCTCTCTCCCACCATGACCATGGGCACAGTTCAGAGATGGGAAAAA
AAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTGGCAGAGATAGAAACTGACAAAGCC
ACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTGGCAAAAATCCTGGTCCCTGAAGGC
ACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATCATTGTAGAAAAAGAGGCAGATATA
TCAGCATTTGCTGACTATAGGCCAACCGAAGTAACAGATTTAAAACCACAAGTGCCACCA
CCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACTCCCCAGCCTTTAGCTCCTACACCT
TCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAGGGAAGGGTGTTTGTTAGCCCTCTT
GCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTTACACAAGTAAAAGGGACAGGACCA
GATGGTAGAATCACCAAGAAGGATATCGACTCTTTTGTGCCTAGTAAAGTTGCTCCTGCT
CCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATGGCACCAGTTCCTACAGGTGTCTTC
ACAGATATCCCAATCAGCAACATTCGTCGGGTTATTGCACAGCGATTAATGCAATCAAAG
CAAACCATACCTCATTATTACCTTTCTATCGATGTAAATATGGGAGAAGTTTTGTTGGTA
CGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGCAAAATTTCTGTCAATGACTTCATC
ATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCCGAAGCAAATTCTTCTTGGATGGAC
ACAGTTATAAGACAAAATCATGTTGTTGATGTCAGTGTTGCGGTCAGTACTCCTGCAGGA
CTCATCACACCTATTGTGTTTAATGCACATATAAAAGGAGTGGAAACCATTGCTAATGAT
GTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAACTACAGCCACATGAATTCCAGGGT
GGCACTTTTACGATCTCCAATTTAGGAATGTTTGGAATTAAGAATTTCTCTGCTATTATT
AACCCACCTCAAGCATGTATTTTGGCAATTGGTGCTTCAGAGGATAAACTGGTCCCTGCA
GATAATGAAAAAGGGTTTGATGTGGCTAGCATGATGTCTGTTACACTCAGTTGTGATCAC
CGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTTGCTGAGTTTAGAAAGTACCTTGAA
AAACCTATCACTATGTTGTTGTAA
|
| Enzyme 116 GenBank Gene ID |
AK057299  |
| Enzyme 116 GeneCard ID |
DLAT  |
| Enzyme 116 GenAtlas ID |
DLAT  |
| Enzyme 116 HGNC ID |
HGNC:2896  |
| Enzyme 116 Chromosome Location |
1 |
| Enzyme 116 Locus |
11q23.1 |
| Enzyme 116 SNPs |
SNPJam Report  |
| Enzyme 116 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 116 Metabolite References |
Not Available |
|
Enzyme 117
[top]
|
| Enzyme 117 ID |
13014 |
| Enzyme 117 Name |
Arylamine N-acetyltransferase 2 |
| Enzyme 117 Synonyms |
Not Available |
| Enzyme 117 Gene Name |
NAT2 |
| Enzyme 117 Protein Sequence |
>Arylamine N-acetyltransferase 2
MDIEAYFERIGYKNSRNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIV
RRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYI
VDAGSGSSSQMWQPLELISGKDQPQVPCIFCLTEERGIWYLDQIRREQYITNKEFLNSHL
LPKKKHQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILT
YRKFNYKDNTDLVEFKTLTEEEVEEVLRNIFKISLGRNLVPKPGDGSLTI
|
| Enzyme 117 Number of Residues |
290 |
| Enzyme 117 Molecular Weight |
33570.2 |
| Enzyme 117 Theoretical pI |
5.67 |
| Enzyme 117 GO Classification |
| Function |
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 117 General Function |
Involved in acetyltransferase activity |
| Enzyme 117 Specific Function |
Not Available |
| Enzyme 117 Pathways |
Not Available |
| Enzyme 117 Reactions |
Not Available |
| Enzyme 117 Pfam Domain Function |
|
| Enzyme 117 Signals |
|
| Enzyme 117 Transmembrane Regions |
|
| Enzyme 117 Essentiality |
Not Available |
| Enzyme 117 GenBank ID Protein |
93211523  |
| Enzyme 117 UniProtKB/Swiss-Prot ID |
A4Z6T7  |
| Enzyme 117 UniProtKB/Swiss-Prot Entry Name |
A4Z6T7_HUMAN  |
| Enzyme 117 PDB ID |
Not Available |
| Enzyme 117 Cellular Location |
Not Available |
| Enzyme 117 Gene Sequence |
>873 bp
ATGGACATTGAAGCATATTTTGAAAGAATTGGCTATAAGAACTCTAGGAACAAATTGGAC
TTGGAAACATTAACTGACATTCTTGAGCACCAGATCCGGGCTGTTCCCTTTGAGAACCTT
AACATGCATTGTGGGCAAGCCATGGAGTTGGGCTTAGAGGCTATTTTTGATCACATTGTA
AGAAGAAACCGGGGTGGGTGGTGTCTCCAGGTCAATCAACTTCTGTACTGGGCTCTGACC
ACAATCGGTTTTCAGACCACAATGTTAGGAGGGTATTTTTATATCCCTCCAGTTAACAAA
TACAGCACTGGCATGGTTCACCTTCTCCTGCAGGTGACCATTGACGGCAGGAATTACATT
GTCGATGCTGGGTCTGGAAGCTCCTCCCAGATGTGGCAGCCTCTAGAATTAATTTCTGGG
AAGGATCAGCCTCAGGTGCCTTGCATTTTCTGCTTGACAGAAGAGAGAGGAATCTGGTAC
CTGGACCAAATCAGGAGAGAGCAGTATATTACAAACAAAGAATTTCTTAATTCTCATCTC
CTGCCAAAGAAGAAACACCAAAAAATATACTTATTTACGCTTGAACCTCGAACAATTGAA
GATTTTGAGTCTATGAATACATACCTGCAGACGTCTCCAACATCTTCATTTATAACCACA
TCATTTTGTTCCTTGCAGACCCCAGAAGGGGTTTACTGTTTGGTGGGCTTCATCCTCACC
TATAGAAAATTCAATTATAAAGACAATACAGATCTGGTCGAGTTTAAAACTCTCACTGAG
GAAGAGGTTGAAGAAGTGCTGAGAAATATATTTAAGATTTCCTTGGGGAGAAATCTCGTG
CCCAAACCTGGTGATGGATCCCTTACTATTTAG
|
| Enzyme 117 GenBank Gene ID |
DQ472738  |
| Enzyme 117 GeneCard ID |
NAT2  |
| Enzyme 117 GenAtlas ID |
NAT2  |
| Enzyme 117 HGNC ID |
HGNC:7646  |
| Enzyme 117 Chromosome Location |
8 |
| Enzyme 117 Locus |
8p22 |
| Enzyme 117 SNPs |
SNPJam Report  |
| Enzyme 117 General References |
- Sabbagh A, Langaney A, Darlu P, Gerard N, Krishnamoorthy R, Poloni ES: Worldwide distribution of NAT2 diversity: implications for NAT2 evolutionary history. BMC Genet. 2008 Feb 27;9:21. [PubMed
]
|
| Enzyme 117 Metabolite References |
Not Available |
|
Enzyme 118
[top]
|
| Enzyme 118 ID |
13020 |
| Enzyme 118 Name |
Putative uncharacterized protein |
| Enzyme 118 Synonyms |
Not Available |
| Enzyme 118 Gene Name |
ACAT1 |
| Enzyme 118 Protein Sequence |
>Putative uncharacterized protein
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLS
LLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCT
TINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIV
KDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTV
TVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADA
AKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVV
LANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGAS
AMLIQKL
|
| Enzyme 118 Number of Residues |
427 |
| Enzyme 118 Molecular Weight |
45200 |
| Enzyme 118 Theoretical pI |
Not Available |
| Enzyme 118 GO Classification |
Not Available |
| Enzyme 118 General Function |
Not Available |
| Enzyme 118 Specific Function |
Not Available |
| Enzyme 118 Pathways |
Not Available |
| Enzyme 118 Reactions |
Not Available |
| Enzyme 118 Pfam Domain Function |
Not Available |
| Enzyme 118 Signals |
|
| Enzyme 118 Transmembrane Regions |
|
| Enzyme 118 Essentiality |
Not Available |
| Enzyme 118 GenBank ID Protein |
Not Available |
| Enzyme 118 UniProtKB/Swiss-Prot ID |
B2R6H1  |
| Enzyme 118 UniProtKB/Swiss-Prot Entry Name |
B2R6H1_HUMAN  |
| Enzyme 118 PDB ID |
Not Available |
| Enzyme 118 Cellular Location |
Not Available |
| Enzyme 118 Gene Sequence |
Not Available |
| Enzyme 118 GenBank Gene ID |
Not Available |
| Enzyme 118 GeneCard ID |
B2R6H1  |
| Enzyme 118 GenAtlas ID |
Not Available |
| Enzyme 118 HGNC ID |
Not Available |
| Enzyme 118 Chromosome Location |
Not Available |
| Enzyme 118 Locus |
Not Available |
| Enzyme 118 SNPs |
SNPJam Report  |
| Enzyme 118 General References |
Not Available |
| Enzyme 118 Metabolite References |
Not Available |
|
Enzyme 119
[top]
|
| Enzyme 119 ID |
13026 |
| Enzyme 119 Name |
Peroxisomal 3,2-trans-enoyl-CoA isomerase |
| Enzyme 119 Synonyms |
- pECI
- DRS-1
- Delta(3),delta(2)-enoyl-CoA isomerase
- D3,D2-enoyl-CoA isomerase
- Diazepam-binding inhibitor-related protein 1
- DBI-related protein 1
- Dodecenoyl-CoA isomerase
- Hepatocellular carcinoma-associated antigen 88
- Renal carcinoma antigen NY-REN-1
|
| Enzyme 119 Gene Name |
PECI |
| Enzyme 119 Protein Sequence |
>Peroxisomal 3,2-trans-enoyl-CoA isomerase
MAMAYLAWRLARRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNE
VKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSP
SLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAAS
KDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIA
VVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEML
IFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNALRISKEVIRKREREKL
HAVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
|
| Enzyme 119 Number of Residues |
394 |
| Enzyme 119 Molecular Weight |
43584.8 |
| Enzyme 119 Theoretical pI |
9.42 |
| Enzyme 119 GO Classification |
| Function |
- acyl-CoA binding
- binding
- catalytic activity
- fatty acid binding
- lipid binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 119 General Function |
Involved in acyl-CoA binding |
| Enzyme 119 Specific Function |
Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates |
| Enzyme 119 Pathways |
|
| Enzyme 119 Reactions |
- (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA [RN:R04100]
|
| Enzyme 119 Pfam Domain Function |
|
| Enzyme 119 Signals |
|
| Enzyme 119 Transmembrane Regions |
|
| Enzyme 119 Essentiality |
Not Available |
| Enzyme 119 GenBank ID Protein |
260274832  |
| Enzyme 119 UniProtKB/Swiss-Prot ID |
O75521  |
| Enzyme 119 UniProtKB/Swiss-Prot Entry Name |
PECI_HUMAN  |
| Enzyme 119 PDB ID |
Not Available |
| Enzyme 119 Cellular Location |
Not Available |
| Enzyme 119 Gene Sequence |
>1185 bp
ATGGCGATGGCGTACTTGGCTTGGAGACTGGCGCGGCGTTCGTGTCCGAGTTCTCTGCAG
GTCACTAGTTTCCCGGTAGTTCAGCTGCACATGAATAGAACAGCAATGAGAGCCAGTCAG
AAGGACTTTGAAAATTCAATGAATCAAGTGAAACTCTTGAAAAAGGATCCAGGAAACGAA
GTGAAGCTAAAACTCTACGCGCTATATAAGCAGGCCACTGAAGGACCTTGTAACATGCCC
AAACCAGGTGTATTTGACTTGATCAACAAGGCCAAATGGGACGCATGGAATGCCCTTGGC
AGCCTGCCCAAGGAAGCTGCCAGGCAGAACTATGTGGATTTGGTGTCCAGTTTGAGTCCT
TCATTGGAATCCTCTAGTCAGGTGGAGCCTGGAACAGACAGGAAATCAACTGGGTTTGAA
ACTCTGGTGGTGACCTCCGAAGATGGCATCACAAAGATCATGTTCAACCGGCCCAAAAAG
AAAAATGCCATAAACACTGAGATGTATCATGAAATTATGCGTGCACTTAAAGCTGCCAGC
AAGGATGACTCAATCATCACTGTTTTAACAGGAAATGGTGACTATTACAGTAGTGGGAAT
GATCTGACTAACTTCACTGATATTCCCCCTGGTGGAGTAGAGGAGAAAGCTAAAAATAAT
GCCGTTTTACTGAGGGAATTTGTGGGCTGTTTTATAGATTTTCCTAAGCCTCTGATTGCA
GTGGTCAATGGTCCAGCTGTGGGCATCTCCGTCACCCTCCTTGGGCTATTCGATGCCGTG
TATGCATCTGACAGGGCAACATTTCATACACCATTTAGTCACCTAGGCCAAAGTCCGGAA
GGATGCTCCTCTTACACTTTTCCGAAGATAATGAGCCCAGCCAAGGCAACAGAGATGCTT
ATTTTTGGAAAGAAGTTAACAGCGGGAGAGGCATGTGCTCAAGGACTTGTTACTGAAGTT
TTCCCTGATAGCACTTTTCAGAAAGAAGTCTGGACCAGGCTGAAGGCATTTGCAAAGCTT
CCCCCAAATGCCTTGAGAATTTCAAAAGAGGTAATCAGGAAAAGAGAGAGAGAAAAACTA
CACGCTGTTAATGCTGAAGAATGCAATGTCCTTCAGGGAAGATGGCTATCAGATGAATGC
ACAAATGCTGTGGTGAACTTCTTATCCAGAAAATCAAAACTGTGA
|
| Enzyme 119 GenBank Gene ID |
NM_206836.2  |
| Enzyme 119 GeneCard ID |
PECI  |
| Enzyme 119 GenAtlas ID |
PECI  |
| Enzyme 119 HGNC ID |
HGNC:14601  |
| Enzyme 119 Chromosome Location |
6 |
| Enzyme 119 Locus |
6p24.3 |
| Enzyme 119 SNPs |
SNPJam Report  |
| Enzyme 119 General References |
- Suk K, Kim YH, Hwang DY, Ihm SH, Yoo HJ, Lee MS: Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor. Biochim Biophys Acta. 1999 May 31;1454(1):126-31. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Geisbrecht BV, Zhang D, Schulz H, Gould SJ: Characterization of PECI, a novel monofunctional Delta(3), Delta(2)-enoyl-CoA isomerase of mammalian peroxisomes. J Biol Chem. 1999 Jul 30;274(31):21797-803. [PubMed
]
- Wang Y, Han KJ, Pang XW, Vaughan HA, Qu W, Dong XY, Peng JR, Zhao HT, Rui JA, Leng XS, Cebon J, Burgess AW, Chen WF: Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies. J Immunol. 2002 Jul 15;169(2):1102-9. [PubMed
]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed
]
- Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S: Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep. 2000 Sep;1(3):287-92. [PubMed
]
- Feng X, Chuhjo T, Sugimori C, Kotani T, Lu X, Takami A, Takamatsu H, Yamazaki H, Nakao S: Diazepam-binding inhibitor-related protein 1: a candidate autoantigen in acquired aplastic anemia patients harboring a minor population of paroxysmal nocturnal hemoglobinuria-type cells. Blood. 2004 Oct 15;104(8):2425-31. Epub 2004 Jun 24. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 119 Metabolite References |
Not Available |
|
Enzyme 120
[top]
|
| Enzyme 120 ID |
13066 |
| Enzyme 120 Name |
Acyl-CoA synthetase family member 4 |
| Enzyme 120 Synonyms |
- Protein NRPS998
|
| Enzyme 120 Gene Name |
AASDH |
| Enzyme 120 Protein Sequence |
>Acyl-CoA synthetase family member 4
MTLQELVHKAASCYMDRVAVCFDECNNQLPVYYTYKTVVNAASELSNFLLLHCDFQGIRE
IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKFK
SFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNLMLNDGKEKYEKEKIKSISSEHVNEEKA
EEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL
TFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQL
IKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPE
KTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL
GTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE
KLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY
INLKSENKLSGKEDLWEKLQYLWKSTLNLPEDLLRVPDESLFLNSGGDSLKSIRLLSEIE
KLVGTSVPGLLEIILSSSILEIYNHILQTVVPDEDVTFRKSCATKRKLSDINQEEASGTS
LHQKAIMTFTCHNEINAFVVLSRGSQILSLNSTRFLTKLGHCSSACPSDSVSQTNIQNLK
GLNSPVLIGKSKDPSCVAKVSEEGKPAIGTQKMELHVRWRSDTGKCVDASPLVVIPTFDK
SSTTVYIGSHSHRMKAVDFYSGKVKWEQILGDRIESSACVSKCGNFIVVGCYNGLVYVLK
SNSGEKYWMFTTEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFS
SPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNL
LCFTHFGEQVWQFSTSGPIFSSPCTSPSEQKIFFGSHDCFIYCCNMKGHLQWKFETTSRV
YATPFAFHNYNGSNEMLLAAASTDGKVWILESQSGQLQSVYELPGEVFSSPVVLESMLII
GCRDNYVYCLDLLGGNQK
|
| Enzyme 120 Number of Residues |
1098 |
| Enzyme 120 Molecular Weight |
122596.1 |
| Enzyme 120 Theoretical pI |
7.26 |
| Enzyme 120 GO Classification |
| Function |
- acyl carrier activity
- binding
- catalytic activity
- cofactor binding
- substrate-specific transporter activity
- transporter activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 120 General Function |
Involved in acyl carrier activity |
| Enzyme 120 Specific Function |
Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA |
| Enzyme 120 Pathways |
Not Available |
| Enzyme 120 Reactions |
Not Available |
| Enzyme 120 Pfam Domain Function |
|
| Enzyme 120 Signals |
|
| Enzyme 120 Transmembrane Regions |
|
| Enzyme 120 Essentiality |
Not Available |
| Enzyme 120 GenBank ID Protein |
45580730  |
| Enzyme 120 UniProtKB/Swiss-Prot ID |
Q4L235  |
| Enzyme 120 UniProtKB/Swiss-Prot Entry Name |
ACSF4_HUMAN  |
| Enzyme 120 PDB ID |
Not Available |
| Enzyme 120 Cellular Location |
Not Available |
| Enzyme 120 Gene Sequence |
>3297 bp
ATGACTCTTCAGGAATTGGTGCATAAGGCTGCCTCCTGTTATATGGACAGAGTAGCTGTA
TGTTTTGATGAATGCAACAACCAGCTTCCAGTTTACTACACCTACAAGACTGTGGTTAAT
GCTGCTTCTGAATTATCAAATTTTCTGCTGTTACACTGTGACTTTCAAGGAATTCGGGAA
ATTGGTCTCTACTGCCAACCTGGGATAGACTTACCCTCTTGGATTTTAGGAATTCTCCAA
GTCCCGGCTGCTTATGTACCTATCGAGCCAGATTCACCACCGTCATTATCAACTCATTTT
ATGAAAAAATGTAATCTAAAGTATATCCTTGTTGAAAAAAAACAAATTAATAAATTTAAA
TCTTTTCATGAAACATTATTGAACTATGATACATTTACAGTGGAACATAATGACCTAGTG
CTCTTCAGACTTCACTGGAAAAATACTGAGGTGAACTTGATGCTAAATGATGGAAAAGAG
AAATATGAAAAAGAAAAAATAAAAAGCATAAGTTCTGAGCATGTCAATGAAGAAAAAGCA
GAAGAACACATGGATCTGAGGCTAAAGCATTGCTTAGCCTATGTTCTACATACATCAGGG
ACTACAGGGATACCGAAGATTGTCAGAGTGCCTCATAAGTGTATAGTACCAAATATCCAG
CATTTTCGGGTACTTTTTGACATCACACAAGAAGATGTTTTGTTTCTGGCTTCACCTCTG
ACCTTCGATCCTTCTGTTGTGGAAATATTTCTTGCTCTATCAAGTGGTGCCTCTCTGCTT
ATTGTACCAACTTCCGTCAAGTTGCTCCCATCAAAATTAGCCAGCGTTCTCTTTTCCCAT
CATAGAGTGACTGTTTTGCAGGCAACACCAACATTGCTTAGAAGATTTGGATCTCAGCTT
ATCAAGTCAACTGTTTTGTCAGCCACTACTTCTCTTCGAGTATTAGCCCTTGGTGGTGAA
GCGTTTCCATCATTGACAGTTCTCAGAAGCTGGAGAGGAGAAGGCAATAAAACACAAATA
TTTAATGTTTATGGTATCACAGAGGTATCAAGTTGGGCGACCATTTATAGGATTCCAGAG
AAGACTCTTAACTCTACTCTCAAATGTGAATTGCCTGTACAACTGGGATTTCCACTTCTT
GGAACAGTAGTTGAAGTCAGAGATACTAATGGCTTCACAATTCAGGAAGGCAGTGGCCAA
GTATTTTTAGGTGGCAGAAACAGAGTGTGTTTTCTTGATGATGAAGTGACAGTACCACTT
GGCACAATGCGAGCTACAGGAGACTTTGTGACTGTGAAAGATGGAGAGATTTTTTTTTTG
GGACGAAAAGACAGTCAGATCAAACGTCATGGCAAACGTCTTAACATTGAACTTGTGCAA
CAGGTTGCTGAAGAGCTTCAGCAAGTGGAGTCTTGTGCAGTTACATGGTATAATCAGGAA
AAATTAATTCTCTTCATGGTGTCTAAAGATGCTTCAGTAAAAGAATACATCTTTAAAGAA
CTGCAGAAATATCTTCCAAGTCATGCAGTCCCGGATGAGCTTGTATTGATCGACTCTCTA
CCATTTACATCCCACGGCAAAATTGATGTTTCTGAGTTAAACAAGATATATTTAAACTAC
ATAAACTTGAAGTCTGAGAATAAGCTCAGTGGGAAAGAGGACCTTTGGGAAAAATTACAG
TATTTGTGGAAGTCTACTCTGAATCTCCCAGAAGATCTTTTGAGGGTTCCTGATGAGTCA
CTCTTCTTAAATAGTGGTGGAGATTCCTTAAAGTCCATCCGGCTCCTCAGTGAGATTGAA
AAACTTGTTGGTACATCAGTACCTGGGCTTCTGGAAATTATTCTCAGCAGTTCCATTTTA
GAGATTTATAATCACATCCTTCAAACAGTGGTTCCAGATGAAGATGTGACATTCAGGAAG
AGTTGTGCCACAAAAAGGAAACTCAGCGACATTAATCAAGAGGAAGCCAGTGGAACATCT
TTACATCAGAAAGCCATCATGACTTTCACTTGCCACAATGAGATTAATGCTTTTGTTGTA
CTGAGCAGAGGGAGTCAAATTTTGTCTCTGAATTCCACTAGGTTTTTAACAAAGTTAGGA
CATTGCTCTTCAGCCTGTCCTTCTGACTCAGTTTCACAGACCAACATTCAAAATTTGAAA
GGCTTAAATTCTCCAGTTCTTATTGGGAAGTCAAAAGATCCATCCTGTGTTGCAAAAGTT
TCTGAAGAGGGGAAACCTGCGATAGGGACTCAGAAAATGGAGTTACATGTGAGGTGGAGG
TCAGACACAGGCAAATGTGTAGATGCTTCACCGCTGGTTGTAATACCCACTTTTGATAAG
TCATCTACAACTGTGTACATTGGTTCCCATTCTCATAGAATGAAGGCAGTTGACTTTTAC
TCTGGGAAGGTAAAATGGGAACAGATTTTGGGAGATCGAATTGAATCCTCAGCATGTGTA
TCTAAGTGTGGAAACTTTATTGTGGTGGGCTGTTATAATGGATTAGTTTATGTTCTGAAA
AGTAATAGTGGAGAAAAATACTGGATGTTTACTACTGAAGATGCTGTCAAAAGCTCGGCA
ACCATGGATCCAACCACAGGACTCATTTACATTGGATCTCATGACCAGCACGCATATGCT
TTAGATATTTATAGAAAGAAGTGTGTTTGGAAGTCAAAATGTGGAGGAACTGTCTTTTCC
TCTCCGTGTTTGAACCTGATTCCACATCATTTGTATTTTGCTACATTGGGAGGACTTTTA
CTGGCTGTAAATCCTGCTACTGGGAACGTTATTTGGAAACATTCCTGTGGAAAACCACTC
TTCTCTTCCCCACAATGTTGCTCACAGTATATTTGTATTGGCTGTGTAGATGGGAATTTA
CTCTGCTTTACTCACTTTGGAGAACAGGTTTGGCAGTTCTCTACCAGTGGACCAATCTTT
TCATCCCCGTGTACCTCACCATCAGAGCAAAAAATATTTTTTGGTTCCCATGATTGCTTT
ATCTACTGTTGTAACATGAAAGGTCACCTGCAGTGGAAATTTGAAACTACTTCAAGGGTC
TATGCAACACCGTTTGCTTTCCATAACTACAATGGCAGCAATGAAATGTTGCTGGCAGCA
GCATCTACTGATGGGAAAGTGTGGATCTTGGAATCTCAGAGTGGACAATTGCAAAGTGTT
TATGAACTTCCTGGAGAAGTCTTCTCTTCTCCTGTGGTCCTGGAATCAATGCTCATTATT
GGGTGTAGAGATAATTATGTTTATTGTCTGGATTTATTGGGTGGCAATCAAAAATAA
|
| Enzyme 120 GenBank Gene ID |
NM_181806.2  |
| Enzyme 120 GeneCard ID |
AASDH  |
| Enzyme 120 GenAtlas ID |
AASDH  |
| Enzyme 120 HGNC ID |
HGNC:23993  |
| Enzyme 120 Chromosome Location |
4 |
| Enzyme 120 Locus |
4q12 |
| Enzyme 120 SNPs |
SNPJam Report  |
| Enzyme 120 General References |
- Wang L, Jil C, Xu Y, Xu J, Dai J, Wu Q, Wu M, Zou X, Sun L, Gu S, Xie Y, Mao Y: Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase. Mol Biol Rep. 2005 Mar;32(1):47-53. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed
]
|
| Enzyme 120 Metabolite References |
Not Available |
|
Enzyme 121
[top]
|
| Enzyme 121 ID |
13088 |
| Enzyme 121 Name |
ACSS2 protein |
| Enzyme 121 Synonyms |
Not Available |
| Enzyme 121 Gene Name |
ACSS2 |
| Enzyme 121 Protein Sequence |
>ACSS2 protein
PMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLK
ELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDL
WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDF
HAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFY
TAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQ
TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMR
TVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA
LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDY
IQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
|
| Enzyme 121 Number of Residues |
534 |
| Enzyme 121 Molecular Weight |
59346.4 |
| Enzyme 121 Theoretical pI |
5.68 |
| Enzyme 121 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 121 General Function |
Involved in acetate-CoA ligase activity |
| Enzyme 121 Specific Function |
Not Available |
| Enzyme 121 Pathways |
Not Available |
| Enzyme 121 Reactions |
Not Available |
| Enzyme 121 Pfam Domain Function |
|
| Enzyme 121 Signals |
|
| Enzyme 121 Transmembrane Regions |
|
| Enzyme 121 Essentiality |
Not Available |
| Enzyme 121 GenBank ID Protein |
40226463  |
| Enzyme 121 UniProtKB/Swiss-Prot ID |
Q96FY7  |
| Enzyme 121 UniProtKB/Swiss-Prot Entry Name |
Q96FY7_HUMAN  |
| Enzyme 121 PDB ID |
Not Available |
| Enzyme 121 Cellular Location |
Not Available |
| Enzyme 121 Gene Sequence |
>1606 bp
GCCTATGATCCCAGAGCTTGTGGTGGCCATGCTGGCATGTGCCCGCATTGGGGCTTTGCA
CTCCATTGTGTTTGCAGGCTTCTCTTCAGAGTCTCTATGTGAACGGATCTTGGATTCCAG
CTGCAGTCTTCTCATCACTACAGATGCCTTCTACAGGGGGGAAAAGCTTGTGAACCTGAA
GGAGCTGGCTGACGAGGCCCTGCAGAAGTGTCAGGAGAAGGGTTTCCCAGTAAGATGCTG
CATTGTGGTCAAGCACCTGGGGCGGGCAGAGCTCGGCATGGGTGACTCCACCAGCCAGTC
CCCCCCAATTAAGAGGTCATGCCCAGATGTGCAGATCTCATGGAACCAAGGGATTGACTT
GTGGTGGCATGAGCTCATGCAAGAGGCAGGGGATGAGTGTGAGCCCGAGTGGTGTGATGC
CGAGGACCCACTCTTCATCCTGTACACCAGTGGCTCCACAGGCAAACCCAAGGGTGTGGT
TCACACAGTTGGGGGCTACATGCTCTATGTAGCCACAACCTTCAAGTATGTGTTTGACTT
CCATGCAGAGGATGTGTTCTGGTGCACGGCAGACATTGGTTGGATCACTGGTCATTCCTA
CGTCACCTATGGGCCACTGGCCAATGGTGCCACCAGTGTTTTGTTTGAGGGGATTCCCAC
ATATCCGGACGTGAACCGCCTGTGGAGCATTGTGGACAAATACAAGGTGACCAAGTTCTA
CACAGCACCCACAGCCATCCGTCTGCTCATGAAGTTTGGAGATGAGCCTGTCACCAAGCA
TAGCCGGGCATCCTTGCAGGTGTTAGGCACAGTGGGTGAACCCATCAACCCTGAGGCCTG
GCTATGGTACCACCGGGTGGTAGGTGCCCAGCGCTGCCCCATCGTGGACACCTTCTGGCA
AACAGAGACAGGTGGCCACATGTTGACTCCCCTTCCTGGTGCCACACCCATGAAACCCGG
TTCTGCTACTTTCCCATTCTTTGGTGTAGCTCCTGCAATCCTGAATGAGTCCGGGGAAGA
GTTGGAAGGTGAAGCTGAAGGTTATCTGGTGTTCAAGCAGCCCTGGCCAGGGATCATGCG
CACAGTCTATGGGAACCACGAACGCTTTGAGACAACCTACTTTAAGAAGTTTCCTGGATA
CTATGTTACAGGAGATGGCTGCCAGCGGGACCAGGATGGCTATTACTGGATCACTGGCAG
GATTGATGACATGCTCAATGTATCTGGACACCTGCTGAGTACAGCAGAGGTGGAGTCAGC
ACTTGTGGAACATGAGGCTGTTGCAGAGGCAGCTGTGGTGGGCCACCCTCATCCTGTGAA
GGGTGAATGCCTCTACTGCTTTGTCACCTTGTGTGATGGCCACACCTTCAGCCCCAAGCT
CACCGAGGAGCTCAAGAAGCAGATTAGAGAAAAGATTGGCCCCATTGCCACACCAGACTA
CATCCAGAATGCACCTGGCTTGCCTAAAACCCGCTCAGGGAAAATCATGAGGCGAGTGCT
TCGGAAGATTGCTCAGAATGACCATGACCTCGGGGACATGTCTACTGTGGCTGACCCATC
TGTCATCAGTCACCTCTTCAGCCACCGCTGCCTGACCATCCAGTGA
|
| Enzyme 121 GenBank Gene ID |
BC010141  |
| Enzyme 121 GeneCard ID |
ACSS2  |
| Enzyme 121 GenAtlas ID |
ACSS2  |
| Enzyme 121 HGNC ID |
HGNC:15814  |
| Enzyme 121 Chromosome Location |
2 |
| Enzyme 121 Locus |
20q11.22 |
| Enzyme 121 SNPs |
SNPJam Report  |
| Enzyme 121 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 121 Metabolite References |
Not Available |
|
Enzyme 122
[top]
|
| Enzyme 122 ID |
13971 |
| Enzyme 122 Name |
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 122 Synonyms |
- VLCAD
|
| Enzyme 122 Gene Name |
ACADVL |
| Enzyme 122 Protein Sequence |
>Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDAL
TRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPA
KNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA
HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY
YTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKM
GIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV
DHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKI
FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDK
GKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRAL
EQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEK
MLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF
|
| Enzyme 122 Number of Residues |
655 |
| Enzyme 122 Molecular Weight |
70389.6 |
| Enzyme 122 Theoretical pI |
9.10 |
| Enzyme 122 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 122 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 122 Specific Function |
Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accomodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons |
| Enzyme 122 Pathways |
Not Available |
| Enzyme 122 Reactions |
Not Available |
| Enzyme 122 Pfam Domain Function |
|
| Enzyme 122 Signals |
|
| Enzyme 122 Transmembrane Regions |
|
| Enzyme 122 Essentiality |
Not Available |
| Enzyme 122 GenBank ID Protein |
12653261  |
| Enzyme 122 UniProtKB/Swiss-Prot ID |
P49748  |
| Enzyme 122 UniProtKB/Swiss-Prot Entry Name |
ACADV_HUMAN  |
| Enzyme 122 PDB ID |
Not Available |
| Enzyme 122 Cellular Location |
Not Available |
| Enzyme 122 Gene Sequence |
>1968 bp
ATGCAGGCGGCTCGGATGGCCGCGAGCTTGGGGCGGCAGCTGCTGAGGCTCGGGGGCGGA
AGCTCGCGGCTCACGGCGCTCCTGGGGCAGCCCCGGCCCGGCCCTGCCCGGCGGCCCTAT
GCCGGGGGTGCCGCTCAGCTGGCTCTGGACAAGTCAGATTCCCACCCCTCTGACGCTCTG
ACCAGGAAAAAACCGGCCAAGGCGGAATCTAAGTCCTTTGCTGTGGGAATGTTCAAAGGC
CAGCTCACCACAGATCAGGTGTTCCCATACCCGTCCGTGCTCAACGAAGAGCAGACACAG
TTTCTTAAAGAGCTGGTGGAGCCTGTGTCCCGTTTCTTCGAGGAAGTGAACGATCCCGCC
AAGAATGACGCTCTGGAGATGGTGGAGGAGACCACTTGGCAGGGCCTCAAGGAGCTGGGG
GCCTTTGGTCTGCAAGTGCCCAGTGAGCTGGGTGGTGTGGGCCTTTGCAACACCCAGTAC
GCCCGTTTGGTGGAGATCGTGGGCATGCATGACCTTGGCGTGGGCATTACCCTGGGGGCC
CATCAGAGCATCGGTTTCAAAGGCATCCTGCTCTTTGGCACAAAGGCCCAGAAAGAAAAA
TACCTCCCCAAGCTGGCATCTGGGGAGACTGTGGCCGCTTTCTGTCTAACCGAGCCCTCA
AGCGGGTCAGATGCAGCCTCCATCCGAACCTCTGCTGTGCCCAGCCCCTGTGGAAAATAC
TATACCCTCAATGGAAGCAAGCTTTGGATCAGTAATGGGGGCCTAGCAGACATCTTCACG
GTCTTTGCCAAGACACCAGTTACAGATCCAGCCACAGGAGCCGTGAAGGAGAAGATCACA
GCTTTTGTGGTGGAGAGGGGCTTCGGGGGCATTACCCATGGGCCCCCTGAGAAGAAGATG
GGCATCAAGGCTTCAAACACAGCAGAGGTGTTCTTTGATGGAGTACGGGTGCCATCGGAG
AACGTGCTGGGTGAGGTTGGGAGTGGCTTCAAGGTTGCCATGCACATCCTCAACAATGGA
AGGTTTGGCATGGCTGCGGCCCTGGCAGGTACCATGAGAGGCATCATTGCTAAGGCGGTA
GATCATGCCACTAATCGTACCCAGTTTGGGGAGAAAATTCACAACTTTGGGCTGATCCAG
GAGAAGCTGGCACGGATGGTTATGCTGCAGTATGTAACTGAGTCCATGGCTTACATGGTG
AGTGCTAACATGGACCAGGGAGCCACGGACTTCCAGATAGAGGCCGCCATCAGCAAAATC
TTTGGCTCGGAGGCAGCCTGGAAGGTGACAGATGAATGCATCCAAATCATGGGGGGTATG
GGCTTCATGAAGGAACCTGGAGTAGAGCGTGTGCTCCGAGATCTTCGCATCTTCCGGATC
TTTGAGGGGACAAATGACATTCTTCGGCTGTTTGTGGCTCTGCAGGGCTGTATGGACAAA
GGAAAGGAGCTCTCTGGGCTTGGCAGTGCTCTAAAGAATCCCTTTGGGAATGCTGGCCTC
CTGCTAGGAGAGGCAGGCAAACAGCTGAGGCGGCGGGCAGGGCTGGGCAGCGGCCTGAGT
CTCAGCGGACTTGTCCACCCGGAGTTGAGTCGGAGTGGCGAGCTGGCAGTACGGGCTCTG
GAGCAGTTTGCCACTGTGGTGGAGGCCAAGCTGATAAAACACAAGAAGGGGATTGTCAAT
GAACAGTTTCTGCTGCAGCGGCTGGCAGACGGGGCCATCGACCTCTATGCCATGGTGGTG
GTTCTCTCGAGGGCCTCAAGATCCCTGAGTGAGGGCCACCCCACGGCCCAGCATGAGAAA
ATGCTCTGTGACACCTGGTGTATCGAGGCTGCAGCTCGGATCCGAGAGGGCATGGCCGCC
CTGCAGTCTGACCCCTGGCAGCAAGAGCTCTACCGCAACTTCAAAAGCATCTCCAAGGCC
TTGGTGGAGCGGGGTGGTGTGGTCACCAGCAACCCACTTGGCTTCTGA
|
| Enzyme 122 GenBank Gene ID |
BC000399  |
| Enzyme 122 GeneCard ID |
ACADVL  |
| Enzyme 122 GenAtlas ID |
ACADVL  |
| Enzyme 122 HGNC ID |
HGNC:92  |
| Enzyme 122 Chromosome Location |
1 |
| Enzyme 122 Locus |
17p13.1 |
| Enzyme 122 SNPs |
SNPJam Report  |
| Enzyme 122 General References |
- Aoyama T, Souri M, Ueno I, Kamijo T, Yamaguchi S, Rhead WJ, Tanaka K, Hashimoto T: Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients. Am J Hum Genet. 1995 Aug;57(2):273-83. [PubMed
]
- Andresen BS, Bross P, Vianey-Saban C, Divry P, Zabot MT, Roe CR, Nada MA, Byskov A, Kruse TA, Neve S, Kristiansen K, Knudsen I, Corydon MJ, Gregersen N: Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. Hum Mol Genet. 1996 Apr;5(4):461-72. [PubMed
]
- Orii KO, Aoyama T, Souri M, Orii KE, Kondo N, Orii T, Hashimoto T: Genomic DNA organization of human mitochondrial very-long-chain acyl-CoA dehydrogenase and mutation analysis. Biochem Biophys Res Commun. 1995 Dec 26;217(3):987-92. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T: Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J Clin Invest. 1995 Jun;95(6):2465-73. [PubMed
]
- Andresen BS, Olpin S, Poorthuis BJ, Scholte HR, Vianey-Saban C, Wanders R, Ijlst L, Morris A, Pourfarzam M, Bartlett K, Baumgartner ER, deKlerk JB, Schroeder LD, Corydon TJ, Lund H, Winter V, Bross P, Bolund L, Gregersen N: Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency. Am J Hum Genet. 1999 Feb;64(2):479-94. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- McAndrew RP, Wang Y, Mohsen AW, He M, Vockley J, Kim JJ: Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J Biol Chem. 2008 Apr 4;283(14):9435-43. Epub 2008 Jan 28. [PubMed
]
- Souri M, Aoyama T, Orii K, Yamaguchi S, Hashimoto T: Mutation analysis of very-long-chain acyl-coenzyme A dehydrogenase (VLCAD) deficiency: identification and characterization of mutant VLCAD cDNAs from four patients. Am J Hum Genet. 1996 Jan;58(1):97-106. [PubMed
]
- Smelt AH, Poorthuis BJ, Onkenhout W, Scholte HR, Andresen BS, van Duinen SG, Gregersen N, Wintzen AR: Very long chain acyl-coenzyme A dehydrogenase deficiency with adult onset. Ann Neurol. 1998 Apr;43(4):540-4. [PubMed
]
- Mathur A, Sims HF, Gopalakrishnan D, Gibson B, Rinaldo P, Vockley J, Hug G, Strauss AW: Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death. Circulation. 1999 Mar 16;99(10):1337-43. [PubMed
]
|
| Enzyme 122 Metabolite References |
Not Available |
|
Enzyme 123
[top]
|
| Enzyme 123 ID |
13972 |
| Enzyme 123 Name |
Acyl-coenzyme A oxidase-like protein |
| Enzyme 123 Synonyms |
- Acyl-CoA oxidase-like protein
|
| Enzyme 123 Gene Name |
ACOXL |
| Enzyme 123 Protein Sequence |
>Acyl-coenzyme A oxidase-like protein
MRALTVQRVKFAMDLPLLKRAGQDLAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWL
FGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVID
TPCENAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDENGSLYPGVTAIDMMY
KEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRL
AVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIEHQTQTLRLMPHLATALALTFV
SRYAGALLDEDVFQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENR
ISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYTKQYEEKPLFGLLQNWAESVGDKLRTS
FLAFNMDTVDDLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDFFHAWNSCLHHVASLS
LAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTR
IRNQERC
|
| Enzyme 123 Number of Residues |
547 |
| Enzyme 123 Molecular Weight |
61795.0 |
| Enzyme 123 Theoretical pI |
8.68 |
| Enzyme 123 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 123 General Function |
Involved in oxidoreductase activity, acting on the CH-CH group of donors |
| Enzyme 123 Specific Function |
Not Available |
| Enzyme 123 Pathways |
Not Available |
| Enzyme 123 Reactions |
Not Available |
| Enzyme 123 Pfam Domain Function |
|
| Enzyme 123 Signals |
|
| Enzyme 123 Transmembrane Regions |
|
| Enzyme 123 Essentiality |
Not Available |
| Enzyme 123 GenBank ID Protein |
119570743  |
| Enzyme 123 UniProtKB/Swiss-Prot ID |
Q9NUZ1  |
| Enzyme 123 UniProtKB/Swiss-Prot Entry Name |
ACOXL_HUMAN  |
| Enzyme 123 PDB ID |
Not Available |
| Enzyme 123 Cellular Location |
Not Available |
| Enzyme 123 Gene Sequence |
>1778 bp
>1743 BP
ATGAGAGCTTTGACAGTTCAGAGAGTGAAGTTTGCCATGGACCTGCCTCTGTTAAAACGT
GCAGGTCAGGATCTGGCAGAGAAAACAAAGAATTTTGTCAGCCGAAGCCTTGTCATAGGA
GAAGTCCTCTCCATGGCGGACATGGCCACAGGAGTGAAGTGCGGAATAATTTATTGGCTA
TTTGGTGGTGCTATCAGGAATCTCGGAAGCCCTGAACATGTTACTAAGTGGTTTCAGCCA
CTCCAGGAGCAGAAATACACTGGGATGTTTGCAATGACCGAGAGGGGCCATGGGAGCAAC
GCGAGAGGGATCCAGACCGAAGCCACCTTTGACCTCTCTGCCCAGGAGTTTGTAATTGAC
ACGCCGTGTGAAAATGCGGAGAAGATGTATATTGGAAATGCCATGTACGGGAATTATGCA
GCTGTCTTTGCCCAGCTCATCATAGATGGAAGATCTCAAGGGCCCCACTGTTTCATCGTT
CCTGTCCGGGATGAAAACGGAAGCTTGTACCCAGGAGTCACAGCTATTGATATGATGTAC
AAGGAGGGTCTGCATGGTGTGGACAATGGGATATTAATATTTGACAAGGTTCGGATACCC
AGGGAGAACCTGCTGGATAAGTTTGGTTCCGTGGCTCCAGATGGACAGTACCATTCGCCT
ATTAGGAACAAGAGTGCAAGATTCAATGCCATGCTGGCAGCACTGACCCCTTCGAGATTA
GCTGTGGCTTTCCAAGCTATGGGTGCCATGAAGCTTGGGTTGACGATAGCCATTCGCTAT
AGCCACAGCCGGAGGCAGTTTGGGCCCAAAACCAAGGAAGAGGTGAAGATCATTGAGCAC
CAAACACAGACCCTGCGGCTGATGCCCCACCTGGCCACAGCCTTGGCCCTGACCTTCGTC
AGCAGGTATGCTGGGGCCCTCCTGGATGAGGATGTCTTCCAGGGAAAGGAGCTGGTCAAC
AGTCGCTCGCTGCAGGCTCTGGTGGCGGGGCTGAAGGCCTACAGCACCTGGGAGAACATC
CGCTGCCTGCAGGACTGCCGCGAGTGCACTGGAGGCATGGTTGTGGGGCGGGAACTGCTG
GCCCAATACACCAAACAGTATGAAGAAAAACCACTCTTTGGCCTGCTCCAAAACTGGGCT
GAATCTGTGGGGGACAAGCTGAGAACCAGTTTCCTGGCATTTAACATGGACACAGTTGAT
GATCTCGCCTTTCTGTTGAAAGCAGTGAAATTTCGTGAAAGGGTTCTTCAGCGGGGTTTG
GTGGCCAGAATTTATTATAAGGTAAAGACCAAGAAGGAGGATTTTTTCCATGCCTGGAAC
TCGTGTCTGCACCACGTGGCTTCTCTGTCCCTGGCACACACTCACCGAGTTACCTTAGAG
CAGTTCTCCCTAGCAGTGAAGAGCTGTCCTGACCAAGAGGACCAGACTTTGTTAATGAAG
TTTTGTCTGTTGTATGGAACCAAGCTGGTGTTTCAGGAGCGGGCCTGGTATTTAGAACAT
AAATACTTGACTCCCATGGCCAGCACGAGGATCAGGAATCAGTTGCTGGATTTGTGCGAC
TCGGTGAAGGATGATGCCCGGAGGGTGATCTCGACCTTTAACATTCCACACACCTACCTC
CACGCACCAATCGCCGGAATCTCCAACCCGCGGGCCGCGTGGGCTTTCTACCCTGCACCG
CTGCAGCCGCGGCCACGGGAAGAGGCGCGCTCCCGGCGGCCCAAGCTGGGAGCCAAGCTC
TAA
|
| Enzyme 123 GenBank Gene ID |
CH471237  |
| Enzyme 123 GeneCard ID |
ACOXL  |
| Enzyme 123 GenAtlas ID |
ACOXL  |
| Enzyme 123 HGNC ID |
HGNC:25621  |
| Enzyme 123 Chromosome Location |
2 |
| Enzyme 123 Locus |
2q13 |
| Enzyme 123 SNPs |
SNPJam Report  |
| Enzyme 123 General References |
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 123 Metabolite References |
Not Available |
|
Enzyme 124
[top]
|
| Enzyme 124 ID |
14011 |
| Enzyme 124 Name |
Acyl-coenzyme A synthetase ACSM6, mitochondrial |
| Enzyme 124 Synonyms |
Not Available |
| Enzyme 124 Gene Name |
ACSM6 |
| Enzyme 124 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM6, mitochondrial
MLGRFQPFSLVRSFRLGFEACCYPNQKCATQTIRPPDSRCLVQAVSQNFNFAKDVLDQWS
QLEKDGLRGPYPALWKVSAKGEEDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPP
TPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCP
TLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQ
YGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPE
TVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRIT
KLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR
IKLNQPASLYCPHMVSWEEYASARGHMLYLTGDRGIMDEDGYFWWSGRVDDVANALGQRL
|
| Enzyme 124 Number of Residues |
480 |
| Enzyme 124 Molecular Weight |
53584.5 |
| Enzyme 124 Theoretical pI |
8.50 |
| Enzyme 124 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 124 General Function |
Involved in catalytic activity |
| Enzyme 124 Specific Function |
ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA |
| Enzyme 124 Pathways |
Not Available |
| Enzyme 124 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 124 Pfam Domain Function |
|
| Enzyme 124 Signals |
|
| Enzyme 124 Transmembrane Regions |
|
| Enzyme 124 Essentiality |
Not Available |
| Enzyme 124 GenBank ID Protein |
195947378  |
| Enzyme 124 UniProtKB/Swiss-Prot ID |
Q6P461  |
| Enzyme 124 UniProtKB/Swiss-Prot Entry Name |
ACSM6_HUMAN  |
| Enzyme 124 PDB ID |
Not Available |
| Enzyme 124 Cellular Location |
Not Available |
| Enzyme 124 Gene Sequence |
>1443 bp
ATGCTAGGCCGATTTCAACCCTTCTCCTTGGTCCGGAGTTTCAGACTGGGATTTGAAGCC
TGCTGCTATCCAAACCAAAAATGTGCTACTCAGACCATCAGACCCCCTGACTCCAGGTGC
CTAGTCCAAGCAGTTTCTCAGAACTTTAATTTTGCAAAGGATGTGTTGGATCAGTGGTCC
CAGCTGGAAAAGGACGGACTCAGAGGGCCTTACCCCGCCCTCTGGAAGGTTAGTGCCAAA
GGAGAAGAGGACAAATGGAGCTTTGAAAGGATGACTCAACTCTCCAAGAAGGCCGCCAGC
ATCCTCTCAGACACCTGTGCCCTTAGCCATGGAGACCGGCTGATGATAATCTTGCCCCCA
ACACCTGAAGCCTACTGGATCTGCCTGGCCTGTGTGCGCTTGGGAATCACCTTTGTGCCT
GGGAGCCCCCAGCTGACTGCCAAGAAAATTCGCTATCAATTACGCATGTCTAAGGCCCAG
TGCATTGTGGCTAATGAAGCTATGGCCCCAGTTGTAAACTCTGCCGTGTCCGACTGCCCC
ACCTTGAAAACCAAGCTCCTGGTGTCAGATAAGAGCTATGATGGGTGGTTGGATTTCAAG
AAGTTGATTCAAGTTGCCCCTCCAAAGCAGACCTACATGAGGACCAAAAGCCAAGATCCA
ATGGCCATATTCTTCACCAAGGGTACAACAGGAGCTCCCAAAATGGTCGAGTATTCCCAG
TATGGTTTGGGAATGGGATTCAGCCAGGCTTCCAGACGGTGGATGGATCTCCAGCCAACA
GATGTCTTGTGGAGTCTGGGTGATGCCTTTGGTGGATCTTTATCCCTGAGCGCTGTCTTG
GGAACTTGGTTCCAAGGAGCCTGTGTGTTTCTGTGTCACATGCCAACCTTCTGCCCTGAG
ACTGTTCTAAATGTCCTGTCCAGATTTCCCATCACCACTCTATCTGCAAATCCAGAGATG
TACCAGGAACTGCTTCAGCACAAGTGTTTCACCAGCTACAGATTCAAGAGTCTGAAGCAG
TGTGTGGCTGCAGGAGGACCCATCAGCCCTGGGGTGATTGAGGACTGGAAACGCATCACT
AAGTTGGACATCTATGAAGGCTATGGGCAGACGGAAACTGGTCTACTCTGTGCCACTTCC
AAAACAATAAAATTGAAGCCAAGCTCTCTGGGGAAGCCATTGCCACCTTATATTGTCCAG
ATTGTGGATGAAAACTCAAATCTCCTGCCTCCAGGGGAAGAAGGAAATATTGCAATCCGC
ATAAAACTAAACCAACCTGCTTCTCTGTACTGTCCACACATGGTGAGCTGGGAGGAATAT
GCTTCAGCAAGAGGCCACATGCTTTACCTCACAGGTGACAGAGGGATCATGGATGAAGAC
GGCTACTTCTGGTGGTCTGGTAGAGTTGATGATGTTGCCAATGCATTGGGTCAGAGATTG
TGA
|
| Enzyme 124 GenBank Gene ID |
NM_207321.2  |
| Enzyme 124 GeneCard ID |
ACSM6  |
| Enzyme 124 GenAtlas ID |
ACSM6  |
| Enzyme 124 HGNC ID |
HGNC:31665  |
| Enzyme 124 Chromosome Location |
Not Available |
| Enzyme 124 Locus |
Not Available |
| Enzyme 124 SNPs |
SNPJam Report  |
| Enzyme 124 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 124 Metabolite References |
Not Available |
|
Enzyme 125
[top]
|
| Enzyme 125 ID |
14420 |
| Enzyme 125 Name |
Acyl-coenzyme A synthetase ACSM2A, mitochondrial |
| Enzyme 125 Synonyms |
- Acyl-CoA synthetase medium-chain family member 2A
- Butyrate--CoA ligase 2A
- Butyryl-coenzyme A synthetase 2A
- Middle-chain acyl-CoA synthetase 2A
|
| Enzyme 125 Gene Name |
ACSM2A |
| Enzyme 125 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM2A, mitochondrial
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN
ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ
|
| Enzyme 125 Number of Residues |
577 |
| Enzyme 125 Molecular Weight |
64222.7 |
| Enzyme 125 Theoretical pI |
8.20 |
| Enzyme 125 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 125 General Function |
Involved in catalytic activity |
| Enzyme 125 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 125 Pathways |
|
| Enzyme 125 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 125 Pfam Domain Function |
|
| Enzyme 125 Signals |
|
| Enzyme 125 Transmembrane Regions |
|
| Enzyme 125 Essentiality |
Not Available |
| Enzyme 125 GenBank ID Protein |
58082049  |
| Enzyme 125 UniProtKB/Swiss-Prot ID |
Q08AH3  |
| Enzyme 125 UniProtKB/Swiss-Prot Entry Name |
ACS2A_HUMAN  |
| Enzyme 125 PDB ID |
Not Available |
| Enzyme 125 Cellular Location |
Not Available |
| Enzyme 125 Gene Sequence |
>1734 bp
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTG
CCGGCCAAGTTTAACTTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGGTGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCTTTATGCCTGGAACCATCCAGATG
AAATCCACTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGTGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGTGCTCACTTATGGAACCTTGGGCATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCCATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCGTCACTGTAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATCC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGATCATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGACAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGGAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGGTCCTGGCCTCGCAGTTCCTGTCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
GCCAAGCTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
|
| Enzyme 125 GenBank Gene ID |
NM_001010845.2  |
| Enzyme 125 GeneCard ID |
ACSM2A  |
| Enzyme 125 GenAtlas ID |
ACSM2A  |
| Enzyme 125 HGNC ID |
HGNC:32017  |
| Enzyme 125 Chromosome Location |
1 |
| Enzyme 125 Locus |
16p12.3 |
| Enzyme 125 SNPs |
SNPJam Report  |
| Enzyme 125 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed
]
- Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW: Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A. J Mol Biol. 2009 May 22;388(5):997-1008. Epub 2009 Apr 1. [PubMed
]
- Iwai N, Mannami T, Tomoike H, Ono K, Iwanaga Y: An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors. Hypertension. 2003 May;41(5):1041-6. Epub 2003 Mar 24. [PubMed
]
- Lindner I, Rubin D, Helwig U, Nitz I, Hampe J, Schreiber S, Schrezenmeir J, Doring F: The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population. Mol Nutr Food Res. 2006 Mar;50(3):270-4. [PubMed
]
|
| Enzyme 125 Metabolite References |
Not Available |
|
Enzyme 126
[top]
|
| Enzyme 126 ID |
14421 |
| Enzyme 126 Name |
Acyl-coenzyme A synthetase ACSM2B, mitochondrial |
| Enzyme 126 Synonyms |
- Acyl-CoA synthetase medium-chain family member 2B
- Butyrate--CoA ligase 2B
- Butyryl-coenzyme A synthetase 2B
- Middle-chain acyl-CoA synthetase 2B
- Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A
|
| Enzyme 126 Gene Name |
ACSM2B |
| Enzyme 126 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM2B, mitochondrial
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKARAQ
|
| Enzyme 126 Number of Residues |
577 |
| Enzyme 126 Molecular Weight |
64270.8 |
| Enzyme 126 Theoretical pI |
8.38 |
| Enzyme 126 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 126 General Function |
Involved in catalytic activity |
| Enzyme 126 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 126 Pathways |
|
| Enzyme 126 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 126 Pfam Domain Function |
|
| Enzyme 126 Signals |
|
| Enzyme 126 Transmembrane Regions |
|
| Enzyme 126 Essentiality |
Not Available |
| Enzyme 126 GenBank ID Protein |
51555772  |
| Enzyme 126 UniProtKB/Swiss-Prot ID |
Q68CK6  |
| Enzyme 126 UniProtKB/Swiss-Prot Entry Name |
ACS2B_HUMAN  |
| Enzyme 126 PDB ID |
Not Available |
| Enzyme 126 Cellular Location |
Not Available |
| Enzyme 126 Gene Sequence |
>1734 bp
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTT
CCGGCCAAGTTTAACTTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGATGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCTTTATGCCTGGAACCATCCAGATG
AAATCCACTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGCGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGGGCTCACTTTTGGAATCTTGGACATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCTATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCCTCGCTGGAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATTC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGGTTATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGAAAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGAAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGATCCTGGCCTCGCAGTTCCTATCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
ACCAAACTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
|
| Enzyme 126 GenBank Gene ID |
AB073604  |
| Enzyme 126 GeneCard ID |
ACSM2B  |
| Enzyme 126 GenAtlas ID |
ACSM2B  |
| Enzyme 126 HGNC ID |
HGNC:30931  |
| Enzyme 126 Chromosome Location |
1 |
| Enzyme 126 Locus |
16p12.3 |
| Enzyme 126 SNPs |
SNPJam Report  |
| Enzyme 126 General References |
- Vessey DA, Lau E, Kelley M, Warren RS: Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria. J Biochem Mol Toxicol. 2003;17(1):1-6. [PubMed
]
- Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Vessey DA, Kelley M, Warren RS: Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids. Biochim Biophys Acta. 1999 Aug 5;1428(2-3):455-62. [PubMed
]
- Boomgaarden I, Vock C, Klapper M, Doring F: Comparative analyses of disease risk genes belonging to the acyl-CoA synthetase medium-chain (ACSM) family in human liver and cell lines. Biochem Genet. 2009 Oct;47(9-10):739-48. Epub 2009 Jul 26. [PubMed
]
|
| Enzyme 126 Metabolite References |
Not Available |
|
Enzyme 127
[top]
|
| Enzyme 127 ID |
14422 |
| Enzyme 127 Name |
Acyl-coenzyme A synthetase ACSM3, mitochondrial |
| Enzyme 127 Synonyms |
- Acyl-CoA synthetase medium-chain family member 3
- Butyrate--CoA ligase 3
- Butyryl-coenzyme A synthetase 3
- Middle-chain acyl-CoA synthetase 3
- Protein SA homolog
|
| Enzyme 127 Gene Name |
ACSM3 |
| Enzyme 127 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM3, mitochondrial
MLARVTRKMLRHAKCFQRLAIFGSVRALHKDNRTATPQNFSNYESMKQDFKLGIPEYFNF
AKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRG
DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPA
VDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG
YPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFT
HHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDV
TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPG
QEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDV
ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIK
EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKTI
|
| Enzyme 127 Number of Residues |
586 |
| Enzyme 127 Molecular Weight |
66152.2 |
| Enzyme 127 Theoretical pI |
9.45 |
| Enzyme 127 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 127 General Function |
Involved in catalytic activity |
| Enzyme 127 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 127 Pathways |
|
| Enzyme 127 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 127 Pfam Domain Function |
|
| Enzyme 127 Signals |
|
| Enzyme 127 Transmembrane Regions |
|
| Enzyme 127 Essentiality |
Not Available |
| Enzyme 127 GenBank ID Protein |
42544132  |
| Enzyme 127 UniProtKB/Swiss-Prot ID |
Q53FZ2  |
| Enzyme 127 UniProtKB/Swiss-Prot Entry Name |
ACSM3_HUMAN  |
| Enzyme 127 PDB ID |
Not Available |
| Enzyme 127 Cellular Location |
Not Available |
| Enzyme 127 Gene Sequence |
>1761 bp
ATGCTAGCTCGTGTCACCAGGAAGATGCTACGTCATGCCAAGTGTTTTCAGCGCCTAGCA
ATTTTTGGTTCTGTGAGGGCACTGCATAAAGATAATAGAACAGCAACCCCTCAGAATTTC
TCCAACTATGAATCCATGAAACAGGACTTCAAACTGGGGATTCCAGAGTATTTCAACTTT
GCTAAAGATGTCCTGGACCAATGGACTGATAAGGAAAAGGCTGGAAAGAAACCTTCAAAT
CCAGCCTTCTGGTGGATCAACAGAAATGGAGAAGAGATGCGATGGAGTTTTGAGGAACTG
GGATCTCTGTCCAGAAAATTTGCCAATATACTTTCAGAAGCCTGTTCCCTACAAAGAGGA
GATCGGGTAATTCTGATTCTGCCCAGGGTCCCAGAGTGGTGGCTTGCAAATGTGGCCTGT
CTGCGAACAGGGACAGTTTTAATTCCAGGAACCACTCAGCTGACCCAGAAAGACATTCTC
TACAGACTACAATCTTCAAAAGCAAACTGCATTATCACCAATGATGTTTTAGCCCCAGCA
GTAGACGCTGTTGCATCCAAATGTGAAAATCTGCACTCCAAGCTGATTGTATCAGAGAAC
TCCAGAGAGGGGTGGGGGAACCTCAAGGAGTTGATGAAACATGCCAGTGACAGCCACACC
TGTGTGAAGACAAAACACAATGAGATCATGGCCATATTCTTTACCAGTGGAACAAGTGGA
TATCCGAAAATGACTGCACACACCCACAGCAGTTTTGGTTTAGGATTATCTGTAAATGGA
AGGTTCTGGCTAGATTTGACACCCTCAGATGTGATGTGGAATACCTCAGATACGGGCTGG
GCAAAGTCTGCATGGAGTAGTGTTTTTTCTCCGTGGATCCAGGGAGCATGTGTATTCACA
CACCATTTACCCCGTTTTGAGCCGACTTCTATCTTGCAAACACTCTCCAAGTACCCCATC
ACAGTCTTCTGTTCAGCACCAACTGTATACCGAATGCTTGTACAGAATGATATAACCAGC
TATAAGTTTAAAAGCTTAAAGCACTGTGTGAGTGCTGGGGAACCAATTACCCCTGACGTG
ACTGAAAAATGGAGAAACAAGACGGGCCTGGATATCTACGAAGGATATGGACAGACTGAA
ACGGTGCTAATCTGTGGAAATTTTAAGGGAATGAAAATTAAACCTGGCTCAATGGGAAAA
CCTTCTCCTGCTTTCGATGTTAAGATTGTAGATGTAAATGGCAATGTTCTACCTCCTGGA
CAAGAAGGAGATATTGGCATTCAAGTTCTACCCAACCGACCATTTGGCCTTTTTACTCAT
TACGTAGATAATCCTTCAAAAACAGCTTCAACTCTACGAGGCAATTTCTATATCACTGGG
GACAGAGGATATATGGATAAAGATGGGTATTTCTGGTTTGTTGCAAGAGCAGATGATGTC
ATATTATCCTCTGGCTATCGAATTGGACCATTTGAGGTAGAAAATGCCCTGAATGAACAC
CCTTCAGTTGCAGAGTCAGCTGTTGTCAGCAGCCCAGACCCCATCAGAGGAGAGGTAGTA
AAGGCTTTTGTCGTTCTAAATCCTGATTACAAGTCACATGATCAAGAACAACTAATAAAG
GAGATTCAGGAGCATGTTAAAAAAACTACAGCACCTTACAAATATCCCAGAAAGGTAGAA
TTTATTCAAGAGCTGCCAAAGACTATCAGTGGGAAGACAAAAAGAAATGAACTGAGGAAG
AAAGAATGGAAGACAATTTAA
|
| Enzyme 127 GenBank Gene ID |
NM_005622.3  |
| Enzyme 127 GeneCard ID |
ACSM3  |
| Enzyme 127 GenAtlas ID |
ACSM3  |
| Enzyme 127 HGNC ID |
HGNC:10522  |
| Enzyme 127 Chromosome Location |
1 |
| Enzyme 127 Locus |
16p13.11 |
| Enzyme 127 SNPs |
SNPJam Report  |
| Enzyme 127 General References |
- Iwai N, Ohmichi N, Hanai K, Nakamura Y, Kinoshita M: Human SA gene locus as a candidate locus for essential hypertension. Hypertension. 1994 Mar;23(3):375-80. [PubMed
]
- Nabika T, Bonnardeaux A, James M, Julier C, Jeunemaitre X, Corvol P, Lathrop M, Soubrier F: Evaluation of the SA locus in human hypertension. Hypertension. 1995 Jan;25(1):6-13. [PubMed
]
- Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed
]
- Telgmann R, Brand E, Nicaud V, Hagedorn C, Beining K, Schonfelder J, Brink-Spalink V, Schmidt-Petersen K, Matanis T, Vischer P, Nofer JR, Hasenkamp S, Plouin PF, Drouet L, Cambien F, Paul M, Tiret L, Brand-Herrmann SM: SAH gene variants are associated with obesity-related hypertension in Caucasians: the PEGASE Study. J Hypertens. 2007 Mar;25(3):557-64. [PubMed
]
|
| Enzyme 127 Metabolite References |
Not Available |
|
Enzyme 128
[top]
|
| Enzyme 128 ID |
14424 |
| Enzyme 128 Name |
Acyl-coenzyme A synthetase ACSM5, mitochondrial |
| Enzyme 128 Synonyms |
Not Available |
| Enzyme 128 Gene Name |
ACSM5 |
| Enzyme 128 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM5, mitochondrial
MRPWLRHLVLQALRNSRAFCGSHGKPAPLPVPQKIVATWEAISLGRQLVPEYFNFAHDVL
DVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMML
VLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIS
AECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMV
EHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV
DAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH
QTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVA
VRIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSY
RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHV
KRVTAPYKYPRKVAFVSELPKTVSGKIQRSKLRSQEWGK
|
| Enzyme 128 Number of Residues |
579 |
| Enzyme 128 Molecular Weight |
64759.6 |
| Enzyme 128 Theoretical pI |
8.52 |
| Enzyme 128 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 128 General Function |
Involved in catalytic activity |
| Enzyme 128 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 128 Pathways |
|
| Enzyme 128 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 128 Pfam Domain Function |
|
| Enzyme 128 Signals |
|
| Enzyme 128 Transmembrane Regions |
|
| Enzyme 128 Essentiality |
Not Available |
| Enzyme 128 GenBank ID Protein |
38505220  |
| Enzyme 128 UniProtKB/Swiss-Prot ID |
Q6NUN0  |
| Enzyme 128 UniProtKB/Swiss-Prot Entry Name |
ACSM5_HUMAN  |
| Enzyme 128 PDB ID |
Not Available |
| Enzyme 128 Cellular Location |
Not Available |
| Enzyme 128 Gene Sequence |
>1740 bp
ATGAGACCATGGCTGAGACACCTAGTCCTCCAGGCACTGAGGAACTCCAGGGCATTCTGT
GGGTCTCATGGGAAGCCAGCACCTCTACCTGTTCCTCAGAAGATCGTGGCCACCTGGGAA
GCCATCAGCCTGGGAAGGCAGCTGGTGCCTGAGTACTTCAACTTCGCCCATGATGTGCTG
GATGTGTGGAGTCGGCTGGAAGAGGCTGGACACCGCCCCCCAAATCCTGCCTTCTGGTGG
GTCAATGGCACAGGAGCAGAGATCAAGTGGAGCTTTGAGGAGCTGGGGAAGCAGTCCAGG
AAGGCAGCCAATGTGCTGGGGGGTGCATGCGGCCTGCAGCCTGGGGACAGAATGATGCTG
GTACTCCCACGGCTCCCGGAGTGGTGGCTGGTCAGTGTGGCTTGCATGCGGACAGGGACT
GTGATGATTCCGGGTGTGACTCAGCTGACAGAGAAGGACCTCAAGTACCGGCTGCAGGCG
TCCAGGGCCAAGTCCATTATCACCAGTGACTCCCTAGCTCCAAGGGTGGATGCCATCAGT
GCCGAATGCCCCTCCCTCCAGACCAAGCTGCTGGTGTCAGACAGCAGTCGGCCAGGCTGG
TTGAACTTCAGGGAACTCCTCCGGGAGGCTTCTACAGAGCACAACTGCATGAGGACAAAG
AGTCGAGACCCGCTGGCCATCTACTTTACCAGCGGAACCACCGGGGCCCCCAAGATGGTC
GAGCACTCCCAGAGCAGCTACGGACTGGGTTTTGTGGCCAGCGGAAGACGGTGGGTGGCC
TTGACCGAATCTGACATCTTCTGGAACACGACTGACACTGGCTGGGTGAAGGCAGCCTGG
ACTCTCTTCTCTGCCTGGCCTAATGGATCTTGCATTTTTGTGCATGAGCTGCCCCGAGTT
GATGCCAAAGTTATCCTGAATACTCTCTCCAAATTCCCGATAACCACCCTCTGCTGTGTC
CCAACCATCTTTCGGCTGCTTGTGCAGGAGGATCTGACCAGGTACCAGTTTCAGAGCCTG
AGGCACTGTCTGACCGGAGGAGAGGCCCTCAACCCTGACGTGAGGGAGAAGTGGAAACAC
CAGACTGGTGTGGAGCTGTACGAAGGCTATGGCCAGTCTGAAACGGTTGTCATCTGTGCC
AATCCAAAAGGCATGAAAATCAAGTCTGGATCCATGGGGAAGGCGTCCCCACCCTACGAT
GTGCAGATTGTGGATGATGAGGGCAACGTCCTGCCTCCTGGAGAAGAGGGGAATGTTGCC
GTCCGTATCAGACCCACTCGGCCCTTCTGTTTCTTCAATTGCTATTTGGACAATCCTGAG
AAGACAGCTGCATCAGAACAAGGGGACTTTTACATCACAGGGGACCGAGCTCGCATGGAC
AAGGATGGCTACTTTTGGTTCATGGGAAGAAACGACGATGTGATCAATTCTTCAAGCTAC
CGGATCGGGCCTGTTGAAGTGGAAAGTGCCCTGGCAGAGCATCCTGCTGTCCTGGAGTCG
GCTGTGGTCAGCAGCCCAGACCCCATCAGGGGAGAGGTGGTAAAGGCATTTATAGTCCTT
ACTCCAGCCTACTCCTCTCATGACCCAGAGGCACTAACGCGGGAACTCCAGGAGCATGTG
AAAAGGGTGACTGCTCCATACAAATACCCCAGGAAGGTGGCCTTTGTTTCAGAACTGCCA
AAGACGGTTTCTGGAAAGATCCAAAGGAGTAAATTGCGAAGTCAGGAGTGGGGGAAATGA
|
| Enzyme 128 GenBank Gene ID |
NM_017888.2  |
| Enzyme 128 GeneCard ID |
ACSM5  |
| Enzyme 128 GenAtlas ID |
ACSM5  |
| Enzyme 128 HGNC ID |
HGNC:26060  |
| Enzyme 128 Chromosome Location |
1 |
| Enzyme 128 Locus |
16p12.3 |
| Enzyme 128 SNPs |
SNPJam Report  |
| Enzyme 128 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Iwai N, Mannami T, Tomoike H, Ono K, Iwanaga Y: An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors. Hypertension. 2003 May;41(5):1041-6. Epub 2003 Mar 24. [PubMed
]
|
| Enzyme 128 Metabolite References |
Not Available |
|
Enzyme 129
[top]
|
| Enzyme 129 ID |
14506 |
| Enzyme 129 Name |
Peroxisomal coenzyme A diphosphatase NUDT7 |
| Enzyme 129 Synonyms |
- Nucleoside diphosphate-linked moiety X motif 7
- Nudix motif 7
|
| Enzyme 129 Gene Name |
NUDT7 |
| Enzyme 129 Protein Sequence |
>Peroxisomal coenzyme A diphosphatase NUDT7
MSRLGLPEEPVRNSLLDDAKARLRKYDIGGKYSHLPYNKYSVLLPLVAKEGKLHLLFTVR
SEKLRRAPGEVCFPGGKRDPTDMDDAATALREAQEEVGLRPHQVEVVCCLVPCLIDTDTL
ITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGHRFINHIFEYTNP
EDGVTYQIKGMTANLAVLVAFIILEKKPTFEVQFNLNDVLASSEELFLKVHKKATSRL
|
| Enzyme 129 Number of Residues |
238 |
| Enzyme 129 Molecular Weight |
26941.9 |
| Enzyme 129 Theoretical pI |
7.06 |
| Enzyme 129 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- ion binding
- magnesium ion binding
- manganese ion binding
- metal ion binding
- transition metal ion binding
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside diphosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 129 General Function |
Involved in hydrolase activity |
| Enzyme 129 Specific Function |
Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. CoA into 3',5'-ADP and 4'- phosphopantetheine. Has no activity toward NDP-sugars, CDP- alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand |
| Enzyme 129 Pathways |
Not Available |
| Enzyme 129 Reactions |
Not Available |
| Enzyme 129 Pfam Domain Function |
|
| Enzyme 129 Signals |
|
| Enzyme 129 Transmembrane Regions |
|
| Enzyme 129 Essentiality |
Not Available |
| Enzyme 129 GenBank ID Protein |
157785656  |
| Enzyme 129 UniProtKB/Swiss-Prot ID |
P0C024  |
| Enzyme 129 UniProtKB/Swiss-Prot Entry Name |
NUDT7_HUMAN  |
| Enzyme 129 PDB ID |
Not Available |
| Enzyme 129 Cellular Location |
Not Available |
| Enzyme 129 Gene Sequence |
>717 bp
ATGTCACGACTTGGTCTTCCCGAGGAGCCAGTCAGAAACAGTTTGCTAGATGATGCTAAG
GCCCGCTTAAGAAAGTATGATATTGGAGGCAAATATTCTCACTTGCCATATAACAAATAC
TCCGTCCTTTTGCCATTGGTGGCTAAAGAAGGAAAACTCCATTTGTTGTTCACCGTCCGG
TCAGAGAAGCTAAGAAGGGCCCCTGGAGAAGTTTGCTTCCCTGGAGGTAAGCGTGACCCT
ACAGACATGGATGATGCAGCCACAGCTCTCCGGGAAGCCCAGGAGGAAGTGGGTCTCCGT
CCTCACCAAGTGGAAGTTGTCTGCTGCCTGGTGCCATGTCTTATTGATACAGATACATTG
ATAACTCCATTTGTGGGTTTAATAGACCACAACTTCCAGGCCCAGCCGAATCCTGCTGAA
GTTAAGGATGTATTCCTGGTGCCTCTGGCCTATTTCCTGCATCCACAGGTCCATGACCAG
CATTACGTCACACGTCTTGGTCACCGTTTTATTAATCATATCTTTGAGTACACAAACCCT
GAAGACGGTGTCACTTACCAGATCAAGGGAATGACGGCAAACCTTGCAGTGTTGGTGGCC
TTTATCATTTTGGAAAAAAAACCCACCTTTGAGGTTCAATTTAATCTTAATGATGTATTA
GCATCCTCTGAAGAGTTATTCCTGAAGGTTCATAAAAAAGCTACAAGCAGGTTATGA
|
| Enzyme 129 GenBank Gene ID |
NM_001105663.1  |
| Enzyme 129 GeneCard ID |
NUDT7  |
| Enzyme 129 GenAtlas ID |
NUDT7  |
| Enzyme 129 HGNC ID |
HGNC:8054  |
| Enzyme 129 Chromosome Location |
1 |
| Enzyme 129 Locus |
16q23.1 |
| Enzyme 129 SNPs |
SNPJam Report  |
| Enzyme 129 General References |
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gasmi L, McLennan AG: The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem J. 2001 Jul 1;357(Pt 1):33-8. [PubMed
]
|
| Enzyme 129 Metabolite References |
Not Available |
|
Enzyme 130
[top]
|
| Enzyme 130 ID |
14717 |
| Enzyme 130 Name |
Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c |
| Enzyme 130 Synonyms |
- SubName: cDNA FLJ78080, highly similar to Human ALAS 5-aminolevulinate synthase
- SubName: cDNA, FLJ93603, highly similar to Homo sapiens aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia) (ALAS2), nuclear gene encoding mitochondrial protein, mRNA
|
| Enzyme 130 Gene Name |
ALAS2 |
| Enzyme 130 Protein Sequence |
>Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
|
| Enzyme 130 Number of Residues |
587 |
| Enzyme 130 Molecular Weight |
64632.9 |
| Enzyme 130 Theoretical pI |
8.19 |
| Enzyme 130 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 130 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 130 Specific Function |
Not Available |
| Enzyme 130 Pathways |
Not Available |
| Enzyme 130 Reactions |
Not Available |
| Enzyme 130 Pfam Domain Function |
|
| Enzyme 130 Signals |
|
| Enzyme 130 Transmembrane Regions |
|
| Enzyme 130 Essentiality |
Not Available |
| Enzyme 130 GenBank ID Protein |
158254562  |
| Enzyme 130 UniProtKB/Swiss-Prot ID |
A8K3F0  |
| Enzyme 130 UniProtKB/Swiss-Prot Entry Name |
A8K3F0_HUMAN  |
| Enzyme 130 PDB ID |
Not Available |
| Enzyme 130 Cellular Location |
Not Available |
| Enzyme 130 Gene Sequence |
>1764 bp
ATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGGGGCCCCACAAGC
CTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGACGCTGTCCCATC
CTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACAAAGGCTGGAGGA
GATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAACTCCAGGATGGG
AAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTGAAGGCTTTCAAG
ACAGATCTGCCTAGCTCCCTGGTCTCAGTCAGCCTAAGGAAGCCATTTTCCGGTCCCCAG
GAGCAGGAGCAGATCTCTGGGAAGGTCACACACCTGATTCAGAACAATATGCCTGGAAAC
TATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATCATGGAGAAGAAACAGGATCAC
ACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGATGCATATCCCTTTGCCCAACAT
TTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTCTGGTGTAGTAATGATTACCTG
GGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAGGAGACCCTGCAGCGTCATGGT
GCTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGTAAGTTTCATGTGGAGCTTGAG
CAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTGCTCTTCTCCTCCTGCTTTGTT
GCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTGCCAGGGTGCGAGATTTACTCA
GACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGTAACAGTGGAGCAGCCAAGTTT
GTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTTCTAGAGAAGTCTAACCCTAAG
ATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATGGATGGTGCCATCTGTCCCCTC
GAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTGACCTTCGTGGATGAGGTCCAT
GCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGGGAGCGTGATGGAATTATGCAT
AAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTTGGCTGTGTGGGCGGCTACATT
GCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTATGCTGCAGGCTTCATCTTTACC
ACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAATCTGTGCGGCTGCTCAAGGGA
GAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAATGTCAAGCACATGCGCCAGCTA
CTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGCCACATCATCCCCATCCGGGTG
GGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTGCTCTCCAAGCATGGCATCTAT
GTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAAGAGCTCCTGCGCTTGGCACCC
TCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTGGAGAAGCTGCTGCTGGCTTGG
ACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCTGCCTGCAATTTCTGTCGCCGT
CCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCCTACTTCGGGAACATGGGGCCC
CAGTATGTCACCACCTATGCCTGA
|
| Enzyme 130 GenBank Gene ID |
AK290565  |
| Enzyme 130 GeneCard ID |
ALAS2  |
| Enzyme 130 GenAtlas ID |
ALAS2  |
| Enzyme 130 HGNC ID |
HGNC:397  |
| Enzyme 130 Chromosome Location |
Not Available |
| Enzyme 130 Locus |
Not Available |
| Enzyme 130 SNPs |
SNPJam Report  |
| Enzyme 130 General References |
Not Available |
| Enzyme 130 Metabolite References |
Not Available |
|
Enzyme 131
[top]
|
| Enzyme 131 ID |
14753 |
| Enzyme 131 Name |
Elongator complex protein 3 |
| Enzyme 131 Synonyms |
- hELP3
|
| Enzyme 131 Gene Name |
ELP3 |
| Enzyme 131 Protein Sequence |
>Elongator complex protein 3
MRQKRKGDLSPAELMMLTIGDVIKQLIEAHEQGKDIDLNKVKTKTAAKYGLSAQPRLVDI
IAAVPPQYRKVLMPKLKAKPIRTASGIAVVAVMCKPHRCPHISFTGNICVYCPGGPDSDF
EYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEE
YRDYFIRNLHDALSGHTSNNIYEAVKYSERSLTKCIGITIETRPDYCMKRHLSDMLTYGC
TRLEIGVQSVYEDVARDTNRGHTVKAVCESFHLAKDSGFKVVAHMMPDLPNVGLERDIEQ
FTEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYKSYSPSDLVELVARILALVPPWT
RVYRVQRDIPMPLVSSGVEHGNLRELALARMKDLGIQCRDVRTREVGIQEIHHKVRPYQV
ELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGS
VVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKIAVISGVGTRNYYRKIGYRLQGP
YMVKMLK
|
| Enzyme 131 Number of Residues |
547 |
| Enzyme 131 Molecular Weight |
62258.4 |
| Enzyme 131 Theoretical pI |
9.12 |
| Enzyme 131 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- iron-sulfur cluster binding
- metal cluster binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 131 General Function |
Involved in N-acetyltransferase activity |
| Enzyme 131 Specific Function |
Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. May also have a methyltransferase activity |
| Enzyme 131 Pathways |
|
| Enzyme 131 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 131 Pfam Domain Function |
|
| Enzyme 131 Signals |
|
| Enzyme 131 Transmembrane Regions |
|
| Enzyme 131 Essentiality |
Not Available |
| Enzyme 131 GenBank ID Protein |
23510283  |
| Enzyme 131 UniProtKB/Swiss-Prot ID |
Q9H9T3  |
| Enzyme 131 UniProtKB/Swiss-Prot Entry Name |
ELP3_HUMAN  |
| Enzyme 131 PDB ID |
Not Available |
| Enzyme 131 Cellular Location |
Not Available |
| Enzyme 131 Gene Sequence |
>1644 bp
ATGAGGCAGAAGCGGAAAGGAGATCTCAGCCCTGCTGAGCTGATGATGCTGACTATAGGA
GATGTTATTAAACAACTGATTGAAGCCCACGAGCAGGGGAAAGACATCGATCTAAATAAG
GTGAAAACCAAGACAGCTGCCAAATATGGCCTTTCTGCCCAGCCCCGCCTGGTGGATATC
ATTGCTGCCGTCCCTCCTCAGTATCGCAAGGTCTTGATGCCCAAGTTAAAGGCGAAACCC
ATCAGAACTGCTAGTGGGATTGCTGTCGTGGCTGTGATGTGCAAACCCCACAGATGTCCA
CACATCAGTTTTACAGGAAATATATGTGTATACTGCCCTGGTGGACCTGATTCTGATTTT
GAGTATTCCACCCAGTCTTACACTGGCTATGAGCCAACCTCCATGAGAGCTATCCGTGCC
AGATATGACCCTTTCCTACAGACAAGACACCGAATAGAACAGTTAAAACAACTTGGTCAT
AGTGTGGATAAAGTGGAGTTTATTGTGATGGGTGGAACGTTTATGGCCCTTCCAGAAGAA
TACAGAGATTATTTTATTCGAAATTTACATGATGCCTTATCAGGACATACTTCCAACAAT
ATTTACGAGGCAGTCAAGTATTCTGAGAGAAGCCTCACAAAGTGTATTGGAATTACTATT
GAAACCAGACCAGATTACTGCATGAAGCGACATTTAAGTGACATGTTGACCTATGGCTGC
ACAAGGCTGGAGATTGGGGTGCAGAGTGTTTATGAAGATGTGGCTAGAGACACCAACAGG
GGCCACACTGTGAAGGCAGTGTGTGAGTCATTTCACCTGGCCAAAGATTCCGGTTTTAAA
GTGGTGGCCCATATGATGCCTGACCTGCCAAACGTGGGACTAGAAAGAGACATTGAACAG
TTCACAGAGTTTTTTGAGAACCCTGCTTTTCGTCCCGATGGGCTGAAACTCTATCCTACC
CTGGTGATTCGTGGGACCGGGCTTTATGAGCTTTGGAAATCAGGAAGATATAAGAGTTAC
TCTCCTAGTGACCTGGTTGAATTGGTGGCTCGGATCCTAGCCCTCGTGCCTCCATGGACT
CGAGTGTACCGAGTACAGAGGGATATTCCAATGCCTTTAGTTAGCTCAGGAGTAGAGCAT
GGTAACCTGAGAGAGCTGGCACTTGCAAGAATGAAAGACCTCGGAATACAGTGTCGAGAT
GTGAGAACCAGAGAAGTTGGAATCCAAGAAATTCATCACAAAGTACGGCCATACCAGGTT
GAATTGGTAAGGAGAGATTATGTTGCAAATGGTGGCTGGGAAACATTCTTGTCATACGAA
GACCCAGATCAAGACATTTTGATTGGCCTCCTACGATTACGCAAGTGTTCAGAAGAAACT
TTCCGTTTCGAATTGGGTGGAGGTGTCTCCATAGTACGAGAGCTGCATGTGTATGGGAGT
GTGGTCCCTGTGAGCAGCCGGGATCCTACTAAATTTCAGCATCAGGGATTTGGCATGCTG
CTGATGGAGGAAGCAGAAAGAATAGCTAGAGAAGAACATGGGTCTGGGAAAATCGCTGTG
ATATCAGGGGTCGGCACCAGGAATTATTATAGAAAGATCGGCTACAGATTACAAGGCCCG
TACATGGTGAAGATGCTGAAATAA
|
| Enzyme 131 GenBank Gene ID |
NM_018091.5  |
| Enzyme 131 GeneCard ID |
ELP3  |
| Enzyme 131 GenAtlas ID |
ELP3  |
| Enzyme 131 HGNC ID |
HGNC:20696  |
| Enzyme 131 Chromosome Location |
8 |
| Enzyme 131 Locus |
8p21.1 |
| Enzyme 131 SNPs |
SNPJam Report  |
| Enzyme 131 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hawkes NA, Otero G, Winkler GS, Marshall N, Dahmus ME, Krappmann D, Scheidereit C, Thomas CL, Schiavo G, Erdjument-Bromage H, Tempst P, Svejstrup JQ: Purification and characterization of the human elongator complex. J Biol Chem. 2002 Jan 25;277(4):3047-52. Epub 2001 Nov 19. [PubMed
]
- Kim JH, Lane WS, Reinberg D: Human Elongator facilitates RNA polymerase II transcription through chromatin. Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1241-6. Epub 2002 Jan 29. [PubMed
]
- Li F, Lu J, Han Q, Zhang G, Huang B: The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast. Mol Genet Genomics. 2005 May;273(3):264-72. Epub 2005 Apr 16. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Close P, Hawkes N, Cornez I, Creppe C, Lambert CA, Rogister B, Siebenlist U, Merville MP, Slaugenhaupt SA, Bours V, Svejstrup JQ, Chariot A: Transcription impairment and cell migration defects in elongator-depleted cells: implication for familial dysautonomia. Mol Cell. 2006 May 19;22(4):521-31. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
|
| Enzyme 131 Metabolite References |
Not Available |
|
Enzyme 132
[top]
|
| Enzyme 132 ID |
14869 |
| Enzyme 132 Name |
Acyl-coenzyme A synthetase ACSM4, mitochondrial |
| Enzyme 132 Synonyms |
Not Available |
| Enzyme 132 Gene Name |
ACSM4 |
| Enzyme 132 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM4, mitochondrial
MKIFFRYQTFRFIWLTKPPGRRLHKDHQLWTPLTLADFEAINRCNRPLPKNFNFAADVLD
QWSQKEKTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANVLTKPCGLQRGDRLAVI
LPRIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVL
ECPDLKTKLLVSPQSWNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQ
HSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQF
DTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRV
QTGLELYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIA
LRLKPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGY
RIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHV
KKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR
|
| Enzyme 132 Number of Residues |
580 |
| Enzyme 132 Molecular Weight |
65702.2 |
| Enzyme 132 Theoretical pI |
8.76 |
| Enzyme 132 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 132 General Function |
Involved in catalytic activity |
| Enzyme 132 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 132 Pathways |
Not Available |
| Enzyme 132 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 132 Pfam Domain Function |
|
| Enzyme 132 Signals |
|
| Enzyme 132 Transmembrane Regions |
|
| Enzyme 132 Essentiality |
Not Available |
| Enzyme 132 GenBank ID Protein |
122937307  |
| Enzyme 132 UniProtKB/Swiss-Prot ID |
P0C7M7  |
| Enzyme 132 UniProtKB/Swiss-Prot Entry Name |
ACSM4_HUMAN  |
| Enzyme 132 PDB ID |
Not Available |
| Enzyme 132 Cellular Location |
Not Available |
| Enzyme 132 Gene Sequence |
>1743 bp
ATGAAGATTTTTTTCCGCTACCAGACATTTAGATTCATCTGGCTCACCAAGCCACCTGGC
CGGCGCTTACACAAAGATCACCAGCTTTGGACGCCTCTGACTCTTGCTGACTTTGAAGCC
ATAAATCGCTGTAACAGGCCATTGCCTAAAAACTTTAACTTTGCTGCAGATGTGCTGGAC
CAGTGGTCCCAAAAGGAGAAGACAGGGGAGAGACCAGCTAACCCAGCCCTGTGGTGGGTG
AATGGCAAAGGGGATGAGGTAAAATGGAGCTTCAGAGAACTGGGCTCCTTGTCCCGAAAA
GCTGCCAACGTGCTCACCAAGCCCTGTGGCCTGCAGAGAGGAGACCGTTTGGCCGTGATT
CTGCCCAGAATCCCTGAGTGGTGGCTGGTCAATGTAGCTTGCATACGAACAGGGATCATC
TTCATGCCGGGAACAATCCAGCTGACAGCAAAAGACATCCTCTACCGGCTGCGAGCATCC
AAGGCCAAGTGCATTGTGGCCAGTGAGGAGGTGGCCCCAGCGGTGGAGTCCATTGTATTG
GAGTGTCCTGACCTTAAGACAAAACTCCTGGTGTCTCCACAAAGCTGGAATGGGTGGCTC
AGCTTCCAGGAGTTATTTCAATTCGCCTCTGAAGAGCACAGCTGTGTGGAAACAGGAAGT
CAAGAACCAATGACCATTTATTTCACCAGTGGGACCACAGGCTTTCCTAAAATGGCCCAG
CACTCTCAGAGCAGCCTCGGCATTGGGTTCACCCTCTGCGGAAGGTATTGGCTGGACTTG
AAGTCCTCAGATATCATATGGAATATGTCTGACACGGGCTGGGTCAAGGCCGCCATTGGC
AGTGTGTTTTCTTCCTGGCTGTGTGGAGCCTGTGTTTTTGTGCATCGAATGGCACAGTTT
GACACTGACACCTTCCTAGACACACTTACTACTTATCCCATCACGACCCTGTGCAGTCCT
CCCACTGTGTACCGGATGCTCGTGCAAAAAGACCTTAAGAGATATAAATTCAAGAGTCTG
CGGCACTGCTTGACCGGAGGGGAGCCACTCAACCCAGAAGTGCTGGAGCAGTGGAGGGTG
CAAACTGGGCTGGAGCTATATGAGGGCTATGGACAGACGGAAGTGGGAATGATTTGTGCC
AATCAGAAAGGCCAAGAAATTAAACCAGGTTCAATGGGGAAAGGAATGCTGCCCTATGAT
GTCCAGATTATAGATGAAAATGGCAATGTTCTACCACCTGGCAAAGAAGGGGAAATTGCC
CTCAGACTCAAACCTACACGGCCCTTCTGTTTCTTCTCTAAATATGTGGACAATCCACAG
AAAACTGCTGCCACGATAAGAGGAGATTTTTATGTCACTGGAGACAGAGGAGTGATGGAC
AGTGATGGGTATTTCTGGTTTGTCGGCAGAGCTGATGATGTCATTATATCCTCTGGGTAC
CGTATTGGGCCATTTGAAGTGGAGAGTGCACTCATTGAGCATCCAGCAGTTGTTGAATCG
GCTGTTGTCAGTAGTCCAGATCAAATCCGCGGAGAGGTGGTGAAAGCTTTTGTTGTCTTA
GCTGCACCCTTTAAGTCCTACAACCCAGAGAAATTAACTCTTGAACTTCAGGATCATGTG
AAAAAATCAACTGCACCTTACAAATATCCAAGAAAGGTGGAATTTGTTCAAGAACTCCCA
AAGACAATCACTGGGAAAATCAAACGCAACGTTTTAAGAGACCAAGAATGGAGAGGAAGA
TAG
|
| Enzyme 132 GenBank Gene ID |
NM_001080454.1  |
| Enzyme 132 GeneCard ID |
ACSM4  |
| Enzyme 132 GenAtlas ID |
ACSM4  |
| Enzyme 132 HGNC ID |
HGNC:32016  |
| Enzyme 132 Chromosome Location |
1 |
| Enzyme 132 Locus |
12p13.31 |
| Enzyme 132 SNPs |
SNPJam Report  |
| Enzyme 132 General References |
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Watkins PA, Maiguel D, Jia Z, Pevsner J: Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J Lipid Res. 2007 Dec;48(12):2736-50. Epub 2007 Aug 30. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 132 Metabolite References |
Not Available |
|
Enzyme 133
[top]
|
| Enzyme 133 ID |
14991 |
| Enzyme 133 Name |
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial |
| Enzyme 133 Synonyms |
- Beta-ketoacyl-ACP synthase
|
| Enzyme 133 Gene Name |
OXSM |
| Enzyme 133 Protein Sequence |
>3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
MSNCLQNFLKITSTRLLCSRLCQQLRSKRKFFGTVPISRLHRRVVITGIGLVTPLGVGTH
LVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTI
MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFV
PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCI
SPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYA
EVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN
KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF
DLNYVPLKAQEWKTEKRFIGLTNSFGFGGTNATLCIAGL
|
| Enzyme 133 Number of Residues |
459 |
| Enzyme 133 Molecular Weight |
48842.4 |
| Enzyme 133 Theoretical pI |
7.72 |
| Enzyme 133 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- biosynthetic process
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 133 General Function |
Involved in catalytic activity |
| Enzyme 133 Specific Function |
May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function |
| Enzyme 133 Pathways |
Not Available |
| Enzyme 133 Reactions |
- an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] [RN:R02768]
|
| Enzyme 133 Pfam Domain Function |
|
| Enzyme 133 Signals |
|
| Enzyme 133 Transmembrane Regions |
|
| Enzyme 133 Essentiality |
Not Available |
| Enzyme 133 GenBank ID Protein |
7020821  |
| Enzyme 133 UniProtKB/Swiss-Prot ID |
Q9NWU1  |
| Enzyme 133 UniProtKB/Swiss-Prot Entry Name |
OXSM_HUMAN  |
| Enzyme 133 PDB ID |
Not Available |
| Enzyme 133 Cellular Location |
Not Available |
| Enzyme 133 Gene Sequence |
>1380 bp
ATGTCCAACTGCCTGCAAAATTTCCTGAAAATTACAAGCACTCGTCTTCTATGTTCAAGA
TTATGCCAACAGTTAAGAAGTAAAAGGAAGTTTTTCGGAACTGTGCCAATATCCAGATTG
CATAGGCGAGTTGTCATTACAGGCATTGGCTTAGTGACTCCTCTTGGTGTTGGAACTCAC
CTGGTTTGGGATCGTCTTATCGGAGGAGAGAGTGGAATTGTTTCACTGGTTGGTGAAGAG
TATAAGAGTATCCCTTGCAGTGTTGCTGCTTATGTGCCAAGAGGTAGTGATGAAGGTCAG
TTCAATGAACAAAACTTTGTGTCCAAATCAGATATCAAGTCCATGTCTTCTCCCACCATC
ATGGCCATTGGGGCTGCAGAATTAGCCATGAAGGATTCTGGCTGGCATCCTCAGTCAGAA
GCTGATCAAGTGGCTACTGGTGTTGCAATTGGCATGGGAATGATTCCTCTTGAAGTTGTT
TCTGAAACTGCTTTGAATTTTCAGACAAAAGGTTACAATAAAGTTAGCCCATTTTTTGTC
CCTAAGATTCTGGTCAATATGGCAGCAGGCCAGGTCAGCATTCGATATAAACTCAAGGGC
CCAAATCATGCAGTATCCACAGCCTGTACCACAGGAGCTCATGCTGTGGGAGACTCATTT
AGATTTATAGCCCATGGTGATGCTGATGTGATGGTGGCTGGAGGTACAGATTCTTGTATT
AGCCCTTTATCTCTTGCTGGGTTTTCCAGAGCCCGGGCTCTGAGCACAAACTCAGATCCC
AAGTTGGCATGTCGACCATTTCATCCAAAGAGAGATGGTTTTGTAATGGGAGAAGGTGCA
GCTGTGCTGGTGCTGGAAGAATATGAACATGCTGTTCAAAGAAGAGCCCGGATCTATGCA
GAAGTTTTGGGCTATGGACTCTCAGGTGATGCTGGTCACATAACTGCCCCTGATCCTGAA
GGAGAAGGTGCCTTAAGGTGTATGGCTGCTGCTTTAAAAGATGCAGGTGTGCAGCCTGAG
GAGATATCCTATATCAATGCACATGCTACTTCCACACCATTGGGAGATGCTGCTGAAAAC
AAAGCTATCAAACATCTCTTCAAAGACCATGCATATGCCCTTGCAGTTTCCTCAACTAAG
GGAGCAACAGGACATCTGCTGGGAGCTGCAGGGGCAGTCGAGGCAGCTTTTACCACATTA
GCTTGTTATTATCAAAAACTACCACCTACTTTAAACCTGGATTGTTCGGAACCAGAATTT
GATCTCAACTATGTTCCACTAAAGGCACAGGAATGGAAAACTGAGAAAAGATTTATTGGC
CTCACCAATTCCTTTGGTTTTGGTGGTACTAATGCAACACTTTGTATTGCTGGACTGTAG
|
| Enzyme 133 GenBank Gene ID |
AK000611  |
| Enzyme 133 GeneCard ID |
OXSM  |
| Enzyme 133 GenAtlas ID |
OXSM  |
| Enzyme 133 HGNC ID |
HGNC:26063  |
| Enzyme 133 Chromosome Location |
3 |
| Enzyme 133 Locus |
3p24.2 |
| Enzyme 133 SNPs |
SNPJam Report  |
| Enzyme 133 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang L, Joshi AK, Hofmann J, Schweizer E, Smith S: Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain. J Biol Chem. 2005 Apr 1;280(13):12422-9. Epub 2005 Jan 24. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 133 Metabolite References |
Not Available |
|
Enzyme 134
[top]
|
| Enzyme 134 ID |
15876 |
| Enzyme 134 Name |
ACAA1 protein |
| Enzyme 134 Synonyms |
Not Available |
| Enzyme 134 Gene Name |
ACAA1 |
| Enzyme 134 Protein Sequence |
>ACAA1 protein
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARA
QSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAG
LTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQAITLLNE
LKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
|
| Enzyme 134 Number of Residues |
331 |
| Enzyme 134 Molecular Weight |
34636.4 |
| Enzyme 134 Theoretical pI |
8.49 |
| Enzyme 134 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 134 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 134 Specific Function |
Not Available |
| Enzyme 134 Pathways |
Not Available |
| Enzyme 134 Reactions |
Not Available |
| Enzyme 134 Pfam Domain Function |
|
| Enzyme 134 Signals |
|
| Enzyme 134 Transmembrane Regions |
|
| Enzyme 134 Essentiality |
Not Available |
| Enzyme 134 GenBank ID Protein |
15680239  |
| Enzyme 134 UniProtKB/Swiss-Prot ID |
Q96CA6  |
| Enzyme 134 UniProtKB/Swiss-Prot Entry Name |
Q96CA6_HUMAN  |
| Enzyme 134 PDB ID |
Not Available |
| Enzyme 134 Cellular Location |
Not Available |
| Enzyme 134 Gene Sequence |
>996 bp
ATGCAGAGGCTGCAGGTAGTGCTGGGCCACCTGAGGGGTCCGGCCGATTCCGGCTGGATG
CCGCAGGCCGCGCCTTGCCTGAGCGGTGCCCCGCAGGCCTCGGCCGCGGACGTGGTGGTG
GTGCACGGGCGGCGCACGGCCATCTGCCGGGCGGGCCGCGGCGGCTTCAAGGACACCACC
CCCGACGAGCTTCTCTCGGCAGTCATGACCGCGGTTCTCAAGGACGTGAATCTGAGGCCG
GAACAGCTGGGGGACATCTGTGTCGGAAATGTGCTGCAGCCTGGGGCCGGGGCAATCATG
GCCCGAATCGCCCAGTTTCTGAGTGACATCCCGGAGACTGTGCCTTTGTCCACTGTCAAT
AGACAGTGTTCGTCGGGGCTACAGGCAGTGGCCAGCATAGCAGGTGGCATCAGAAATGGG
TCTTATGACATTGGCATGGCCTGTGGGATAACCTCTGAGAATGTGGCTGAGCGGTTTGGC
ATTTCACGGGAGAAGCAGGATACCTTTGCCCTGGCTTCCCAGCAGAAGGCAGCAAGAGCC
CAGAGCAAGGGCTGTTTCCAAGCTGAGATTGTGCCTGTGACCACCACGGTCCATGATGAC
AAGGGCACCAAGAGGAGCATCACTGTGACCCAGGATGAGGGTATCCGCCCCAGCACCACC
ATGGAGGGCCTGGCCAAACTGAAGCCTGCCTTCAAGAAAGATGGTTCTACCACAGCTGGG
CTGACAGTGAGTGACGTGGACATCTTCGAGATCAATGAGGCCTTTGCAAGCCAGGCTGCC
TACTGTGTGGAGAAGCTACGACTCCCCCCTGAGAAGGTGAACCCCCTGGGGGGTGCAGTG
GCCTTAGGGCACCCACTGGGCTGCACTGGGGCACGACAGGCCATCACGCTGCTCAATGAG
CTGAAGCGCCGTGGGAAGAGGGCATACGGAGTGGTGTCCATGTGCATCGGGACTGGAATG
GGAGCCGCTGCCGTCTTTGAATACCCTGGGAACTGA
|
| Enzyme 134 GenBank Gene ID |
BC014474  |
| Enzyme 134 GeneCard ID |
ACAA1  |
| Enzyme 134 GenAtlas ID |
ACAA1  |
| Enzyme 134 HGNC ID |
HGNC:82  |
| Enzyme 134 Chromosome Location |
3 |
| Enzyme 134 Locus |
3p23-p22 |
| Enzyme 134 SNPs |
SNPJam Report  |
| Enzyme 134 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 134 Metabolite References |
Not Available |
|
Enzyme 135
[top]
|
| Enzyme 135 ID |
15916 |
| Enzyme 135 Name |
CREBBP variant protein |
| Enzyme 135 Synonyms |
Not Available |
| Enzyme 135 Gene Name |
CREBBP variant protein |
| Enzyme 135 Protein Sequence |
>CREBBP variant protein
LRGAVAVAEIWPPPPPPGLRPPSPSAPARPLAARARSSPSQPAGPPTPVRALAGPAARAR
GCFREQVKMAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELG
LLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANM
ASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTG
PGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQ
GASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATG
VNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRK
LIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQAILGSPA
SGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPA
QPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGN
IGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLV
AYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGA
QPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHS
VQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGM
GQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQ
HTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQP
QTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGP
DVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDE
KKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLP
FRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK
TSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSY
QNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKM
HQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQN
HPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFF
GMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGH
IWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDR
LTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNN
KKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIV
DPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNEC
KHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRL
SIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHA
KHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPP
GTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQ
PPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSG
PVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDL
LRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQ
PGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYR
EMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRM
QQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQ
PNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQ
PSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDT
TGDTLEKFVEGL
|
| Enzyme 135 Number of Residues |
2472 |
| Enzyme 135 Molecular Weight |
267906.8 |
| Enzyme 135 Theoretical pI |
8.81 |
| Enzyme 135 GO Classification |
| Function |
- N-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cation binding
- histone acetyltransferase activity
- ion binding
- lysine N-acetyltransferase activity
- metal ion binding
- protein binding
- transcription coactivator activity
- transcription cofactor activity
- transcription factor binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- covalent chromatin modification
- histone acetylation
- histone modification
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- histone acetyltransferase complex
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- nucleus
- organelle
- protein complex
|
|
| Enzyme 135 General Function |
Involved in transcription cofactor activity |
| Enzyme 135 Specific Function |
Not Available |
| Enzyme 135 Pathways |
Not Available |
| Enzyme 135 Reactions |
Not Available |
| Enzyme 135 Pfam Domain Function |
|
| Enzyme 135 Signals |
|
| Enzyme 135 Transmembrane Regions |
|
| Enzyme 135 Essentiality |
Not Available |
| Enzyme 135 GenBank ID Protein |
68533141  |
| Enzyme 135 UniProtKB/Swiss-Prot ID |
Q4LE28  |
| Enzyme 135 UniProtKB/Swiss-Prot Entry Name |
Q4LE28_HUMAN  |
| Enzyme 135 PDB ID |
1JSP  |
| Enzyme 135 PDB File |
Show |
| Enzyme 135 3D Structure |
|
| Enzyme 135 Cellular Location |
Not Available |
| Enzyme 135 Gene Sequence |
>7419 bp
CTGCGGGGCGCTGTTGCTGTGGCTGAGATTTGGCCGCCGCCTCCCCCACCCGGCCTGCGC
CCTCCCTCTCCCTCGGCGCCCGCCCGCCCGCTCGCGGCCCGCGCTCGCTCCTCTCCCTCG
CAGCCGGCAGGGCCCCCGACCCCCGTCCGGGCCCTCGCCGGCCCGGCCGCCCGTGCCCGG
GGCTGTTTTCGCGAGCAGGTGAAAATGGCTGAGAACTTGCTGGACGGACCGCCCAACCCC
AAAAGAGCCAAACTCAGCTCGCCCGGTTTCTCGGCGAATGACAGCACAGATTTTGGATCA
TTGTTTGACTTGGAAAATGATCTTCCTGATGAGCTGATACCCAATGGAGGAGAATTAGGC
CTTTTAAACAGTGGGAACCTTGTTCCAGATGCTGCTTCCAAACATAAACAACTGTCGGAG
CTTCTACGAGGAGGCAGCGGCTCTAGTATCAACCCAGGAATAGGAAATGTGAGCGCCAGC
AGCCCCGTGCAGCAGGGCCTGGGTGGCCAGGCTCAAGGGCAGCCGAACAGTGCTAACATG
GCCAGCCTCAGTGCCATGGGCAAGAGCCCTCTGAGCCAGGGAGATTCTTCAGCCCCCAGC
CTGCCTAAACAGGCAGCCAGCACCTCTGGGCCCACCCCCGCTGCCTCCCAAGCACTGAAT
CCGCAAGCACAAAAGCAAGTGGGGCTGGCGACTAGCAGCCCTGCCACGTCACAGACTGGA
CCTGGTATCTGCATGAATGCTAACTTTAACCAGACCCACCCAGGCCTCCTCAATAGTAAC
TCTGGCCATAGCTTAATTAATCAGGCTTCACAAGGGCAGGCGCAAGTCATGAATGGATCT
CTTGGGGCTGCTGGCAGAGGAAGGGGAGCTGGAATGCCGTACCCTACTCCAGCCATGCAG
GGCGCCTCGAGCAGCGTGCTGGCTGAGACCCTAACGCAGGTTTCCCCGCAAATGACTGGT
CACGCGGGACTGAACACCGCACAGGCAGGAGGCATGGCCAAGATGGGAATAACTGGGAAC
ACAAGTCCATTTGGACAGCCCTTTAGTCAAGCTGGAGGGCAGCCAATGGGAGCCACTGGA
GTGAACCCCCAGTTAGCCAGCAAACAGAGCATGGTCAACAGTTTGCCCACCTTCCCTACA
GATATCAAGAATACTTCAGTCACCAACGTGCCAAATATGTCTCAGATGCAAACATCAGTG
GGAATTGTACCCACACAAGCAATTGCAACAGGCCCCACTGCAGATCCTGAAAAACGCAAA
CTGATACAGCAGCAGCTGGTTCTACTGCTTCATGCTCATAAGTGTCAGAGACGAGAGCAA
GCAAACGGAGAGGTTCGGGCCTGCTCGCTCCCGCATTGTCGAACCATGAAAAACGTTTTG
AATCACATGACGCATTGTCAGGCTGGGAAAGCCTGCCAAGCCATCCTGGGGTCTCCAGCT
AGTGGAATTCAAAACACAATTGGTTCTGTTGGCACAGGGCAACAGAATGCCACTTCTTTA
AGTAACCCAAATCCCATAGACCCCAGCTCCATGCAGCGAGCCTATGCTGCTCTCGGACTC
CCCTACATGAACCAGCCCCAGACGCAGCTGCAGCCTCAGGTTCCTGGCCAGCAACCAGCA
CAGCCTCAAACCCACCAGCAGATGAGGACTCTCAACCCCCTGGGAAATAATCCAATGAAC
ATTCCAGCAGGAGGAATAACAACAGATCAGCAGCCCCCAAACTTGATTTCAGAATCAGCT
CTTCCGACTTCCCTGGGGGCCACAAACCCACTGATGAACGATGGCTCCAACTCTGGTAAC
ATTGGAACCCTCAGCACTATACCAACAGCAGCTCCTCCTTCTAGCACCGGTGTAAGGAAA
GGCTGGCACGAACATGTCACTCAGGACCTGCGGAGCCATCTAGTGCATAAACTCGTCCAA
GCCATCTTCCCAACACCTGATCCCGCAGCTCTAAAGGATCGCCGCATGGAAAACCTGGTA
GCCTATGCTAAGAAAGTGGAAGGGGACATGTACGAGTCTGCCAACAGCAGGGATGAATAT
TATCACTTATTAGCAGAGAAAATCTACAAGATACAAAAAGAACTAGAAGAAAAACGGAGG
TCGCGTTTACATAAACAAGGCATCTTGGGGAACCAGCCAGCCTTACCAGCCCCGGGGGCT
CAGCCCCCTGTGATTCCACAGGCACAACCTGTGAGACCTCCAAATGGACCCCTGTCCCTG
CCAGTGAATCGCATGCAAGTTTCTCAAGGGATGAATTCATTTAACCCCATGTCCTTGGGG
AACGTCCAGTTGCCACAAGCACCCATGGGACCTCGTGCAGCCTCCCCAATGAACCACTCT
GTCCAGATGAACAGCATGGGCTCAGTGCCAGGGATGGCCATTTCTCCTTCCCGAATGCCT
CAGCCTCCGAACATGATGGGTGCACACACCAACAACATGATGGCCCAGGCGCCCGCTCAG
AGCCAGTTTCTGCCACAGAACCAGTTCCCGTCATCCAGCGGGGCGATGAGTGTGGGCATG
GGGCAGCCGCCAGCCCAAACAGGCGTGTCACAGGGACAGGTGCCTGGTGCTGCTCTTCCT
AACCCTCTCAACATGCTGGGGCCTCAGGCCAGCCAGCTACCTTGCCCTCCAGTGACACAG
TCACCACTGCACCCAACACCGCCTCCTGCTTCCACGGCTGCTGGCATGCCATCTCTCCAG
CACACGACACCACCTGGGATGACTCCTCCCCAGCCAGCAGCTCCCACTCAGCCATCAACT
CCTGTGTCGTCTTCCGGGCAGACTCCCACCCCGACTCCTGGCTCAGTGCCCAGTGCTACC
CAAACCCAGAGCACCCCTACAGTCCAGGCAGCAGCCCAGGCCCAGGTGACCCCGCAGCCT
CAAACCCCAGTTCAGCCCCCGTCTGTGGCTACCCCTCAGTCATCGCAGCAACAGCCGACG
CCTGTGCACGCCCAGCCTCCTGGCACACCGCTTTCCCAGGCAGCAGCCAGCATTGATAAC
AGAGTCCCTACCCCCTCCTCGGTGGCCAGCGCAGAAACCAATTCCCAGCAGCCAGGACCT
GACGTACCTGTGCTGGAAATGAAGACGGAGACCCAAGCAGAGGACACTGAGCCCGATCCT
GGTGAATCCAAAGGGGAGCCCAGGTCTGAGATGATGGAGGAGGATTTGCAAGGAGCTTCC
CAAGTTAAAGAAGAAACAGACATAGCAGAGCAGAAATCAGAACCAATGGAAGTGGATGAA
AAGAAACCTGAAGTGAAAGTAGAAGTTAAAGAGGAAGAAGAGAGTAGCAGTAACGGCACA
GCCTCTCAGTCAACATCTCCTTCGCAGCCGCGCAAAAAAATCTTTAAACCAGAGGAGTTA
CGCCAGGCCCTCATGCCAACCCTAGAAGCACTGTATCGACAGGACCCAGAGTCATTACCT
TTCCGGCAGCCTGTAGATCCCCAGCTCCTCGGAATTCCAGACTATTTTGACATCGTAAAG
AATCCCATGGACCTCTCCACCATCAAGCGGAAGCTGGACACAGGGCAATACCAAGAGCCC
TGGCAGTACGTGGACGACGTCTGGCTCATGTTCAACAATGCCTGGCTCTATAATCGCAAG
ACATCCCGAGTCTATAAGTTTTGCAGTAAGCTTGCAGAGGTCTTTGAGCAGGAAATTGAC
CCTGTCATGCAGTCCCTTGGATATTGCTGTGGACGCAAGTATGAGTTTTCCCCACAGACT
TTGTGCTGCTATGGGAAGCAGCTGTGTACCATTCCTCGCGATGCTGCCTACTACAGCTAT
CAGAATAGGTATCATTTCTGTGAGAAGTGTTTCACAGAGATCCAGGGCGAGAATGTGACC
CTGGGTGACGACCCTTCACAGCCCCAGACGACAATTTCAAAGGATCAGTTTGAAAAGAAG
AAAAATGATACCTTAGACCCCGAACCTTTCGTTGATTGCAAGGAGTGTGGCCGGAAGATG
CATCAGATTTGCGTTCTGCACTATGACATCATTTGGCCTTCAGGTTTTGTGTGCGACAAC
TGCTTGAAGAAAACTGGCAGACCTCGAAAAGAAAACAAATTCAGTGCTAAGAGGCTGCAG
ACCACAAGACTGGGAAACCACTTGGAAGACCGAGTGAACAAATTTTTGCGGCGCCAGAAT
CACCCTGAAGCCGGGGAGGTTTTTGTCCGAGTGGTGGCCAGCTCAGACAAGACGGTGGAG
GTCAAGCCCGGGATGAAGTCACGGTTTGTGGATTCTGGGGAAATGTCTGAATCTTTCCCA
TATCGAACCAAAGCTCTGTTTGCTTTTGAGGAAATTGACGGCGTGGATGTCTGCTTTTTT
GGAATGCACGTCCAAGAATACGGCTCTGATTGCCCCCCTCCAAACACGAGGCGTGTGTAC
ATTTCTTATCTGGATAGTATTCATTTCTTCCGGCCACGTTGCCTCCGCACAGCCGTTTAC
CATGAGATCCTTATTGGATATTTAGAGTATGTGAAGAAATTAGGGTATGTGACAGGGCAC
ATCTGGGCCTGTCCTCCAAGTGAAGGAGATGATTACATCTTCCATTGCCACCCACCTGAT
CAAAAAATACCCAAGCCAAAACGGCTGCAGGAGTGGTACAAAAAGATGCTGGACAAGGCG
TTTGCAGAGCGGATCATCCATGACTACAAGGATATTTTCAAACAAGCAACTGAAGACAGG
CTCACCAGTGCCAAGGAACTGCCCTATTTTGAAGGTGATTTCTGGCCCAATGTGTTAGAA
GAGAGCATTAAGGAACTAGAACAAGAAGAAGAGGAGAGGAAAAAGGAAGAGAGCACTGCA
GCCAGTGAAACCACTGAGGGCAGTCAGGGCGACAGCAAGAATGCCAAGAAGAAGAACAAC
AAGAAAACCAACAAGAACAAAAGCAGCATCAGCCGCGCCAACAAGAAGAAGCCCAGCATG
CCCAACGTGTCCAATGACCTGTCCCAGAAGCTGTATGCCACCATGGAGAAGCACAAGGAG
GTCTTCTTCGTGATCCACCTGCACGCTGGGCCTGTCATCAACACCCTGCCCCCCATCGTC
GACCCCGACCCCCTGCTCAGCTGTGACCTCATGGATGGGCGCGACGCCTTCCTCACCCTC
GCCAGAGACAAGCACTGGGAGTTCTCCTCCTTGCGCCGCTCCAAGTGGTCCACGCTCTGC
ATGCTGGTGGAGCTGCACACCCAGGGCCAGGACCGCTTTGTCTACACCTGCAACGAGTGC
AAGCACCACGTGGAGACGCGCTGGCACTGCACTGTGTGCGAGGACTACGACCTCTGCATC
AACTGCTATAACACGAAGAGCCATGCCCATAAGATGGTGAAGTGGGGGCTGGGCCTGGAT
GACGAGGGCAGCAGCCAGGGCGAGCCACAGTCAAAGAGCCCCCAGGAGTCACGCCGGCTG
AGCATCCAGCGCTGCATCCAGTCGCTGGTGCACGCGTGCCAGTGCCGCAACGCCAACTGC
TCGCTGCCATCCTGCCAGAAGATGAAGCGGGTGGTGCAGCACACCAAGGGCTGCAAACGC
AAGACCAACGGGGGCTGCCCGGTGTGCAAGCAGCTCATCGCCCTCTGCTGCTACCACGCC
AAGCACTGCCAAGAAAACAAATGCCCCGTGCCCTTCTGCCTCAACATCAAACACAAGCTC
CGCCAGCAGCAGATCCAGCACCGCCTGCAGCAGGCCCAGCTCATGCGCCGGCGGATGGCC
ACCATGAACACCCGCAACGTGCCTCAGCAGAGTCTGCCTTCTCCTACCTCAGCACCGCCC
GGGACCCCCACACAGCAGCCCAGCACACCCCAGACGCCGCAGCCCCCTGCCCAGCCCCAA
CCCTCACCCGTGAGCATGTCACCAGCTGGCTTCCCCAGCGTGGCCCGGACTCAGCCCCCC
ACCACGGTGTCCACAGGGAAGCCTACCAGCCAGGTGCCGGCCCCCCCACCCCCGGCCCAG
CCCCCTCCTGCAGCGGTGGAAGCGGCTCGGCAGATCGAGCGTGAGGCCCAGCAGCAGCAG
CACCTGTACCGGGTGAACATCAACAACAGCATGCCCCCAGGACGCACGGGCATGGGGACC
CCGGGGAGCCAGATGGCCCCCGTGAGCCTGAATGTGCCCCGACCCAACCAGGTGAGCGGG
CCCGTCATGCCCAGCATGCCTCCCGGGCAGTGGCAGCAGGCGCCCCTTCCCCAGCAGCAG
CCCATGCCAGGCTTGCCCAGGCCTGTGATATCCATGCAGGCCCAGGCGGCCGTGGCTGGG
CCCCGGATGCCCAGCGTGCAGCCACCCAGGAGCATCTCACCCAGCGCTCTGCAAGACCTG
CTGCGGACCCTGAAGTCGCCCAGCTCCCCTCAGCAGCAACAGCAGGTGCTGAACATTCTC
AAATCAAACCCGCAGCTAATGGCAGCTTTCATCAAACAGCGCACAGCCAAGTACGTGGCC
AATCAGCCCGGCATGCAGCCCCAGCCTGGCCTCCAGTCCCAGCCCGGCATGCAACCCCAG
CCTGGCATGCACCAGCAGCCCAGCCTGCAGAACCTGAATGCCATGCAGGCTGGCGTGCCG
CGGCCCGGTGTGCCTCCACAGCAGCAGGCGATGGGAGGCCTGAACCCCCAGGGCCAGGCC
TTGAACATCATGAACCCAGGACACAACCCCAACATGGCGAGTATGAATCCACAGTACCGA
GAAATGTTACGGAGGCAGCTGCTGCAGCAGCAGCAGCAACAGCAGCAGCAACAACAGCAG
CAACAGCAGCAGCAGCAAGGGAGTGCCGGCATGGCTGGGGGCATGGCGGGGCACGGCCAG
TTCCAGCAGCCTCAAGGACCCGGAGGCTACCCACCGGCCATGCAGCAGCAGCAGCGCATG
CAGCAGCATCTCCCCCTCCAGGGCAGCTCCATGGGCCAGATGGCGGCTCAGATGGGACAG
CTTGGCCAGATGGGGCAGCCGGGGCTGGGGGCAGACAGCACCCCCAACATCCAGCAAGCC
CTGCAGCAGCGGATTCTGCAGCAACAGCAGATGAAGCAGCAGATTGGGTCCCCAGGCCAG
CCGAACCCCATGAGCCCCCAGCAACACATGCTCTCAGGACAGCCACAGGCCTCGCATCTC
CCTGGCCAGCAGATCGCCACGTCCCTTAGTAACCAGGTGCGGTCTCCAGCCCCTGTCCAG
TCTCCACGGCCCCAGTCCCAGCCTCCACATTCCAGCCCGTCACCACGGATACAGCCCCAG
CCTTCGCCACACCACGTCTCACCCCAGACTGGTTCCCCCCACCCCGGACTCGCAGTCACC
ATGGCCAGCTCCATAGATCAGGGACACTTGGGGAACCCCGAACAGAGTGCAATGCTCCCC
CAGCTGAACACCCCCAGCAGGAGTGCGCTGTCCAGCGAACTGTCCCTGGTCGGGGACACC
ACGGGGGACACGCTAGAGAAGTTTGTGGAGGGCTTGTAG
|
| Enzyme 135 GenBank Gene ID |
AB210043  |
| Enzyme 135 GeneCard ID |
CREBBP variant prote  |
| Enzyme 135 GenAtlas ID |
CREBBP+variant+prote  |
| Enzyme 135 HGNC ID |
HGNC:2348  |
| Enzyme 135 Chromosome Location |
Not Available |
| Enzyme 135 Locus |
Not Available |
| Enzyme 135 SNPs |
SNPJam Report  |
| Enzyme 135 General References |
Not Available |
| Enzyme 135 Metabolite References |
Not Available |
|
Enzyme 136
[top]
|
| Enzyme 136 ID |
15917 |
| Enzyme 136 Name |
Histone acetyltransferase MYST4 |
| Enzyme 136 Synonyms |
- MYST-4
- Histone acetyltransferase MORF
- Histone acetyltransferase MOZ2
- MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
- Monocytic leukemia zinc finger protein-related factor
|
| Enzyme 136 Gene Name |
MYST4 |
| Enzyme 136 Protein Sequence |
>Histone acetyltransferase MYST4
MVKLANPLYTEWILEAIQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSV
LKVTNKGLASYKDPDNPGRFSSVKPGTFPKSAKGSRGSCNDLRNVDWNKLLRRAIEGLEE
PNGSSLKNIEKYLRSQSDLTSTTNNPAFQQRLRLGAKRAVNNGRLLKDGPQYRVNYGSLD
GKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADC
GSSGHPSCLKFCPELTTNVKALRWQCIECKTCSACRVQGRNADNMLFCDSCDRGFHMECC
DPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDE
GSMNAFTGRGSPGRGQKTKVCTTPSSGHAASGKDSSSRLAVTDPTRPGATTKITTTSTYI
SASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLA
TGTTQKLKPPPSSLPPPTPISGQSPSSQKSSTATSSPSPQSSSSQCSVPSLSSLTTNSQL
KALFDGLSHIYTTQGQSRKKGHPSYAPPKRMRRKTELSSTAKSKAHFFGKRDIRSRFISH
SSSSSWGMARGSIFKAIAHFKRTTFLKKHRMLGRLKYKVTPQMGTPSPGKGSLTDGRIKP
DQDDDTEIKINIKQESADVNVIGNKDVVTEEDLDVFKQAQELSWEKIECESGVEDCGRYP
SVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANE
IYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLV
GYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRL
SYLAYWKSVILEYLYHHHERHISIKAISRATGMCPHDIATTLQHLHMIDKRDGRFVIIRR
EKLILSHMEKLKTCSRANELDPDSLRWTPILISNAAVSEEEREAEKEAERLMEQASCWEK
EEQEILSTRANSRQSPAKVQSKNKYLHSPESRPVTGERGQLLELSKESSEEEEEEEDEEE
EEEEEEEEEDEEEEEEEEEEEEEENIQSSPPRLTKPQSVAIKRKRPFVLKKKRGRKRRRI
NSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIEVEEDGRKPVLRKAFQHQPGKK
RQTEEEEGKDNHCFKNADPCRNNMNDDSSNLKEGSKDNPEPLKCKQVWPKGTKRGLSKWR
QNKERKTGFKLNLYTPPETPMEPDEQVTVEEQKETSEGKTSPSPIRIEEEVKETGEALLP
QEENRREETCAPVSPNTSPGEKPEDDLIKPEEEEEEEEEEEEEEEEEEGEEEEGGGNVEK
DPDGAKSQEKEEPEISTEKEDSARLDDHEEEEEEDEEPSHNEDHDADDEDDSHMESAEVE
KEELPRESFKEVLENQETFLDLNVQPGHSNPEVLMDCGVDLTASCNSEPKELAGDPEAVP
ESDEEPPPGEQAQKQDQKNSKEVDTEFKEGNPATMEIDSETVQAVQSLTQESSEQDDTFQ
DCAETQEACRSLQNYTRADQSPQIATTLDDCQQSDHSSPVSSVHSHPGQSVRSVNSPSVP
ALENSYAQISPDQSAISVPSLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENY
ENPSSYDSTMGGSICGNGSSQNSCSYSNLTSSSLTQSSCAVTQQMSNISGSCSMLQQTSI
SSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLAEIPETSNANIGLYERMGQ
SDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQ
LSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASK
GHISMRTKSASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVN
SVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGTQPYAQQPMQT
PPHGNMMYTAPGHHGYMNTGMSKQSLNGSYMRR
|
| Enzyme 136 Number of Residues |
2073 |
| Enzyme 136 Molecular Weight |
231376.3 |
| Enzyme 136 Theoretical pI |
5.82 |
| Enzyme 136 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin organization
- chromosome organization
- nucleosome assembly
- nucleosome organization
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
|
| Component |
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- nucleosome
- nucleus
- organelle
- protein-DNA complex
|
|
| Enzyme 136 General Function |
Involved in DNA binding |
| Enzyme 136 Specific Function |
Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity |
| Enzyme 136 Pathways |
Not Available |
| Enzyme 136 Reactions |
- acetyl-CoA + histone = CoA + acetylhistone
|
| Enzyme 136 Pfam Domain Function |
|
| Enzyme 136 Signals |
|
| Enzyme 136 Transmembrane Regions |
|
| Enzyme 136 Essentiality |
Not Available |
| Enzyme 136 GenBank ID Protein |
100816397  |
| Enzyme 136 UniProtKB/Swiss-Prot ID |
Q8WYB5  |
| Enzyme 136 UniProtKB/Swiss-Prot Entry Name |
MYST4_HUMAN  |
| Enzyme 136 PDB ID |
Not Available |
| Enzyme 136 Cellular Location |
Not Available |
| Enzyme 136 Gene Sequence |
>6222 bp
ATGGTAAAACTTGCAAACCCACTTTATACAGAGTGGATTCTTGAAGCTATACAGAAAATA
AAAAAGCAAAAGCAAAGGCCCTCTGAAGAGAGAATCTGCCATGCGGTCAGTACTTCCCAT
GGGTTGGATAAGAAGACAGTCTCTGAACAGCTGGAACTCAGTGTTCAGGATGGCTCAGTT
CTCAAAGTCACCAACAAAGGCCTTGCCTCCTATAAGGACCCAGACAACCCTGGGCGCTTT
TCATCAGTTAAACCAGGCACTTTTCCTAAGTCAGCCAAGGGGTCTAGAGGATCATGTAAT
GATCTCCGCAATGTGGATTGGAATAAACTTTTAAGGAGAGCAATTGAAGGACTTGAGGAG
CCGAATGGCTCCTCCCTGAAGAACATAGAGAAGTATCTCAGAAGTCAAAGTGATCTCACA
AGCACCACCAACAACCCAGCCTTTCAGCAGCGGCTGCGACTGGGGGCCAAACGCGCTGTG
AATAATGGGAGGTTACTGAAAGACGGACCGCAGTACAGGGTCAATTATGGGAGCTTAGAT
GGCAAAGGGGCACCTCAGTATCCCAGTGCATTCCCATCCTCGCTCCCACCTGTCAGCCTT
CTACCCCATGAGAAAGACCAGCCCCGTGCTGATCCCATTCCAATATGTAGCTTCTGTTTG
GGGACTAAAGAATCAAATCGTGAAAAGAAACCAGAAGAACTCCTCTCTTGTGCAGATTGT
GGCAGTAGTGGACACCCATCCTGTTTGAAATTTTGTCCTGAATTAACAACAAATGTAAAG
GCCTTAAGGTGGCAGTGCATCGAATGCAAGACATGCAGTGCCTGTAGAGTCCAAGGCAGA
AATGCTGATAATATGCTTTTTTGTGATTCCTGTGATAGAGGATTTCATATGGAATGCTGT
GACCCACCACTTTCCAGAATGCCAAAAGGGATGTGGATTTGCCAAGTCTGCAGACCAAAG
AAAAAGGGAAGAAAACTACTTCATGAGAAAGCTGCACAAATAAAACGACGATATGCAAAA
CCCATTGGACGACCGAAAAATAAATTAAAGCAACGATTGTTGTCTGTAACCAGTGATGAA
GGATCCATGAATGCATTCACAGGAAGGGGGTCACCTGGTAGGGGTCAAAAGACTAAAGTC
TGTACCACACCTTCATCTGGTCATGCTGCATCTGGGAAGGACTCAAGCAGCAGATTGGCT
GTTACAGACCCCACTCGGCCTGGTGCCACCACCAAAATCACCACCACCTCCACCTACATT
TCTGCCTCTACACTTAAAGTTAACAAGAAAACCAAAGGGCTCATTGATGGCCTTACTAAG
TTTTTTACACCATCACCTGATGGTCGCAGATCACGAGGTGAAATTATAGACTTTTCAAAG
CACTATCGTCCAAGGAAAAAGGTCTCTCAGAAACAGTCATGCACTTCTCATGTGTTGGCT
ACAGGTACCACACAAAAGCTAAAACCTCCACCTTCTTCACTTCCACCCCCAACCCCCATC
TCCGGTCAGAGCCCCAGTTCACAAAAGTCCAGCACGGCCACTTCTTCTCCCTCTCCCCAG
AGTTCTTCCAGCCAGTGCAGTGTGCCCTCCCTGAGCAGCCTTACCACTAACAGCCAGCTG
AAGGCACTCTTTGATGGGCTTTCTCATATCTATACCACTCAGGGACAGTCTCGCAAAAAG
GGACACCCGAGTTATGCACCACCCAAACGTATGCGTCGTAAAACTGAATTATCTTCCACG
GCAAAATCTAAAGCCCACTTCTTTGGCAAAAGAGATATTAGAAGTCGGTTTATTTCTCAC
TCCTCCTCCTCTAGCTGGGGGATGGCTAGAGGAAGTATTTTTAAAGCAATTGCTCACTTC
AAGCGAACAACTTTCCTTAAAAAGCACAGGATGCTAGGCAGATTAAAATATAAAGTGACC
CCTCAGATGGGGACCCCCTCACCAGGGAAGGGGAGCTTGACAGACGGAAGGATTAAACCT
GATCAGGATGATGATACTGAAATAAAAATAAACATCAAACAAGAAAGTGCAGATGTAAAT
GTGATTGGAAACAAGGATGTCGTTACTGAAGAGGATTTGGATGTTTTTAAGCAGGCCCAG
GAACTTTCTTGGGAGAAAATAGAGTGTGAGAGTGGGGTGGAAGACTGTGGCCGGTACCCT
TCTGTGATTGAATTTGGTAAATATGAAATCCAAACCTGGTACTCCTCGCCTTACCCACAG
GAATATGCAAGATTACCAAAGCTTTACCTGTGTGAATTCTGTCTTAAATATATGAAAAGT
AAAAATATTTTGCTAAGACACTCCAAGAAGTGTGGATGGTTTCATCCTCCAGCAAATGAA
ATTTACCGAAGGAAAGACCTTTCAGTATTTGAGGTTGATGGGAATATGAGCAAAATTTAT
TGCCAAAACCTTTGCTTGTTAGCCAAGCTCTTCCTGGACCACAAAACGTTGTATTATGAT
GTCGAGCCATTCCTTTTTTATGTCCTTACAAAAAATGATGAAAAGGGCTGTCATCTGGTT
GGATACTTCTCTAAGGAAAAGCTTTGCCAGCAGAAGTATAATGTCTCCTGCATAATGATC
ATGCCCCAGCACCAAAGGCAAGGATTTGGACGGTTTCTCATTGATTTCAGCTATTTGCTT
TCTAGAAGAGAAGGCCAAGCAGGGTCTCCTGAAAAGCCTCTCTCCGATCTGGGCCGTCTC
TCCTACCTGGCATATTGGAAGAGCGTCATCTTGGAGTATCTCTACCACCACCATGAGAGG
CACATCAGCATCAAGGCAATTAGCAGAGCGACGGGCATGTGCCCACATGACATTGCCACC
ACTCTGCAGCACCTCCACATGATCGACAAGAGAGATGGCAGATTTGTCATCATTAGACGG
GAAAAGTTGATATTGAGCCACATGGAAAAGCTGAAAACCTGTTCCAGAGCCAATGAACTT
GATCCAGACAGTCTGAGGTGGACCCCAATTTTAATTTCTAATGCTGCAGTGTCTGAAGAA
GAGCGAGAAGCTGAGAAAGAGGCTGAGCGGCTAATGGAACAAGCTAGCTGCTGGGAGAAG
GAGGAACAAGAAATCCTGTCAACTAGAGCTAACAGTAGGCAATCACCTGCAAAAGTACAA
TCGAAAAATAAATATTTGCATTCCCCGGAGAGCCGGCCAGTCACAGGGGAGCGAGGGCAG
CTGCTGGAGCTGTCTAAAGAGAGCAGTGAAGAAGAAGAGGAGGAGGAGGACGAGGAGGAG
GAAGAAGAGGAGGAAGAAGAGGAAGAGGATGAAGAGGAGGAAGAAGAGGAAGAAGAAGAA
GAAGAAGAAGAAAATATTCAAAGCTCTCCCCCAAGATTGACGAAACCACAGTCAGTTGCC
ATAAAGAGAAAGAGGCCTTTTGTACTAAAGAAGAAAAGGGGTCGTAAACGCAGGAGGATC
AACAGCAGTGTAACAACAGAGACCATTTCAGAGACGACAGAAGTACTGAATGAGCCCTTT
GACAACTCAGATGAAGAGAGGCCAATGCCACAGCTGGAGCCTACCTGTGAGATTGAAGTG
GAGGAAGATGGCAGGAAGCCAGTCCTGAGAAAAGCATTCCAGCATCAGCCTGGGAAGAAA
AGACAAACAGAGGAAGAGGAAGGAAAAGACAATCATTGCTTCAAGAATGCTGACCCTTGT
AGAAACAATATGAATGATGATTCAAGTAACTTGAAAGAAGGCAGTAAAGACAATCCCGAA
CCTCTAAAGTGCAAACAAGTGTGGCCAAAAGGAACAAAGCGCGGTCTATCTAAGTGGAGG
CAAAACAAAGAGAGGAAGACCGGATTTAAACTGAATTTGTACACCCCGCCAGAAACACCC
ATGGAGCCTGACGAGCAGGTAACAGTGGAAGAACAGAAGGAGACTTCAGAAGGAAAAACC
AGCCCCAGTCCCATCAGGATTGAGGAGGAGGTCAAGGAAACTGGGGAAGCCCTGTTGCCT
CAAGAGGAAAACAGAAGGGAAGAAACATGTGCCCCTGTAAGTCCAAACACATCACCAGGT
GAAAAACCAGAAGATGATCTCATCAAACCTGAGGAAGAGGAAGAGGAGGAGGAGGAGGAA
GAGGAAGAAGAGGAAGAAGAGGAAGGGGAAGAAGAAGAAGGAGGAGGAAATGTAGAAAAA
GATCCAGATGGTGCTAAAAGCCAAGAAAAAGAGGAACCAGAAATCTCCACGGAAAAAGAA
GACTCTGCACGTTTGGATGATCACGAAGAGGAGGAGGAAGAGGATGAAGAGCCATCCCAC
AACGAGGACCATGATGCCGATGACGAGGATGACAGCCACATGGAGTCTGCCGAAGTGGAG
AAGGAAGAGCTGCCCAGAGAAAGCTTCAAAGAAGTACTGGAAAACCAGGAGACTTTTTTA
GACCTTAATGTGCAGCCTGGTCACTCGAACCCAGAGGTCTTAATGGACTGTGGCGTCGAC
CTGACAGCTTCTTGTAACAGTGAGCCCAAGGAGCTTGCTGGGGACCCTGAAGCTGTACCC
GAATCTGACGAGGAGCCACCCCCAGGAGAACAGGCACAGAAGCAGGACCAAAAGAACAGC
AAGGAAGTCGATACAGAGTTCAAAGAGGGAAACCCAGCAACCATGGAAATCGACTCTGAG
ACTGTCCAGGCCGTTCAGTCTTTGACCCAGGAGAGCAGCGAACAGGACGACACCTTTCAG
GATTGTGCCGAGACTCAAGAGGCCTGTAGAAGCCTACAGAACTACACCCGTGCAGACCAA
AGTCCACAGATTGCCACCACGCTCGACGATTGCCAACAGTCGGACCACAGTAGCCCAGTT
TCATCCGTCCACTCCCATCCTGGCCAGTCCGTACGTTCTGTCAACAGCCCAAGTGTCCCT
GCTCTGGAAAACAGCTACGCCCAAATCAGCCCAGATCAAAGTGCCATCTCAGTGCCATCT
CTGCAGAACATGGAAACCAGTCCCATGATGGATGTCCCATCAGTTTCAGATCATTCACAG
CAAGTCGTAGACAGTGGATTTAGTGACCTGGGCAGTATCGAGAGCACAACTGAGAACTAC
GAAAACCCAAGCAGCTACGATTCTACTATGGGAGGCAGCATCTGTGGAAACGGCTCTTCA
CAGAACAGCTGCTCCTATAGCAACCTCACCTCCAGCAGTCTGACACAGAGCAGCTGTGCT
GTCACCCAGCAGATGTCCAACATCAGCGGGAGCTGCAGCATGCTGCAGCAAACCAGCATC
AGCTCCCCTCCGACCTGCAGCGTCAAGTCTCCTCAAGGCTGTGTGGTGGAGAGGCCTCCG
AGCAGCAGCCAGCAGCTGGCTCAGTGCAGCATGGCTGCTAACTTCACCCCACCCATGCAG
CTGGCTGAAATCCCCGAGACGAGCAACGCCAACATTGGCTTATACGAGCGAATGGGTCAG
AGTGATTTTGGGGCTGGGCATTACCCGCAGCCGTCAGCCACCTTCAGCCTTGCCAAACTG
CAGCAGTTAACTAATACACTTATTGATCATTCATTGCCTTACAGCCATTCCGCTGCTGTG
ACTTCCTATGCAAACAGTGCCTCTTTGTCCACACCATTAAGTAACACAGGGCTTGTTCAA
CTTTCTCAGTCTCCACACTCCGTCCCTGGGGGACCCCAAGCACAAGCTACCATGACCCCA
CCCCCCAACCTGACTCCTCCTCCAATGAATCTGCCGCCGCCTCTTTTGCAACGGAACATG
GCTGCATCAAATATTGGCATCTCTCACAGCCAAAGACTGCAAACCCAGATTGCCAGCAAG
GGCCACATCTCCATGAGAACCAAGTCAGCGTCTCTGTCACCAGCCGCTGCCACCCATCAG
TCACAAATCTATGGGCGCTCCCAGACTGTAGCCATGCAGGGTCCTGCACGGACTTTAACG
ATGCAAAGAGGCATGAACATGAGTGTGAACCTGATGCCAGCGCCAGCCTACAATGTCAAC
TCTGTGAACATGAACATGAACACTCTCAACGCCATGAATGGGTACAGCATGTCCCAGCCA
ATGATGAACAGTGGCTACCACAGCAATCATGGCTATATGAATCAAACGCCCCAATACCCT
ATGCAGATGCAGATGGGCATGATGGGCACCCAGCCATATGCCCAGCAGCCAATGCAGACC
CCACCCCACGGTAACATGATGTACACGGCCCCCGGACATCACGGCTACATGAACACAGGC
ATGTCCAAACAGTCTCTCAATGGCTCCTACATGAGAAGGTAG
|
| Enzyme 136 GenBank Gene ID |
NM_012330.2  |
| Enzyme 136 GeneCard ID |
MYST4  |
| Enzyme 136 GenAtlas ID |
MYST4  |
| Enzyme 136 HGNC ID |
HGNC:17582  |
| Enzyme 136 Chromosome Location |
1 |
| Enzyme 136 Locus |
10q22.2 |
| Enzyme 136 SNPs |
SNPJam Report  |
| Enzyme 136 General References |
- Champagne N, Bertos NR, Pelletier N, Wang AH, Vezmar M, Yang Y, Heng HH, Yang XJ: Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein. J Biol Chem. 1999 Oct 1;274(40):28528-36. [PubMed
]
- Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Panagopoulos I, Fioretos T, Isaksson M, Samuelsson U, Billstrom R, Strombeck B, Mitelman F, Johansson B: Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). Hum Mol Genet. 2001 Feb 15;10(4):395-404. [PubMed
]
- Pelletier N, Champagne N, Stifani S, Yang XJ: MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2. Oncogene. 2002 Apr 18;21(17):2729-40. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J: ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Ullah M, Pelletier N, Xiao L, Zhao SP, Wang K, Degerny C, Tahmasebi S, Cayrou C, Doyon Y, Goh SL, Champagne N, Cote J, Yang XJ: Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes. Mol Cell Biol. 2008 Nov;28(22):6828-43. Epub 2008 Sep 15. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 136 Metabolite References |
Not Available |
|
Enzyme 137
[top]
|
| Enzyme 137 ID |
15918 |
| Enzyme 137 Name |
MYST3 protein |
| Enzyme 137 Synonyms |
Not Available |
| Enzyme 137 Gene Name |
MYST3 |
| Enzyme 137 Protein Sequence |
>MYST3 protein
MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTI
LKVSNKGLNSYKDPDNPGRIALPKPRNHGKLDNKQNVDWNKLIKRAVEGLAESGGSTLKS
IERFLKGQKDVSALFGGSAASGFHQQLRLAIKRAIGHGRLLKDGPLYRLNTKATNVDGKE
SCESLSCLPPVSLLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPS
CLKFSPELTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRM
PKGMWICQICRPRKKGRKLLQKKAAQIKRRYTNPIGRPKNRLKKQNTVSKGPFSKVRTGP
GRGRKRKITLSSQSASSSSEEGYLERIDGLDFCRDSNVSLKFNKKTKGLIDGLTKFFTPS
PDGRKARGEVVDYSEQYRIRKRGNRKSSTSDWPTDNQDGWDGKQENEERLFGSQEIMTEK
DMELFRDIQEQALQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLC
EFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLF
LDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGR
FLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLT
GICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVI
VSNSVVSEEEEEEAEEGENEEPQCQERELEISVGKSVSHENKEQDSYSVESEKKPEVMAP
VSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYG
ECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKC
RLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRR
RRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELF
PREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEP
DTSTPLKKK
|
| Enzyme 137 Number of Residues |
1149 |
| Enzyme 137 Molecular Weight |
131768.3 |
| Enzyme 137 Theoretical pI |
8.54 |
| Enzyme 137 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- protein binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin organization
- chromosome organization
- nucleosome assembly
- nucleosome organization
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
|
| Component |
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- nucleosome
- nucleus
- organelle
- protein-DNA complex
|
|
| Enzyme 137 General Function |
Involved in DNA binding |
| Enzyme 137 Specific Function |
Not Available |
| Enzyme 137 Pathways |
Not Available |
| Enzyme 137 Reactions |
Not Available |
| Enzyme 137 Pfam Domain Function |
|
| Enzyme 137 Signals |
|
| Enzyme 137 Transmembrane Regions |
|
| Enzyme 137 Essentiality |
Not Available |
| Enzyme 137 GenBank ID Protein |
148745647  |
| Enzyme 137 UniProtKB/Swiss-Prot ID |
A5PKX7  |
| Enzyme 137 UniProtKB/Swiss-Prot Entry Name |
A5PKX7_HUMAN  |
| Enzyme 137 PDB ID |
Not Available |
| Enzyme 137 Cellular Location |
Not Available |
| Enzyme 137 Gene Sequence |
>3449 bp
ATGGTAAAACTCGCAAACCCGCTTTATACTGAGTGGATTTTGGAGGCCATCAAAAAAGTG
AAAAAGCAGAAACAGCGTCCTTCAGAAGAAAGGATATGCAATGCTGTGTCTTCATCCCAT
GGCTTGGATCGTAAAACTGTTTTAGAACAATTGGAGTTGAGTGTTAAAGATGGAACAATT
TTAAAAGTCTCAAATAAAGGACTCAATTCCTATAAAGATCCTGATAATCCTGGGCGAATA
GCACTTCCTAAGCCTCGGAACCATGGAAAATTGGATAATAAACAAAATGTGGATTGGAAT
AAACTGATAAAGCGGGCAGTTGAGGGCTTGGCAGAGTCTGGTGGCTCAACTTTGAAAAGC
ATTGAACGTTTTTTGAAAGGTCAGAAGGATGTGTCTGCATTATTCGGAGGCAGTGCTGCC
TCTGGCTTTCACCAGCAGTTACGATTGGCTATCAAACGTGCCATTGGCCACGGCAGACTC
CTTAAAGATGGACCTCTTTATCGGCTCAACACTAAAGCAACCAACGTGGATGGGAAAGAG
AGTTGTGAGTCTCTTTCCTGTTTACCTCCAGTGTCCCTTCTTCCACATGAAAAGGATAAG
CCGGTTGCTGAACCAATCCCCATCTGTAGTTTCTGTCTTGGTACAAAAGAACAAAACCGA
GAAAAGAAGCCAGAGGAACTCATCTCCTGTGCCGACTGTGGCAACAGTGGCCATCCATCC
TGTTTAAAGTTTTCCCCTGAACTAACGGTTCGAGTGAAGGCCTTACGGTGGCAGTGCATC
GAGTGTAAAACATGCAGCTCCTGTCGAGATCAAGGCAAAAATGCGGATAACATGCTCTTT
TGTGATTCATGTGACCGAGGTTTTCACATGGAGTGTTGTGATCCGCCACTCACCCGTATG
CCAAAAGGCATGTGGATATGTCAAATATGTCGACCTAGGAAAAAAGGACGAAAACTTCTA
CAAAAGAAGGCAGCACAGATAAAACGGCGCTATACTAATCCAATAGGACGTCCAAAAAAC
AGGTTAAAGAAACAAAACACGGTATCAAAAGGTCCCTTCAGCAAAGTTCGAACTGGCCCT
GGAAGGGGTAGGAAACGAAAAATCACTCTTTCCAGCCAATCAGCATCATCATCATCAGAA
GAAGGATATTTAGAGCGGATAGATGGCTTGGACTTCTGCAGAGATAGCAATGTCTCCTTG
AAGTTCAACAAGAAAACCAAAGGGCTCATTGATGGCCTTACCAAATTTTTTACCCCTTCC
CCTGATGGGCGGAAAGCTCGGGGGGAAGTGGTGGACTACTCTGAGCAATATCGAATCAGA
AAGAGGGGCAACAGGAAATCAAGCACTTCAGATTGGCCCACAGACAATCAGGATGGCTGG
GATGGCAAACAAGAAAATGAGGAGCGACTTTTTGGGAGCCAGGAAATCATGACTGAGAAA
GATATGGAATTATTTCGTGATATCCAAGAACAAGCACTGCAGAAAGTTGGAGTGACTGGT
CCCCCTGATCCACAAGTCCGCTGTCCCTCTGTCATTGAGTTTGGGAAGTATGAAATTCAC
ACCTGGTACTCCTCCCCATATCCTCAAGAATACTCAAGGCTGCCCAAATTGTATCTTTGT
GAATTTTGTCTAAAATATATGAAAAGTAGAACTATTCTGCAGCAGCACATGAAGAAATGT
GGTTGGTTCCATCCTCCTGCCAATGAGATTTACAGAAAGAATAATATTTCTGTCTTTGAG
GTTGATGGGAATGTGAGTACCATTTATTGTCAAAACCTGTGTCTTTTGGCAAAGTTGTTT
CTTGACCACAAAACCCTCTATTACGATGTGGAGCCATTTCTTTTTTATGTACTAACACAG
AATGATGTCAAGGGCTGCCACCTTGTTGGCTACTTTTCTAAGGAAAAGCACTGCCAACAG
AAGTACAATGTTTCCTGTATAATGATTCTTCCTCAATACCAGCGTAAGGGCTATGGCAGG
TTTCTCATCGATTTCAGTTATTTGTTATCAAAGCGTGAAGGCCAAGCAGGGTCTCCAGAG
AAACCGTTATCTGATCTGGGTCGTCTTTCCTACATGGCATATTGGAAAAGTGTAATATTG
GAGTGCCTTTATCACCAAAATGACAAGCAGATCAGCATTAAGAAGTTAAGCAAGTTGACT
GGAATCTGCCCTCAAGACATCACTTCCACACTCCACCACCTACGAATGCTGGACTTCCGT
AGTGACCAATTTGTGATTATCCGCCGGGAAAAACTTATCCAGGATCACATGGCAAAGCTT
CAGCTGAATTTGCGACCTGTAGATGTAGATCCAGAATGTTTGCGCTGGACTCCAGTCATA
GTGTCCAACTCTGTGGTCTCAGAGGAGGAAGAAGAGGAGGCTGAGGAAGGAGAAAACGAA
GAGCCACAGTGCCAGGAAAGAGAATTAGAGATCAGTGTGGGAAAGTCTGTGTCTCATGAG
AACAAAGAACAAGATTCTTATTCAGTAGAAAGTGAAAAGAAACCAGAAGTTATGGCTCCA
GTCAGTTCTACACGTTTGAGCAAACAAGTCCTTCCTCATGATAGTCTTCCTGCAAATAGC
CAGCCATCTCGGAGGGGCCGCTGGGGGAGGAAGAACAGAAAAACCCAGGAACGTTTTGGT
GATAAAGATTCTAAACTGCTCTTGGAAGAGACGTCTTCAGCTCCTCAGGAACAATATGGA
GAATGTGGGGAGAAATCAGAAGCCACCCAGGAACAATACACTGAAAGTGAAGAACAGCTG
GTGGCTTCTGAGGAGCAGCCAAGCCAGGACGGGAAACCTGACCTTCCCAAGAGAAGACTC
AGTGAGGGGGTTGAGCCCTGGCGAGGACAGCTCAAGAAAAGCCCTGAGGCTCTGAAGTGC
AGATTAACAGAAGGAAGTGAGAGGCTGCCCCGTCGCTACAGTGAGGGTGACAGGGCTGTC
CTCAGGGGCTTCAGTGAGAGCAGCGAGGAGGAGGAGGAGCCGGAAAGCCCTCGGTCAAGC
TCGCCACCAATTCTCACAAAGCCCACGCTGAAGCGAAAGAAACCATTTCTCCACCGAAGG
AGGAGAGTCCGAAAGCGCAAACACCACAATAGCAGTGTAGTCACAGAAACTATTTCTGAG
ACCACTGAAGTGTTAGATGAACCTTTTGAAGATTCTGACTCCGAGAGGCCAATGCCAAGA
TTAGAACCCACGTTTGAGATCGATGAAGAAGAGGAGGAAGAGGATGAAAATGAACTTTTC
CCTAGAGAATACTTCCGTCGTTTGTCTTCGCAGGATGTACTCAGGTGTCAGTCCTCTTCT
AAGAGGAAGTCTAAAGATGAAGAAGAAGATGAAGAGTCAGATGATGCTGATGACACTCCT
ATCTTAAAGCCAGTATCTCTTTTGCGAAAACGTGATGTGAAGAATTCTCCTCTTGAGCCA
GATACATCCACACCTTTGAAAAAAAAAAA
|
| Enzyme 137 GenBank Gene ID |
BC142659  |
| Enzyme 137 GeneCard ID |
MYST3  |
| Enzyme 137 GenAtlas ID |
MYST3  |
| Enzyme 137 HGNC ID |
HGNC:13013  |
| Enzyme 137 Chromosome Location |
8 |
| Enzyme 137 Locus |
8p11 |
| Enzyme 137 SNPs |
SNPJam Report  |
| Enzyme 137 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 137 Metabolite References |
Not Available |
|
Enzyme 138
[top]
|
| Enzyme 138 ID |
15919 |
| Enzyme 138 Name |
Nuclear receptor coactivator 3 (Nuclear receptor coactivator 3, isoform CRA_g) |
| Enzyme 138 Synonyms |
Not Available |
| Enzyme 138 Gene Name |
NCOA3 |
| Enzyme 138 Protein Sequence |
>Nuclear receptor coactivator 3 (Nuclear receptor coactivator 3, isoform CRA_g)
MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDID
NFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQA
LDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNG
VSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGE
DLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRC
IQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDR
HGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLA
DPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNI
MISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLST
LSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKE
SSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVS
SSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGN
VVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQE
KDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLK
SSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGS
SMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPT
LPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQV
SHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPE
LVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMN
QMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTA
GGAAVMRPMMQPQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQ
QQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQ
|