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Enzyme 1
[top]
|
| Enzyme 1 ID |
5235 |
| Enzyme 1 Name |
Deoxycytidine kinase |
| Enzyme 1 Synonyms |
- dCK
|
| Enzyme 1 Gene Name |
DCK |
| Enzyme 1 Protein Sequence |
>Deoxycytidine kinase
MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL
|
| Enzyme 1 Number of Residues |
260 |
| Enzyme 1 Molecular Weight |
30518.3 |
| Enzyme 1 Theoretical pI |
4.88 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in ATP binding |
| Enzyme 1 Specific Function |
Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- NTP + deoxycytidine = NDP + dCMP [RN:R02321]
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| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P27707  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DCK_HUMAN |
| Enzyme 1 PDB ID |
1P62 |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>783 bp
ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA
|
| Enzyme 1 GenBank Gene ID |
M60527 |
| Enzyme 1 GeneCard ID |
DCK |
| Enzyme 1 GenAtlas ID |
DCK |
| Enzyme 1 HGNC ID |
HGNC:2704 |
| Enzyme 1 Chromosome Location |
4 |
| Enzyme 1 Locus |
4q13.3-q21.1 |
| Enzyme 1 SNPs |
SNPJam Report |
| Enzyme 1 General References |
- Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [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 ]
- Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed ]
- Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [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 ]
- Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A: Structure of human dCK suggests strategies to improve anticancer and antiviral therapy. Nat Struct Biol. 2003 Jul;10(7):513-9. [PubMed ]
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| Enzyme 1 Metabolite References |
Not Available |
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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
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| 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
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| 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 |
5247 |
| Enzyme 3 Name |
Acetyl-CoA carboxylase 2 |
| Enzyme 3 Synonyms |
- ACC-beta
- Biotin carboxylase
|
| Enzyme 3 Gene Name |
ACACB |
| Enzyme 3 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 3 Number of Residues |
2458 |
| Enzyme 3 Molecular Weight |
276538.6 |
| Enzyme 3 Theoretical pI |
6.46 |
| Enzyme 3 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 3 General Function |
Involved in acetyl-CoA carboxylase activity |
| Enzyme 3 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 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
134142062 |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O00763 |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ACACB_HUMAN |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 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 3 GenBank Gene ID |
NM_001093.3 |
| Enzyme 3 GeneCard ID |
ACACB |
| Enzyme 3 GenAtlas ID |
ACACB |
| Enzyme 3 HGNC ID |
HGNC:85 |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
12q24.11 |
| Enzyme 3 SNPs |
SNPJam Report |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5248 |
| Enzyme 4 Name |
Pyruvate carboxylase, mitochondrial |
| Enzyme 4 Synonyms |
- Pyruvic carboxylase
- PCB
|
| Enzyme 4 Gene Name |
PC |
| Enzyme 4 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 4 Number of Residues |
1178 |
| Enzyme 4 Molecular Weight |
129632.6 |
| Enzyme 4 Theoretical pI |
6.83 |
| Enzyme 4 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 4 General Function |
Involved in catalytic activity |
| Enzyme 4 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 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate [RN:R00344]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
458236 |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P11498 |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PYC_HUMAN |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 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 4 GenBank Gene ID |
U04641 |
| Enzyme 4 GeneCard ID |
PC |
| Enzyme 4 GenAtlas ID |
PC |
| Enzyme 4 HGNC ID |
HGNC:8636 |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
11q13.4-q13.5 |
| Enzyme 4 SNPs |
SNPJam Report |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5271 |
| Enzyme 5 Name |
Acetyl-coenzyme A synthetase 2-like, mitochondrial |
| Enzyme 5 Synonyms |
- Acetate--CoA ligase 2
- Acetyl-CoA synthetase 2
- AceCS2
- Acyl-CoA synthetase short-chain family member 1
|
| Enzyme 5 Gene Name |
ACSS1 |
| Enzyme 5 Protein Sequence |
>Acetyl-coenzyme A synthetase 2-like, mitochondrial
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
|
| Enzyme 5 Number of Residues |
689 |
| Enzyme 5 Molecular Weight |
74856.1 |
| Enzyme 5 Theoretical pI |
7.11 |
| Enzyme 5 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 5 General Function |
Involved in acetate-CoA ligase activity |
| Enzyme 5 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 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA [RN:R00235]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
24659677 |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9NUB1 |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ACS2L_HUMAN |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 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 5 GenBank Gene ID |
BC039261 |
| Enzyme 5 GeneCard ID |
ACSS1 |
| Enzyme 5 GenAtlas ID |
ACSS1 |
| Enzyme 5 HGNC ID |
HGNC:16091 |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
20p11.23-p11.21 |
| Enzyme 5 SNPs |
SNPJam Report |
| Enzyme 5 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5276 |
| Enzyme 6 Name |
Acetyl-CoA carboxylase 1 |
| Enzyme 6 Synonyms |
- ACC-alpha
- Biotin carboxylase
|
| Enzyme 6 Gene Name |
ACACA |
| Enzyme 6 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 6 Number of Residues |
2346 |
| Enzyme 6 Molecular Weight |
265551.7 |
| Enzyme 6 Theoretical pI |
6.32 |
| Enzyme 6 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 6 General Function |
Involved in acetyl-CoA carboxylase activity |
| Enzyme 6 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 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA [RN:R00742]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
38679967 |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q13085 |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ACACA_HUMAN |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 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 6 GenBank Gene ID |
NM_198836.1 |
| Enzyme 6 GeneCard ID |
ACACA |
| Enzyme 6 GenAtlas ID |
ACACA |
| Enzyme 6 HGNC ID |
HGNC:84 |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
17q21 |
| Enzyme 6 SNPs |
SNPJam Report |
| Enzyme 6 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5312 |
| Enzyme 7 Name |
Thymidylate kinase |
| Enzyme 7 Synonyms |
- dTMP kinase
|
| Enzyme 7 Gene Name |
DTYMK |
| Enzyme 7 Protein Sequence |
>Thymidylate kinase
MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK
|
| Enzyme 7 Number of Residues |
212 |
| Enzyme 7 Molecular Weight |
23819.1 |
| Enzyme 7 Theoretical pI |
8.49 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- thymidylate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- dTDP biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- pyrimidine deoxyribonucleoside diphosphate biosynthetic process
- pyrimidine nucleoside diphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in thymidylate kinase activity |
| Enzyme 7 Specific Function |
Catalyzes the conversion of dTMP to dTDP |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- ATP + dTMP = ADP + dTDP [RN:R02094]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
37206 |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P23919 |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
KTHY_HUMAN |
| Enzyme 7 PDB ID |
1E9A |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>636 bp
ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA
|
| Enzyme 7 GenBank Gene ID |
X54729 |
| Enzyme 7 GeneCard ID |
DTYMK |
| Enzyme 7 GenAtlas ID |
DTYMK |
| Enzyme 7 HGNC ID |
HGNC:3061 |
| Enzyme 7 Chromosome Location |
2 |
| Enzyme 7 Locus |
2q37.3 |
| Enzyme 7 SNPs |
SNPJam Report |
| Enzyme 7 General References |
- Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed ]
- Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [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 ]
- 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 ]
- Ostermann N, Segura-Pena D, Meier C, Veit T, Monnerjahn C, Konrad M, Lavie A: Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds. Biochemistry. 2003 Mar 11;42(9):2568-77. [PubMed ]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5313 |
| Enzyme 8 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 8 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase 1
- Ecto-ATPDase 1
- Ecto-ATPase 1
- Ecto-apyrase
- Lymphoid cell activation antigen
- CD39 antigen
|
| Enzyme 8 Gene Name |
ENTPD1 |
| Enzyme 8 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 8 Number of Residues |
510 |
| Enzyme 8 Molecular Weight |
57964.1 |
| Enzyme 8 Theoretical pI |
6.29 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in hydrolase activity |
| Enzyme 8 Specific Function |
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
45580700 |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P49961 |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
|
| Enzyme 8 GenBank Gene ID |
NM_001776.5 |
| Enzyme 8 GeneCard ID |
ENTPD1 |
| Enzyme 8 GenAtlas ID |
ENTPD1 |
| Enzyme 8 HGNC ID |
HGNC:3363 |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
10q24 |
| Enzyme 8 SNPs |
SNPJam Report |
| Enzyme 8 General References |
- Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed ]
- Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed ]
- Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [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 ]
- Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed ]
- Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed ]
- Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed ]
- Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed ]
- Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed ]
- Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5314 |
| Enzyme 9 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 9 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative MAPK-activating protein PM09
- Putative NF-kappa-B-activating protein 107
|
| Enzyme 9 Gene Name |
CANT1 |
| Enzyme 9 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 9 Number of Residues |
401 |
| Enzyme 9 Molecular Weight |
44839.2 |
| Enzyme 9 Theoretical pI |
5.98 |
| Enzyme 9 GO Classification |
| Function |
- binding
- calcium ion 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
- metal ion binding
- pyrophosphatase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in calcium ion binding |
| Enzyme 9 Specific Function |
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
229577440 |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q8WVQ1 |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN |
| Enzyme 9 PDB ID |
1S1D |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1206 bp
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
|
| Enzyme 9 GenBank Gene ID |
NM_001159772.1 |
| Enzyme 9 GeneCard ID |
CANT1 |
| Enzyme 9 GenAtlas ID |
CANT1 |
| Enzyme 9 HGNC ID |
HGNC:19721 |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
17q25.3 |
| Enzyme 9 SNPs |
SNPJam Report |
| Enzyme 9 General References |
- Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed ]
- Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [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 ]
- Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed ]
- Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed ]
- Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed ]
- Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed ]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5317 |
| Enzyme 10 Name |
Thymidine kinase, cytosolic |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
TK1 |
| Enzyme 10 Protein Sequence |
>Thymidine kinase, cytosolic
MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTR
YSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVI
VAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADK
YHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN
|
| Enzyme 10 Number of Residues |
234 |
| Enzyme 10 Molecular Weight |
25469 |
| Enzyme 10 Theoretical pI |
8.61 |
| Enzyme 10 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- deoxynucleoside kinase activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- nucleotide binding
- purine nucleotide binding
- thymidine kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Nucleotide transport and metabolism |
| Enzyme 10 Specific Function |
ATP + thymidine = ADP + thymidine 5'- phosphate |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- ATP + thymidine = ADP + thymidine 5'-phosphate
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
339709 |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P04183 |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
KITH_HUMAN |
| Enzyme 10 PDB ID |
1XBT |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>705 bp
ATGAGCTGCATTAACCTGCCCACTGTGCTGCCCGGCTCCCCCAGCAAGACCCGGGGGCAG
ATCCAGGTGATTCTCGGGCCGATGTTCTCAGGAAAAAGCACAGAGTTGATGAGACGCGTC
CGTCGCTTCCAGATTGCTCAGTACAAGTGCCTGGTGATCAAGTATGCCAAAGACACTCGC
TACAGCAGCAGCTTCTGCACACATGACCGGAACACCATGGAGGCGCTGCCCGCCTGCCTG
CTCCGAGACGTGGCCCAGGAGGCCCTGGGCGTGGCTGTCATAGGCATCGACGAGGGGCAG
TTTTTCCCTGACATCATGGAGTTCTGCGAGGCCATGGCCAACGCCGGGAAGACCGTAATT
GTGGCTGCACTGGATGGGACCTTCCAGAGGAAGCCATTTGGGGCCATCCTGAACCTGGTG
CCGCTGGCCGAGAGCGTGGTGAAGCTGACGGCGGTGTGCATGGAGTGCTTCCGGGAAGCC
GCCTATACCAAGAGGCTCGGCACAGAGAAGGAGGTCGAGGTGATTGGGGGAGCAGACAAG
TACCACTCCGTGTGTCGGCTCTGCTACTTCAAGAAGGCCTCAGGCCAGCCTGCCGGGCCG
GACAACAAAGAGAACTGCCCAGTGCCAGGAAAGCCAGGGGAAGCCGTGGCTGCCAGGAAG
CTCTTTGCCCCACAGCAGATTCTGCAATGCAGCCCTGCCAACTGA
|
| Enzyme 10 GenBank Gene ID |
K02581 |
| Enzyme 10 GeneCard ID |
TK1 |
| Enzyme 10 GenAtlas ID |
TK1 |
| Enzyme 10 HGNC ID |
HGNC:11830 |
| Enzyme 10 Chromosome Location |
17 |
| Enzyme 10 Locus |
17q23.2-q25.3 |
| Enzyme 10 SNPs |
SNPJam Report |
| Enzyme 10 General References |
- Bradshaw HD Jr, Deininger PL: Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol. 1984 Nov;4(11):2316-20. [PubMed ]
- Flemington E, Bradshaw HD Jr, Traina-Dorge V, Slagel V, Deininger PL: Sequence, structure and promoter characterization of the human thymidine kinase gene. Gene. 1987;52(2-3):267-77. [PubMed ]
- Chang ZF, Huang DY, Chi LM: Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J Biol Chem. 1998 May 15;273(20):12095-100. [PubMed ]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5318 |
| Enzyme 11 Name |
Ectonucleoside triphosphate diphosphohydrolase 3 |
| Enzyme 11 Synonyms |
- NTPDase 3
- CD39 antigen-like 3
- Ecto-ATP diphosphohydrolase 3
- Ecto-ATPDase 3
- Ecto-ATPase 3
- Ecto-apyrase 3
- HB6
|
| Enzyme 11 Gene Name |
ENTPD3 |
| Enzyme 11 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 11 Number of Residues |
529 |
| Enzyme 11 Molecular Weight |
59104.8 |
| Enzyme 11 Theoretical pI |
6.40 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in hydrolase activity |
| Enzyme 11 Specific Function |
Has a threefold preference for the hydrolysis of ATP over ADP |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
13817037 |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
O75355 |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
ENTP3_HUMAN |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
|
| Enzyme 11 GenBank Gene ID |
AF034840 |
| Enzyme 11 GeneCard ID |
ENTPD3 |
| Enzyme 11 GenAtlas ID |
ENTPD3 |
| Enzyme 11 HGNC ID |
HGNC:3365 |
| Enzyme 11 Chromosome Location |
3 |
| Enzyme 11 Locus |
3p21.3 |
| Enzyme 11 SNPs |
SNPJam Report |
| Enzyme 11 General References |
- Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed ]
- Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [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 ]
- Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed ]
- Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed ]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5321 |
| Enzyme 12 Name |
Serum paraoxonase/lactonase 3 |
| Enzyme 12 Synonyms |
Not Available |
| Enzyme 12 Gene Name |
PON3 |
| Enzyme 12 Protein Sequence |
>Serum paraoxonase/lactonase 3
MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL
|
| Enzyme 12 Number of Residues |
354 |
| Enzyme 12 Molecular Weight |
39607.2 |
| Enzyme 12 Theoretical pI |
5.10 |
| Enzyme 12 GO Classification |
| Function |
- arylesterase activity
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
|
|
| Enzyme 12 General Function |
Involved in arylesterase activity |
| Enzyme 12 Specific Function |
Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol [RN:R03979]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
29788996 |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q15166 |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PON3_HUMAN |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1065 bp
ATGGGGAAGCTCGTGGCGCTGGTCCTGCTGGGGGTCGGCCTGTCCTTAGTCGGGGAGATG
TTCCTGGCGTTTAGAGAAAGGGTGAATGCCTCTCGAGAAGTGGAGCCAGTAGAACCTGAA
AACTGCCACCTTATTGAGGAACTTGAAAGTGGCTCTGAAGATATTGATATACTTCCTAGT
GGGCTGGCTTTTATCTCCAGTGGATTAAAATATCCAGGCATGCCAAACTTTGCGCCAGAT
GAACCAGGAAAAATCTTCTTGATGGATCTGAATGAACAAAACCCAAGGGCACAAGCGCTA
GAAATCAGTGGTGGATTTGACAAAGAATTATTTAATCCACATGGGATCAGTATTTTCATC
GACAAAGACAATACTGTGTATCTTTATGTTGTGAATCATCCCCACATGAAGTCCACTGTG
GAGATATTTAAATTTGAGGAACAACAACGTTCTCTGGTATACCTGAAAACTATAAAACAT
GAACTTCTCAAAAGTGTGAATGACATTGTGGTTCTTGGACCAGAACAGTTCTATGCCACC
AGAGACCACTATTTTACCAACTCCCTCCTGTCATTTTTTGAGATGATCTTGGATCTTCGC
TGGACTTATGTTCTTTTCTACAGCCCAAGGGAGGTTAAAGTGGTGGCCAAAGGATTTTGT
AGTGCCAATGGGATCACAGTCTCAGCAGACCAGAAGTATGTCTATGTAGCTGATGTAGCA
GCTAAGAACATTCACATAATGGAAAAACATGATAACTGGGATTTAACTCAACTGAAGGTG
ATACAGTTGGGCACCTTAGTGGATAACCTGACTGTCGATCCTGCCACAGGAGACATTTTG
GCAGGATGCCATCCTAATCCTATGAAGCTACTGAACTATAACCCTGAGGACCCTCCAGGA
TCAGAAGTACTTCGCATCCAGAATGTTTTGTCTGAGAAGCCCAGGGTGAGCACCGTGTAT
GCCAACAATGGCTCTGTGCTTCAGGGCACCTCTGTGGCTTCTGTGTACCATGGGAAAATT
CTCATAGGCACCGTATTTCACAAAACTCTGTACTGTGAGCTCTAG
|
| Enzyme 12 GenBank Gene ID |
NM_000940.2 |
| Enzyme 12 GeneCard ID |
PON3 |
| Enzyme 12 GenAtlas ID |
PON3 |
| Enzyme 12 HGNC ID |
HGNC:9206 |
| Enzyme 12 Chromosome Location |
7 |
| Enzyme 12 Locus |
7q21.3 |
| Enzyme 12 SNPs |
SNPJam Report |
| Enzyme 12 General References |
- 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 ]
- 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 ]
- Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed ]
- Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN: Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res. 2005 Jun;46(6):1239-47. Epub 2005 Mar 16. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [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 |
5338 |
| Enzyme 13 Name |
Nucleoside diphosphate kinase, mitochondrial |
| Enzyme 13 Synonyms |
- NDK
- NDP kinase, mitochondrial
- Nucleoside diphosphate kinase D
- NDPKD
- nm23-H4
|
| Enzyme 13 Gene Name |
NME4 |
| Enzyme 13 Protein Sequence |
>Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
|
| Enzyme 13 Number of Residues |
187 |
| Enzyme 13 Molecular Weight |
20658.5 |
| Enzyme 13 Theoretical pI |
10.75 |
| Enzyme 13 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 13 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
14336697 |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O00746 |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
NDKM_HUMAN |
| Enzyme 13 PDB ID |
1EHW |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
|
| Enzyme 13 GenBank Gene ID |
AE006463 |
| Enzyme 13 GeneCard ID |
NME4 |
| Enzyme 13 GenAtlas ID |
NME4 |
| Enzyme 13 HGNC ID |
HGNC:7852 |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
16p13.3 |
| Enzyme 13 SNPs |
SNPJam Report |
| Enzyme 13 General References |
- Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed ]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [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 ]
- Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [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 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5340 |
| Enzyme 14 Name |
Ribonucleoside-diphosphate reductase large subunit |
| Enzyme 14 Synonyms |
- Ribonucleoside-diphosphate reductase subunit M1
- Ribonucleotide reductase large subunit
|
| Enzyme 14 Gene Name |
RRM1 |
| Enzyme 14 Protein Sequence |
>Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
|
| Enzyme 14 Number of Residues |
792 |
| Enzyme 14 Molecular Weight |
90069.4 |
| Enzyme 14 Theoretical pI |
7.16 |
| Enzyme 14 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
- protein binding
- purine nucleoside binding
- ribonucleoside-diphosphate reductase activity
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
- oxidation reduction
|
| Component |
- macromolecular complex
- protein complex
- ribonucleoside-diphosphate reductase complex
|
|
| Enzyme 14 General Function |
Involved in oxidation reduction |
| Enzyme 14 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
36065 |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P23921 |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
RIR1_HUMAN |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>2379 bp
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
|
| Enzyme 14 GenBank Gene ID |
X59543 |
| Enzyme 14 GeneCard ID |
RRM1 |
| Enzyme 14 GenAtlas ID |
RRM1 |
| Enzyme 14 HGNC ID |
HGNC:10451 |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
11p15.5 |
| Enzyme 14 SNPs |
SNPJam Report |
| Enzyme 14 General References |
- Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed ]
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
- Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [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 ]
- Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed ]
- Harrington JA, Spector T: Human ribonucleotide reductase. Activation and inhibition by analogs of ATP. Biochem Pharmacol. 1991 Jul 25;42(4):759-63. [PubMed ]
- Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed ]
- Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 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 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5341 |
| Enzyme 15 Name |
Nucleoside diphosphate kinase A |
| Enzyme 15 Synonyms |
- NDK A
- NDP kinase A
- Granzyme A-activated DNase
- GAAD
- Metastasis inhibition factor nm23
- Tumor metastatic process-associated protein
- nm23-H1
|
| Enzyme 15 Gene Name |
NME1 |
| Enzyme 15 Protein Sequence |
>Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
|
| Enzyme 15 Number of Residues |
152 |
| Enzyme 15 Molecular Weight |
17148.6 |
| Enzyme 15 Theoretical pI |
6.11 |
| Enzyme 15 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 15 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
4557797 |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P15531 |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
NDKA_HUMAN |
| Enzyme 15 PDB ID |
1JXV |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
|
| Enzyme 15 GenBank Gene ID |
NM_000269.2 |
| Enzyme 15 GeneCard ID |
NME1 |
| Enzyme 15 GenAtlas ID |
NME1 |
| Enzyme 15 HGNC ID |
HGNC:7849 |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
17q21.3 |
| Enzyme 15 SNPs |
SNPJam Report |
| Enzyme 15 General References |
- Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed ]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed ]
- Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed ]
- Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed ]
- Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [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, 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 ]
- Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed ]
- MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed ]
- Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed ]
- Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed ]
- Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed ]
- Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed ]
- Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [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 ]
- Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed ]
- Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed ]
- Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed ]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5342 |
| Enzyme 16 Name |
Nucleoside diphosphate kinase 7 |
| Enzyme 16 Synonyms |
- NDK 7
- NDP kinase 7
- nm23-H7
|
| Enzyme 16 Gene Name |
NME7 |
| Enzyme 16 Protein Sequence |
>Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
|
| Enzyme 16 Number of Residues |
376 |
| Enzyme 16 Molecular Weight |
42491.4 |
| Enzyme 16 Theoretical pI |
6.44 |
| Enzyme 16 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 16 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
4960169 |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9Y5B8 |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
NDK7_HUMAN |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
|
| Enzyme 16 GenBank Gene ID |
AF153191 |
| Enzyme 16 GeneCard ID |
NME7 |
| Enzyme 16 GenAtlas ID |
NME7 |
| Enzyme 16 HGNC ID |
HGNC:20461 |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
1q24 |
| Enzyme 16 SNPs |
SNPJam Report |
| Enzyme 16 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 ]
- 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 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5343 |
| Enzyme 17 Name |
Ribonucleoside-diphosphate reductase subunit M2 |
| Enzyme 17 Synonyms |
- Ribonucleotide reductase small chain
- Ribonucleotide reductase small subunit
|
| Enzyme 17 Gene Name |
RRM2 |
| Enzyme 17 Protein Sequence |
>Ribonucleoside-diphosphate reductase subunit M2
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
|
| Enzyme 17 Number of Residues |
389 |
| Enzyme 17 Molecular Weight |
44877.2 |
| Enzyme 17 Theoretical pI |
5.05 |
| Enzyme 17 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
- ribonucleoside-diphosphate reductase activity
- transition metal ion binding
|
| Process |
- cellular nitrogen compound metabolic process
- deoxyribonucleoside diphosphate 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
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in oxidoreductase activity |
| Enzyme 17 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
36155 |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P31350 |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
RIR2_HUMAN |
| Enzyme 17 PDB ID |
1H0N |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
|
| Enzyme 17 GenBank Gene ID |
X59618 |
| Enzyme 17 GeneCard ID |
RRM2 |
| Enzyme 17 GenAtlas ID |
RRM2 |
| Enzyme 17 HGNC ID |
HGNC:10452 |
| Enzyme 17 Chromosome Location |
2 |
| Enzyme 17 Locus |
2p25-p24 |
| Enzyme 17 SNPs |
SNPJam Report |
| Enzyme 17 General References |
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
- Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5344 |
| Enzyme 18 Name |
Nucleoside diphosphate kinase B |
| Enzyme 18 Synonyms |
- NDK B
- NDP kinase B
- C-myc purine-binding transcription factor PUF
- nm23-H2
|
| Enzyme 18 Gene Name |
NME2 |
| Enzyme 18 Protein Sequence |
>Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
|
| Enzyme 18 Number of Residues |
152 |
| Enzyme 18 Molecular Weight |
17297.9 |
| Enzyme 18 Theoretical pI |
8.69 |
| Enzyme 18 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 18 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752) |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
4467843 |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P22392 |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
NDKB_HUMAN |
| Enzyme 18 PDB ID |
1NSK |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
|
| Enzyme 18 GenBank Gene ID |
X58965 |
| Enzyme 18 GeneCard ID |
NME2 |
| Enzyme 18 GenAtlas ID |
NME2 |
| Enzyme 18 HGNC ID |
HGNC:7850 |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
17q21.3 |
| Enzyme 18 SNPs |
SNPJam Report |
| Enzyme 18 General References |
- Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed ]
- Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed ]
- Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed ]
- Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [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 ]
- Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed ]
- Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [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 ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [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 ]
- Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed ]
- Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed ]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5345 |
| Enzyme 19 Name |
Nucleoside diphosphate kinase 3 |
| Enzyme 19 Synonyms |
- NDK 3
- NDP kinase 3
- DR-nm23
- Nucleoside diphosphate kinase C
- NDPKC
- nm23-H3
|
| Enzyme 19 Gene Name |
NME3 |
| Enzyme 19 Protein Sequence |
>Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
|
| Enzyme 19 Number of Residues |
169 |
| Enzyme 19 Molecular Weight |
19014.9 |
| Enzyme 19 Theoretical pI |
7.97 |
| Enzyme 19 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 19 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
14336763 |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q13232 |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
NDK3_HUMAN |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>510 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGGCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAAGAACCTGATTCACGGCAGCGACTCGGTG
GAGAGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAG
GACAGCGCTGGGCACTGGCTGTATGAGTAG
|
| Enzyme 19 GenBank Gene ID |
AE006639 |
| Enzyme 19 GeneCard ID |
NME3 |
| Enzyme 19 GenAtlas ID |
NME3 |
| Enzyme 19 HGNC ID |
HGNC:7851 |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
16q13 |
| Enzyme 19 SNPs |
SNPJam Report |
| Enzyme 19 General References |
- Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed ]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [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 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5346 |
| Enzyme 20 Name |
Nucleoside diphosphate kinase 6 |
| Enzyme 20 Synonyms |
- NDK 6
- NDP kinase 6
- Inhibitor of p53-induced apoptosis-alpha
- IPIA-alpha
- nm23-H6
|
| Enzyme 20 Gene Name |
NME6 |
| Enzyme 20 Protein Sequence |
>Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
|
| Enzyme 20 Number of Residues |
186 |
| Enzyme 20 Molecular Weight |
21142.0 |
| Enzyme 20 Theoretical pI |
8.49 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- nucleoside diphosphate kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- CTP biosynthetic process
- GTP biosynthetic process
- UTP biosynthetic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- pyrimidine nucleoside triphosphate biosynthetic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
- pyrimidine ribonucleoside triphosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in nucleoside diphosphate kinase activity |
| Enzyme 20 Specific Function |
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
3228530 |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
O75414 |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
NDK6_HUMAN |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
|
| Enzyme 20 GenBank Gene ID |
AF051941 |
| Enzyme 20 GeneCard ID |
NME6 |
| Enzyme 20 GenAtlas ID |
NME6 |
| Enzyme 20 HGNC ID |
HGNC:20567 |
| Enzyme 20 Chromosome Location |
3 |
| Enzyme 20 Locus |
3p21 |
| Enzyme 20 SNPs |
SNPJam Report |
| Enzyme 20 General References |
- Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [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 ]
- 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 ]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5442 |
| Enzyme 21 Name |
Glucokinase |
| Enzyme 21 Synonyms |
- Hexokinase type IV
- HK IV
- Hexokinase-4
- HK4
- Hexokinase-D
|
| Enzyme 21 Gene Name |
GCK |
| Enzyme 21 Protein Sequence |
>Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
|
| Enzyme 21 Number of Residues |
465 |
| Enzyme 21 Molecular Weight |
52191.1 |
| Enzyme 21 Theoretical pI |
4.85 |
| Enzyme 21 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in ATP binding |
| Enzyme 21 Specific Function |
Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- ATP + D-glucose = ADP + D-glucose 6-phosphate [RN:R00299]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
179427 |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P35557 |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
HXK4_HUMAN |
| Enzyme 21 PDB ID |
1V4T |
| Enzyme 21 PDB File |
Show |
| Enzyme 21 3D Structure |
|
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
|
| Enzyme 21 GenBank Gene ID |
M88011 |
| Enzyme 21 GeneCard ID |
GCK |
| Enzyme 21 GenAtlas ID |
GCK |
| Enzyme 21 HGNC ID |
HGNC:4195 |
| Enzyme 21 Chromosome Location |
7 |
| Enzyme 21 Locus |
7p15.3-p15.1 |
| Enzyme 21 SNPs |
SNPJam Report |
| Enzyme 21 General References |
- Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed ]
- Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed ]
- Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed ]
- Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed ]
- Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed ]
- Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [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 ]
- St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed ]
- Kamata K, Mitsuya M, Nishimura T, Eiki J, Nagata Y: Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase. Structure. 2004 Mar;12(3):429-38. [PubMed ]
- Mitsuya M, Kamata K, Bamba M, Watanabe H, Sasaki Y, Sasaki K, Ohyama S, Hosaka H, Nagata Y, Eiki J, Nishimura T: Discovery of novel 3,6-disubstituted 2-pyridinecarboxamide derivatives as GK activators. Bioorg Med Chem Lett. 2009 May 15;19(10):2718-21. Epub 2009 Mar 29. [PubMed ]
- Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed ]
- Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed ]
- Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed ]
- Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed ]
- Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed ]
- Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed ]
- Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed ]
- Guazzini B, Gaffi D, Mainieri D, Multari G, Cordera R, Bertolini S, Pozza G, Meschi F, Barbetti F: Three novel missense mutations in the glucokinase gene (G80S; E221K; G227C) in Italian subjects with maturity-onset diabetes of the young (MODY). Mutations in brief no. 162. Online. Hum Mutat. 1998;12(2):136. [PubMed ]
- Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed ]
- Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed ]
- Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed ]
- Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed ]
- Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed ]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5444 |
| Enzyme 22 Name |
Hexokinase-3 |
| Enzyme 22 Synonyms |
- Hexokinase type III
- HK III
|
| Enzyme 22 Gene Name |
HK3 |
| Enzyme 22 Protein Sequence |
>Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRENRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
|
| Enzyme 22 Number of Residues |
923 |
| Enzyme 22 Molecular Weight |
99024.6 |
| Enzyme 22 Theoretical pI |
5.06 |
| Enzyme 22 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in ATP binding |
| Enzyme 22 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate [RN:R02848]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
20380888 |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P52790 |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
HXK3_HUMAN |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTCAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGATGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGAGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
|
| Enzyme 22 GenBank Gene ID |
BC028129 |
| Enzyme 22 GeneCard ID |
HK3 |
| Enzyme 22 GenAtlas ID |
HK3 |
| Enzyme 22 HGNC ID |
HGNC:4925 |
| Enzyme 22 Chromosome Location |
5 |
| Enzyme 22 Locus |
5q35.2 |
| Enzyme 22 SNPs |
SNPJam Report |
| Enzyme 22 General References |
- Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [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 ]
- Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5445 |
| Enzyme 23 Name |
Hexokinase-2 |
| Enzyme 23 Synonyms |
- Hexokinase type II
- HK II
- Muscle form hexokinase
|
| Enzyme 23 Gene Name |
HK2 |
| Enzyme 23 Protein Sequence |
>Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
|
| Enzyme 23 Number of Residues |
917 |
| Enzyme 23 Molecular Weight |
102379.1 |
| Enzyme 23 Theoretical pI |
5.93 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in ATP binding |
| Enzyme 23 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate [RN:R02848]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
4809269 |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P52789 |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
HXK2_HUMAN |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCATTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTGCTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCATCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
|
| Enzyme 23 GenBank Gene ID |
AF148513 |
| Enzyme 23 GeneCard ID |
HK2 |
| Enzyme 23 GenAtlas ID |
HK2 |
| Enzyme 23 HGNC ID |
HGNC:4923 |
| Enzyme 23 Chromosome Location |
2 |
| Enzyme 23 Locus |
2p13 |
| Enzyme 23 SNPs |
SNPJam Report |
| Enzyme 23 General References |
- Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed ]
- Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [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 ]
- Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed ]
- Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed ]
- Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed ]
- Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed ]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5465 |
| Enzyme 24 Name |
Diacylglycerol kinase alpha |
| Enzyme 24 Synonyms |
- DAG kinase alpha
- 80 kDa diacylglycerol kinase
- Diglyceride kinase alpha
- DGK-alpha
|
| Enzyme 24 Gene Name |
DGKA |
| Enzyme 24 Protein Sequence |
>Diacylglycerol kinase alpha
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
|
| Enzyme 24 Number of Residues |
735 |
| Enzyme 24 Molecular Weight |
82629.5 |
| Enzyme 24 Theoretical pI |
6.71 |
| Enzyme 24 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 24 Specific Function |
Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity |
| Enzyme 24 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 24 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
30823 |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P23743 |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
DGKA_HUMAN |
| Enzyme 24 PDB ID |
1TUZ |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>2208 bp
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
|
| Enzyme 24 GenBank Gene ID |
X62535 |
| Enzyme 24 GeneCard ID |
DGKA |
| Enzyme 24 GenAtlas ID |
DGKA |
| Enzyme 24 HGNC ID |
HGNC:2849 |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
12q13.3 |
| Enzyme 24 SNPs |
SNPJam Report |
| Enzyme 24 General References |
- Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [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 ]
- Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed ]
- Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [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 ]
- 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 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5466 |
| Enzyme 25 Name |
Diacylglycerol kinase delta |
| Enzyme 25 Synonyms |
- DAG kinase delta
- 130 kDa diacylglycerol kinase
- Diglyceride kinase delta
- DGK-delta
|
| Enzyme 25 Gene Name |
DGKD |
| Enzyme 25 Protein Sequence |
>Diacylglycerol kinase delta
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
|
| Enzyme 25 Number of Residues |
1214 |
| Enzyme 25 Molecular Weight |
134524.2 |
| Enzyme 25 Theoretical pI |
7.58 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 25 Specific Function |
Isoform 2 may be involved in cell growth and tumorigenesis. Involved in clathrin-dependent endocytosis |
| Enzyme 25 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 25 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
22773821 |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q16760 |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
DGKD_HUMAN |
| Enzyme 25 PDB ID |
1R79 |
| Enzyme 25 PDB File |
Show |
| Enzyme 25 3D Structure |
|
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>3645 bp
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
|
| Enzyme 25 GenBank Gene ID |
AB078966 |
| Enzyme 25 GeneCard ID |
DGKD |
| Enzyme 25 GenAtlas ID |
DGKD |
| Enzyme 25 HGNC ID |
HGNC:2851 |
| Enzyme 25 Chromosome Location |
2 |
| Enzyme 25 Locus |
2q37.1 |
| Enzyme 25 SNPs |
SNPJam Report |
| Enzyme 25 General References |
- Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed ]
- Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed ]
- Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [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 ]
- Imai S, Sakane F, Kanoh H: Phorbol ester-regulated oligomerization of diacylglycerol kinase delta linked to its phosphorylation and translocation. J Biol Chem. 2002 Sep 20;277(38):35323-32. Epub 2002 Jun 25. [PubMed ]
- Kawasaki T, Kobayashi T, Ueyama T, Shirai Y, Saito N: Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha. Biochem J. 2008 Jan 15;409(2):471-9. [PubMed ]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5470 |
| Enzyme 26 Name |
Diacylglycerol kinase beta |
| Enzyme 26 Synonyms |
- DAG kinase beta
- 90 kDa diacylglycerol kinase
- Diglyceride kinase beta
- DGK-beta
|
| Enzyme 26 Gene Name |
DGKB |
| Enzyme 26 Protein Sequence |
>Diacylglycerol kinase beta
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
|
| Enzyme 26 Number of Residues |
804 |
| Enzyme 26 Molecular Weight |
90594.7 |
| Enzyme 26 Theoretical pI |
7.90 |
| Enzyme 26 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 26 Specific Function |
Exhibits high phosphorylation activity for long-chain diacylglycerols |
| Enzyme 26 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 26 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
22027632 |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9Y6T7 |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
DGKB_HUMAN |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>2415 bp
ATGACAAACCAGGAAAAATGGGCCCACCTCAGCCCTTCGGAATTTTCCCAACTTCAGAAA
TATGCTGAGTATTCTACAAAGAAATTAAAGGATGTTCTTGAAGAATTCCATGGTAATGGT
GTGCTTGCAAAGTATAATCCTGAAGGGAAACAAGACATTCTTAACCAAACAATAGATTTT
GAAGGTTTCAAACTATTCATGAAGACATTCCTGGAAGCCGAGCTTCCTGATGATTTCACT
GCACACCTTTTCATGTCATTTAGCAACAAGTTTCCTCATTCTAGTCCAATGGTAAAAAGT
AAGCCTGCTCTCCTATCAGGCGGTCTGAGAATGAATAAAGGTGCCATCACCCCTCCCCGG
ACTACTTCTCCTGCAAATACGTGTTCCCCAGAAGTAATCCATCTGAAGGACATTGTCTGT
TACCTGTCTCTGCTTGAAAGAGGAAGACCTGAGGATAAGCTTGAGTTTATGTTTCGCCTT
TATGACACGGATGGGAATGGCTTCCTGGACAGCTCGGAGCTAGAAAATATCATCAGTCAG
ATGATGCATGTTGCAGAATACCTTGAGTGGGATGTCACTGAACTTAATCCAATCCTCCAT
GAAATGATGGAAGAAATTGACTATGATCATGATGGAACCGTGTCTCTGGAGGAATGGATT
CAAGGAGGAATGACAACGATTCCACTTCTTGTGCTCCTGGGCTTAGAAAATAACGTGAAG
GATGATGGACAGCACGTGTGGCGACTGAAGCACTTTAACAAACCTGCCTATTGCAACCTT
TGCCTGAACATGCTGATTGGCGTGGGGAAGCAGGGCCTCTGCTGTTCCTTCTGCAAGTAC
ACAGTCCATGAGCGCTGTGTGGCTCGAGCACCTCCCTCTTGCATCAAGACCTATGTGAAG
TCCAAAAGGAACACTGATGTCATGCACCATTACTGGGTTGAAGGTAACTGCCCAACCAAG
TGTGATAAGTGCCACAAAACTGTTAAATGTTACCAGGGCCTGACAGGACTGCATTGTGTT
TGGTGTCAGATCACACTGCATAATAAATGTGCTTCTCATCTAAAACCTGAATGTGACTGT
GGACCTTTGAAGGACCATATTTTACCACCCACAACAATCTGTCCAGTGGTACTGCAGACT
CTGCCCACTTCAGGAGTTTCAGTTCCTGAGGAAAGACAATCAACAGTGAAAAAGGAAAAG
AGTGGTTCCCAGCAGCCAAACAAAGTGATTGACAAGAATAAAATGCAAAGAGCCAACTCT
GTTACTGTAGATGGACAAGGCCTGCAGGTCACTCCTGTGCCTGGTACTCACCCACTTTTA
GTTTTTGTGAACCCCAAAAGTGGTGGAAAACAAGGAGAACGAATTTACAGAAAATTCCAG
TATCTATTAAATCCTCGTCAGGTTTACAGTCTTTCTGGAAATGGACCAATGCCAGGGTTA
AACTTTTTCCGTGATGTTCCTGACTTCAGAGTGTTAGCCTGTGGTGGAGATGGAACCGTG
GGCTGGGTTTTGGATTGCATAGAAAAGGCCAATGTAGGCAAGCATCCTCCAGTTGCGATT
CTGCCTCTTGGGACTGGCAATGATCTAGCAAGATGCCTGCGATGGGGAGGAGGTTACGAA
GGTGAGAATCTGATGAAAATTCTAAAAGACATTGAAAACAGCACAGAAATCATGTTGGAC
AGGTGGAAGTTTGAAGTCATACCTAATGACAAAGATGAGAAAGGAGACCCAGTGCCTTAC
AGTATCATCAATAATTACTTTTCCATTGGCGTGGATGCCTCCATTGCACACAGATTCCAC
ATCATGAGAGAAAAACACCCAGAGAAATTCAACAGTAGAATGAAGAACAAATTTTGGTAT
TTTGAGTTTGGCACATCTGAAACTTTCTCAGCCACCTGCAAGAAGCTACATGAATCTGTA
GAAATAGAATGTGATGGAGTACAGATAGATTTAATAAACATCTCTCTGGAAGGAATTGCT
ATTTTGAATATACCAAGCATGCATGGAGGATCCAATCTTTGGGGAGAGTCTAAGAAAAGA
CGAAGCCATCGACGAATAGAGAAAAAAGGGTCTGACAAAAGGACCACCGTCACAGATGCC
AAAGAGTTGAAGTTTGCAAGTCAAGATCTCAGTGACCAGCTGCTGGAGGTGGTCGGCTTG
GAAGGAGCCATGGAGATGGGGCAAATATACACAGGCCTGAAAAGTGCTGGCCGGCGGCTG
GCTCAGTGCTCCTGCGTGGTCATCAGGACGAGCAAGTCTCTGCCAATGCAAATTGATGGG
GAGCCATGGATGCAGACCCCATGCACAATAAAAATTACACACAAGAACCAAGCCCCAATG
CTGATGGGCCCGCCTCCAAAAACCGGTTTATTCTGCTCCCTCGTCAAAAGGACAAGAAAC
CGAAGCAAGGAATAA
|
| Enzyme 26 GenBank Gene ID |
NM_004080.2 |
| Enzyme 26 GeneCard ID |
DGKB |
| Enzyme 26 GenAtlas ID |
DGKB |
| Enzyme 26 HGNC ID |
HGNC:2850 |
| Enzyme 26 Chromosome Location |
7 |
| Enzyme 26 Locus |
7p21.2 |
| Enzyme 26 SNPs |
SNPJam Report |
| Enzyme 26 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 ]
- 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 ]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed ]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5472 |
| Enzyme 27 Name |
Diacylglycerol kinase iota |
| Enzyme 27 Synonyms |
- DAG kinase iota
- Diglyceride kinase iota
- DGK-iota
|
| Enzyme 27 Gene Name |
DGKI |
| Enzyme 27 Protein Sequence |
>Diacylglycerol kinase iota
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
|
| Enzyme 27 Number of Residues |
1065 |
| Enzyme 27 Molecular Weight |
116996.2 |
| Enzyme 27 Theoretical pI |
7.81 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 27 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 27 Specific Function |
ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate |
| Enzyme 27 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 27 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
3676530 |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
O75912 |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
DGKI_HUMAN |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>3198 bp
ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA
|
| Enzyme 27 GenBank Gene ID |
AF061936 |
| Enzyme 27 GeneCard ID |
DGKI |
| Enzyme 27 GenAtlas ID |
DGKI |
| Enzyme 27 HGNC ID |
HGNC:2855 |
| Enzyme 27 Chromosome Location |
7 |
| Enzyme 27 Locus |
7q32.3-q33 |
| Enzyme 27 SNPs |
SNPJam Report |
| Enzyme 27 General References |
- Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [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 ]
- Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [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 ]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5478 |
| Enzyme 28 Name |
Diacylglycerol kinase zeta |
| Enzyme 28 Synonyms |
- DAG kinase zeta
- Diglyceride kinase zeta
- DGK-zeta
|
| Enzyme 28 Gene Name |
DGKZ |
| Enzyme 28 Protein Sequence |
>Diacylglycerol kinase zeta
METFFRRHFRGKVPGPGEGQQRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYLRRASSHLLPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
|
| Enzyme 28 Number of Residues |
1117 |
| Enzyme 28 Molecular Weight |
124127.3 |
| Enzyme 28 Theoretical pI |
9.31 |
| Enzyme 28 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 28 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 28 Specific Function |
Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols. Isoform 2 but not isoform 1 regulates RASGRP1 activity |
| Enzyme 28 Pathways |
- Glycerolipid Metabolism (map00561 )
- Phospholipid Synthesis (map00564 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 28 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
157688564 |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q13574 |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
DGKZ_HUMAN |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>3354 bp
ATGGAGACTTTCTTTAGGAGACATTTCCGGGGGAAGGTGCCAGGCCCTGGAGAGGGGCAG
CAGCGGCCCAGCAGCGTGGGGCTGCCCACAGGCAAGGCCCGGCGTCGCTCCCCCGCTGGG
CAGGCCTCCTCCTCACTGGCACAGCGGCGCCGCTCCAGCGCCCAGCTCCAGGGCTGCCTC
CTGAGTTGCGGGGTGAGGGCCCAGGGTTCCAGCCGCCGGCGCTCCAGCACTGTGCCCCCT
TCCTGCAACCCCCGCTTCATCGTGGATAAGGTGCTCACTCCACAGCCTACCACCGTGGGG
GCCCAGCTTCTGGGTGCACCCCTGCTGTTGACCGGGCTTGTGGGCATGAATGAGGAGGAG
GGTGTCCAGGAGGATGTGGTAGCCGAGGCATCGAGCGCCATCCAGCCAGGCACCAAGACA
CCAGGGCCACCCCCACCTCGGGGCGCCCAGCCGCTGTTGCCCCTACCCCGCTACCTGCGC
CGAGCCTCCTCCCACCTGCTCCCCGCGGATGCCGTATATGACCACGCTCTCTGGGGCCTG
CACGGCTACTATCGGCGCCTCAGCCAGCGGCGGCCCTCAGGCCAGCACCCTGGCCCTGGG
GGCCGAAGAGCCTCAGGCACCACCGCCGGCACCATGCTGCCCACCCGTGTGCGCCCACTG
TCCCGCAGGCGCCAGGTAGCCCTACGGCGCAAGGCGGCCGGACCCCAGGCCTGGAGCGCC
CTGCTCGCGAAAGCCATCACCAAGTCGGGCCTCCAGCACCTGGCCCCCCCTCCGCCCACC
CCTGGGGCCCCGTGCAGCGAGTCAGAGCGGCAGATCCGGAGTACAGTGGACTGGAGCGAG
TCAGCGACATATGGGGAGCACATCTGGTTCGAGACCAACGTGTCCGGGGACTTCTGCTAC
GTTGGGGAGCAGTACTGTGTAGCCAGGATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCA
GCCTGCAAGATTGTGGTGCACACGCCCTGCATCGAGCAGCTGGAGAAGATAAATTTCCGC
TGTAAGCCGTCCTTCCGTGAATCAGGCTCCAGGAATGTCCGCGAGCCAACCTTTGTACGG
CACCACTGGGTACACAGACGACGCCAGGACGGCAAGTGTCGGCACTGTGGGAAGGGATTC
CAGCAGAAGTTCACCTTCCACAGCAAGGAGATTGTGGCCATCAGCTGCTCGTGGTGCAAG
CAGGCATACCACAGCAAGGTGTCCTGCTTCATGCTGCAGCAGATCGAGGAGCCGTGCTCG
CTGGGGGTCCACGCAGCCGTGGTCATCCCGCCCACCTGGATCCTCCGCGCCCGGAGGCCC
CAGAATACTCTGAAAGCAAGCAAGAAGAAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGC
AAGAAAGGGCCTGAGGAGGGCCGCTGGAGACCCTTCATCATCAGGCCCACCCCCTCCCCG
CTCATGAAGCCCCTGCTGGTGTTTGTGAACCCCAAGAGTGGGGGCAACCAGGGTGCAAAG
ATCATCCAGTCTTTCCTCTGGTATCTCAATCCCCGACAAGTCTTCGACCTGAGCCAGGGA
GGGCCCAAGGAGGCGCTGGAGATGTACCGCAAAGTGCACAACCTGCGGATCCTGGCGTGC
GGGGGCGACGGCACGGTGGGCTGGATCCTCTCCACCCTGGACCAGCTACGCCTGAAGCCG
CCACCCCCTGTTGCCATCCTGCCCCTGGGTACTGGCAACGACTTGGCCCGAACCCTCAAC
TGGGGTGGGGGCTACACAGATGAGCCTGTGTCCAAGATCCTCTCCCACGTGGAGGAGGGG
AACGTGGTACAGCTGGACCGCTGGGACCTCCACGCTGAGCCCAACCCCGAGGCAGGGCCT
GAGGACCGAGATGAAGGCGCCACCGACCGGTTGCCCCTGGATGTCTTCAACAACTACTTC
AGCCTGGGCTTTGACGCCCACGTCACCCTGGAGTTCCACGAGTCTCGAGAGGCCAACCCA
GAGAAATTCAACAGCCGCTTTCGGAATAAGATGTTCTACGCCGGGACAGCTTTCTCTGAC
TTCCTGATGGGCAGCTCCAAGGACCTGGCCAAGCACATCCGAGTGGTGTGTGATGGAATG
GACTTGACTCCCAAGATCCAGGACCTGAAACCCCAGTGTGTTGTTTTCCTGAACATCCCC
AGGTACTGTGCGGGCACCATGCCCTGGGGCCACCCTGGGGAGCACCACGACTTTGAGCCC
CAGCGGCATGACGACGGCTACCTCGAGGTCATTGGCTTCACCATGACGTCGTTGGCCGCG
CTGCAGGTGGGCGGACACGGCGAGCGGCTGACGCAGTGTCGCGAGGTGGTGCTCACCACA
TCCAAGGCCATCCCGGTGCAGGTGGATGGCGAGCCCTGCAAGCTTGCAGCCTCACGCATC
CGCATCGCCCTGCGCAACCAGGCCACCATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCC
CCCCTGCACAGCGACCAGCAGCCGGTGCCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTC
AGCATGCACGACTATGAGGCCCTGCACTACGACAAGGAGCAGCTCAAGGAGGCCTCTGTG
CCGCTGGGCACTGTGGTGGTCCCAGGAGACAGTGACCTAGAGCTCTGCCGTGCCCACATT
GAGAGACTCCAGCAGGAGCCCGATGGTGCTGGAGCCAAGTCCCCGACATGCCAGAAACTG
TCCCCCAAGTGGTGCTTCCTGGACGCCACCACTGCCAGCCGCTTCTACAGGATCGACCGA
GCCCAGGAGCACCTCAACTATGTGACTGAGATCGCACAGGATGAGATTTATATCCTGGAC
CCTGAGCTGCTGGGGGCATCGGCCCGGCCTGACCTCCCAACCCCCACTTCCCCTCTCCCC
ACCTCACCCTGCTCACCCACGCCCCGGTCACTGCAAGGGGATGCTGCACCCCCTCAAGGT
GAAGAGCTGATTGAGGCTGCCAAGAGGAACGACTTCTGTAAGCTCCAGGAGCTGCACCGA
GCTGGGGGCGACCTCATGCACCGAGACGAGCAGAGTCGCACGCTCCTGCACCACGCAGTC
AGCACTGGCAGCAAGGATGTGGTCCGCTACCTGCTGGACCACGCCCCCCCAGAGATCCTT
GATGCGGTGGAGGAAAACGGGGAGACCTGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGC
ACCATCTGCCACTACATCGTGGAGGCCGGGGCCTCGCTCATGAAGACAGACCAGCAGGGC
GACACTCCCCGGCAGCGGGCTGAGAAGGCTCAGGACACCGAGCTGGCCGCCTACCTGGAG
AACCGGCAGCACTACCAGATGATCCAGCGGGAGGACCAGGAGACGGCTGTGTAG
|
| Enzyme 28 GenBank Gene ID |
NM_001105540.1 |
| Enzyme 28 GeneCard ID |
DGKZ |
| Enzyme 28 GenAtlas ID |
DGKZ |
| Enzyme 28 HGNC ID |
HGNC:2857 |
| Enzyme 28 Chromosome Location |
1 |
| Enzyme 28 Locus |
11p11.2 |
| Enzyme 28 SNPs |
SNPJam Report |
| Enzyme 28 General References |
- Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed ]
- Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [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 ]
- Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed ]
- Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed ]
- Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed ]
- Rincon E, Santos T, Avila-Flores A, Albar JP, Lalioti V, Lei C, Hong W, Merida I: Proteomics identification of sorting nexin 27 as a diacylglycerol kinase zeta-associated protein: new diacylglycerol kinase roles in endocytic recycling. Mol Cell Proteomics. 2007 Jun;6(6):1073-87. Epub 2007 Mar 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 ]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5487 |
| Enzyme 29 Name |
L-fucose kinase |
| Enzyme 29 Synonyms |
- Fucokinase
|
| Enzyme 29 Gene Name |
FUK |
| Enzyme 29 Protein Sequence |
>L-fucose kinase
MEQPKGVDWTVIILTCQYKDSVQVFQRELEVRQKREQIPAGTLLLAVEDPEKRVGSGGAT
LNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPEAPV
EALVCNLDCLLDIMTYRLGPGSPPGVWVCSTDMLLSVPANPGISWDSFRGARVIALPGSP
AYAQNHGVYLTDPQGLVLDIYYQGTEAEIQRCVRPDGRVPLVSGVVFFSVETAERLLATH
VSPPLDACTYLGLDSGARPVQLSLFFDILHCMAENVTREDFLVGRPPELGQGDADVAGYL
QSARAQLWRELRDQPLTMAYVSSGSYSYMTSSASEFLLSLTLPGAPGAQIVHSQVEEQQL
LAAGSSVVSCLLEGPVQLGPGSVLQHCHLQGPIHIGAGCLVTGLDTAHSKALHGRELRDL
VLQGHHTRLHGSPGHAFTLVGRLDSWERQGAGTYLNVPWSEFFKRTGVRAWDLWDPETLP
AEYCLPSARLFPVLHPSRELGPQDLLWMLDHQEDGGEALRAWRASWRLSWEQLQPCLDRA
ATLASRRDLFFRQALHKARHVLEARQDLSLRPLIWAAVREGCPGPLLATLDQVAAGAGDP
GVAARALACVADVLGCMAEGRGGLRSGPAANPEWMRPFSYLECGDLAAGVEALAQERDKW
LSRPALLVRAARHYEGAGQILIRQAVMSAQHFVSTEQVELPGPGQWVVAECPARVDFSGG
WSDTPPLAYELGGAVLGLAVRVDGRRPIGARARRIPEPELWLAVGPRQDEMTVKIVCRCL
ADLRDYCQPHAPGALLKAAFICAGIVHVHSELQLSEQLLRTFGGGFELHTWSELPHGSGL
GTSSILAGTALAALQRAAGRVVGTEALIHAVLHLEQVLTTGGGWQDQVGGLMPGIKVGRS
RAQLPLKVEVEEVTVPEGFVQKLNDHLLLVYTGKTRLARNLLQDVLRSWYARLPAVVQNA
HSLVRQTEECAEGFRQGSLPLLGQCLTSYWEQKKLMAPGCEPLTVRRMMDVLAPHVHGQS
LAGAGGGGFLYLLTKEPQQKEALEAVLAKTEGLGNYSIHLVEVDTQGLSLKLLGTEASTC
CPFP
|
| Enzyme 29 Number of Residues |
1084 |
| Enzyme 29 Molecular Weight |
117621.8 |
| Enzyme 29 Theoretical pI |
6.21 |
| Enzyme 29 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 29 General Function |
Involved in ATP binding |
| Enzyme 29 Specific Function |
Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides |
| Enzyme 29 Pathways |
- Fructose and Mannose Metabolism (map00051 )
|
| Enzyme 29 Reactions |
- ATP + L-fucose = ADP + beta-L-fucose 1-phosphate [RN:R03161]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
63175654 |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q8N0W3 |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
FUK_HUMAN |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>3255 bp
ATGGAGCAGCCGAAGGGAGTTGATTGGACAGTCATCATCCTGACCTGCCAGTACAAGGAC
AGTGTCCAGGTCTTTCAGAGAGAACTGGAAGTGCGGCAGAAGCGGGAGCAGATCCCTGCT
GGGACGCTGTTACTGGCCGTGGAGGACCCAGAGAAGCGTGTGGGCAGCGGAGGAGCCACC
CTCAACGCCCTGCTGGTGGCTGCTGAACACCTGAGTGCCCGGGCAGGCTTCACTGTGGTC
ACATCCGATGTCCTGCACTCGGCCTGGATCCTCATTCTGCACATGGGTCGAGACTTCCCC
TTTGATGACTGTGGCAGGGCTTTCACCTGCCTCCCCGTGGAGAACCCCGAGGCCCCCGTG
GAAGCCTTGGTCTGCAACCTGGACTGCCTGCTGGACATCATGACCTATCGGCTGGGCCCG
GGCTCCCCGCCAGGCGTGTGGGTCTGCAGCACCGACATGCTGCTGTCTGTTCCTGCAAAT
CCTGGTATCAGCTGGGACAGCTTCCGGGGAGCCAGAGTGATCGCCCTCCCAGGGAGCCCG
GCCTACGCTCAGAATCATGGCGTCTACCTAACTGACCCCCAGGGCCTTGTTTTGGACATT
TACTACCAGGGCACTGAGGCAGAGATTCAGCGGTGTGTCAGGCCTGATGGGCGGGTGCCA
CTGGTCTCTGGGGTTGTCTTCTTCTCTGTGGAGACTGCCGAGCGCCTCCTAGCCACCCAC
GTGAGCCCGCCCCTGGATGCCTGCACCTACCTAGGCTTGGACTCCGGAGCCCGGCCTGTC
CAGCTGTCTCTGTTTTTTGACATTCTCCACTGCATGGCTGAGAACGTGACCAGGGAGGAC
TTCCTGGTGGGGAGGCCCCCAGAGTTGGGGCAAGGCGATGCAGATGTAGCGGGTTATCTG
CAGAGCGCCCGGGCCCAGCTGTGGAGGGAGCTTCGCGATCAGCCCCTTACCATGGCCTAT
GTCTCCAGCGGCAGCTACAGCTACATGACCTCCTCAGCCAGTGAGTTCCTGCTCAGCCTC
ACACTCCCCGGGGCTCCTGGGGCCCAGATTGTGCACTCCCAGGTGGAGGAGCAGCAGCTT
CTGGCGGCCGGGAGCTCTGTGGTCAGCTGCCTGCTGGAGGGCCCTGTCCAGCTGGGTCCT
GGGAGCGTCCTGCAGCACTGCCACCTGCAGGGCCCCATTCACATAGGCGCTGGCTGCTTG
GTGACTGGCCTGGATACAGCCCACTCCAAGGCCCTGCATGGCCGGGAGCTGCGTGACCTT
GTCCTGCAGGGACACCACACGCGGCTACACGGCTCCCCGGGCCACGCCTTCACCCTCGTT
GGCCGTCTGGACAGCTGGGAGAGACAGGGGGCAGGCACATATCTCAACGTGCCCTGGAGT
GAATTCTTCAAGAGGACAGGTGTTCGAGCCTGGGACCTGTGGGACCCTGAGACGCTGCCC
GCAGAGTACTGCCTTCCCAGCGCCCGCCTCTTTCCTGTGCTCCACCCCTCGAGGGAGCTG
GGACCCCAGGACCTGCTGTGGATGCTGGACCACCAGGAGGATGGGGGCGAGGCCCTGCGA
GCCTGGCGGGCCTCCTGGCGCCTGTCCTGGGAGCAGCTGCAGCCGTGCCTGGATCGGGCT
GCCACGCTGGCCTCTCGCCGGGACCTGTTCTTCCGCCAGGCCCTGCATAAGGCGCGGCAC
GTGCTGGAGGCCCGGCAGGACCTCAGCCTGCGCCCGCTGATCTGGGCTGCTGTCCGCGAG
GGCTGCCCCGGGCCCCTGCTGGCCACGCTGGACCAGGTTGCAGCTGGGGCAGGAGACCCT
GGTGTGGCGGCACGGGCACTGGCCTGTGTGGCGGACGTCCTGGGCTGCATGGCAGAGGGC
CGTGGGGGCTTGCGGAGCGGGCCAGCTGCCAACCCTGAGTGGATGCGGCCCTTCTCATAC
CTGGAGTGTGGAGACCTGGCAGCGGGCGTGGAGGCGCTTGCCCAGGAGAGGGACAAGTGG
CTAAGCAGGCCAGCCTTGCTGGTGCGAGCGGCCCGCCACTATGAGGGGGCTGGTCAGATC
CTGATCCGCCAGGCTGTGATGTCAGCCCAGCACTTTGTCTCCACAGAGCAGGTGGAACTG
CCGGGACCTGGGCAGTGGGTGGTGGCTGAGTGCCCGGCCCGTGTGGATTTCTCTGGGGGC
TGGAGTGACACGCCACCCCTTGCCTATGAGCTTGGCGGGGCTGTGCTGGGCCTGGCTGTG
CGAGTGGACGGCCGCCGGCCCATCGGAGCCAGGGCACGCCGCATCCCGGAGCCTGAGCTG
TGGCTGGCGGTGGGGCCTCGGCAGGATGAGATGACTGTGAAGATAGTGTGCCGGTGCCTG
GCTGACCTGCGGGACTACTGCCAGCCTCATGCCCCAGGGGCCCTGCTGAAGGCGGCCTTC
ATCTGTGCAGGGATCGTGCATGTCCACTCGGAACTCCAGCTGAGTGAGCAGCTGCTCCGC
ACCTTCGGGGGCGGCTTTGAGCTGCACACCTGGTCTGAGCTGCCCCACGGCTCTGGCCTG
GGCACCAGCAGCATCCTGGCAGGCACTGCCCTGGCTGCCTTGCAGCGAGCCGCAGGCCGG
GTGGTGGGCACGGAAGCCCTGATCCACGCAGTGCTGCACCTGGAGCAGGTGCTCACCACT
GGAGGTGGCTGGCAGGACCAAGTAGGTGGCCTAATGCCTGGCATCAAGGTGGGGCGCTCC
CGGGCTCAGCTGCCACTGAAGGTGGAGGTAGAAGAGGTCACGGTGCCTGAGGGCTTTGTC
CAGAAGCTCAATGACCACCTGCTCTTGGTGTACACTGGCAAGACCCGCCTGGCTCGGAAC
CTGCTGCAGGATGTGCTGAGGAGCTGGTATGCCCGACTTCCTGCTGTGGTGCAGAATGCC
CACAGCCTGGTACGGCAAACTGAGGAGTGTGCTGAAGGCTTCCGCCAAGGAAGCCTGCCT
CTGCTGGGCCAGTGCCTGACCTCGTACTGGGAGCAGAAGAAGCTCATGGCTCCAGGCTGT
GAGCCCCTGACTGTGCGGCGTATGATGGATGTCCTGGCCCCCCACGTGCATGGCCAGAGC
CTGGCTGGGGCAGGCGGTGGAGGCTTTCTCTATCTGTTGACCAAGGAGCCACAGCAAAAG
GAGGCCTTGGAGGCGGTGCTGGCCAAGACCGAGGGCCTTGGGAATTACAGCATCCACCTG
GTTGAAGTGGACACTCAGGGCCTGAGCCTGAAGCTGCTGGGGACCGAGGCCTCAACCTGT
TGCCCTTTCCCATGA
|
| Enzyme 29 GenBank Gene ID |
NM_145059.2 |
| Enzyme 29 GeneCard ID |
FUK |
| Enzyme 29 GenAtlas ID |
FUK |
| Enzyme 29 HGNC ID |
HGNC:29500 |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
16q22.1 |
| Enzyme 29 SNPs |
SNPJam Report |
| Enzyme 29 General References |
- Hinderlich S, Berger M, Blume A, Chen H, Ghaderi D, Bauer C: Identification of human L-fucose kinase amino acid sequence. Biochem Biophys Res Commun. 2002 Jun 14;294(3):650-4. [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 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5490 |
| Enzyme 30 Name |
Propionyl-CoA carboxylase beta chain, mitochondrial |
| Enzyme 30 Synonyms |
- PCCase subunit beta
- Propanoyl-CoA:carbon dioxide ligase subunit beta
|
| Enzyme 30 Gene Name |
PCCB |
| Enzyme 30 Protein Sequence |
>Propionyl-CoA carboxylase beta chain, mitochondrial
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
|
| Enzyme 30 Number of Residues |
539 |
| Enzyme 30 Molecular Weight |
58215.1 |
| Enzyme 30 Theoretical pI |
7.69 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- ligase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 30 General Function |
Involved in ligase activity |
| Enzyme 30 Specific Function |
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA |
| Enzyme 30 Pathways |
- Propanoate Metabolism (map00640 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 30 Reactions |
- ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA [RN:R01859]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
312812 |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P05166 |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PCCB_HUMAN |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1620 bp
ATGGCGGCGGCATTACGGGTGGCGGCGGTCGGGGCAAGGCTCAGCGTTCTGGCGAGCGGT
CTCCGCGCCGCGGTCCGCAGCCTTTGCAGCCAGGCCACCTCTGTTAACGAACGCATCGAA
AACAAGCGCCGGACCGCGCTGCTGGGAGGGGGCCAACGCCGTATTGACGCGCAGCACAAG
CGAGGAAAGCTAACAGCCAGGGAGAGGATCAGTCTCTTGCTGGACCCTGGCAGCTTTGTT
GAGAGCGACATGTTTGTGGAACACAGATGTGCAGATTTTGGAATGGCTGCTGACAAGAAT
AAGTTTCCTGGAGACAGCGTGGTCACTGGACGAGGCCGAATCAATGGAAGATTGGTTTAT
GTCTTCAGTCAGGATTTTACAGTTTTTGGAGGCAGTCTGTCAGGAGCACATGCCCAAAAG
ATCTGCAAAATCATGGACCAGGCCATAACGGTGGGGGCTCCAGTGATTGGGCTGAATGAC
TCTGGGGGAGCACGGATCCAAGAAGGAGTGGAGTCTTTGGCTGGCTATGCAGACATCTTT
CTGAGGAATGTTACGGCATCCGGAGTCATCCCTCAGATTTCTCTGATCATGGGCCCATGT
GCTGGTGGGGCCGTCTACTCCCCAGCCCTAACAGACTTCACGTTCATGGTAAAGGACACC
TCCTACCTGTTCATCACTGGCCCTGATGTTGTGAAGTCTGTCACCAATGAGGATGTTACC
CAGGAGGAGCTCGGTGGTGCCAAGACCCACACCACCATGTCAGGTGTGGCCCACAGAGCT
TTTGAAAATGATGTTGATGCCTTGTGTAATCTCCGGGATTTCTTCAACTACCTGCCCCTG
AGCAGTCAGGACCCGGCTTCCGTCCGTGAGTGCCACGATCCCAGTGACCGTCTGGTTCCT
GAGCTTGACACAATTGTCCCTTTGGAATCAACCAAAGCCTACAACATGGTGGACATCATA
CACTCTGTTGTTGATGAGCGTGAATTTTTTGAGATCATGCCCAATTATGCCAAGAACATC
ATTGTTGGTTTTGCAAGAATGAATGGGAGGACTGTTGGAATTGTTGGCAACCAACCTAAG
GTGGCCTCAGGATGCTTGGATATTAATTCATCTGTGAAAGGGGCTCGTTTTGTCAGATTC
TGTGATGCATTCAATATTCCACTCATCACTTTTGTTGATGTCCCTGGCTTTCTACCTGGC
ACAGCACAGGAATACGGGGGCATCATCCGGCATGGTGCCAAGCTTCTCTACGCATTTGCT
GAGGCAACTGTACCCAAAGTCACAGTCATCACCAGGAAGGCCTATGGAGGTGCCTATGAT
GTCATGAGCTCTAAGCACCTTTGTGGTGATACCAACTATGCCTGGCCCACCGCAGAGATT
GCAGTCATGGGAGCAAAGGGCGCTGTGGAGATCATCTTCAAAGGGCATGAGAATGTGGAA
GCTGCTCAGGCAGAGTACATCGAGAAGTTTGCCAACCCTTTCCCTGCAGCAGTGCGAGGG
TTTGTGGATGACATCATCCAACCTTCTTCCACACGTGCCCGAATCTGCTGTGACCTGGAT
GTCTTGGCCAGCAAGAAGGTACAACGTCCTTGGAGAAAACATGCAAATATTCCATTGTAA
|
| Enzyme 30 GenBank Gene ID |
X73424 |
| Enzyme 30 GeneCard ID |
PCCB |
| Enzyme 30 GenAtlas ID |
PCCB |
| Enzyme 30 HGNC ID |
HGNC:8654 |
| Enzyme 30 Chromosome Location |
3 |
| Enzyme 30 Locus |
3q21-q22 |
| Enzyme 30 SNPs |
SNPJam Report |
| Enzyme 30 General References |
- Lamhonwah AM, Leclerc D, Loyer M, Clarizio R, Gravel RA: Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Genomics. 1994 Feb;19(3):500-5. [PubMed ]
- Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet. 1993 Oct;92(4):397-402. [PubMed ]
- Rodriguez-Pombo P, Hoenicka J, Muro S, Perez B, Perez-Cerda C, Richard E, Desviat LR, Ugarte M: Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Am J Hum Genet. 1998 Aug;63(2):360-9. [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 ]
- Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed ]
- Tahara T, Kraus JP, Rosenberg LE: An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1372-6. [PubMed ]
- Tahara T, Kraus JP, Ohura T, Rosenberg LE, Fenton WA: Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia. J Inherit Metab Dis. 1993;16(2):353-60. [PubMed ]
- Muro S, Rodriguez-Pombo P, Perez B, Perez-Cerda C, Desviat LR, Sperl W, Skladal D, Sass JO, Ugarte M: Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Hum Mutat. 1999;14(1):89-90. [PubMed ]
- Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed ]
- Muro S, Perez B, Desviat LR, Rodriguez-Pombo P, Perez-Cerda C, Clavero S, Ugarte M: Effect of PCCB gene mutations on the heteromeric and homomeric assembly of propionyl-CoA carboxylase. Mol Genet Metab. 2001 Dec;74(4):476-83. [PubMed ]
- Yorifuji T, Kawai M, Muroi J, Mamada M, Kurokawa K, Shigematsu Y, Hirano S, Sakura N, Yoshida I, Kuhara T, Endo F, Mitsubuchi H, Nakahata T: Unexpectedly high prevalence of the mild form of propionic acidemia in Japan: presence of a common mutation and possible clinical implications. Hum Genet. 2002 Aug;111(2):161-5. Epub 2002 Jul 4. [PubMed ]
- Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed ]
- Yang X, Sakamoto O, Matsubara Y, Kure S, Suzuki Y, Aoki Y, Yamaguchi S, Takahashi Y, Nishikubo T, Kawaguchi C, Yoshioka A, Kimura T, Hayasaka K, Kohno Y, Iinuma K, Ohura T: Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia. Mol Genet Metab. 2004 Apr;81(4):335-42. [PubMed ]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5491 |
| Enzyme 31 Name |
Propionyl-CoA carboxylase alpha chain, mitochondrial |
| Enzyme 31 Synonyms |
- PCCase subunit alpha
- Propanoyl-CoA:carbon dioxide ligase subunit alpha
|
| Enzyme 31 Gene Name |
PCCA |
| Enzyme 31 Protein Sequence |
>Propionyl-CoA carboxylase alpha chain, mitochondrial
MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNE
KTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKS
YLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIES
KLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRD
GFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVV
EEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPV
TECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQY
QEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTH
NIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRA
QHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLAS
PLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSS
VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGE
GDLLVELE
|
| Enzyme 31 Number of Residues |
728 |
| Enzyme 31 Molecular Weight |
80058.3 |
| Enzyme 31 Theoretical pI |
7.56 |
| Enzyme 31 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in catalytic activity |
| Enzyme 31 Specific Function |
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA |
| Enzyme 31 Pathways |
- Propanoate Metabolism (map00640 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 31 Reactions |
- ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA [RN:R01859]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
18252315 |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P05165 |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PCCA_HUMAN |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>2187 bp
ATGGCGGGGTTCTGGGTCGGGACAGCACCGCTGGTCGCTGCCGGACGGCGTGGGCGGTGG
CCGCCGCAGCAGCTGATGCTGAGCGCGGCGCTGCGGACCCTGAAGCATGTTCTGTACTAT
TCAAGACAGTGCTTAATGGTGTCCCGTAATCTTGGTTCAGTGGGATATGATCCTAATGAA
AAAACTTTTGATAAAATTCTTGTTGCTAATAGAGGAGAAATTGCATGTCGGGTTATTAGA
ACTTGCAAGAAGATGGGCATTAAGACAGTTGCCATCCACAGTGATGTTGATGCTAGTTCT
GTTCATGTGAAAATGGCGGATGAGGCTGTCTGTGTTGGCCCAGCTCCCACCAGTAAAAGC
TACCTCAACATGGATGCCATCATGGAAGCCATTAAGAAAACCAGGGCCCAAGCTGTACAT
CCAGGTTATGGATTCCTTTCAGAAAACAAAGAATTTGCCAGATGTTTGGCAGCAGAAGAT
GTCGTTTTCATTGGACCTGACACACATGCTATTCAAGCCATGGGCGACAAGATTGAAAGC
AAATTATTAGCTAAGAAAGCAGAGGTTAATACAATCCCTGGCTTTGATGGAGTAGTCAAG
GATGCAGAAGAAGCTGTCAGAATTGCAAGGGAAATTGGCTACCCTGTCATGATCAAGGCC
TCAGCAGGTGGTGGTGGGAAAGGCATGCGCATTGCTTGGGATGATGAAGAGACCAGGGAT
GGTTTTAGATTGTCATCTCAAGAAGCTGCTTCTAGTTTTGGCGATGATAGACTACTAATA
GAAAAATTTATTGATAATCCTCGTCATATAGAAATCCAGGTTCTAGGTGATAAACATGGG
AATGCTTTATGGCTTAATGAAAGAGAGTGCTCAATTCAGAGAAGAAATCAGAAGGTGGTG
GAGGAAGCACCAAGCATTTTTTTGGATGCGGAGACTCGAAGAGCGATGGGAGAACAAGCT
GTAGCTCTTGCCAGAGCAGTAAAATATTCCTCTGCTGGGACCGTGGAGTTCCTTGTGGAC
TCTAAGAAGAATTTTTATTTCTTGGAAATGAATACAAGACTCCAGGTTGAGCATCCTGTC
ACAGAATGCATTACTGGCCTGGACCTAGTCCAGGAAATGATCCGTGTTGCTAAGGGCTAC
CCTCTCAGGCACAAACAAGCTGATATTCGCATCAACGGCTGGGCAGTTGAATGTCGGGTT
TATGCTGAGGACCCCTACAAGTCTTTTGGTTTACCATCTATTGGGAGATTGTCTCAGTAC
CAAGAACCGTTACATCTACCTGGTGTCCGAGTGGACAGTGGCATCCAACCAGGAAGTGAT
ATTAGCATTTATTATGATCCTATGATTTCAAAACTAATCACATATGGCTCTGATAGAACT
GAGGCACTGAAGAGAATGGCAGATGCACTGGATAACTATGTTATTCGAGGTGTTACACAT
AATATTGCATTACTTCGAGAGGTGATAATCAACTCACGCTTTGTAAAAGGAGACATCAGC
ACTAAATTTCTCTCCGATGTGTATCCTGATGGCTTCAAAGGACACATGCTAACCAAGAGT
GAGAAGAACCAGTTATTGGCAATAGCATCATCATTGTTTGTGGCATTCCAGTTAAGAGCA
CAACATTTTCAAGAAAATTCAAGAATGCCTGTTATTAAACCAGACATAGCCAACTGGGAG
CTCTCAGTAAAATTGCATGATAAAGTTCATACCGTAGTAGCATCAAACAATGGGTCAGTG
TTCTCGGTGGAAGTTGATGGGTCGAAACTAAATGTGACCAGCACGTGGAACCTGGCTTCG
CCCTTATTGTCTGTCAGCGTTGATGGCACTCAGAGGACTGTCCAGTGTCTTTCTCGAGAA
GCAGGTGGAAACATGAGCATTCAGTTTCTTGGTACAGTGTACAAGGTGAATATCTTAACC
AGACTTGCCGCAGAATTGAACAAATTTATGCTGGAAAAAGTGACTGAGGACACAAGCAGT
GTTCTGCGTTCCCCGATGCCCGGAGTGGTGGTGGCCGTCTCTGTCAAGCCTGGAGACGCG
GTAGCAGAAGGTCAAGAAATTTGTGTGATTGAAGCCATGAAAATGCAGAATAGTATGACA
GCTGGGAAAACTGGCACGGTGAAATCTGTGCACTGTCAAGCTGGAGACACAGTTGGAGAA
GGGGATCTGCTCGTGGAGCTGGAATGA
|
| Enzyme 31 GenBank Gene ID |
AF385926 |
| Enzyme 31 GeneCard ID |
PCCA |
| Enzyme 31 GenAtlas ID |
PCCA |
| Enzyme 31 HGNC ID |
HGNC:8653 |
| Enzyme 31 Chromosome Location |
1 |
| Enzyme 31 Locus |
13q32 |
| Enzyme 31 SNPs |
SNPJam Report |
| Enzyme 31 General References |
- Campeau E, Desviat LR, Leclerc D, Wu X, Perez B, Ugarte M, Gravel RA: Structure of the PCCA gene and distribution of mutations causing propionic acidemia. Mol Genet Metab. 2001 Sep-Oct;74(1-2):238-47. [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 A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [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 ]
- Lamhonwah AM, Mahuran D, Gravel RA: Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA. Nucleic Acids Res. 1989 Jun 12;17(11):4396. [PubMed ]
- Stankovics J, Ledley FD: Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts. Am J Hum Genet. 1993 Jan;52(1):144-51. [PubMed ]
- Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [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 ]
- 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 ]
- Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed ]
- Richard E, Desviat LR, Perez B, Perez-Cerda C, Ugarte M: Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects. Identification of five novel mutations, one of them causing instability of the protein. Biochim Biophys Acta. 1999 Mar 30;1453(3):351-8. [PubMed ]
- Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed ]
- Yang X, Sakamoto O, Matsubara Y, Kure S, Suzuki Y, Aoki Y, Yamaguchi S, Takahashi Y, Nishikubo T, Kawaguchi C, Yoshioka A, Kimura T, Hayasaka K, Kohno Y, Iinuma K, Ohura T: Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia. Mol Genet Metab. 2004 Apr;81(4):335-42. [PubMed ]
- Campeau E, Dupuis L, Leon-Del-Rio A, Gravel R: Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia. Mol Genet Metab. 1999 May;67(1):11-22. [PubMed ]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5507 |
| Enzyme 32 Name |
Phenylalanyl-tRNA synthetase, mitochondrial |
| Enzyme 32 Synonyms |
- Phenylalanine--tRNA ligase
- PheRS
|
| Enzyme 32 Gene Name |
FARS2 |
| Enzyme 32 Protein Sequence |
>Phenylalanyl-tRNA synthetase, mitochondrial
MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQ
DDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVV
TTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRR
DQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVE
FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVN
SAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKY
PAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRH
MERTLSQREVRHIHQALQEAAVQLLGVEGRF
|
| Enzyme 32 Number of Residues |
451 |
| Enzyme 32 Molecular Weight |
52356.2 |
| Enzyme 32 Theoretical pI |
7.48 |
| Enzyme 32 GO Classification |
| Function |
- ATP binding
- RNA binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- cation binding
- ion binding
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- magnesium ion binding
- metal ion binding
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- phenylalanine-tRNA ligase activity
- purine nucleoside binding
- tRNA binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- phenylalanyl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- tRNA processing
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 32 General Function |
Involved in nucleotide binding |
| Enzyme 32 Specific Function |
Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins |
| Enzyme 32 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Phenylalanine and Tyrosine Metabolism (map00400 )
|
| Enzyme 32 Reactions |
- ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe [RN:R03660]
|
| 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 |
O95363 |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
SYFM_HUMAN |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1356 bp
ATGGTGGGCTCAGCTCTCAGGAGAGGTGCCCATGCATATGTCTACCTGGTGAGTAAGGCC
AGTCACATCTCCAGAGGCCATCAGCACCAGGCCTGGGGATCGAGGCCTCCTGCAGCAGAG
TGTGCCACCCAAAGAGCTCCAGGCAGTGTGGTGGAGCTGCTGGGCAAATCCTACCCTCAG
GACGACCACAGCAACCTCACCCGGAAGGTCCTCACCAGAGTTGGCAGGAACCTGCACAAC
CAGCAGCATCACCCTCTGTGGCTGATCAAGGAGAGGGTGAAGGAGCACTTCTACAAGCAG
TATGTGGGCCGCTTTGGGACCCCGTTGTTCTCGGTCTACGACAACCTTTCTCCAGTGGTC
ACGACCTGGCAGAACTTTGACAGCCTGCTCATCCCAGCTGATCACCCCAGCAGGAAGAAG
GGGGACAACTATTACCTGAATCGGACTCACATGCTGAGAGCGCACACGTCTGCACACCAG
TGGGACTTGCTGCACGCGGGACTGGATGCCTTCCTGGTGGTGGGTGATGTCTACAGGCGT
GACCAGATCGACTCCCAGCACTACCCTATTTTCCACCAGCTGGAGGCCGTGCGGCTCTTC
TCCAAGCATGAGTTATTTGCTGGTATAAAGGATGGAGAAAGCCTGCAGCTCTTTGAACAA
AGTTCTCGCTCTGCGCATAAACAAGAGACACACACCATGGAGGCCGTGAAGCTTGTAGAG
TTTGATCTTAAGCAAACGCTTACCAGGCTCATGGCACATCTTTTTGGAGATGAGCTGGAG
ATAAGATGGGTAGACTGCTACTTCCCTTTTACACATCCTTCCTTTGAGATGGAGATCAAC
TTTCATGGAGAATGGCTGGAAGTTCTTGGCTGCGGGGTGATGGAACAACAACTGGTCAAT
TCAGCTGGTGCTCAAGACCGAATCGGCTGGGCTTTTGGCCTAGGATTAGAAAGGCTAGCC
ATGATCCTCTACGACATCCCTGATATCCGTCTCTTCTGGTGTGAGGACGAGCGCTTCCTG
AAGCAGTTCTGTGTATCCAACATTAATCAGAAGGTGAAGTTTCAGCCTCTTAGCAAATAT
CCGGCTGTGATCAATGATATTTCATTCTGGTTGCCCTCTGAGAATTACGCAGAAAATGAT
TTCTATGACTTAGTCCGAACAATTGGAGGAGACCTGGTGGAAAAGGTTGATCTCATAGAC
AAGTTTGTACATCCAAAGACGCACAAGACCAGCCACTGCTACCGCATCACGTACCGCCAC
ATGGAACGGACTCTGTCCCAGAGAGAGGTCAGGCACATCCACCAGGCCTTGCAGGAGGCT
GCAGTCCAGCTGTTGGGTGTGGAGGGCAGGTTCTGA
|
| Enzyme 32 GenBank Gene ID |
AF097441 |
| Enzyme 32 GeneCard ID |
FARS2 |
| Enzyme 32 GenAtlas ID |
FARS2 |
| Enzyme 32 HGNC ID |
HGNC:21062 |
| Enzyme 32 Chromosome Location |
6 |
| Enzyme 32 Locus |
6p25.1 |
| Enzyme 32 SNPs |
SNPJam Report |
| Enzyme 32 General References |
- Bullard JM, Cai YC, Demeler B, Spremulli LL: Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase. J Mol Biol. 1999 May 14;288(4):567-77. [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 ]
- 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 ]
- Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M: The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase. Structure. 2008 Jul;16(7):1095-104. [PubMed ]
- Klipcan L, Moor N, Kessler N, Safro MG: Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine. Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11045-8. Epub 2009 Jun 22. [PubMed ]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5566 |
| Enzyme 33 Name |
Trifunctional purine biosynthetic protein adenosine-3 |
| Enzyme 33 Synonyms |
- Phosphoribosylamine--glycine ligase
- Glycinamide ribonucleotide synthetase
- GARS
- Phosphoribosylglycinamide synthetase
- Phosphoribosylformylglycinamidine cyclo-ligase
- AIR synthase
- AIRS
- Phosphoribosyl-aminoimidazole synthetase
- Phosphoribosylglycinamide formyltransferase
- 5'-phosphoribosylglycinamide transformylase
- GAR transformylase
- GART
|
| Enzyme 33 Gene Name |
GART |
| Enzyme 33 Protein Sequence |
>Trifunctional purine biosynthetic protein adenosine-3
MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
|
| Enzyme 33 Number of Residues |
1010 |
| Enzyme 33 Molecular Weight |
107766.3 |
| Enzyme 33 Theoretical pI |
6.68 |
| Enzyme 33 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cyclo-ligase activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- methyltransferase activity
- nucleoside binding
- phosphoribosylamine-glycine ligase activity
- phosphoribosylformylglycinamidine cyclo-ligase activity
- phosphoribosylglycinamide formyltransferase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 'de novo' IMP biosynthetic process
- IMP biosynthetic process
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine base biosynthetic process
- purine base metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 33 General Function |
Involved in catalytic activity |
| Enzyme 33 Specific Function |
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide [RN:R04144]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
31642 |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
P22102 |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PUR2_HUMAN |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>3033 bp
ATGGCAGCCCGAGTACTTATAATTGGCAGTGGAGGAAGGGAACATACGCTGGCCTGGAAA
CTTGCACAGTCTCATCATGTCAAACAAGTGTTGGTTGCCCCAGGAAACGCAGGCACTGCC
TGCTCTGAAAAGATTTCAAATACCGCCATCTCAATCAGTGACCACACTGCCCTTGCTCAA
TTCTGCAAAGAGAAGAAAATTGAATTTGTAGTTGTTGGACCAGAAGCACCTCTGGCTGCT
GGGATTGTTGGGAACCTGAGGTCTGCAGGAGTGCAATGCTTTGGCCCAACAGCAGAAGCG
GCTCAGTTAGAGTCCAGCAAAAGGTTTGCCAAAGAGTTTATGGACAGACATGGAATCCCA
ACCGCACAATGGAAGGCTTTCACCAAACCTGAAGAAGCCTGCAGCTTCATTTTGAGTGCA
GACTTCCCTGCTTTGGTTGTGAAGGCCAGTGGTCTTGCAGCTGGAAAAGGGGTGATTGTT
GCAAAGAGCAAAGAAGAGGCCTGCAAAGCTGTACAAGAGATCATGCAGGAGAAAGCCTTT
GGGGCAGCTGGAGAAACAATTGTCATTGAAGAACTTCTTGACGGAGAAGAGGTGTCGTGT
CTGTGTTTCACTGATGGCAAGACTGTGGCCCCCATGCCCCCAGCACAGGACCATAAGCGA
TTACTGGAGGGAGATGGTGGCCCTAACACAGGGGGAATGGGAGCCTATTGTCCAGCCCCT
CAGGTTTCTAATGATCTATTACTAAAAATTAAAGATACTGTTCTTCAGAGGACAGTGGAT
GGCATGCAGCAAGAGGGTACTCCATATACAGGTATTCTCTATGCTGGAATAATGCTGACC
AAGAATGGCCCAAAAGTTCTAGAGTTTAATTGCCGTTTTGGTGATCCAGAGTGCCAAGTA
ATCCTCCCACTTCTTAAAAGTGATCTTTATGAAGTGATTCAGTCCACCTTAGATGGACTG
CTCTGCACATCTCTGCCTGTTTGGCTAGAAAACCACACCGCCCTAACTGTTGTCATGGCA
AGTAAAGGTTATCCTGGAGACTACACCAAGGGTGTAGAGATAACAGGGTTTCCTGAGGCT
CAAGCTCTAGGACTGGAGGTGTTCCATGCAGGCACTGCCCTCAAAAATGGCAAAGTAGTA
ACTCATGGGGGTAGAGTTCTTGCAGTCACAGCCATCCGGGAAAATCTCATATCAGCCCTT
GAGGAAGCCAAGAAAGGACTAGCTGCTATAAAGTTTGAGGGAGCAATTTATAGGAAAGAC
GTCGGCTTTCGTGCCATAGCTTTCCTCCAGCAGCCCAGGAGTTTGACTTACAAGGAATCT
GGAGTAGATATCGCAGCTGGAAATATGCTGGTCAAGAAAATTCAGCCTTTAGCAAAAGCC
ACTTCCAGATCAGGCTGTAAAGTTGATCTTGGAGGTTTTGCTGGTCTTTTTGATTTAAAA
GCAGCTGGTTTCAAAGATCCCCTTCTGGCCTCTGGAACAGATGGCGTTGGAACTAAACTA
AAGATTGCCCAGCTATGCAATAAACATGATACCATTGGTCAAGATTTGGTAGCAATGTGT
GTTAATGATATTCTGGCACAAGGAGCAGAGCCCCTCTTCTTCCTTGATTACTTTTCCTGT
GGAAAACTTGACCTCAGTGTAACTGAAGCTGTTGTTGCTGGAATTGCTAAAGCTTGTGGA
AAAGCTGGATGTGCTCTCCTTGGAGGTGAAACAGCAGAAATGCCTGACATGTATCCCCCT
GGAGAGTATGACCTAGCTGGGTTTGCCGTTGGTGCCATGGAGCGAGATCAGAAACTCCCT
CACCTGGAAAGAATCACTGAGGGTGATGTTGTTGTTGGAATAGCTTCATCTGGTCTTCAT
AGCAATGGATTTAGCCTTGTGAGGAAAATCGTTGCAAAATCTTCCCTCCAGTACTCCTCT
CCAGCACCTGATGGTTGTGGTGACCAGACTTTAGGGGACTTACTTCTCACGCCTACCAGA
ATCTACAGCCATTCACTGTTACCTGTCCTACGTTCAGGACATGTCAAAGCCTTTGCCCAT
ATTACTGGTGGAGGATTACTAGAGAACATCCCCAGAGTCCTCCCTGAGAAACTTGGGGTA
GATTTAGATGCCCAGACCTGGAGGATCCCCAGGGTTTTCTCATGGTTGCAGCAGGAAGGA
CACCTCTCTGAGGAAGAGATGGCCAGAACATTTAACTGTGGGGTTGGCGCTGTCCTTGTG
GTATCAAAGGAGCAGACAGAGCAGATTCTGAGGGATATCCAGCAGCACAAGGAAGAAGCC
TGGGTGATTGGCAGTGTGGTTGCACGAGCTGAAGGTTCCCCACGTGTGAAAGTCAAGAAT
CTGATTGAAAGCATGCAAATAAATGGGTCAGTGTTGAAGAATGGCTCCCTGACAAATCAT
TTCTCTTTTGAAAAAAAAAAGGCCAGAGTGGCTGTCTTAATATCTGGAACAGGATCGAAC
CTGCAAGCACTTATAGACAGTACTCGGGAACCAAATAGCTCTGCACAAATTGATATTGTT
ATCTCCAACAAAGCCGCAGTAGCTGGGTTAGATAAAGCGGAAAGAGCTGGTATTCCCACT
AGAGTAATTAATCATAAACTGTATAAAAATCGTGTAGAATTTGACAGTGCAATTGACCTA
GTCCTTGAAGAGTTCTCCATAGACATAGTCTGTCTTGCAGGATTCATGAGAATTCTTTCT
GGCCCCTTTGTCCAAAAGTGGAATGGAAAAATGCTCAATATCCACCCATCCTTGCTCCCT
TCTTTTAAGGGTTCAAATGCCCATGAGCAAGCCCTGGAAACCGGAGTCACAGTTACTGGG
TGCACTGTACACTTTGTAGCTGAAGATGTGGATGCTGGACAGATTATTTTGCAAGAAGCT
GTTCCCGTGAAGAGGGGTGATACTGTCGCAACTCTTTCTGAAAGAGTAAAATTAGCAGAA
CATAAAATATTTCCTGCAGCCCTTCAGCTGGTGGCCAGTGGAACTGTACAGCTTGGAGAA
AATGGCAAGATCTGTTGGGTTAAAGAGGAATGA
|
| Enzyme 33 GenBank Gene ID |
X54199 |
| Enzyme 33 GeneCard ID |
GART |
| Enzyme 33 GenAtlas ID |
GART |
| Enzyme 33 HGNC ID |
HGNC:4163 |
| Enzyme 33 Chromosome Location |
2 |
| Enzyme 33 Locus |
21q22.1|21q22.11 |
| Enzyme 33 SNPs |
SNPJam Report |
| Enzyme 33 General References |
- Aimi J, Qiu H, Williams J, Zalkin H, Dixon JE: De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. Nucleic Acids Res. 1990 Nov 25;18(22):6665-72. [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 ]
- Kan JL, Moran RG: Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. Nucleic Acids Res. 1997 Aug 1;25(15):3118-23. [PubMed ]
- Schild D, Brake AJ, Kiefer MC, Young D, Barr PJ: Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2916-20. [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 ]
- 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 ]
- Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA: Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR. Biochemistry. 2002 Dec 3;41(48):14206-15. [PubMed ]
- Zhang Y, Desharnais J, Marsilje TH, Li C, Hedrick MP, Gooljarsingh LT, Tavassoli A, Benkovic SJ, Olson AJ, Boger DL, Wilson IA: Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry. 2003 May 27;42(20):6043-56. [PubMed ]
- Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL: The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry. 2005 Jul 26;44(29):9841-50. [PubMed ]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5570 |
| Enzyme 34 Name |
N-acylglucosamine 2-epimerase |
| Enzyme 34 Synonyms |
- AGE
- GlcNAc 2-epimerase
- N-acetyl-D-glucosamine 2-epimerase
- Renin-binding protein
- RnBP
|
| Enzyme 34 Gene Name |
RENBP |
| Enzyme 34 Protein Sequence |
>N-acylglucosamine 2-epimerase
MSKGLPARQDMEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYD
DLKYVWLQGRQVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTR
DGRPVKVQRTIFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQL
QGAPAAEPMAVPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVS
EGGKELPGCLGRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHG
GLFYFQDADNFCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQF
RDPEYGEWFGYLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPT
PACRGAE
|
| Enzyme 34 Number of Residues |
427 |
| Enzyme 34 Molecular Weight |
48830.6 |
| Enzyme 34 Theoretical pI |
6.32 |
| Enzyme 34 GO Classification |
| Function |
- catalytic activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, interconverting aldoses and ketoses
- isomerase activity
- mannose-6-phosphate isomerase activity
|
| Process |
- alcohol metabolic process
- hexose metabolic process
- mannose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 34 General Function |
Involved in catalytic activity |
| Enzyme 34 Specific Function |
Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity |
| Enzyme 34 Pathways |
|
| Enzyme 34 Reactions |
- N-acyl-D-glucosamine = N-acyl-D-mannosamine [RN:R02652]
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
213417820 |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P51606 |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
RENBP_HUMAN |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1284 bp
ATGAGCAAGGGTCTCCCAGCGCGACAGGACATGGAGAAAGAGCGAGAGACTCTGCAGGCC
TGGAAGGAGCGCGTGGGGCAGGAGCTGGACCGCGTGGTGGCTTTCTGGATGGAGCACTCC
CACGACCAGGAGCACGGGGGCTTCTTCACGTGCCTTGGCCGCGAGGGGCGGGTGTATGAT
GACCTCAAGTATGTGTGGCTGCAGGGGAGGCAGGTATGGATGTATTGTCGCCTGTACCGC
ACTTTCGAGCGCTTCCGCCATGCTCAGCTTCTGGACGCAGCAAAAGCAGGTGGTGAGTTC
TTGCTGCGGTATGCCCGGGTGGCACCTCCTGGCAAGAAGTGTGCCTTTGTGCTGACTCGG
GACGGCCGCCCGGTCAAGGTGCAGCGAACCATCTTCAGTGAGTGTTTCTACACCATGGCC
ATGAACGAGCTGTGGAGAGCCACAGGGGAAGTGCGGTACCAGACGGAAGCGGTGGAGATG
ATGGATCAGATCGTCCACTGGGTGCAGGAGGACGCGTCGGGACTGGGCCGGCCCCAGCTC
CAGGGGGCCCCGGCTGCGGAGCCCATGGCGGTGCCCATGATGCTACTGAACCTGGTGGAG
CAGCTCGGGGAGGCAGATGAGGAGCTGGCGGGCAAATACGCAGAGCTGGGGGACTGGTGC
GCCCGGAGGATTCTGCAGCACGTGCAGAGGGATGGACAAGCTGTGCTGGAGAATGTGTCA
GAGGGTGGCAAGGAACTTCCTGGCTGCCTGGGGAGACAGCAGAACCCAGGCCACACGCTG
GAAGCCGGCTGGTTTCTGCTCCGTCATTGCATTCGGAAAGGCGACCCCGAACTTCGAGCC
CACGTGATTGACAAGTTCCTATTGTTGCCCTTCCACTCCGGATGGGACCCTGACCACGGA
GGCCTCTTTTACTTCCAGGATGCTGATAACTTCTGCCCCACCCAGCTGGAGTGGGCCATG
AAGCTCTGGTGGCCACACAGTGAAGCCATGATTGCCTTCCTCATGGGTTACAGTGACAGT
GGGGACCCTGTGCTGCTGCGCCTCTTCTACCAAGTGGCTGAGTACACCTTCCGCCAGTTT
CGCGATCCCGAGTACGGGGAATGGTTTGGCTACCTGAGCCGAGAGGGCAAGGTGGCCCTC
TCCATCAAGGGAGGTCCTTTCAAAGGCTGCTTCCACGTGCCGCGGTGCCTAGCCATGTGC
GAGGAGATGCTGGGCGCCCTGCTGAGCCGCCCCGCCCCCGCCCCCTCCCCCGCCCCCACC
CCCGCCTGCCGAGGCGCGGAATAA
|
| Enzyme 34 GenBank Gene ID |
NM_002910.5 |
| Enzyme 34 GeneCard ID |
RENBP |
| Enzyme 34 GenAtlas ID |
RENBP |
| Enzyme 34 HGNC ID |
HGNC:9959 |
| Enzyme 34 Chromosome Location |
Not Available |
| Enzyme 34 Locus |
Not Available |
| Enzyme 34 SNPs |
SNPJam Report |
| Enzyme 34 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 ]
- 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 ]
- Inoue H, Takahashi S, Fukui K, Miyake Y: Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif. J Biochem (Tokyo). 1991 Oct;110(4):493-500. [PubMed ]
- Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Kobayashi M: Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase. J Biochem (Tokyo). 1999 Feb;125(2):348-53. [PubMed ]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
5572 |
| Enzyme 35 Name |
Nicotinamide mononucleotide adenylyltransferase 3 |
| Enzyme 35 Synonyms |
- NMN adenylyltransferase 3
- Nicotinate-nucleotide adenylyltransferase 3
- NaMN adenylyltransferase 3
- Pyridine nucleotide adenylyltransferase 3
- PNAT-3
|
| Enzyme 35 Gene Name |
NMNAT3 |
| Enzyme 35 Protein Sequence |
>Nicotinamide mononucleotide adenylyltransferase 3
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAA
SHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKAL
FSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESP
ILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWK
GKSTQSTEGKTS
|
| Enzyme 35 Number of Residues |
252 |
| Enzyme 35 Molecular Weight |
28321.5 |
| Enzyme 35 Theoretical pI |
9.69 |
| Enzyme 35 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- NAD biosynthetic process
- biosynthetic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Involved in nucleotidyltransferase activity |
| Enzyme 35 Specific Function |
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following injury |
| Enzyme 35 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
|
| Enzyme 35 Reactions |
- ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD+ [RN:R03005]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
14029540 |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q96T66 |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
NMNA3_HUMAN |
| Enzyme 35 PDB ID |
1NUU |
| Enzyme 35 PDB File |
Show |
| Enzyme 35 3D Structure |
|
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>759 bp
ATGAAGAGCCGAATACCTGTGGTGCTCCTGGCCTGTGGCTCCTTTAACCCCATCACCAAC
ATGCACCTGCGCATGTTTGAGGTGGCCAGAGATCACCTACACCAAACAGGAATGTACCAG
GTCATCCAGGGTATCATCTCTCCTGTCAACGACACCTATGGGAAGAAAGACCTCGCAGCT
TCTCATCACCGAGTGGCCATGGCCCGGCTGGCCCTGCAGACATCCGACTGGATCCGGGTG
GACCCTTGGGAGAGTGAGCAGGCACAGTGGATGGAGACAGTGAAGGTGCTGAGGCATCAT
CACAGCAAACTGCTCAGATCTCCACCCCAGATGGAAGGCCCAGACCATGGCAAGGCACTC
TTCTCGACCCCTGCAGCTGTGCCTGAGCTGAAGCTTCTCTGTGGGGCAGACGTCTTGAAG
ACCTTCCAGACCCCCAACCTCTGGAAGGATGCGCACATCCAGGAAATAGTGGAGAAGTTT
GGCTTGGTGTGCGTGGGCCGAGTAAGTCACGACCCAAAAGGTTACATCGCAGAATCTCCC
ATCCTACGGATGCACCAGCACAACATTCACCTGGCCAAGGAGCCTGTGCAGAATGAGATC
AGTGCCACATACATCAGGCGAGCCTTGGGCCAAGGGCAGAGCGTAAAGTACCTGATTCCC
GATGCTGTCATCACGTACATCAAGGACCATGGCCTCTACACCAAGGGCAGTACCTGGAAA
GGCAAAAGCACCCAGAGCACTGAGGGCAAGACAAGCTAG
|
| Enzyme 35 GenBank Gene ID |
AF345564 |
| Enzyme 35 GeneCard ID |
NMNAT3 |
| Enzyme 35 GenAtlas ID |
NMNAT3 |
| Enzyme 35 HGNC ID |
HGNC:20989 |
| Enzyme 35 Chromosome Location |
3 |
| Enzyme 35 Locus |
3q23 |
| Enzyme 35 SNPs |
SNPJam Report |
| Enzyme 35 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 ]
- Berger F, Lau C, Dahlmann M, Ziegler M: Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J Biol Chem. 2005 Oct 28;280(43):36334-41. Epub 2005 Aug 23. [PubMed ]
- Sorci L, Cimadamore F, Scotti S, Petrelli R, Cappellacci L, Franchetti P, Orsomando G, Magni G: Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis. Biochemistry. 2007 Apr 24;46(16):4912-22. Epub 2007 Apr 3. [PubMed ]
- Zhang X, Kurnasov OV, Karthikeyan S, Grishin NV, Osterman AL, Zhang H: Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis. J Biol Chem. 2003 Apr 11;278(15):13503-11. Epub 2003 Feb 6. [PubMed ]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
5574 |
| Enzyme 36 Name |
Nicotinamide mononucleotide adenylyltransferase 2 |
| Enzyme 36 Synonyms |
- NMN adenylyltransferase 2
- Nicotinate-nucleotide adenylyltransferase 2
- NaMN adenylyltransferase 2
|
| Enzyme 36 Gene Name |
NMNAT2 |
| Enzyme 36 Protein Sequence |
>Nicotinamide mononucleotide adenylyltransferase 2
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGL
VSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTP
SMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENA
NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRI
MNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQ
LYINASG
|
| Enzyme 36 Number of Residues |
307 |
| Enzyme 36 Molecular Weight |
34438.4 |
| Enzyme 36 Theoretical pI |
7.07 |
| Enzyme 36 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- NAD biosynthetic process
- biosynthetic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Involved in nucleotidyltransferase activity |
| Enzyme 36 Specific Function |
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannnot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+) |
| Enzyme 36 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
|
| Enzyme 36 Reactions |
- ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD+ [RN:R03005]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
24307989 |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q9BZQ4 |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
NMNA2_HUMAN |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>924 bp
ATGACCGAGACCACCAAGACCCACGTTATCTTGCTCGCCTGCGGCAGCTTCAATCCCATC
ACCAAAGGGCACATTCAGATGTTTGAAAGAGCCAGGGATTATCTGCACAAAACTGGAAGG
TTTATTGTGATTGGCGGGATTGTCTCCCCTGTCCACGACTCCTATGGAAAACAGGGCCTC
GTGTCAAGCCGGCACCGTCTCATCATGTGTCAGCTGGCCGTCCAGAATTCTGATTGGATC
AGGGTGGACCCTTGGGAGTGCTACCAGGACACCTGGCAGACGACCTGCAGCGTGTTGGAA
CACCACCGGGACCTCATGAAGAGGGTGACTGGCTGCATCCTCTCCAATGTCAACACACCT
TCCATGACACCTGTGATCGGACAGCCACAAAACGAGACCCCCCAGCCCATTTACCAGAAC
AGCAACGTGGCCACCAAGCCCACTGCAGCCAAGATCTTGGGGAAGGTGGGAGAAAGCCTC
AGCCGGATCTGCTGTGTCCGCCCGCCGGTGGAGCGTTTCACCTTTGTAGATGAGAATGCC
AATCTGGGCACGGTGATGCGGTATGAAGAGATTGAGCTACGGATCCTGCTGCTGTGTGGT
AGTGACCTGCTGGAGTCCTTCTGCATCCCAGGGCTCTGGAACGAGGCAGATATGGAGGTG
ATTGTTGGTGACTTTGGGATTGTGGTGGTGCCCCGGGATGCAGCCGACACAGACCGAATC
ATGAATCACTCCTCAATACTCCGCAAATACAAAAACAACATCATGGTGGTGAAGGATGAC
ATCAACCATCCCATGTCTGTTGTCAGCTCAACCAAGAGCAGGCTGGCCCTGCAGCATGGG
GACGGCCATGTTGTGGATTACCTGTCCCAGCCGGTCATCGACTACATCCTCAAAAGCCAG
CTGTACATCAATGCCTCCGGCTAG
|
| Enzyme 36 GenBank Gene ID |
NM_015039.2 |
| Enzyme 36 GeneCard ID |
NMNAT2 |
| Enzyme 36 GenAtlas ID |
NMNAT2 |
| Enzyme 36 HGNC ID |
HGNC:16789 |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
1q25 |
| Enzyme 36 SNPs |
SNPJam Report |
| Enzyme 36 General References |
- Sood R, Bonner TI, Makalowska I, Stephan DA, Robbins CM, Connors TD, Morgenbesser SD, Su K, Faruque MU, Pinkett H, Graham C, Baxevanis AD, Klinger KW, Landes GM, Trent JM, Carpten JD: Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus. Genomics. 2001 Apr 15;73(2):211-22. [PubMed ]
- Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, Nomura N, Ohara O: Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. DNA Res. 1997 Oct 31;4(5):345-9. [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 ]
- Raffaelli N, Sorci L, Amici A, Emanuelli M, Mazzola F, Magni G: Identification of a novel human nicotinamide mononucleotide adenylyltransferase. Biochem Biophys Res Commun. 2002 Oct 4;297(4):835-40. [PubMed ]
- Yalowitz JA, Xiao S, Biju MP, Antony AC, Cummings OW, Deeg MA, Jayaram HN: Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas. Biochem J. 2004 Jan 15;377(Pt 2):317-26. [PubMed ]
- Berger F, Lau C, Dahlmann M, Ziegler M: Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J Biol Chem. 2005 Oct 28;280(43):36334-41. Epub 2005 Aug 23. [PubMed ]
- Sorci L, Cimadamore F, Scotti S, Petrelli R, Cappellacci L, Franchetti P, Orsomando G, Magni G: Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis. Biochemistry. 2007 Apr 24;46(16):4912-22. Epub 2007 Apr 3. [PubMed ]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
5581 |
| Enzyme 37 Name |
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 |
| Enzyme 37 Synonyms |
- PAPS synthase 1
- PAPSS 1
- Sulfurylase kinase 1
- SK 1
- SK1
- Sulfate adenylyltransferase
- ATP-sulfurylase
- Sulfate adenylate transferase
- SAT
- Adenylyl-sulfate kinase
- 3'-phosphoadenosine-5'-phosphosulfate synthase
- APS kinase
- Adenosine-5'-phosphosulfate 3'-phosphotransferase
- Adenylylsulfate 3'-phosphotransferase
|
| Enzyme 37 Gene Name |
PAPSS1 |
| Enzyme 37 Protein Sequence |
>Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA
|
| Enzyme 37 Number of Residues |
624 |
| Enzyme 37 Molecular Weight |
70832.7 |
| Enzyme 37 Theoretical pI |
6.85 |
| Enzyme 37 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylyltransferase activity
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- nucleotidyltransferase activity
- purine nucleoside binding
- sulfate adenylyltransferase (ATP) activity
- sulfate adenylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- sulfate assimilation
- sulfur metabolic process
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in ATP binding |
| Enzyme 37 Specific Function |
Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells |
| Enzyme 37 Pathways |
|
| Enzyme 37 Reactions |
- ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
2673862 |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
O43252 |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
PAPS1_HUMAN |
| Enzyme 37 PDB ID |
1X6V |
| Enzyme 37 PDB File |
Show |
| Enzyme 37 3D Structure |
|
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>1875 bp
ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG
|
| Enzyme 37 GenBank Gene ID |
Y10387 |
| Enzyme 37 GeneCard ID |
PAPSS1 |
| Enzyme 37 GenAtlas ID |
PAPSS1 |
| Enzyme 37 HGNC ID |
HGNC:8603 |
| Enzyme 37 Chromosome Location |
4 |
| Enzyme 37 Locus |
4q24 |
| Enzyme 37 SNPs |
SNPJam Report |
| Enzyme 37 General References |
- Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed ]
- Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed ]
- Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed ]
- Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [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 ]
- Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed ]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
5589 |
| Enzyme 38 Name |
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 |
| Enzyme 38 Synonyms |
- PAPS synthase 2
- PAPSS 2
- Sulfurylase kinase 2
- SK 2
- SK2
- Sulfate adenylyltransferase
- ATP-sulfurylase
- Sulfate adenylate transferase
- SAT
- Adenylyl-sulfate kinase
- 3'-phosphoadenosine-5'-phosphosulfate synthase
- APS kinase
- Adenosine-5'-phosphosulfate 3'-phosphotransferase
- Adenylylsulfate 3'-phosphotransferase
|
| Enzyme 38 Gene Name |
PAPSS2 |
| Enzyme 38 Protein Sequence |
>Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN
|
| Enzyme 38 Number of Residues |
614 |
| Enzyme 38 Molecular Weight |
69500.2 |
| Enzyme 38 Theoretical pI |
8.13 |
| Enzyme 38 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylyltransferase activity
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- nucleotidyltransferase activity
- purine nucleoside binding
- sulfate adenylyltransferase (ATP) activity
- sulfate adenylyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- sulfate assimilation
- sulfur metabolic process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Involved in ATP binding |
| Enzyme 38 Specific Function |
Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important role in skeletogenesis during postnatal growth |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
5052075 |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
O95340 |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
PAPS2_HUMAN |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1845 bp
ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAAGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACTCGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCTAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA
|
| Enzyme 38 GenBank Gene ID |
AF074331 |
| Enzyme 38 GeneCard ID |
PAPSS2 |
| Enzyme 38 GenAtlas ID |
PAPSS2 |
| Enzyme 38 HGNC ID |
HGNC:8604 |
| Enzyme 38 Chromosome Location |
1 |
| Enzyme 38 Locus |
10q24 |
| Enzyme 38 SNPs |
SNPJam Report |
| Enzyme 38 General References |
- ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed ]
- Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed ]
- Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [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 ]
- Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed ]
- Noordam C, Dhir V, McNelis JC, Schlereth F, Hanley NA, Krone N, Smeitink JA, Smeets R, Sweep FC, Claahsen-van der Grinten HL, Arlt W: Inactivating PAPSS2 mutations in a patient with premature pubarche. N Engl J Med. 2009 May 28;360(22):2310-8. [PubMed ]
- Xu ZH, Freimuth RR, Eckloff B, Wieben E, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (PAPSS2) pharmacogenetics: gene resequencing, genetic polymorphisms and functional characterization of variant allozymes. Pharmacogenetics. 2002 Jan;12(1):11-21. [PubMed ]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
5595 |
| Enzyme 39 Name |
Carbamoyl-phosphate synthase [ammonia], mitochondrial |
| Enzyme 39 Synonyms |
- Carbamoyl-phosphate synthetase I
- CPSase I
|
| Enzyme 39 Gene Name |
CPS1 |
| Enzyme 39 Protein Sequence |
>Carbamoyl-phosphate synthase [ammonia], mitochondrial
MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYS
FGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKY
LESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTML
GKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGA
EVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLIT
GLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQT
NEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRV
EVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQAD
TVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVES
IMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGIC
PNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHT
GDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLS
RSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDR
FHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLR
KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMT
EETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYV
TYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETV
STDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSP
LQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMN
VVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAG
VHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRA
SRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRD
ADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQ
LHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPN
NNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
|
| Enzyme 39 Number of Residues |
1500 |
| Enzyme 39 Molecular Weight |
164938.1 |
| Enzyme 39 Theoretical pI |
6.71 |
| Enzyme 39 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbamoyl-phosphate synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- glutamine metabolic process
- metabolic process
- nitrogen compound metabolic process
|
| Component |
| — |
|
| Enzyme 39 General Function |
Involved in catalytic activity |
| Enzyme 39 Specific Function |
Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell |
| Enzyme 39 Pathways |
|
| Enzyme 39 Reactions |
- 2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate [RN:R00149]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
5020420 |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P31327 |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
CPSM_HUMAN |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>4503 bp
ATGACGAGGATTTTGACAGCTTTCAAAGTGGTGAGGACACTGAAGACTGGTTTTGGCTTT
ACCAATGTGACTGCACACCAAAAATGGAAATTTTCAAGACCTGGCATCAGGCTCCTTTCT
GTCAAGGCACAGACAGCACACATTGTCCTGGAAGATGGAACTAAGATGAAAGGTTACTCC
TTTGGCCATCCATCCTCTGTTGCTGGTGAAGTGGTTTTTAATACTGGCCTGGGAGGGTAC
CCAGAAGCTATTACTGACCCTGCCTACAAAGGACAGATTCTCACAATGGCCAACCCTATT
ATTGGGAATGGTGGAGCTCCTGATACTACTGCTCTGGATGAACTGGGACTTAGCAAATAT
TTGGAGTCTAATGGAATCAAGGTTTCAGGTTTGCTGGTGCTGGATTATAGTAAAGACTAC
AACCACTGGCTGGCTACCAAGAGTTTAGGGCAATGGCTACAGGAAGAAAAGGTTCCTGCA
ATTTATGGAGTGGACACAAGAATGCTGACTAAAATAATTCGGGATAAGGGTACCATGCTT
GGGAAGATTGAATTTGAAGGTCAGCCTGTGGATTTTGTGGATCCAAATAAACAGAATTTG
ATTGCTGAGGTTTCAACCAAGGATGTCAAAGTGTACGGCAAAGGAAACCCCACAAAAGTG
GTAGCTGTAGACTGTGGGATTAAAAACAATGTAATCCGCCTGCTAGTAAAGCGAGGAGCT
GAAGTGCACTTAGTTCCCTGGAACCATGATTTCACCAAGATGGAGTATGATGGGATTTTG
ATCGCGGGAGGACCGGGGAACCCAGCTCTTGCAGAACCACTAATTCAGAATGTCAGAAAG
ATTTTGGAGAGTGATCGCAAGGAGCCATTGTTTGGAATCAGTACAGGAAACTTAATAACA
GGATTGGCTGCTGGTGCCAAAACCTACAAGATGTCCATGGCCAACAGAGGGCAGAATCAG
CCTGTTTTGAATATCACAAACAAACAGGCTTTCATTACTGCTCAGAATCATGGCTATGCC
TTGGACAACACCCTCCCTGCTGGCTGGAAACCACTTTTTGTGAATGTCAACGATCAAACA
AATGAGGGGATTATGCATGAGAGCAAACCCTTCTTCGCTGTGCAGTTCCACCCAGAGGTC
ACCCCGGGGCCAATAGACACTGAGTACCTGTTTGATTCCTTTTTCTCACTGATAAAGAAA
GGAAAAGCTACCACCATTACATCAGTCTTACCGAAGCCAGCACTAGTTGCATCTCGGGTT
GAGGTTTCCAAAGTCCTTATTCTAGGATCAGGAGGTCTGTCCATTGGTCAGGCTGGAGAA
TTTGATTACTCAGGATCTCAAGCTGTAAAAGCCATGAAGGAAGAAAATGTCAAAACTGTT
CTGATGAACCCAAACATTGCATCAGTCCAGACCAATGAGGTGGGCTTAAAGCAAGCGGAT
ACTGTCTACTTTCTTCCCATCACCCCTCAGTTTGTCACAGAGGTCATCAAGGCAGAACAG
CCAGATGGGTTAATTCTGGGCATGGGTGGCCAGACAGCTCTGAACTGTGGAGTGGAACTA
TTCAAGAGAGGTGTGCTCAAGGAATATGGTGTGAAAGTCCTGGGAACTTCAGTTGAGTCC
ATTATGGCTACGGAAGACAGGCAGCTGTTTTCAGATAAACTAAATGAGATCAATGAAAAG
ATTGCTCCAAGTTTTGCAGTGGAATCGATTGAGGATGCACTGAAGGCAGCAGACACCATT
GGCTACCCAGTGATGATCCGTTCCGCCTATGCACTGGGTGGGTTAGGCTCAGGCATCTGT
CCCAACAGAGAGACTTTGATGGACCTCAGCACAAAGGCCTTTGCTATGACCAACCAAATT
CTGGTGGAGAAGTCAGTGACAGGTTGGAAAGAAATAGAATATGAAGTGGTTCGAGATGCT
GATGACAATTGTGTCACTGTCTGTAACATGGAAAATGTTGATGCCATGGGTGTTCACACA
GGTGACTCAGTTGTTGTGGCTCCTGCCCAGACACTCTCCAATGCCGAGTTTCAGATGTTG
AGACGTACTTCAATCAATGTTGTTCGCCACTTGGGCATTGTGGGTGAATGCAACATTCAG
TTTGCCCTTCATCCTACCTCAATGGAATACTGCATCATTGAAGTGAATGCCAGACTGTCC
CGAAGCTCTGCTCTGGCCTCAAAAGCCACTGGCTACCCATTGGCATTCATTGCTGCAAAG
ATTGCCCTAGGAATCCCACTTCCAGAAATTAAGAACGTCGTATCCGGGAAGACATCAGCC
TGTTTTGAACCTAGCCTGGATTACATGGTCACCAAGATTCCCCGCTGGGATCTTGACCGT
TTTCATGGAACATCTAGCCGAATTGGTAGCTCTATGAAAAGTGTAGGAGAGGTCATGGCT
ATTGGTCGTACCTTTGAGGAGAGTTTCCAGAAAGCTTTACGGATGTGCCACCCATCTATA
GAAGGTTTCACTCCCCGTCTCCCAATGAACAAAGAATGGCCATCTAATTTAGATCTTAGA
AAAGAGTTGTCTGAACCAAGCAGCACGCGTATCTATGCCATTGCCAAGGCCATTGATGAC
AACATGTCCCTTGATGAGATTGAGAAGCTCACATACATTGACAAGTGGTTTTTGTATAAG
ATGCGTGATATTTTAAACATGGAAAAGACACTGAAAGGGCTCAACAGTGAGTCCATGACA
GAAGAAACCCTGAAAAGGGCAAAGGAGATTGGGTTCTCAGATAAGCAGATTTCAAAATGC
CTTGGGCTCACTGAGGCCCAGACAAGGGAGCTGAGGTTAAAGAAAAACATCCACCCTTGG
GTTAAACAGATTGATACACTGGCTGCAGAATACCCATCAGTAACAAACTATCTCTATGTT
ACCTACAATGGTCAGGAGCATGATGTCAATTTTGATGACCATGGAATGATGGTGCTAGGC
TGTGGTCCATATCACATTGGCAGCAGTGTGGAATTTGATTGGTGTGCTGTCTCTAGTATC
CGCACACTGCGTCAACTTGGCAAGAAGACGGTGGTGGTGAATTGCAATCCTGAGACTGTG
AGCACAGACTTTGATGAGTGTGACAAACTGTACTTTGAAGAGTTGTCCTTGGAGAGAATC
CTAGACATCTACCATCAGGAGGCATGTGGTGGCTGCATCATATCAGTTGGAGGCCAGATT
CCAAACAACCTGGCAGTTCCTCTATACAAGAATGGTGTCAAGATCATGGGCACAAGCCCC
CTGCAGATCGACAGGGCTGAGGATCGCTCCATCTTCTCAGCTGTCTTGGATGAGCTGAAG
GTGGCTCAGGCACCTTGGAAAGCTGTTAATACTTTGAATGAAGCACTGGAATTTGCAAAG
TCTGTGGACTACCCCTGCTTGTTGAGGCCTTCCTATGTTTTGAGTGGGTCTGCTATGAAT
GTGGTATTCTCTGAGGATGAGATGAAAAAATTCCTAGAAGAGGCGACTAGAGTTTCTCAG
GAGCACCCAGTGGTCCTGACAAAATTTGTTGAAGGGGCCCGAGAAGTAGAAATGGACGCT
GTTGGCAAAGATGGAAGGGTTATCTCTCATGCCATCTCTGAACATGTTGAAGATGCAGGT
GTCCACTCGGGAGATGCCACTCTGATGCTGCCCACACAAACCATCAGCCAAGGGGCCATT
GAAAAGGTGAAGGATGCTACCCGGAAGATTGCAAAGGCTTTTGCCATCTCTGGTCCATTC
AACGTCCAATTTCTTGTCAAAGGAAATGATGTCTTGGTGATTGAGTGTAACTTGAGAGCT
TCTCGATCCTTCCCCTTTGTTTCCAAGACTCTTGGGGTTGACTTCATTGATGTGGCCACC
AAGGTGATGATTGGAGAGAATGTTGATGAGAAACATCTTCCAACATTGGACCATCCCATA
ATTCCTGCTGACTATGTTGCAATTAAGGCTCCCATGTTTTCCTGGCCCCGGTTGAGGGAT
GCTGACCCCATTCTGAGATGTGAGATGGCTTCCACTGGAGAGGTGGCTTGCTTTGGTGAA
GGTATTCATACAGCCTTCCTAAAGGCAATGCTTTCCACAGGATTTAAGATACCCCAGAAA
GGCATCCTGATAGGCATCCAGCAATCATTCCGGCCAAGATTCCTTGGTGTGGCTGAACAA
TTACACAATGAAGGTTTCAAGCTGTTTGCCACGGAAGCCACATCAGACTGGCTCAACGCC
AACAATGTCCCTGCCACCCCAGTGGCATGGCCGTCTCAAGAAGGACAGAATCCCAGCCTC
TCTTCCATCAGAAAATTGATTAGAGATGGCAGCATTGACCTAGTGATTAACCTTCCCAAC
AACAACACTAAATTTGTCCATGATAATTATGTGATTCGGAGGACAGCTGTTGATAGTGGA
ATCCCTCTCCTCACTAATTTTCAGGTGACCAAACTTTTTGCTGAAGCTGTGCAGAAATCT
CGCAAGGTGGACTCCAAGAGTCTTTTCCACTACAGGCAGTACAGTGCTGGAAAAGCAGCA
TAG
|
| Enzyme 39 GenBank Gene ID |
AF154830 |
| Enzyme 39 GeneCard ID |
CPS1 |
| Enzyme 39 GenAtlas ID |
CPS1 |
| Enzyme 39 HGNC ID |
HGNC:2323 |
| Enzyme 39 Chromosome Location |
2 |
| Enzyme 39 Locus |
2q35 |
| Enzyme 39 SNPs |
SNPJam Report |
| Enzyme 39 General References |
- Haraguchi Y, Uchino T, Takiguchi M, Endo F, Mori M, Matsuda I: Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia. Gene. 1991 Nov 15;107(2):335-40. [PubMed ]
- Finckh U, Kohlschutter A, Schafer H, Sperhake K, Colombo JP, Gal A: Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1. Hum Mutat. 1998;12(3):206-11. [PubMed ]
- Summar ML, Hall LD, Eeds AM, Hutcheson HB, Kuo AN, Willis AS, Rubio V, Arvin MK, Schofield JP, Dawson EP: Characterization of genomic structure and polymorphisms in the human carbamyl phosphate synthetase I gene. Gene. 2003 Jun 5;311:51-7. [PubMed ]
- Funghini S, Donati MA, Pasquini E, Zammarchi E, Morrone A: Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions. Hum Mutat. 2003 Oct;22(4):340-1. [PubMed ]
- Haberle J, Schmidt E, Pauli S, Rapp B, Christensen E, Wermuth B, Koch HG: Gene structure of human carbamylphosphate synthetase 1 and novel mutations in patients with neonatal onset. Hum Mutat. 2003 Apr;21(4):444. [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 ]
- Aoshima T, Kajita M, Sekido Y, Kikuchi S, Yasuda I, Saheki T, Watanabe K, Shimokata K, Niwa T: Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency. Hum Hered. 2001;52(2):99-101. [PubMed ]
- Pearson DL, Dawling S, Walsh WF, Haines JL, Christman BW, Bazyk A, Scott N, Summar ML: Neonatal pulmonary hypertension--urea-cycle intermediates, nitric oxide production, and carbamoyl-phosphate synthetase function. N Engl J Med. 2001 Jun 14;344(24):1832-8. [PubMed ]
- Wakutani Y, Nakayasu H, Takeshima T, Adachi M, Kawataki M, Kihira K, Sawada H, Bonno M, Yamamoto H, Nakashima K: Mutational analysis of carbamoylphosphate synthetase I deficiency in three Japanese patients. J Inherit Metab Dis. 2004;27(6):787-8. [PubMed ]
- Haberle J, Koch HG: Genetic approach to prenatal diagnosis in urea cycle defects. Prenat Diagn. 2004 May;24(5):378-83. [PubMed ]
- Kurokawa K, Yorifuji T, Kawai M, Momoi T, Nagasaka H, Takayanagi M, Kobayashi K, Yoshino M, Kosho T, Adachi M, Otsuka H, Yamamoto S, Murata T, Suenaga A, Ishii T, Terada K, Shimura N, Kiwaki K, Shintaku H, Yamakawa M, Nakabayashi H, Wakutani Y, Nakahata T: Molecular and clinical analyses of Japanese patients with carbamoylphosphate synthetase 1 (CPS1) deficiency. J Hum Genet. 2007;52(4):349-54. Epub 2007 Feb 20. [PubMed ]
- Moonen RM, Reyes I, Cavallaro G, Gonzalez-Luis G, Bakker JA, Villamor E: The T1405N carbamoyl phosphate synthetase polymorphism does not affect plasma arginine concentrations in preterm infants. PLoS One. 2010 May 25;5(5):e10792. [PubMed ]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
5655 |
| Enzyme 40 Name |
S-adenosylmethionine synthase isoform type-1 |
| Enzyme 40 Synonyms |
- AdoMet synthase 1
- Methionine adenosyltransferase 1
- MAT 1
- Methionine adenosyltransferase I/III
- MAT-I/III
|
| Enzyme 40 Gene Name |
MAT1A |
| Enzyme 40 Protein Sequence |
>S-adenosylmethionine synthase isoform type-1
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
|
| Enzyme 40 Number of Residues |
395 |
| Enzyme 40 Molecular Weight |
43647.6 |
| Enzyme 40 Theoretical pI |
6.24 |
| Enzyme 40 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- methionine adenosyltransferase activity
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- cellular metabolic process
- metabolic process
- one-carbon metabolic process
|
| Component |
| — |
|
| Enzyme 40 General Function |
Involved in methionine adenosyltransferase activity |
| Enzyme 40 Specific Function |
Catalyzes the formation of S-adenosylmethionine from methionine and ATP |
| Enzyme 40 Pathways |
|
| Enzyme 40 Reactions |
- ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine [RN:R00177]
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
55959182 |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q00266 |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
METK1_HUMAN |
| Enzyme 40 PDB ID |
1O9T |
| Enzyme 40 PDB File |
Show |
| Enzyme 40 3D Structure |
|
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1188 bp
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCTACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGGCGGCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTAGACCGCTCAGCTGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGATTTGGACTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
|
| Enzyme 40 GenBank Gene ID |
AL359195 |
| Enzyme 40 GeneCard ID |
MAT1A |
| Enzyme 40 GenAtlas ID |
MAT1A |
| Enzyme 40 HGNC ID |
HGNC:6903 |
| Enzyme 40 Chromosome Location |
1 |
| Enzyme 40 Locus |
10q22 |
| Enzyme 40 SNPs |
SNPJam Report |
| Enzyme 40 General References |
- Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed ]
- Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [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 ]
- Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed ]
- Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed ]
- Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed ]
- Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed ]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
5668 |
| Enzyme 41 Name |
Inosine triphosphate pyrophosphatase |
| Enzyme 41 Synonyms |
- ITPase
- Inosine triphosphatase
- Putative oncogene protein hlc14-06-p
|
| Enzyme 41 Gene Name |
ITPA |
| Enzyme 41 Protein Sequence |
>Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
|
| Enzyme 41 Number of Residues |
194 |
| Enzyme 41 Molecular Weight |
21445.5 |
| Enzyme 41 Theoretical pI |
5.34 |
| Enzyme 41 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 41 General Function |
Involved in hydrolase activity |
| Enzyme 41 Specific Function |
Hydrolyzes ITP and dITP to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. May be the major enzyme responsible for regulating ITP concentration in cells |
| Enzyme 41 Pathways |
|
| Enzyme 41 Reactions |
- a nucleoside triphosphate + H2O = a nucleotide + diphosphate [RN:R01532]
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
21104378 |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q9BY32 |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
ITPA_HUMAN |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCATGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAAGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAATACTTTGGCAGTTTGGCAGCTTGA
|
| Enzyme 41 GenBank Gene ID |
AB062127 |
| Enzyme 41 GeneCard ID |
ITPA |
| Enzyme 41 GenAtlas ID |
ITPA |
| Enzyme 41 HGNC ID |
HGNC:6176 |
| Enzyme 41 Chromosome Location |
2 |
| Enzyme 41 Locus |
20p |
| Enzyme 41 SNPs |
SNPJam Report |
| Enzyme 41 General References |
- Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [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 ]
- Stenmark P, Kursula P, Flodin S, Graslund S, Landry R, Nordlund P, Schuler H: Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T. J Biol Chem. 2007 Feb 2;282(5):3182-7. Epub 2006 Nov 29. [PubMed ]
- Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed ]
- Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed ]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
5755 |
| Enzyme 42 Name |
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial |
| Enzyme 42 Synonyms |
- MCCase subunit beta
- 3-methylcrotonyl-CoA carboxylase 2
- 3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit
- 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
|
| Enzyme 42 Gene Name |
MCCC2 |
| Enzyme 42 Protein Sequence |
>Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERV
EHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGII
TGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPR
QADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIF
LAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKL
DVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFA
RIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAK
DGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAAN
VLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLV
LGLSFSAALNAPIEKTDFGIFRM
|
| Enzyme 42 Number of Residues |
563 |
| Enzyme 42 Molecular Weight |
61332.7 |
| Enzyme 42 Theoretical pI |
7.75 |
| Enzyme 42 GO Classification |
| Function |
- catalytic activity
- ligase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 42 General Function |
Involved in ligase activity |
| Enzyme 42 Specific Function |
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA |
| Enzyme 42 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 42 Reactions |
- ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA [RN:R04138]
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
Not Available |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q9HCC0 |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
MCCB_HUMAN |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1692 bp
ATGTGGGCCGTCCTGAGGTTAGCCCTGCGGCCGTGTGCCCGCGCCTCTCCCGCCGGGCCG
CGCGCCTATCACGGGGACTCGGTGGCCTCGCTGGGCACCCAGCCGGACTTGGGCTCTGCC
CTCTACCAGGAGAACTACAAGCAGATGAAAGCACTAGTAAATCAGCTCCATGAACGAGTG
GAGCATATAAAACTAGGAGGTGGTGAGAAAGCCCGAGCACTTCACATATCAAGAGGAAAA
CTATTGCCCAGAGAAAGAATTGACAATCTCATAGACCCAGGGTCTCCATTTCTGGAATTA
TCCCAGTTTGCAGGTTACCAGTTATATGACAATGAGGAGGTGCCAGGAGGTGGCATTATT
ACAGGCATTGGAAGAGTATCAGGAGTAGAATGCATGATTATTGCCAATGATGCCACCGTC
AAAGGAGGTGCCTACTACCCAGTGACTGTGAAAAAACAATTACGGGCCCAAGAAATTGCC
ATGCAAAACAGGCTCCCCTGCATCTACTTAGTTGATTCGGGAGGAGCATACTTACCTCGA
CAAGCAGATGTGTTTCCAGATCGAGACCACTTTGGCCGTACATTCTATAATCAGGCAATT
ATGTCTTCTAAAAATATTGCACAGATCGCAGTGGTCATGGGCTCCTGCACCGCAGGAGGA
GCCTATGTGCCTGCCATGGCTGATGAAAACATCATTGTACGCAAGCAGGGTACCATTTTC
TTGGCAGGACCCCCCTTGGTTAAAGCGGCAACTGGGGAAGAAGTATCTGCTGAGGATCTT
GGAGGTGCTGATCTTCATTGCAGAAAGTCTGGAGTAAGTGACCACTGGGCTTTGGATGAT
CATCATGCCCTTCACTTAACTAGGAAGGTTGTGAGGAATCTAAATTATCAGAAGAAATTG
GATGTCACCATTGAACCTTCTGAAGAGCCTTTATTTCCTGCTGATGAATTGTATGGAATA
GTTGGTGCTAACCTTAAGAGGAGCTTTGATGTCCGAGAGGTCATTGCTAGAATCGTGGAT
GGAAGCAGATTCACTGAGTTCAAAGCCTTTTATGGAGACACATTAGTTACAGGATTTGCT
CGAATATTTGGGTACCCAGTAGGTATCGTTGGAAACAACGGAGTTCTCTTTTCTGAATCT
GCAAAAAAGGGTACTCACTTTGTCCAGTTATGCTGCCAAAGAAATATTCCTCTGCTGTTC
CTTCAAAACATTACTGGATTTATGGTTGGTAGAGAGTATGAAGCTGAAGGAATTGCCAAG
GATGGTGCCAAGATGGTGGCCGCTGTGGCCTGTGCCCAAGTGCCTAAGATAACCCTCATC
ATTGGGGGCTCCTATGGAGCCGGAAACTATGGGATGTGTGGCAGAGCGTATAGCCCAAGA
TTTCTCTACATTTGGCCAAATGCTCGTATCTCAGTGATGGGAGGAGAGCAGGCAGCCAAT
GTGTTGGCCACGATAACAAAGGACCAAAGAGCCCGGGAAGGAAAGCAGTTCTCCAGTGCT
GATGAAGCGGCTTTAAAAGAGCCCATCATTAAGAAGTTTGAAGAGGAAGGAAACCCTTAC
TATTCCAGCGCAAGGGTATGGGATGATGGGATCATTGATCCAGCAGACACCAGACTGGTC
TTGGGTCTCAGTTTTAGTGCAGCCCTCAACGCACCAATAGAGAAGACTGACTTCGGTATC
TTCAGGATGTAA
|
| Enzyme 42 GenBank Gene ID |
AB050049 |
| Enzyme 42 GeneCard ID |
MCCC2 |
| Enzyme 42 GenAtlas ID |
MCCC2 |
| Enzyme 42 HGNC ID |
HGNC:6937 |
| Enzyme 42 Chromosome Location |
5 |
| Enzyme 42 Locus |
5q12-q13 |
| Enzyme 42 SNPs |
SNPJam Report |
| Enzyme 42 General References |
- Gallardo ME, Desviat LR, Rodriguez JM, Esparza-Gordillo J, Perez-Cerda C, Perez B, Rodriguez-Pombo P, Criado O, Sanz R, Morton DH, Gibson KM, Le TP, Ribes A, de Cordoba SR, Ugarte M, Penalva MA: The molecular basis of 3-methylcrotonylglycinuria, a disorder of leucine catabolism. Am J Hum Genet. 2001 Feb;68(2):334-46. Epub 2001 Jan 17. [PubMed ]
- Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed ]
- Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [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 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
5756 |
| Enzyme 43 Name |
Biotin--protein ligase |
| Enzyme 43 Synonyms |
- Biotin apo-protein ligase
- Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
- Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase
- Holocarboxylase synthetase
- HCS
- Biotin--[methylcrotonoyl-CoA-carboxylase] ligase
- Biotin--[acetyl-CoA-carboxylase] ligase
|
| Enzyme 43 Gene Name |
HLCS |
| Enzyme 43 Protein Sequence |
>Biotin--protein ligase
MEDRLHMDNGLVPQKIVSVHLQDSTLKEVKDQVSNKQAQILEPKPEPSLEIKPEQDGMEH
VGRDDPKALGEEPKQRRGSASGSEPAGDSDRGGGPVEHYHLHLSSCHECLELENSTIESV
KFASAENIPDLPYDYSSSLESVADETSPEREGRRVNLTGKAPNILLYVGSDSQEALGRFH
EVRSVLADCVDIDSYILYHLLEDSALRDPWTDNCLLLVIATRESIPEDLYQKFMAYLSQG
GKVLGLSSSFTFGGFQVTSKGALHKTVQNLVFSKADQSEVKLSVLSSGCRYQEGPVRLSP
GRLQGHLENEDKDRMIVHVPFGTRGGEAVLCQVHLELPPSSNIVQTPEDFNLLKSSNFRR
YEVLREILTTLGLSCDMKQVPALTPLYLLSAAEEIRDPLMQWLGKHVDSEGEIKSGQLSL
RFVSSYVSEVEITPSCIPVVTNMEAFSSEHFNLEIYRQNLQTKQLGKVILFAEVTPTTMR
LLDGLMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPF
VQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGC
GFNVTNSNPTICINDLITEYNKQHKAELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVL
PLYYRYWVHSGQQVHLGSAEGPKVSIVGLDDSGFLQVHQEGGEVVTVHPDGNSFDMLRNL
ILPKRR
|
| Enzyme 43 Number of Residues |
726 |
| Enzyme 43 Molecular Weight |
80759.3 |
| Enzyme 43 Theoretical pI |
5.34 |
| Enzyme 43 GO Classification |
| Function |
- biotin-[acetyl-CoA-carboxylase] ligase activity
- biotin-protein ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein modification process
|
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in biotin-[acetyl-CoA-carboxylase] ligase activity |
| Enzyme 43 Specific Function |
Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase |
| Enzyme 43 Pathways |
|
| Enzyme 43 Reactions |
- ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)] [RN:R04562]
|
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
Not Available |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P50747 |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
BPL1_HUMAN |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>2181 bp
ATGGAAGATAGACTCCACATGGATAATGGACTGGTACCCCAAAAGATTGTGTCGGTGCAC
TTGCAGGACTCCACTCTGAAGGAAGTTAAGGATCAGGTCTCAAACAAGCAAGCCCAGATC
CTAGAGCCGAAGCCTGAACCTTCTCTTGAGATTAAGCCTGAGCAGGACGGTATGGAGCAT
GTTGGCAGAGATGACCCAAAGGCTCTTGGTGAAGAACCCAAACAAAGGAGAGGCAGTGCC
TCTGGGAGTGAGCCTGCTGGGGACAGTGACAGGGGAGGGGGCCCCGTTGAGCATTATCAC
CTCCATCTGTCTAGTTGCCACGAGTGTCTGGAACTTGAGAACAGCACCATTGAGTCAGTC
AAGTTTGCGTCTGCCGAGAACATTCCAGACCTTCCCTACGATTATAGCAGCAGTTTGGAG
AGTGTTGCTGATGAGACCTCCCCCGAAAGAGAAGGGAGGAGAGTCAACCTCACGGGAAAG
GCACCCAACATCCTCCTCTATGTGGGCTCCGACTCCCAGGAAGCCCTCGGCCGGTTCCAC
GAGGTCCGGTCTGTGCTGGCCGACTGTGTGGACATTGACAGTTATATTCTCTACCACCTG
CTGGAGGACAGTGCTCTCAGAGACCCGTGGACGGACAACTGTCTGCTGTTGGTCATTGCT
ACCAGGGAGTCCATTCCCGAAGACCTGTACCAGAAGTTCATGGCCTATCTTTCTCAGGGA
GGGAAGGTGTTGGGCCTGTCTTCATCCTTCACCTTTGGTGGCTTTCAGGTGACAAGCAAG
GGTGCACTGCACAAGACAGTCCAGAACTTGGTTTTCTCCAAGGCTGACCAGAGCGAGGTG
AAGCTCAGCGTCTTGAGCAGTGGCTGCAGGTACCAGGAAGGCCCCGTCCGGCTCAGCCCC
GGCAGGCTCCAGGGCCACCTGGAGAATGAGGACAAGGACAGGATGATTGTGCATGTGCCT
TTTGGAACTCGCGGGGGAGAAGCTGTTCTTTGCCAGGTGCACTTAGAACTACCTCCCAGC
TCCAACATAGTGCAAACTCCAGAAGATTTTAACTTGCTCAAGTCAAGCAATTTTAGAAGA
TACGAAGTCCTTAGAGAGATTCTGACAACCCTTGGCCTCAGCTGTGACATGAAACAAGTT
CCTGCCTTAACTCCTCTTTACTTGCTGTCAGCTGCGGAGGAAATCAGGGATCCTCTTATG
CAGTGGCTTGGGAAACATGTGGACTCCGAGGGAGAAATAAAATCCGGCCAGCTCTCTCTT
AGATTTGTTTCATCCTACGTGTCTGAAGTAGAAATAACCCCATCTTGTATACCTGTGGTG
ACCAACATGGAGGCCTTCTCATCAGAACATTTCAACTTAGAGATCTATCGCCAAAATCTG
CAGACCAAGCAGTTGGGGAAAGTAATTTTGTTTGCCGAAGTGACCCCCACAACGATGCGT
CTCCTGGATGGGCTGATGTTTCAGACACCGCAGGAAATGGGCTTAATAGTGATCGCGGCC
CGGCAGACCGAGGGCAAAGGACGGGGAGGGAATGTGTGGCTGAGCCCTGTGGGATGTGCT
CTTTCTACTCTGCTCATCTCCATTCCACTGAGATCCCAGCTGGGACAGAGGATCCCGTTT
GTCCAGCATCTGATGTCCGTGGCTGTCGTGGAAGCAGTGAGGTCCATTCCCGAGTATCAG
GATATCAACTTACGAGTGAAGTGGCCCAACGATATTTATTACAGTGACCTCATGAAGATC
GGCGGAGTTCTGGTTAACTCAACACTCATGGGAGAAACATTTTATATACTTATTGGCTGT
GGATTTAATGTGACTAACAGTAACCCTACCATCTGCATCAACGACCTCATCACAGAATAC
AATAAACAACACAAGGCAGAACTGAAGCCCTTAAGAGCCGATTATCTCATCGCCAGAGTC
GTGACTGTGCTGGAGAAACTGATCAAAGAGTTTCAGGACAAAGGGCCCAACAGCGTCCTT
CCCCTTTATTACCGATACTGGGTCCACAGTGGTCAGCAAGTCCATCTGGGCAGCGCAGAG
GGACCAAAGGTGTCCATCGTTGGCCTGGACGATTCTGGCTTCCTCCAGGTTCACCAGGAG
GGCGGCGAGGTTGTGACTGTGCACCCGGACGGCAACTCCTTCGACATGCTGAGAAACCTC
ATCCTCCCCAAACGGCGGTAA
|
| Enzyme 43 GenBank Gene ID |
D23672 |
| Enzyme 43 GeneCard ID |
HLCS |
| Enzyme 43 GenAtlas ID |
HLCS |
| Enzyme 43 HGNC ID |
HGNC:4976 |
| Enzyme 43 Chromosome Location |
2 |
| Enzyme 43 Locus |
21q22.1|21q22.13 |
| Enzyme 43 SNPs |
SNPJam Report |
| Enzyme 43 General References |
- Suzuki Y, Aoki Y, Ishida Y, Chiba Y, Iwamatsu A, Kishino T, Niikawa N, Matsubara Y, Narisawa K: Isolation and characterization of mutations in the human holocarboxylase synthetase cDNA. Nat Genet. 1994 Oct;8(2):122-8. [PubMed ]
- Yang X, Aoki Y, Li X, Sakamoto O, Hiratsuka M, Kure S, Taheri S, Christensen E, Inui K, Kubota M, Ohira M, Ohki M, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Minoshima S, Shimizu N, Narisawa K, Matsubara Y, Suzuki Y: Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiency. Hum Genet. 2001 Nov;109(5):526-34. Epub 2001 Oct 5. [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 ]
- Dahmane N, Ghezala GA, Gosset P, Chamoun Z, Dufresne-Zacharia MC, Lopes C, Rabatel N, Gassanova-Maugenre S, Chettouh Z, Abramowski V, Fayet E, Yaspo ML, Korn B, Blouin JL, Lehrach H, Poutska A, Antonarakis SE, Sinet PM, Creau N, Delabar JM: Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21 involved in Down syndrome. Genomics. 1998 Feb 15;48(1):12-23. [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 ]
- Aoki Y, Suzuki Y, Sakamoto O, Li X, Takahashi K, Ohtake A, Sakuta R, Ohura T, Miyabayashi S, Narisawa K: Molecular analysis of holocarboxylase synthetase deficiency: a missense mutation and a single base deletion are predominant in Japanese patients. Biochim Biophys Acta. 1995 Dec 12;1272(3):168-74. [PubMed ]
- Dupuis L, Leon-Del-Rio A, Leclerc D, Campeau E, Sweetman L, Saudubray JM, Herman G, Gibson KM, Gravel RA: Clustering of mutations in the biotin-binding region of holocarboxylase synthetase in biotin-responsive multiple carboxylase deficiency. Hum Mol Genet. 1996 Jul;5(7):1011-6. [PubMed ]
- Aoki Y, Suzuki Y, Li X, Sakamoto O, Chikaoka H, Takita S, Narisawa K: Characterization of mutant holocarboxylase synthetase (HCS): a Km for biotin was not elevated in a patient with HCS deficiency. Pediatr Res. 1997 Dec;42(6):849-54. [PubMed ]
- Aoki Y, Li X, Sakamoto O, Hiratsuka M, Akaishi H, Xu L, Briones P, Suormala T, Baumgartner ER, Suzuki Y, Narisawa K: Identification and characterization of mutations in patients with holocarboxylase synthetase deficiency. Hum Genet. 1999 Feb;104(2):143-8. [PubMed ]
- Sakamoto O, Suzuki Y, Li X, Aoki Y, Hiratsuka M, Suormala T, Baumgartner ER, Gibson KM, Narisawa K: Relationship between kinetic properties of mutant enzyme and biochemical and clinical responsiveness to biotin in holocarboxylase synthetase deficiency. Pediatr Res. 1999 Dec;46(6):671-6. [PubMed ]
- Morrone A, Malvagia S, Donati MA, Funghini S, Ciani F, Pela I, Boneh A, Peters H, Pasquini E, Zammarchi E: Clinical findings and biochemical and molecular analysis of four patients with holocarboxylase synthetase deficiency. Am J Med Genet. 2002 Jul 22;111(1):10-8. [PubMed ]
- Tang NL, Hui J, Yong CK, Wong LT, Applegarth DA, Vallance HD, Law LK, Fung SL, Mak TW, Sung YM, Cheung KL, Fok TF: A genomic approach to mutation analysis of holocarboxylase synthetase gene in three Chinese patients with late-onset holocarboxylase synthetase deficiency. Clin Biochem. 2003 Mar;36(2):145-9. [PubMed ]
- Suzuki Y, Yang X, Aoki Y, Kure S, Matsubara Y: Mutations in the holocarboxylase synthetase gene HLCS. Hum Mutat. 2005 Oct;26(4):285-90. [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 ]
- Bailey LM, Ivanov RA, Jitrapakdee S, Wilson CJ, Wallace JC, Polyak SW: Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency. Hum Mutat. 2008 Jun;29(6):E47-57. [PubMed ]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
5757 |
| Enzyme 44 Name |
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial |
| Enzyme 44 Synonyms |
- MCCase subunit alpha
- 3-methylcrotonyl-CoA carboxylase 1
- 3-methylcrotonyl-CoA carboxylase biotin-containing subunit
- 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
|
| Enzyme 44 Gene Name |
MCCC1 |
| Enzyme 44 Protein Sequence |
>Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEI
ACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTS
AAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEG
YHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFN
DDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRK
KLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQL
RIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGV
RQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFE
AGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSS
SGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKC
SVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKV
FVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESD
KRESE
|
| Enzyme 44 Number of Residues |
725 |
| Enzyme 44 Molecular Weight |
80472.4 |
| Enzyme 44 Theoretical pI |
7.86 |
| Enzyme 44 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- nucleoside binding
- purine nucleoside binding
- vitamin binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 44 General Function |
Involved in catalytic activity |
| Enzyme 44 Specific Function |
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA |
| Enzyme 44 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 44 Reactions |
- ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA [RN:R04138]
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
Not Available |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
Q96RQ3 |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
MCCA_HUMAN |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>2178 bp
ATGGCGGCGGCCTCTGCGGTGTCGGTGCTGCTGGTGGCGGCGGAGAGGAACCGGTGGCAT
CGTCTCCCGAGCCTGCTCCTGCCGCCGAGGACATGGGTGTGGAGGCAAAGAACCATGAAG
TACACAACAGCCACAGGAAGAAACATTACCAAGGTCCTCATTGCAAACAGAGGAGAAATT
GCCTGCAGGGTGATGCGCACAGCCAAAAAACTGGGTGTACAGACTGTGGCGGTTTATAGT
GAGGCTGACAGAAATTCCATGCATGTAGATATGGCAGATGAAGCATATTCCATCGGCCCC
GCTCCCTCCCAGCAGAGCTACCTATCTATGGAGAAAATCATTCAAGTGGCCAAGACCTCT
GCTGCACAGGCTATCCATCCAGGATGCGGTTTTCTTTCAGAAAACATGGAATTTGCTGAA
CTTTGTAAGCAAGAAGGAATTATTTTTATAGGCCCTCCTCCATCTGCAATTAGAGACATG
GGTATAAAGAGCACATCCAAATCCATAATGGCTGCTGCTGGAGTACCTGTTGTGGAGGGT
TATCATGGTGAGGACCAATCAGACCAGTGCCTGAAGGAACACGCCAGGAGAATTGGCTAT
CCTGTCATGATTAAAGCCGTCCGGGGTGGAGGAGGAAAAGGAATGAGGATTGTTAGATCA
GAACAAGAATTTCAAGAACAGTTAGAGTCAGCACGGAGAGAAGCTAAGAAGTCTTTCAAT
GATGATGCTATGCTGATCGAGAAGTTTGTAGACACACCGAGGCATGTAGAAGTCCAGGTG
TTTGGTGATCACCATGGCAATGCTGTGTACTTGTTTGAAAGAGACTGTAGTGTGCAGAGG
CGACATCAGAAGATCATTGAGGAGGCCCCAGCGCCTGGTATTAAATCTGAAGTAAGAAAA
AAGCTGGGAGAAGCTGCAGTCAGAGCTGCTAAAGCTGTAAATTATGTTGGAGCAGGGACT
GTGGAGTTTATTATGGACTCAAAACATAATTTCTGTTTCATGGAGATGAATACAAGGCTG
CAAGTGGAACATCCTGTTACTGAGATGATCACAGGAACTGACTTGGTGGAGTGGCAGCTT
AGAATTGCAGCAGGAGAGAAGATTCCTTTGAGCCAGGAAGAAATAACTCTGCAGGGCCAT
GCCTTCGAAGCTAGAATATATGCAGAAGATCCTAGCAATAACTTCATGCCTGTGGCAGGC
CCATTAGTGCACCTCTCTACTCCTCGAGCAGACCCTTCCACCAGGATTGAAACTGGAGTA
CGGCAAGGAGACGAAGTTTCCGTGCATTATGACCCCATGATTGCGAAGCTGGTCGTGTGG
GCAGCAGATCGCCAGGCGGCATTGACAAAACTGAGGTACAGCCTTCGTCAGTACAATATT
GTTGGACTGCACACCAACATTGACTTCTTACTCAACCTGTCTGGCCACCCAGAGTTTGAA
GCTGGGAACGTGCACACTGATTTCATCCCTCAACACCACAAACAGTTGTTGCTCAGTCGG
AAGGCTGCAGCCAAAGAGTCTTTATGCCAGGCAGCCCTGGGTCTCATCCTCAAGGAGAAA
GCCATGACCGACACTTTCACTCTTCAGGCACATGATCAATTCTCTCCATTTTCGTCTAGC
AGTGGAAGAAGACTGAATATCTCGTATACCAGAAACATGACTCTTAAAGATGGTAAAAAC
AATGTAGCCATAGCTGTAACGTATAACCATGATGGGTCTTATAGCATGCAGATTGAAGAT
AAAACTTTCCAAGTCCTTGGTAATCTTTACAGCGAGGGAGACTGCACTTACCTGAAATGT
TCTGTTAATGGAGTTGCTAGTAAAGCGAAGCTGATTATCCTGGAAAACACTATTTACCTA
TTTTCCAAGGAAGGAAGTATTGAGATTGACATTCCAGTCCCCAAATACTTATCTTCTGTG
AGCTCACAAGAAACTCAGGGCGGCCCCTTAGCTCCTATGACTGGAACCATTGAAAAGGTG
TTTGTCAAAGCTGGAGACAAAGTGAAAGCGGGAGATTCCCTCATGGTTATGATCGCCATG
AAGATGGAGCATACCATAAAGTCTCCAAAGGATGGCACAGTAAAGAAAGTGTTCTACAGA
GAAGGTGCTCAGGCCAACAGACACACTCCTTTAGTCGAGTTTGAGGAGGAAGAATCAGAC
AAAAGGGAATCGGAATAA
|
| Enzyme 44 GenBank Gene ID |
AF310972 |
| Enzyme 44 GeneCard ID |
MCCC1 |
| Enzyme 44 GenAtlas ID |
MCCC1 |
| Enzyme 44 HGNC ID |
HGNC:6936 |
| Enzyme 44 Chromosome Location |
3 |
| Enzyme 44 Locus |
3q27 |
| Enzyme 44 SNPs |
SNPJam Report |
| Enzyme 44 General References |
- Gallardo ME, Desviat LR, Rodriguez JM, Esparza-Gordillo J, Perez-Cerda C, Perez B, Rodriguez-Pombo P, Criado O, Sanz R, Morton DH, Gibson KM, Le TP, Ribes A, de Cordoba SR, Ugarte M, Penalva MA: The molecular basis of 3-methylcrotonylglycinuria, a disorder of leucine catabolism. Am J Hum Genet. 2001 Feb;68(2):334-46. Epub 2001 Jan 17. [PubMed ]
- Obata K, Fukuda T, Morishita R, Abe S, Asakawa S, Yamaguchi S, Yoshino M, Ihara K, Murayama K, Shigemoto K, Shimizu N, Kondo I: Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase gene (MCCA): cDNA sequence, genomic organization, localization to chromosomal band 3q27, and expression. Genomics. 2001 Mar 1;72(2):145-52. [PubMed ]
- Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed ]
- Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [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 ]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
5759 |
| Enzyme 45 Name |
Glutamate--cysteine ligase catalytic subunit |
| Enzyme 45 Synonyms |
- GCS heavy chain
- Gamma-ECS
- Gamma-glutamylcysteine synthetase
|
| Enzyme 45 Gene Name |
GCLC |
| Enzyme 45 Protein Sequence |
>Glutamate--cysteine ligase catalytic subunit
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
|
| Enzyme 45 Number of Residues |
637 |
| Enzyme 45 Molecular Weight |
72765.1 |
| Enzyme 45 Theoretical pI |
5.98 |
| Enzyme 45 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- glutamate-cysteine ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- cellular metabolic process
- glutathione biosynthetic process
- glutathione metabolic process
- metabolic process
- peptide metabolic process
|
| Component |
| — |
|
| Enzyme 45 General Function |
Involved in glutamate-cysteine ligase activity |
| Enzyme 45 Specific Function |
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine |
| Enzyme 45 Pathways |
|
| Enzyme 45 Reactions |
- ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine [RN:R00894]
|
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
Not Available |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
P48506 |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
GSH1_HUMAN |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1914 bp
ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG
|
| Enzyme 45 GenBank Gene ID |
M90656 |
| Enzyme 45 GeneCard ID |
GCLC |
| Enzyme 45 GenAtlas ID |
GCLC |
| Enzyme 45 HGNC ID |
HGNC:4311 |
| Enzyme 45 Chromosome Location |
6 |
| Enzyme 45 Locus |
6p12 |
| Enzyme 45 SNPs |
SNPJam Report |
| Enzyme 45 General References |
- Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [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 ]
- Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed ]
- Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed ]
- Misra I, Griffith OW: Expression and purification of human gamma-glutamylcysteine synthetase. Protein Expr Purif. 1998 Jul;13(2):268-76. [PubMed ]
- Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed ]
- Hamilton D, Wu JH, Alaoui-Jamali M, Batist G: A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production. Blood. 2003 Jul 15;102(2):725-30. Epub 2003 Mar 27. [PubMed ]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
5770 |
| Enzyme 46 Name |
Phenylalanyl-tRNA synthetase beta chain |
| Enzyme 46 Synonyms |
- Phenylalanine--tRNA ligase beta chain
- PheRS
|
| Enzyme 46 Gene Name |
FARSB |
| Enzyme 46 Protein Sequence |
>Phenylalanyl-tRNA synthetase beta chain
MPTVSVKRDLLFQALGRTYTDEEFDELCFEFGLELDEITSEKEIISKEQGNVKAAGASDV
VLYKIDVPANRYDLLCLEGLVRGLQVFKERIKAPVYKRVMPDGKIQKLIITEETAKIRPF
AVAAVLRNIKFTKDRYDSFIELQEKLHQNICRKRALVAIGTHDLDTLSGPFTYTAKRPSD
IKFKPLNKTKEYTACELMNIYKTDNHLKHYLHIIENKPLYPVIYDSNGVVLSMPPIINGD
HSRITVNTRNIFIECTGTDFTKAKIVLDIIVTMFSEYCENQFTVEAAEVVFPNGKSHTFP
ELAYRKEMVRADLINKKVGIRETPENLAKLLTRMYLKSEVIGDGNQIEIEIPPTRADIIH
ACDIVEDAAIAYGYNNIQMTLPKTYTIANQFPLNKLTELLRHDMAAAGFTEALTFALCSQ
EDIADKLGVDISATKAVHISNPKTAEFQVARTTLLPGLLKTIAANRKMPLPLKLFEISDI
VIKDSNTDVGAKNYRHLCAVYYNKNPGFEIIHGLLDRIMQLLDVPPGEDKGGYVIKASEG
PAFFPGRCAEIFARGQSVGKLGVLHPDVITKFELTMPCSSLEINVGPFL
|
| Enzyme 46 Number of Residues |
589 |
| Enzyme 46 Molecular Weight |
66114.9 |
| Enzyme 46 Theoretical pI |
6.83 |
| Enzyme 46 GO Classification |
| Function |
- ATP binding
- RNA binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- cation binding
- ion binding
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- magnesium ion binding
- metal ion binding
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- phenylalanine-tRNA ligase activity
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- phenylalanyl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 46 General Function |
Involved in RNA binding |
| Enzyme 46 Specific Function |
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe) |
| Enzyme 46 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Phenylalanine and Tyrosine Metabolism (map00400 )
|
| Enzyme 46 Reactions |
- ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe [RN:R03660]
|
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
124028525 |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q9NSD9 |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
SYFB_HUMAN |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1770 bp
ATGCCGACTGTCAGCGTGAAGCGTGATCTGCTCTTCCAAGCCCTGGGCCGCACCTACACT
GACGAAGAATTTGATGAACTATGTTTTGAATTTGGTCTGGAGCTTGATGAAATTACATCT
GAGAAGGAAATAATAAGTAAAGAACAAGGTAATGTAAAGGCAGCAGGAGCCTCTGATGTT
GTTCTTTACAAAATTGACGTCCCTGCCAATAGATATGATCTCCTGTGTCTGGAAGGATTG
GTTCGAGGACTTCAGGTCTTCAAAGAAAGGATAAAGGCTCCAGTGTATAAACGGGTAATG
CCTGATGGAAAAATCCAGAAATTGATTATCACAGAAGAGACAGCTAAGATACGTCCTTTT
GCGGTAGCAGCAGTTCTCCGTAATATAAAGTTTACTAAAGATCGATATGACAGCTTCATT
GAACTTCAGGAGAAATTACATCAGAATATTTGCAGGAAAAGAGCACTGGTTGCCATTGGT
ACCCATGATTTGGACACTTTGTCGGGCCCATTTACTTATACTGCAAAGCGTCCTTCAGAT
ATCAAATTCAAGCCTCTAAATAAGACCAAGGAGTATACAGCCTGTGAACTGATGAACATA
TACAAGACTGACAATCACCTGAAACATTATTTACATATCATTGAAAACAAACCCCTGTAT
CCAGTTATCTATGATAGCAATGGTGTCGTCCTTTCAATGCCTCCCATCATCAATGGGGAT
CATTCCAGAATAACAGTAAATACTAGAAATATTTTTATTGAATGCACGGGAACTGACTTT
ACTAAGGCAAAAATAGTTCTTGATATTATTGTCACCATGTTCAGTGAATATTGTGAGAAT
CAATTTACGGTCGAAGCTGCTGAAGTGGTTTTTCCTAATGGAAAATCACATACCTTTCCA
GAATTAGCTTACCGAAAGGAGATGGTGAGAGCTGACCTAATTAACAAAAAAGTTGGAATC
AGAGAAACTCCAGAAAATCTTGCCAAACTTCTGACCAGGATGTATTTAAAATCAGAAGTC
ATAGGTGATGGGAATCAGATTGAGATTGAAATCCCTCCAACCAGAGCTGACATTATCCAT
GCATGTGATATTGTAGAAGATGCAGCTATTGCTTATGGATATAACAACATTCAGATGACT
CTCCCGAAAACTTACACCATAGCTAATCAATTTCCTCTTAATAAGCTCACTGAACTTCTC
CGACATGACATGGCAGCCGCTGGCTTCACTGAAGCACTTACCTTTGCCCTGTGCTCCCAA
GAAGATATTGCTGATAAACTAGGTGTGGATATCTCTGCAACAAAGGCAGTCCACATAAGT
AATCCTAAAACAGCTGAATTTCAGGTGGCACGCACTACCCTTCTTCCTGGCCTCCTGAAG
ACCATAGCAGCAAATCGTAAGATGCCCCTTCCACTGAAACTGTTTGAAATCTCTGACATT
GTAATAAAAGATTCTAATACAGATGTAGGTGCAAAAAACTACAGACATCTCTGTGCTGTT
TATTACAACAAGAATCCTGGGTTTGAGATCATTCATGGGCTGCTGGACAGAATTATGCAG
TTGCTCGATGTGCCTCCTGGTGAAGACAAGGGGGGATATGTGATCAAAGCATCAGAAGGG
CCTGCTTTCTTCCCCGGGCGATGTGCAGAGATCTTTGCCAGGGGTCAAAGCGTCGGGAAG
CTTGGGGTCCTTCATCCTGACGTTATCACCAAATTTGAGCTGACCATGCCCTGCTCCTCC
CTAGAAATCAATGTTGGACCCTTTTTGTGA
|
| Enzyme 46 GenBank Gene ID |
NM_005687.3 |
| Enzyme 46 GeneCard ID |
FARSB |
| Enzyme 46 GenAtlas ID |
FARSB |
| Enzyme 46 HGNC ID |
HGNC:17800 |
| Enzyme 46 Chromosome Location |
2 |
| Enzyme 46 Locus |
2q36.1 |
| Enzyme 46 SNPs |
SNPJam Report |
| Enzyme 46 General References |
- Rodova M, Ankilova V, Safro MG: Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells. Biochem Biophys Res Commun. 1999 Feb 24;255(3):765-73. [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 ]
- 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 ]
- Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [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 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
5832 |
| Enzyme 47 Name |
Ubiquitin-conjugating enzyme E2 A |
| Enzyme 47 Synonyms |
- RAD6 homolog A
- HR6A
- hHR6A
- Ubiquitin carrier protein A
- Ubiquitin-protein ligase A
|
| Enzyme 47 Gene Name |
UBE2A |
| Enzyme 47 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 A
MSTPARRRLMRDFKRLQEDPPAGVSGAPSENNIMVWNAVIFGPEGTPFEDGTFKLTIEFT
EEYPNKPPTVRFVSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWRDC
|
| Enzyme 47 Number of Residues |
152 |
| Enzyme 47 Molecular Weight |
17315.3 |
| Enzyme 47 Theoretical pI |
4.79 |
| Enzyme 47 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 47 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 47 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA |
| Enzyme 47 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 47 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
32967280 |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
P49459 |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
UBE2A_HUMAN |
| Enzyme 47 PDB ID |
1JAS |
| Enzyme 47 PDB File |
Show |
| Enzyme 47 3D Structure |
|
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>459 bp
ATGTCCACCCCGGCTCGGCGGCGCCTCATGCGGGACTTCAAGAGGTTGCAGGAGGATCCT
CCAGCCGGAGTCAGCGGGGCTCCGTCCGAGAACAACATAATGGTGTGGAACGCGGTCATT
TTCGGGCCTGAAGGGACCCCGTTTGAGGATGGAACATTTAAACTTACAATAGAATTCACT
GAAGAATATCCAAATAAACCACCTACAGTTAGATTTGTCTCTAAGATGTTCCATCCAAAT
GTCTATGCAGATGGTAGTATATGTCTGGACATACTTCAGAACCGTTGGAGTCCAACCTAT
GATGTGTCTTCCATTCTAACATCCATACAGTCTCTGTTGGATGAACCCAATCCCAATAGT
CCAGCAAACAGCCAGGCTGCTCAGCTGTACCAGGAGAACAAACGGGAATATGAAAAGCGT
GTTTCTGCAATAGTAGAACAAAGCTGGCGTGATTGTTGA
|
| Enzyme 47 GenBank Gene ID |
NM_003336.2 |
| Enzyme 47 GeneCard ID |
UBE2A |
| Enzyme 47 GenAtlas ID |
UBE2A |
| Enzyme 47 HGNC ID |
HGNC:12472 |
| Enzyme 47 Chromosome Location |
Not Available |
| Enzyme 47 Locus |
Not Available |
| Enzyme 47 SNPs |
SNPJam Report |
| Enzyme 47 General References |
- Koken MH, Reynolds P, Jaspers-Dekker I, Prakash L, Prakash S, Bootsma D, Hoeijmakers JH: Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8865-9. [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 ]
- 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 ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
5834 |
| Enzyme 48 Name |
Adenylate kinase isoenzyme 1 |
| Enzyme 48 Synonyms |
- AK 1
- ATP-AMP transphosphorylase 1
- Myokinase
|
| Enzyme 48 Gene Name |
AK1 |
| Enzyme 48 Protein Sequence |
>Adenylate kinase isoenzyme 1
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEI
MEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDA
GPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVD
SVFSQVCTHLDALK
|
| Enzyme 48 Number of Residues |
194 |
| Enzyme 48 Molecular Weight |
21634.7 |
| Enzyme 48 Theoretical pI |
8.99 |
| Enzyme 48 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- ATP metabolic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate metabolic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 48 General Function |
Involved in ATP binding |
| Enzyme 48 Specific Function |
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth |
| Enzyme 48 Pathways |
|
| Enzyme 48 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
Not Available |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
P00568 |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
KAD1_HUMAN |
| Enzyme 48 PDB ID |
1Z83 |
| Enzyme 48 PDB File |
Show |
| Enzyme 48 3D Structure |
|
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>585 bp
ATGGAAGAGAAGCTGAAGAAAACCAAGATCATCTTTGTGGTGGGTGGGCCTGGCTCAGGG
AAGGGCACCCAGTGTGAGAAGATCGTGCAGAAGTATGGCTACACCCACCTCTCCACCGGG
GACCTCCTGCGGTCCGAGGTCAGCTCAGGCTCGGCCAGGGGCAAGAAGCTGTCGGAAATC
ATGGAGAAGGGGCAGCTGGTTCCACTGGAGACAGTGTTGGACATGCTCCGGGATGCCATG
GTGGCCAAAGTCAATACTTCCAAAGGCTTCCTGATTGATGGCTACCCGCGGGAGGTGCAG
CAAGGAGAAGAGTTTGAGCGACGGATTGGACAGCCCACACTGCTGCTGTATGTGGACGCA
GGCCCTGAGACCATGACCCAGCGGCTCTTGAAACGTGGAGAGACCAGCGGGCGTGTGGAC
GACAATGAGGAGACCATCAAAAAGCGGCTGGAGACCTATTACAAGGCCACAGAACCCGTC
ATCGCCTTCTATGAGAAACGTGGCATTGTGCGCAAGGTCAACGCTGAGGGCTCCGTGGAC
AGTGTCTTCTCCCAGGTCTGCACCCACCTGGACGCCCTAAAGTAG
|
| Enzyme 48 GenBank Gene ID |
AB021871 |
| Enzyme 48 GeneCard ID |
AK1 |
| Enzyme 48 GenAtlas ID |
AK1 |
| Enzyme 48 HGNC ID |
HGNC:361 |
| Enzyme 48 Chromosome Location |
9 |
| Enzyme 48 Locus |
9q34.1 |
| Enzyme 48 SNPs |
SNPJam Report |
| Enzyme 48 General References |
- Von Zabern I, Wittmann-Liebold B, Untucht-Grau R, Schirmer RH, Pai EF: Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281-90. [PubMed ]
- Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. [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 ]
- Qualtieri A, Pedace V, Bisconte MG, Bria M, Gulino B, Andreoli V, Brancati C: Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia. Br J Haematol. 1997 Dec;99(4):770-6. [PubMed ]
- Corrons JL, Garcia E, Tusell JJ, Varughese KI, West C, Beutler E: Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia. Blood. 2003 Jul 1;102(1):353-6. Epub 2003 Mar 20. [PubMed ]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
5835 |
| Enzyme 49 Name |
NEDD8-conjugating enzyme Ubc12 |
| Enzyme 49 Synonyms |
- NEDD8 carrier protein
- NEDD8 protein ligase
- Ubiquitin-conjugating enzyme E2 M
|
| Enzyme 49 Gene Name |
UBE2M |
| Enzyme 49 Protein Sequence |
>NEDD8-conjugating enzyme Ubc12
MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNF
KLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWK
PVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFER
CLK
|
| Enzyme 49 Number of Residues |
183 |
| Enzyme 49 Molecular Weight |
20899.8 |
| Enzyme 49 Theoretical pI |
7.84 |
| Enzyme 49 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 49 General Function |
Involved in ATP binding |
| Enzyme 49 Specific Function |
Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation |
| Enzyme 49 Pathways |
Not Available |
| Enzyme 49 Reactions |
Not Available |
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
3599674 |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
P61081 |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
UBC12_HUMAN |
| Enzyme 49 PDB ID |
1Y8X |
| Enzyme 49 PDB File |
Show |
| Enzyme 49 3D Structure |
|
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>552 bp
ATGATCAAGCTGTTCTCGCTGAAGCAGCAGAAGAAGGAGGAGGAGTCGGCGGGCGGCACC
AAGGGCAGCAGCAAGAAGGCGTCGGCGGCGCAGCTGCGGATCCAGAAGGACATAAACGAG
CTGAACCTGCCCAAGACGTGTGATATCAGCTTCTCAGATCCAGACGACCTCCTCAACTTC
AAGCTGGTCATCTGTCCTGATGAGGGCTTCTACAAGAGTGGGAAGTTTGTGTTCAGTTTT
AAGGTGGGCCAGGGTTACCCGCATGATCCCCCCAAGGTGAAGTGTGAGACAATGGTCTAT
CACCCCAACATTGACCTCGAGGGCAACGTCTGCCTCAACATCCTCAGAGAGGACTGGAAG
CCAGTCCTTACGATAAACTCCATAATTTATGGCCTGCAGTATCTCTTCTTGGAGCCCAAC
CCCGAGGACCCACTGAACAAGGAGGCCGCAGAGGTCCTGCAGAACAACCGGCGGCTGTTT
GAGCAGAACGTGCAGCGCTCCATGCGGGGTGGCTACATCGGCTCCACCTACTTTGAGCGC
TGCCTGAAATAG
|
| Enzyme 49 GenBank Gene ID |
AB012191 |
| Enzyme 49 GeneCard ID |
UBE2M |
| Enzyme 49 GenAtlas ID |
UBE2M |
| Enzyme 49 HGNC ID |
HGNC:12491 |
| Enzyme 49 Chromosome Location |
1 |
| Enzyme 49 Locus |
19q13.43 |
| Enzyme 49 SNPs |
SNPJam Report |
| Enzyme 49 General References |
- Osaka F, Kawasaki H, Aida N, Saeki M, Chiba T, Kawashima S, Tanaka K, Kato S: A new NEDD8-ligating system for cullin-4A. Genes Dev. 1998 Aug 1;12(15):2263-8. [PubMed ]
- Gong L, Yeh ET: Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J Biol Chem. 1999 Apr 23;274(17):12036-42. [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 ]
- Wada H, Yeh ET, Kamitani T: A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo. J Biol Chem. 2000 Jun 2;275(22):17008-15. [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 ]
- Huang DT, Ayrault O, Hunt HW, Taherbhoy AM, Duda DM, Scott DC, Borg LA, Neale G, Murray PJ, Roussel MF, Schulman BA: E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Mol Cell. 2009 Feb 27;33(4):483-95. [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 ]
- Huang DT, Miller DW, Mathew R, Cassell R, Holton JM, Roussel MF, Schulman BA: A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8. Nat Struct Mol Biol. 2004 Oct;11(10):927-35. Epub 2004 Sep 7. [PubMed ]
- Huang DT, Paydar A, Zhuang M, Waddell MB, Holton JM, Schulman BA: Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1. Mol Cell. 2005 Feb 4;17(3):341-50. [PubMed ]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
5836 |
| Enzyme 50 Name |
Ubiquitin/ISG15-conjugating enzyme E2 L6 |
| Enzyme 50 Synonyms |
- Retinoic acid-induced gene B protein
- RIG-B
- UbcH8
- Ubiquitin carrier protein L6
- Ubiquitin-protein ligase L6
|
| Enzyme 50 Gene Name |
UBE2L6 |
| Enzyme 50 Protein Sequence |
>Ubiquitin/ISG15-conjugating enzyme E2 L6
MMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPE
YPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREP
LRMDLADLLTQNPELFRKNAEEFTLRFGVDRPS
|
| Enzyme 50 Number of Residues |
153 |
| Enzyme 50 Molecular Weight |
17768.5 |
| Enzyme 50 Theoretical pI |
8.06 |
| Enzyme 50 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 50 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 50 Specific Function |
Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53 |
| Enzyme 50 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 50 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
4759282 |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
O14933 |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
UB2L6_HUMAN |
| Enzyme 50 PDB ID |
1WZW |
| Enzyme 50 PDB File |
Show |
| Enzyme 50 3D Structure |
|
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>462 bp
ATGATGGCGAGCATGCGAGTGGTGAAGGAGCTGGAGGATCTTCAGAAGAAGCCTCCCCCA
TACCTGCGGAACCTGTCCAGCGATGATGCCAATGTCCTGGTGTGGCACGCTCTCCTCCTA
CCCGACCAACCTCCCTACCACCTGAAAGCCTTCAACCTGCGCATCAGCTTCCCGCCGGAG
TATCCGTTCAAGCCTCCCATGATCAAATTCACAACCAAGATCTACCACCCCAACGTGGAC
GAGAACGGACAGATTTGCCTGCCCATCATCAGCAGTGAGAACTGGAAGCCTTGCACCAAG
ACTTGCCAAGTCCTGGAGGCCCTCAATGTGCTGGTGAATAGACCGAATATCAGGGAGCCC
CTGCGGATGGACCTCGCTGACCTGCTGACACAGAATCCGGAGCTGTTCAGAAAGAATGCC
GAAGAGTTCACCCTCCGATTCGGAGTGGACCGGCCCTCCTAA
|
| Enzyme 50 GenBank Gene ID |
NM_004223.3 |
| Enzyme 50 GeneCard ID |
UBE2L6 |
| Enzyme 50 GenAtlas ID |
UBE2L6 |
| Enzyme 50 HGNC ID |
HGNC:12490 |
| Enzyme 50 Chromosome Location |
1 |
| Enzyme 50 Locus |
11q12 |
| Enzyme 50 SNPs |
SNPJam Report |
| Enzyme 50 General References |
- Ardley HC, Rose SA, Tan N, Leek JP, Markham AF, Robinson PA: Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12. Cytogenet Cell Genet. 2000;89(1-2):137-40. [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 ]
- 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 ]
- Kumar S, Kao WH, Howley PM: Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J Biol Chem. 1997 May 23;272(21):13548-54. [PubMed ]
- Zhao C, Beaudenon SL, Kelley ML, Waddell MB, Yuan W, Schulman BA, Huibregtse JM, Krug RM: The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7578-82. Epub 2004 May 6. [PubMed ]
- Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G: A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem Biophys Res Commun. 2001 Mar 2;281(3):706-13. [PubMed ]
- Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H: Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. J Biochem. 2005 Dec;138(6):711-9. [PubMed ]
- Huang J, Xu LG, Liu T, Zhai Z, Shu HB: The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis. FEBS Lett. 2006 Feb 6;580(3):940-7. Epub 2006 Jan 18. [PubMed ]
- Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed ]
- Serniwka SA, Shaw GS: The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin interaction site. Biochemistry. 2009 Dec 29;48(51):12169-79. [PubMed ]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
5837 |
| Enzyme 51 Name |
Glycyl-tRNA synthetase |
| Enzyme 51 Synonyms |
- Diadenosine tetraphosphate synthetase
- AP-4-A synthetase
- Glycine--tRNA ligase
- GlyRS
|
| Enzyme 51 Gene Name |
GARS |
| Enzyme 51 Protein Sequence |
>Glycyl-tRNA synthetase
MPSPRPVLLRGARAALLLLLPPRLLARPSLLLRRSLSAASCAPISLPAAASRSSMDGAGA
EEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVD
RAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDC
TMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSVEKKSEME
SVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGGNMPGYLRPET
AQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEK
DHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKV
GISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPL
VAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEMEMLLNEKGEF
TIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDE
QRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYAR
TDEIGVAFGVTIDFDTVNKTPHTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVE
ARYPLFEGQETGKKETIEE
|
| Enzyme 51 Number of Residues |
739 |
| Enzyme 51 Molecular Weight |
83138.8 |
| Enzyme 51 Theoretical pI |
7.04 |
| Enzyme 51 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- glycine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- glycyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 51 General Function |
Involved in nucleotide binding |
| Enzyme 51 Specific Function |
Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs |
| Enzyme 51 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 51 Reactions |
- ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly [RN:R03654]
|
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
Not Available |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
P41250 |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
SYG_HUMAN |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
>2220 bp
ATGCCCTCTCCGCGTCCAGTGCTGCTTAGAGGTGCTCGCGCCGCTCTGCTGCTGCTGCTG
CCGCCCCGGCTCTTAGCCCGACCCTCGCTCCTGCTCCGCCGGTCCCTCAGCGCGGCCTCC
TGCGCCCCGATCTCCTTGCCCGCCGCCGCCTCCCGGAGCAGCATGGACGGCGCGGGGGCT
GAGGAGGTGCTGGCACCTCTGAGGCTAGCAGTGCGCCAGCAGGGAGATCTTGTGCGAAAA
CTCAAAGAAGATAAAGCACCCCAAGTAGACGTAGACAAAGCAGTGGCTGAGCTCAAAGCC
CGCAAGAGGGTTCTGGAAGCAAAGGAGCTGGCGTTACAGCCCAAAGATGATATTGTAGAC
CGAGCAAAAATGGAAGATACCCTGAAGAGGAGGTTTTTCTATGATCAAGCTTTTGCTATT
TATGGAGGTGTTAGTGGTCTGTATGACTTTGGGCCAGTTGGCTGTGCTTTGAAGAACAAT
ATTATTCAGACCTGGAGGCAGCACTTTATCCAAGAGGAACAGATCCTGGAGATCGATTGC
ACCATGCTCACCCCTGAGCCAGTTTTAAAGACCTCTGGCCATGTAGACAAATTTGCTGAC
TTCATGGTGAAAGACGTAAAAAATGGAGAATGTTTTCGTGCTGACCATCTATTAAAAGCT
CATTTACAGAAATTGATGTCTGATAAGAAGTGTTCTGTCGAAAAGAAATCAGAAATGGAA
AGTGTTTTGGCCCAGCTTGATAACTATGGACAGCAAGAACTTGCGGATCTTTTTGTGAAC
TATAATGTAAAATCTCCCATTACTGGAAATGATCTATCCCCTCCAGTGTCTTTTAACTTA
ATGTTCAAGACTTTCATTGGGCCTGGAGGAAACATGCCTGGGTACTTGAGACCAGAAACT
GCACAGGGGATTTTCTTGAATTTCAAACGACTTTTGGAGTTCAACCAAGGAAAGTTGCCT
TTTGCTGCTGCCCAGATTGGAAATTCTTTTAGAAATGAGATCTCCCCTCGATCTGGACTG
ATCAGAGTCAGAGAATTCACAATGGCAGAAATTGAGCACTTTGTAGATCCCAGTGAGAAA
GACCACCCCAAGTTCCAGAATGTGGCAGACCTTCACCTTTATTTGTATTCAGCAAAAGCC
CAGGTCAGCGGACAGTCCGCTCGGAAAATGCGCCTGGGAGATGCTGTTGAACAGGGTGTG
ATTAATAACACAGTATTAGGCTATTTCATTGGCCGCATCTACCTCTACCTCACGAAGGTT
GGAATATCTCCAGATAAACTCCGCTTCCGGCAGCACATGGAGAATGAGATGGCCCATTAT
GCCTGTGACTGTTGGGATGCAGAATCCAAAACATCCTACGGTTGGATTGAGATTGTTGGA
TGTGCTGATCGTTCCTGTTATGACCTCTCCTGTCATGCACGAGCCACCAAAGTCCCACTT
GTAGCTGAGAAACCTCTGAAAGAACCCAAAACAGTCAATGTTGTTCAGTTTGAACCCAGT
AAGGGAGCAATTGGTAAGGCATATAAGAAGGATGCAAAACTGGTGATGGAGTATCTTGCC
ATTTGTGATGAGTGCTACATTACAGAAATGGAGATGCTGCTGAATGAGAAAGGGGAATTC
ACAATTGAAACTGAAGGGAAAACATTTCAGTTAACAAAAGACATGATCAATGTGAAGAGA
TTCCAGAAAACACTATATGTGGAAGAAGTTGTTCCGAATGTAATTGAACCTTCCTTCGGC
CTGGGTAGGATCATGTATACGGTATTTGAACATACATTCCATGTACGAGAAGGAGATGAA
CAGAGAACATTCTTCAGTTTCCCTGCTGTAGTTGCTCCATTCAAATGTTCCGTCCTCCCA
CTGAGCCAAAACCAGGAGTTCATGCCATTTGTCAAGGAATTATCGGAAGCCCTGACCAGG
CATGGAGTATCTCACAAAGTAGACGATTCCTCTGGGTCAATCGGAAGGCGCTATGCCAGG
ACTGATGAGATTGGCGTGGCTTTTGGTGTCACCATTGACTTTGACACAGTGAACAAGACC
CCCCACACTGCAACTCTGAGGGACCGTGACTCAATGCGGCAGATAAGAGCAGAGATCTCT
GAGCTGCCCAGCATAGTCCAAGACCTAGCCAATGGCAACATCACATGGGCTGATGTGGAG
GCCAGGTATCCTCTGTTTGAAGGGCAAGAGACTGGTAAAAAAGAGACAATCGAGGAATGA
|
| Enzyme 51 GenBank Gene ID |
D30658 |
| Enzyme 51 GeneCard ID |
GARS |
| Enzyme 51 GenAtlas ID |
GARS |
| Enzyme 51 HGNC ID |
HGNC:4162 |
| Enzyme 51 Chromosome Location |
7 |
| Enzyme 51 Locus |
7p15 |
| Enzyme 51 SNPs |
SNPJam Report |
| Enzyme 51 General References |
- Shiba K, Schimmel P, Motegi H, Noda T: Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J Biol Chem. 1994 Nov 25;269(47):30049-55. [PubMed ]
- Williams J, Osvath S, Khong TF, Pearse M, Power D: Cloning, sequencing and bacterial expression of human glycine tRNA synthetase. Nucleic Acids Res. 1995 Apr 25;23(8):1307-10. [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, 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 ]
- Ge Q, Trieu EP, Targoff IN: Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis. J Biol Chem. 1994 Nov 18;269(46):28790-7. [PubMed ]
- Mudge SJ, Williams JH, Eyre HJ, Sutherland GR, Cowan PJ, Power DA: Complex organisation of the 5'-end of the human glycine tRNA synthetase gene. Gene. 1998 Mar 16;209(1-2):45-50. [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 ]
- Cader MZ, Ren J, James PA, Bird LE, Talbot K, Stammers DK: Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy. FEBS Lett. 2007 Jun 26;581(16):2959-64. Epub 2007 May 29. [PubMed ]
- Xie W, Nangle LA, Zhang W, Schimmel P, Yang XL: Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase. Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):9976-81. Epub 2007 Jun 1. [PubMed ]
- Guo RT, Chong YE, Guo M, Yang XL: Crystal structures and biochemical analyses suggest a unique mechanism and role for human glycyl-tRNA synthetase in Ap4A homeostasis. J Biol Chem. 2009 Oct 16;284(42):28968-76. Epub 2009 Aug 26. [PubMed ]
- Antonellis A, Ellsworth RE, Sambuughin N, Puls I, Abel A, Lee-Lin SQ, Jordanova A, Kremensky I, Christodoulou K, Middleton LT, Sivakumar K, Ionasescu V, Funalot B, Vance JM, Goldfarb LG, Fischbeck KH, Green ED: Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V. Am J Hum Genet. 2003 May;72(5):1293-9. Epub 2003 Apr 10. [PubMed ]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
5838 |
| Enzyme 52 Name |
Ribose-phosphate pyrophosphokinase 3 |
| Enzyme 52 Synonyms |
- Phosphoribosyl pyrophosphate synthase 1-like 1
- PRPS1-like 1
- Phosphoribosyl pyrophosphate synthase III
- PRS-III
|
| Enzyme 52 Gene Name |
PRPS1L1 |
| Enzyme 52 Protein Sequence |
>Ribose-phosphate pyrophosphokinase 3
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIDESVRGEDVYIVQSGC
GEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRSPISAKLVANMLSIAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPTVLKWIRENIPEWKNCIIVSPDAGGAKRVTS
IADQLNVDFALIHKERKKANEVDCIVLVGDVNDRVAILVDDMADTCVTICLAADKLLSAG
ATRVYAILTHGIFSGPAISRINTACFEAVVVTNTIPQDEKMKHCSKIRVIDISMILAEAI
RRTHNGESVSYLFSHVPL
|
| Enzyme 52 Number of Residues |
318 |
| Enzyme 52 Molecular Weight |
34838.9 |
| Enzyme 52 Theoretical pI |
6.31 |
| Enzyme 52 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- diphosphotransferase activity
- ion binding
- magnesium ion binding
- metal ion binding
- ribose phosphate diphosphokinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular biosynthetic 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 metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide biosynthetic process
- nucleotide metabolic process
- ribonucleoside monophosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 52 General Function |
Involved in magnesium ion binding |
| Enzyme 52 Specific Function |
Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis |
| Enzyme 52 Pathways |
|
| Enzyme 52 Reactions |
- ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01049]
|
| Enzyme 52 Pfam Domain Function |
|
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
110611809 |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
P21108 |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
PRPS3_HUMAN |
| Enzyme 52 PDB ID |
Not Available |
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
>957 bp
ACGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCCCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGCGTGGAAATTGATGAGAGTGTGCGTGGAGAGGATGTCTACATCGTTCAGAGTGGTTGT
GGCGAAATCAACGACAGTCTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCTAGCCGAGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGACAGGATAAGAAG
GATAAGAGCCGGTCCCCAATCTCTGCCAAGCTTGTTGCAAATATGCTCTCTATAGCAGGT
GCGGATCATATCATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAACTTGTATGCAGAGCCAACTGTCCTGAAGTGGATAAGGGAGAATATCCCT
GAGTGGAAGAACTGCATTATTGTCTCGCCAGATGCTGGTGGAGCTAAAAGAGTGACCTCC
ATTGCAGACCAGTTGAATGTGGACTTTGCTTTGATTCATAAAGAACGGAAGAAGGCCAAT
GAAGTGGACTGCATAGTGCTAGTGGGAGATGTGAATGATCGTGTGGCTATCCTTGTAGAT
GACATGGCAGACACTTGTGTTACAATCTGCCTCGCAGCTGACAAACTTCTCTCAGCTGGA
GCAACCAGAGTTTATGCTATCTTGACTCATGGAATCTTTTCTGGCCCAGCCATTTCTCGC
ATCAACACTGCATGCTTTGAAGCAGTGGTAGTCACCAATACCATACCTCAAGATGATAAG
ATGAAGCATTGCTCCAAAATACGAGTAATTGACATCTCCATGATCCTTGCAGAAGCCATA
AGGAGAACTCATAATGGGGAATCTGTTTCCTACCTGTTCAGCCATGTTCCTTTATAA
|
| Enzyme 52 GenBank Gene ID |
BC062797 |
| Enzyme 52 GeneCard ID |
PRPS1L1 |
| Enzyme 52 GenAtlas ID |
PRPS1L1 |
| Enzyme 52 HGNC ID |
HGNC:9463 |
| Enzyme 52 Chromosome Location |
7 |
| Enzyme 52 Locus |
7p21.1 |
| Enzyme 52 SNPs |
SNPJam Report |
| Enzyme 52 General References |
- Taira M, Iizasa T, Shimada H, Kudoh J, Shimizu N, Tatibana M: A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon. J Biol Chem. 1990 Sep 25;265(27):16491-7. [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 ]
- 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 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
5839 |
| Enzyme 53 Name |
Bifunctional aminoacyl-tRNA synthetase |
| Enzyme 53 Synonyms |
- Cell proliferation-inducing gene 32 protein
- Glutamyl-tRNA synthetase
- Glutamate--tRNA ligase
- GluRS
- Prolyl-tRNA synthetase
- Proline--tRNA ligase
|
| Enzyme 53 Gene Name |
EPRS |
| Enzyme 53 Protein Sequence |
>Bifunctional aminoacyl-tRNA synthetase
MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLAR
VATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLA
DLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEK
KQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTN
PEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMK
AEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCK
IQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYI
WEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGS
SRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVG
LKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKD
YKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPC
LKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTK
VEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAA
VKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKL
KAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPE
AKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAED
KDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKK
EENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPM
FVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDL
PIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEEL
LAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPK
IPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDK
EALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFV
AVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSG
KIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKN
PAKYYTLFGRSY
|
| Enzyme 53 Number of Residues |
1512 |
| Enzyme 53 Molecular Weight |
170589.7 |
| Enzyme 53 Theoretical pI |
7.34 |
| Enzyme 53 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- glutamate-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- proline-tRNA ligase activity
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- glutamyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- prolyl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 53 General Function |
Involved in nucleotide binding |
| Enzyme 53 Specific Function |
Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction:the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA |
| Enzyme 53 Pathways |
|
| Enzyme 53 Reactions |
- ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu [RN:R05578]
|
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
Not Available |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
P07814 |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
SYEP_HUMAN |
| Enzyme 53 PDB ID |
Not Available |
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>4539 bp
ATGGCGACGCTCTCTCTGACCGTGAATTCAGGAGACCCTCCGCTAGGAGCTTTGCTGGCA
GTAGAACACGTGAAAGACGATGTCAGCATTTCCGTTGAAGAAGGGAAAGAGAATATTCTT
CATGTTTCTGAAAATGTGATATTCACAGATGTGAATTCTATACTTCGCTACTTGGCTAGA
GTTGCAACTACAGCTGGGTTATATGGCTCTAATCTGATGGAACATACTGAGATTGATCAC
TGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGTGATTCCTTTACTTCTACAATTAAT
GAACTCAATCATTGCCTGTCTCTGAGAACATACTTAGTTGGAAACTCCTTGAGTTTAGCA
GATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCTGCCTGGCAAGAACAGTTGAAACAG
AAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGCTTTCTTGAAGCCCAGCAGGCCTTC
CAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACCAAAGCTCGAGTGGCACCTGAGAAA
AAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGTGCGGAGATGGGAAAGGTTACCGTC
AGATTTCCTCCAGAGGCCAGTGGTTACTTACACATTGGGCATGCAAAAGCTGCTCTTCTG
AACCAGCACTACCAGGTTAACTTTAAAGGGAAACTGATCATGAGATTTGATGACACAAAT
CCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATCTTGGAAGATGTTGCAATGTTGCAT
ATCAAACCAGATCAATTTACTTATACTTCGGATCATTTTGAAACTATAATGAAGTATGCA
GAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGATGATACTCCTGCTGAACAGATGAAA
GCAGAACGTGAGCAGAGGATAGAATCTAAACATAGAAAAAACCCTATTGAGAAGAATCTA
CAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTTGGTCAGTCCTGTTGTTTGCGAGCA
AAAATTGACATGAGTAGTAACAATGGATGCATGAGAGATCCAACCCTTTATCGCTGCAAA
ATTCAACCACATCCAAGAACTGGAAATAAATACAATGTTTATCCAACATATGATTTTGCC
TGCCCCATAGTTGACAGCATCGAAGGTGTTACACATGCCCTGAGAACAACAGAATACCAT
GACAGAGATGAGCAGTTTTACTGGATTATTGAAGCTTTAGGCATAAGAAAACCATATATT
TGGGAATATAGTCGGCTAAATCTCAACAACACAGTGCTATCCAAAAGAAAACTCACATGG
TTTGTCAATGAAGGACTAGTAGATGGATGGGATGACCCAAGATTTCCTACGGTTCGTGGT
GTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAACAGTTTATTGCTGCTCAGGGCTCC
TCACGTTCAGTCGTGAACATGGAGTGGGACAAAATCTGGGCGTTTAACAAAAAGGTTATT
GACCCAGTGGCTCCACGATATGTTGCATTACTGAAGAAAGAAGTGATCCCAGTGAATGTA
CCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAGACACCCAAAGAATCCTGAGGTTGGC
TTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATTGAAGGTGCTGATGCAGAGACTTTT
TCGGAGGGTGAGATGGTTACATTTATAAATTGGGGCAACCTCAACATTACAAAAATACAC
AAAAATGCAGATGGAAAAATCATATCTCTTGATGCAAAGTTGAATTTGGAAAACAAAGAC
TACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAGACTACACATGCTCTTCCTATTCCA
GTAATCTGTGTCACTTATGAGCACTTGATCACAAAGCCAGTGCTAGGAAAAGACGAGGAC
TTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAAGAGCTAATGCTAGGGGATCCCTGC
CTTAAGGATTTGAAAAAAGGAGATATTATACAACTCCAGAGAAGAGGATTCTTCATATGT
GATCAACCTTATGAACCTGTTAGCCCATATAGTTGCAAGGAAGCCCCGTGTGTTTTGATA
TACATTCCTGATGGGCACACAAAGGAAATGCCAACATCAGGGTCAAAGGAAAAGACCAAA
GTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTTAAGGAAAGACCAACACCTTCTCTG
AATAATAATTGTACTACATCTGAGGATTCCTTGGTCCTTTACAATAGAGTGGCTGTTCAA
GGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCACCAAAGGAAGATGTAGATGCAGCT
GTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAGGAGAAAACTGGCCAGGAATATAAA
CCTGGAAACCCTCCTGCTGAAATAGGACAGAATATTTCTTCTAATTCCTCAGCAAGTATT
CTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCACAAGGGGAGGTGGTTCGTAAGCTA
AAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAAGCTGTAGAATGCTTACTGTCCCTG
AAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTACATACCTGGTCAGCCCCCATTATCT
CAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAACCTGCTGGTTTAGAAACACCAGAA
GCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGGGAAGTAGTTCGGAAACTTAAAACT
GAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTTCAAGAACTCCTTCAGCTAAAGGCA
CAGTACGAGTCTTTGATAGGAGTAGAGTATAAGCCTGTGTCGGCCACTGGAGCTGAGGAC
AAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCTGAAAAGCAGAATAAGCCTCAGAAA
CAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAACCAAGGAGGTGGGCTCTCATCAAGT
GGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACCAGGTTGGGTCTTGAGGCAAAAAAA
GAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATCACAAAATCAGAAATGATTGAATAC
CATGACGTAAGTGGCTGTTATATTCTTCGTCCCTGGGCCTATGCCATTTGGGAAGCCATC
AAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGTGTTGAAAACTGCTACTTCCCCATG
TTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACTCATGTTGCTGACTTTGCCCCAGAG
GTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTGGCAGAACCAATTGCCATTCGTCCT
ACTAGTGAAACAGTAATGTATCCTGCATATGCAAAATGGGTACAATCACACAGAGACCTG
CCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGTTGGGAATTCAAGCATCCTCAGCCT
TTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGGCACAGTGCTTTTGTTACCGTGGAA
GAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTATATGCTCAGGTATATGAAGAACTC
CTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAAAAGGAAAAATTTGCAGGAGGAGAC
TATACAACTACAATAGAAGCATTTATATCTGCTAGTGGAAGAGCTATCCAGGGAGGAACA
TCACATCATTTAGGGCAGAATTTTTCCAAAATGTTTGAAATCGTTTTTGAAGATCCAAAG
ATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCCTGGGGCCTGACAACTCGAACTATT
GGTGTTATGACCATGGTTCATGGGGACAACATGGGTTTAGTATTACCACCCCGTGTAGCA
TGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACCAATGCACTTTCTGAAGAAGACAAA
GAAGCGCTGATTGCAAAATGCAATGATTATCGAAGGCGATTACTCAGTGTTAACATCCGC
GTTAGAGCTGATTTACGAGATAATTATTCTCCAGGTTGGAAATTCAATCACTGGGAGCTC
AAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGTGATATGAAGAGCTGTCAGTTTGTA
GCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTTGCTGAAAATGAGGCAGAGACTAAA
CTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTTTTCACAAGGGCTTCTGAAGACCTT
AAGACTCATATGGTTGTGGCTAATACAATGGAAGACTTTCAGAAGATACTAGATTCTGGA
AGGATTGTTCAGATTCCATTCTGTGGGGAAATTGACTGTGAGGACTGGATCAAAAAGACC
ACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCATCCATGGGAGCTAAAAGCCTTTGC
ATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGAGCCAAATGTGTCTGTGGCAAGAAC
CCTGCCAAGTACTACACCTTATTTGGTCGCAGCTACTGA
|
| Enzyme 53 GenBank Gene ID |
CR933648 |
| Enzyme 53 GeneCard ID |
EPRS |
| Enzyme 53 GenAtlas ID |
EPRS |
| Enzyme 53 HGNC ID |
HGNC:3418 |
| Enzyme 53 Chromosome Location |
1 |
| Enzyme 53 Locus |
1q41-q42 |
| Enzyme 53 SNPs |
SNPJam Report |
| Enzyme 53 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 ]
- 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 ]
- Fett R, Knippers R: The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. J Biol Chem. 1991 Jan 25;266(3):1448-55. [PubMed ]
- Thommes P, Fett R, Schray B, Kunze N, Knippers R: The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988 Jun 24;16(12):5391-406. [PubMed ]
- Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M: A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. [PubMed ]
- Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [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 ]
- Kato T, Daigo Y, Hayama S, Ishikawa N, Yamabuki T, Ito T, Miyamoto M, Kondo S, Nakamura Y: A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis. Cancer Res. 2005 Jul 1;65(13):5638-46. [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 ]
- 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 ]
- 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 ]
- 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 ]
- Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed ]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
5842 |
| Enzyme 54 Name |
Long-chain-fatty-acid--CoA ligase 4 |
| Enzyme 54 Synonyms |
- Long-chain acyl-CoA synthetase 4
- LACS 4
|
| Enzyme 54 Gene Name |
ACSL4 |
| Enzyme 54 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 4
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
|
| Enzyme 54 Number of Residues |
711 |
| Enzyme 54 Molecular Weight |
79187.4 |
| Enzyme 54 Theoretical pI |
8.51 |
| Enzyme 54 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 54 General Function |
Involved in catalytic activity |
| Enzyme 54 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 54 Pathways |
|
| Enzyme 54 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
12669909 |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
O60488 |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
ACSL4_HUMAN |
| Enzyme 54 PDB ID |
Not Available |
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 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 54 GenBank Gene ID |
NM_022977.2 |
| Enzyme 54 GeneCard ID |
ACSL4 |
| Enzyme 54 GenAtlas ID |
ACSL4 |
| Enzyme 54 HGNC ID |
HGNC:3571 |
| Enzyme 54 Chromosome Location |
Not Available |
| Enzyme 54 Locus |
Not Available |
| Enzyme 54 SNPs |
SNPJam Report |
| Enzyme 54 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 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
5846 |
| Enzyme 55 Name |
Tryptophanyl-tRNA synthetase, cytoplasmic |
| Enzyme 55 Synonyms |
- Interferon-induced protein 53
- IFP53
- Tryptophan--tRNA ligase
- TrpRS
- hWRS
- T1-TrpRS
- T2-TrpRS
|
| Enzyme 55 Gene Name |
WARS |
| Enzyme 55 Protein Sequence |
>Tryptophanyl-tRNA synthetase, cytoplasmic
MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKA
DCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRI
ERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFT
KWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDY
MGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDR
TDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIF
LTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDY
TSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ
|
| Enzyme 55 Number of Residues |
471 |
| Enzyme 55 Molecular Weight |
53164.9 |
| Enzyme 55 Theoretical pI |
6.15 |
| Enzyme 55 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- tryptophan-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
- tryptophanyl-tRNA aminoacylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 55 General Function |
Involved in nucleotide binding |
| Enzyme 55 Specific Function |
Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression |
| Enzyme 55 Pathways |
|
| Enzyme 55 Reactions |
- ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp [RN:R03664]
|
| Enzyme 55 Pfam Domain Function |
|
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
184657 |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
P23381 |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
SYWC_HUMAN |
| Enzyme 55 PDB ID |
1R6T |
| Enzyme 55 PDB File |
Show |
| Enzyme 55 3D Structure |
|
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
>1416 bp
ATGCCCAACAGTGAGCCCGCATCTCTGCTGGAGCTGTTCAACAGCATCGCCACACAAGGG
GAGCTCGTAAGGTCCCTCAAAGCGGGAAATGCGTCAAAGGATGAAATTGATTCTGCAGTA
AAGATGTTGGTGTCATTAAAAATGAGCTACAAAGCTGCCGCGGGGGAGGATTACAAGGCT
GACTGTCCTCCAGGGAACCCAGCACCTACCAGTAATCATGGCCCAGATGCCACAGAAGCT
GAAGAGGATTTTGTGGACCCATGGACAGTACAGACAAGCAGTGCAAAAGGCATAGACTAC
GATAAGCTCATTGTTCGGTTTGGAAGTAGTAAAATTGACAAAGAGCTAATAAACCGAATA
GAGAGAGCCACCGGCCAAAGACCACACCACTTCCTGCGCAGAGGCATCTTCTTCTCACAC
AGAGATATGAATCAGGTTCTTGATGCCTATGAAAATAAGAAGCCATTTTATCTGTACACG
GGCCGGGGCCCCTCTTCTGAAGCAATGCATGTAGGTCACCTCATTCCATTTATTTTCACA
AAGTGGCTCCAGGATGTATTTAACGTGCCCTTGGTGATCCAGATGACGGATGACGAGAAG
TATCTGTGGAAGGACCTGACCCTGGACCAGGCCTATAGCTATGCTGTGGAGAATGCCAAG
GACATCATCGCCTGTGGCTTTGACATCAACAAGACTTTCATATTCTCTGACCTGGACTAC
ATGGGGATGAGCTCAGGTTTCTACAAAAATGTGGTGAAGATTCAAAAGCATGTTACCTTC
AACCAAGTGAAAGGCATTTTCGGCTTCACTGACAGCGACTGCATTGGGAAGATCAGTTTT
CCTGCCATCCAGGCTGCTCCCTCCTTCAGCAACTCATTCCCACAGATCTTCCGAGACAGG
ACGGATATCCAGTGCCTTATCCCATGTGCCATTGACCAGGATCCTTACTTTAGAATGACA
AGGGACGTCGCCCCCAGGATCGGCTATCCTAAACCAGCCCTGTTGCACTCCACCTTCTTC
CCAGCCCTGCAGGGCGCCCAGACCAAAATGAGTGCCAGCGACCCCAACTCCTCCATCTTC
CTCACCGACACGGCCAAGCAGATCAAAACCAAGGTCAATAAGCATGCGTTTTCTGGAGGG
AGAGACACCATCGAGGAGCACAGGCAGTTTGGGGGCAACTGTGATGTGGACGTGTCTTTC
ATGTACCTGACCTTCTTCCTCGAGGACGACGACAAGCTCGAGCAGATCAGGAAGGATTAC
ACCAGCGGAGCCATGCTCACCGGTGAGCTCAAGAAGGCACTCATAGAGGTTCTGCAGCCC
TTGATCGCAGAGCACCAGGCCCGGCGCAAGGAGGTCACGGATGAGATAGTGAAAGAGTTC
ATGACTCCCCGGAAGCTGTCCTTCGACTTTCAGTAG
|
| Enzyme 55 GenBank Gene ID |
M77804 |
| Enzyme 55 GeneCard ID |
WARS |
| Enzyme 55 GenAtlas ID |
WARS |
| Enzyme 55 HGNC ID |
HGNC:12729 |
| Enzyme 55 Chromosome Location |
1 |
| Enzyme 55 Locus |
14q32.31 |
| Enzyme 55 SNPs |
SNPJam Report |
| Enzyme 55 General References |
- Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP: Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J Biol Chem. 1991 Dec 25;266(36):24245-8. [PubMed ]
- Fleckner J, Rasmussen HH, Justesen J: Human interferon gamma potently induces the synthesis of a 55-kDa protein (gamma 2) highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11520-4. [PubMed ]
- Frolova LYu, Sudomoina MA, Grigorieva AYu, Zinovieva OL, Kisselev LL: Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. Gene. 1991 Dec 30;109(2):291-6. [PubMed ]
- Buwitt U, Flohr T, Bottger EC: Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor. EMBO J. 1992 Feb;11(2):489-96. [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 ]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [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 ]
- Sokolova IV, Narovlianskii AN, Amchenkova AM, Turpaev KT: [Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene] Mol Biol (Mosk). 1996 Mar-Apr;30(2):319-29. [PubMed ]
- Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL: The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. Gene. 1993 Jun 30;128(2):237-45. [PubMed ]
- Reano A, Richard MH, Denoroy L, Viac J, Benedetto JP, Schmitt D: Gamma interferon potently induces tryptophanyl-tRNA synthetase expression in human keratinocytes. J Invest Dermatol. 1993 Jun;100(6):775-9. [PubMed ]
- Wakasugi K, Slike BM, Hood J, Otani A, Ewalt KL, Friedlander M, Cheresh DA, Schimmel P: A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):173-7. Epub 2002 Jan 2. [PubMed ]
- Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed ]
- Bange FC, Flohr T, Buwitt U, Bottger EC: An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase. FEBS Lett. 1992 Mar 30;300(2):162-6. [PubMed ]
- Tolstrup AB, Bejder A, Fleckner J, Justesen J: Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-tRNA synthetase includes alternative splicing. J Biol Chem. 1995 Jan 6;270(1):397-403. [PubMed ]
- Otani A, Slike BM, Dorrell MI, Hood J, Kinder K, Ewalt KL, Cheresh D, Schimmel P, Friedlander M: A fragment of human TrpRS as a potent antagonist of ocular angiogenesis. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):178-83. Epub 2002 Jan 2. [PubMed ]
- Tzima E, Reader JS, Irani-Tehrani M, Ewalt KL, Schwartz MA, Schimmel P: Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells. Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14903-7. Epub 2003 Nov 20. [PubMed ]
- Wakasugi K, Nakano T, Morishima I: Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase. Biochemistry. 2005 Jan 11;44(1):225-32. [PubMed ]
- Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [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 ]
- Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L: Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15376-80. Epub 2003 Dec 11. [PubMed ]
- Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J: Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity. J Biol Chem. 2004 Feb 27;279(9):8378-88. Epub 2003 Dec 5. [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 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
5849 |
| Enzyme 56 Name |
Long-chain-fatty-acid--CoA ligase 1 |
| Enzyme 56 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 56 Gene Name |
ACSL1 |
| Enzyme 56 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 1
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
|
| Enzyme 56 Number of Residues |
698 |
| Enzyme 56 Molecular Weight |
77942.7 |
| Enzyme 56 Theoretical pI |
7.16 |
| Enzyme 56 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 56 General Function |
Involved in catalytic activity |
| Enzyme 56 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 56 Pathways |
|
| Enzyme 56 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 56 Pfam Domain Function |
|
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
Not Available |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
P33121 |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
ACSL1_HUMAN |
| Enzyme 56 PDB ID |
Not Available |
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 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 56 GenBank Gene ID |
D10040 |
| Enzyme 56 GeneCard ID |
ACSL1 |
| Enzyme 56 GenAtlas ID |
ACSL1 |
| Enzyme 56 HGNC ID |
HGNC:3569 |
| Enzyme 56 Chromosome Location |
4 |
| Enzyme 56 Locus |
4q35 |
| Enzyme 56 SNPs |
SNPJam Report |
| Enzyme 56 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 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
5851 |
| Enzyme 57 Name |
Ubiquitin-conjugating enzyme E2 G1 |
| Enzyme 57 Synonyms |
- E217K
- UBC7
- Ubiquitin carrier protein G1
- Ubiquitin-protein ligase G1
|
| Enzyme 57 Gene Name |
UBE2G1 |
| Enzyme 57 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 G1
MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLT
FPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETI
MISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE
|
| Enzyme 57 Number of Residues |
170 |
| Enzyme 57 Molecular Weight |
19509.0 |
| Enzyme 57 Theoretical pI |
4.95 |
| Enzyme 57 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 57 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 57 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4 |
| Enzyme 57 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 57 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
Not Available |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
P62253 |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
UB2G1_HUMAN |
| Enzyme 57 PDB ID |
Not Available |
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>513 bp
ATGACGGAGCTGCAGTCGGCACTGCTACTGCGAAGACAGCTGGCAGAACTCAACAAAAAT
CCAGTGGAAGGCTTTTCTGCAGGTTTAATAGATGACAATGATCTCTACCGATGGGAAGTC
CTTATTATTGGCCCTCCAGATACACTTTATGAAGGTGGTGTTTTTAAGGCTCATCTTACT
TTCCCAAAAGATTATCCCCTCCGACCTCCTAAAATGAAATTCATTACAGAAATCTGGCAC
CCAAATGTTGATAAAAATGGTGATGTGTGCATTTCTATTCTTCATGAGCCTGGGGAAGAT
AAGTATGGTTATGAAAAGCCAGAGGAACGCTGGCTCCCTATCCACACTGTGGAAACCATC
ATGATTAGTGTCATTTCTATGCTGGCAGACCCTAATGGAGACTCACCTGCTAATGTTGAT
GCTGCGAAAGAATGGAGGGAAGATAGAAATGGAGAATTTAAAAGAAAAGTTGCCCGCTGT
GTAAGAAAAAGCCAAGAGACTGCTTTTGAGTGA
|
| Enzyme 57 GenBank Gene ID |
D78514 |
| Enzyme 57 GeneCard ID |
UBE2G1 |
| Enzyme 57 GenAtlas ID |
UBE2G1 |
| Enzyme 57 HGNC ID |
HGNC:12482 |
| Enzyme 57 Chromosome Location |
1 |
| Enzyme 57 Locus |
1q42|17p13.2 |
| Enzyme 57 SNPs |
SNPJam Report |
| Enzyme 57 General References |
- Watanabe TK, Kawai A, Fujiwara T, Maekawa H, Hirai Y, Nakamura Y, Takahashi E: Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans. Cytogenet Cell Genet. 1996;74(1-2):146-8. [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 ]
- 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 ]
- Pabarcus MK, Hoe N, Sadeghi S, Patterson C, Wiertz E, Correia MA: CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch Biochem Biophys. 2009 Mar 1;483(1):66-74. Epub 2008 Dec 10. [PubMed ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
5852 |
| Enzyme 58 Name |
Glutaminyl-tRNA synthetase |
| Enzyme 58 Synonyms |
- Glutamine--tRNA ligase
- GlnRS
|
| Enzyme 58 Gene Name |
QARS |
| Enzyme 58 Protein Sequence |
>Glutaminyl-tRNA synthetase
MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLA
SRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPE
QIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPK
LEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKT
PGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFL
RFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQ
RGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRV
KYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPV
QWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVG
VTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADET
KGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVES
LEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASL
HVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV
|
| Enzyme 58 Number of Residues |
775 |
| Enzyme 58 Molecular Weight |
87798.0 |
| Enzyme 58 Theoretical pI |
7.16 |
| Enzyme 58 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- glutamine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- glutaminyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 58 General Function |
Involved in nucleotide binding |
| Enzyme 58 Specific Function |
ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln) |
| Enzyme 58 Pathways |
|
| Enzyme 58 Reactions |
- ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln [RN:R03652]
|
| Enzyme 58 Pfam Domain Function |
|
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
558586 |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
P47897 |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
SYQ_HUMAN |
| Enzyme 58 PDB ID |
Not Available |
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
>2328 bp
ATGGCGGCTCTAGACTCCCTGTCGCTCTTCACTAGCCTCGGCCTGAGCGAGCAGAAGGCC
CGCGAGACGCTCAAGAACTCGGCTCTGAGCGCGCAGCTGCGCGAGGCCGCTACTCAGGCT
CAGCAGACCCTGGGTTCCACCATTGACAAAGCTACCGGGATCCTGTTATATGGCTTGGCC
TCCCGACTCAGGGATACCCGGCGTCTCTCCTTCCTTGTAAGCTACATAGCCAGTAAGAAG
ATCCACACTGAGCCCCAGCTAAGCGCTGCCCTTGAGTATGTGCGGAGTCACCCCTTGGAC
CCCATCGACACTGTGGACTTCGAGCGGGAATGTGGCGTGGGTGTCATTGTGACCCCAGAG
CAGATTGAGGAGGCTGTGGAGGCTGCTATTAACAGGCACCGGCCCCAGCTCCTGGTGGAA
CGTTACCATTTCAACATGGGGCTGCTGATGGGAGAGGCTCGGGCTGTGCTGAAGTGGGCA
GATGGCAAAATGATCAAGAATGAAGTGGACATGCAGGTCCTCCACCTTCTGGGCCCCAAG
TTGGAGGCTGATCTGGAGAAGAAGTTCAAGGTGGCAAAAGCTCGGCTAGAAGAAACAGAC
CGGAGGACGGCAAAGGATGTGGTGGAGAATGGCGAGACTGCTGACCAGACCCTGTCTCTG
ATGGAGCAGCTCCGGGGGGAGGCCCTTAAGTTCCACAAGCCTGGTGAGAACTACAAGACC
CCAGGCTATGTGGTCACTCCACACACCATGAATCTACTAAAGCAGCACCTGGAGATTACT
GGTGGGCAGGTACGTACCCGGTTCCCGCCAGAACCCAATGGAATCCTGCATATTGGACAT
GCCAAAGCCATCAATTTCAACTTTGGCTATGCCAAGGCCAACAATGGCATCTGTTTTCTG
CGTTTTGATGACACCAACCCTGAGAAGGAGGAAGCAAAGTTCTTCACGGCCATCTGTGAC
ATGGTAGCCTGGCTAGGCTACACACCTTACAAAGTCACATATGCGTCTGACTATTTTGAC
CAGCTATATGCGTGGGCTGTGGAGCTCATCCGCAGGGGTCTGGCTTATGTGTGCCACCAG
CGAGGAGAGGAGCTCAAAGGCCATAATACTCTGCCTTCACCCTGGAGAGACCGTCCCATG
GAGGAGTCACTGCTGCTCTTTGAGGCAATGCGCAAGGGCAAGTTTTCAGAGGGCGAGGCC
ACACTACGGATGAAGCTGGTGATGGAGGATGGCAAGATGGACCCTGTAGCCTATCGAGTC
AAGTATACACCACACCACCGCACAGGGGACAAATGGTGCATCTATCCCACCTACGACTAC
ACACACTGCCTCTGTGACTCCATCGAGCACATCACTCACTCACTCTGCACCAAGGAATTC
CAGGCCCGACGCTCTTCCTACTTCTGGCTTTGCAATGCACTGGACGTCTATTGCCCTGTG
CAGTGGGAGTATGGCCGCCTCAACCTGCACTATGCTGTTGTCTCTAAGAGGAAGATCCTC
CAGCTTGTAGCAACTGGTGCTGTGCGGGACTGGGATGACCCACGGCTCTTTACACTCACG
GCCCTGCGACGGCGGGGCTTCCCACCTGAGGCCATCAACAACTTCTGTGCCCGGGTGGGA
GTGACTGTGGCACAAACCACAATGGAGCCACATCTTCTAGAAGCCTGTGTGCGTGATGTG
CTGAATGACACAGCCCCACGAGCCATGGCTGTGCTGGAGTCACTACGGGTCATCATCACC
AACTTTCCTGCTGCCAAGTCCTTGGACATCCAGGTGCCCAACTTCCCAGCTGATGAGACC
AAAGGCTTCCATCAGGTTCCCTTTGCACCCATTGTCTTCATTGAGAGGACTGACTTCAAG
GAGGAGCCAGAGCCAGGATTTAAGCGCCTGGCTTGGGGCCAGCCTGTGGGCCTGAGGCAT
ACAGGCTACGTCATTGAGCTGCAGCATGTTGTCAAGGGCCCCAGTGGTTGTGTAGAGAGT
CTGGAGGTGACCTGCAGACGGGCAGATGCTGGAGAGAAGCCAAAGGCCTTTATTCACTGG
GTGTCACAGCCTTTGATGTGTGAGGTTCGCCTCTATGAGCGACTATTCCAGCACAAGAAC
CCTGAAGATCCTACTGAGGTGCCTGGTGGATTTTTAAGTGACCTGAACCTGGCATCACTA
CACGTGGTGGATGCAGCATTAGTGGACTGCTCTGTGGCCCTGGCAAAACCCTTCGACAAG
TTCCAGTTTGAGCGTCTTGGATATTTCTCCGTGGATCCAGACAGCCATCAGGGAAAGCTT
GTCTTTAACCGAACTGTCACACTGAAGGAAGACCCAGGAAAGGTGTGA
|
| Enzyme 58 GenBank Gene ID |
X76013 |
| Enzyme 58 GeneCard ID |
QARS |
| Enzyme 58 GenAtlas ID |
QARS |
| Enzyme 58 HGNC ID |
HGNC:9751 |
| Enzyme 58 Chromosome Location |
3 |
| Enzyme 58 Locus |
3p21.31 |
| Enzyme 58 SNPs |
SNPJam Report |
| Enzyme 58 General References |
- Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M: Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8670-4. [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 ]
- 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 ]
- 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 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
5853 |
| Enzyme 59 Name |
Threonyl-tRNA synthetase, cytoplasmic |
| Enzyme 59 Synonyms |
- Threonine--tRNA ligase
- ThrRS
|
| Enzyme 59 Gene Name |
TARS |
| Enzyme 59 Protein Sequence |
>Threonyl-tRNA synthetase, cytoplasmic
MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF
|
| Enzyme 59 Number of Residues |
723 |
| Enzyme 59 Molecular Weight |
83434.5 |
| Enzyme 59 Theoretical pI |
6.64 |
| Enzyme 59 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- threonine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- threonyl-tRNA aminoacylation
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 59 General Function |
Involved in nucleotide binding |
| Enzyme 59 Specific Function |
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) |
| Enzyme 59 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 59 Reactions |
- ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr [RN:R03663]
|
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
158258124 |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
P26639 |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
SYTC_HUMAN |
| Enzyme 59 PDB ID |
Not Available |
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>2172 bp
ATGTTTGAGGAGAAGGCCAGCAGTCCTTCAGGGAAGATGGGAGGCGAGGAGAAGCCGATT
GGTGCTGGTGAAGAGAAGCAAAAGGAAGGAGGCAAAAAGAAGAACAAAGAAGGATCTGGA
GATGGAGGTCGAGCTGAGTTGAATCCTTGGCCTGAATATATTTACACACGTCTTGAGATG
TATAATATACTAAAAGCAGAACATGATTCCATTCTGGCAGAAAAGGCAGAAAAAGATAGC
AAGCCAATTAAAGTCACTTTGCCTGATGGTAAACAGGTTGATGCGGAATCTTGGAAAACT
ACACCATATCAAATTGCCTGTGGAATTAGTCAAGGCCTGGCCGACAACACCGTTATTGCT
AAAGTAAATAATGTTGTGTGGGACCTGGACCGCCCTCTGGAAGAAGATTGTACCTTGGAG
CTTCTCAAGTTTGAGGATGAGGAAGCTCAGGCAGTGTATTGGCACTCTAGTGCTCACATA
ATGGGTGAAGCCATGGAAAGAGTCTATGGTGGATGTTTATGCTACGGTCCGCCAATAGAA
AATGGATTCTATTATGACATGTACCTCGAAGAAGGGGGTGTGTCTAGCAATGATTTCTCT
TCTCTGGAGGCTTTGTGTAAGAAAATCATTAAAGAAAAACAAGCTTTTGAAAGACTGGAA
GTTAAGAAAGAAACTTTACTGGCAATGTTTAAGTACAACAAGTTCAAATGCCGGATATTG
AATGAAAAGGTGAATACTCCAACTACCACAGTCTATAGATGTGGCCCTTTGATAGATCTC
TGCCGGGGTCCTCATGTTAGACACACGGGCAAAATTAAGGCTTTAAAAATACACAAAAAT
TCCTCCACGTACTGGGAAGGCAAAGCAGATATGGAGACTCTCCAGAGAATTTATGGCATT
TCATTCCCAGATCCTAAAATGTTGAAAGAGTGGGAGAAGTTCCAAGAGGAAGCTAAAAAC
CGAGATCATAGGAAAATTGGCAGGGACCAAGAACTATATTTCTTTCATGAACTCAGCCCT
GGAAGTTGCTTTTTTCTGCCAAAAGGAGCCTACATTTATAATGCACTTATTGAATTCATT
AGGAGCGAATATAGGAAAAGAGGATTCCAGGAGGTAGTCACCCCAAACATCTTCAACAGC
CGACTCTGGATGACCTCGGGCCACTGGCAGCACTACAGCGAGAACATGTTCTCCTTTGAG
GTGGAGAAGGAGCTGTTTGCCCTGAAACCCATGAACTGCCCAGGACACTGCCTTATGTTT
GATCATCGGCCAAGGTCCTGGCGAGAACTGCCTCTGCGGCTAGCTGATTTTGGGGTACTT
CATAGGAACGAGCTGTCTGGAGCACTCACAGGACTCACCCGGGTACGAAGATTCCAACAG
GATGATGCTCACATATTCTGTGCCATGGAGCAGATTGAAGATGAAATAAAAGGTTGTTTG
GATTTTCTACGTACGGTATATAGCGTATTTGGATTTTCTTTTAAACTAAACCTTTCTACT
CGCCCGGAAAAATTCCTTGGAGATATCGAAGTATGGGATCAAGCTGAGAAACAACTTGAA
AACAGTCTGAATGAATTTGGTGAAAAGTGGGAGTTAAACTCTGGAGATGGAGCTTTCTAT
GGCCCAAAGATTGACATACAGATTAAAGATGCGATTGGGCGGTACCACCAGTGTGCAACC
ATCCAGCTGGATTTCCAGTTGCCCATCAGATTTAATCTTACTTATGTAAGCCATGATGGT
GATGATAAGAAAAGGCCAGTGATTGTTCATCGAGCCATCTTGGGATCAGTGGAAAGAATG
ATTGCTATCCTCACAGAAAACTATGGGGGCAAATGGCCCTTTTGGCTGTCCCCTCGCCAG
GTAATGGTAGTTCCAGTGGGACCAACCTGTGATGAATATGCCCAAAAGGTACGACAACAA
TTCCACGATGCCAAATTCATGGCAGACATTGATCTGGATCCAGGCTGTACATTGAATAAA
AAGATTCGAAATGCACAGTTAGCACAGTATAACTTCATTTTAGTTGTTGGTGAAAAAGAG
AAAATCAGTGGCACTGTTAATATCCGCACAAGAGACAATAAGGTCCACGGGGAACGCACC
ATTTCTGAAACTATCGAGCGGCTACAGCAGCTCAAAGAGTTCCGCAGCAAACAGGCAGAA
GAAGAATTTTAA
|
| Enzyme 59 GenBank Gene ID |
AK292346 |
| Enzyme 59 GeneCard ID |
TARS |
| Enzyme 59 GenAtlas ID |
TARS |
| Enzyme 59 HGNC ID |
HGNC:11572 |
| Enzyme 59 Chromosome Location |
5 |
| Enzyme 59 Locus |
5p13.2 |
| Enzyme 59 SNPs |
SNPJam Report |
| Enzyme 59 General References |
- Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes. J Biol Chem. 1991 May 25;266(15):9919-23. [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 ]
- 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 ]
- Vasilescu J, Zweitzig DR, Denis NJ, Smith JC, Ethier M, Haines DS, Figeys D: The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells. J Proteome Res. 2007 Jan;6(1):298-305. [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 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
5855 |
| Enzyme 60 Name |
Asparagine synthetase [glutamine-hydrolyzing] |
| Enzyme 60 Synonyms |
- Cell cycle control protein TS11
- Glutamine-dependent asparagine synthetase
|
| Enzyme 60 Gene Name |
ASNS |
| Enzyme 60 Protein Sequence |
>Asparagine synthetase [glutamine-hydrolyzing]
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQ
PIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGV
FAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPF
LPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFN
NAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAAR
KVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVV
IFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPF
LDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNS
WFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPK
WINATDPSARTLTHYKSAVKA
|
| Enzyme 60 Number of Residues |
561 |
| Enzyme 60 Molecular Weight |
64369.4 |
| Enzyme 60 Theoretical pI |
6.85 |
| Enzyme 60 GO Classification |
| Function |
- asparagine synthase (glutamine-hydrolyzing) activity
- asparagine synthase (glutamine-hydrolyzing) activity
- carbon-nitrogen ligase activity, with glutamine as amido-N-donor
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- asparagine biosynthetic process
- asparagine metabolic process
- aspartate family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 60 General Function |
Involved in asparagine synthase (glutamine-hydrolyzing) activity |
| Enzyme 60 Specific Function |
ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate |
| Enzyme 60 Pathways |
|
| Enzyme 60 Reactions |
- (1) ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate [RN:R00578]
- (2) (1a) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
- (3) (1b) ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine [RN:R00483]
|
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
179100 |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
P08243 |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
ASNS_HUMAN |
| Enzyme 60 PDB ID |
Not Available |
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>1686 bp
ATGTGTGGCATTTGGGCGCTGTTTGGCAGTGATGATTGCCTTTCTGTTCAGTGTCTGAGT
GCTATGAAGATTGCACACAGAGGTCCAGATGCATTCCGTTTTGAGAATGTCAATGGATAC
ACCAACTGCTGCTTTGGATTTCACCGGTTGGCGGTAGTTGACCCGCTGTTTGGAATGCAG
CCAATTCGAGTGAAGAAATATCCGTATTTGTGGCTCTGTTACAATGGTGAAATCTACAAC
CATAAGAAGATGCAACAGCATTTTGAATTTGAATACCAGACCAAAGTGGATGGTGAGATA
ATCCTTCATCTTTATGACAAAGGAGGAATTGAGCAAACAATTTGTATGTTGGATGGTGTG
TTTGCATTTGTTTTACTGGATACTGCCAATAAGAAAGTGTTCCTGGGTAGAGATACATAT
GGAGTCAGACCTTTGTTTAAAGCAATGACAGAAGATGGATTTTTGGCTGTATGTTCAGAA
GCTAAAGGTCTTGTTACATTGAAGCACTCCGCGACTCCCTTTTTAAAAGTGGAGCCTTTT
CTTCCTGGACACTATGAAGTTTTGGATTTAAAGCCAAATGGCAAAGTTGCATCCGTGGAA
ATGGTTAAATATCATCACTGTCGGGATGTACCCCTGCACGCCCTCTATGACAATGTGGAG
AAACTCTTTCCAGGTTTTGAGATAGAAACTGTGAAGAACAACCTCAGGATCCTTTTTAAT
AATGCTGTAAAGAAACGTTTGATGACAGACAGAAGGATTGGCTGCCTTTTATCAGGGGGC
TTGGACTCCAGCTTGGTTGCTGCCACTCTGTTGAAGCAGCTGAAAGAAGCCCAAGTACAG
TATCCTCTCCAGACATTTGCAATTGGCATGGAAGACAGCCCCGATTTACTGGCTGCTAGA
AAGGTGGCAGATCATATTGGAAGTGAACATTATGAAGTCCTTTTTAACTCTGAGGAAGGC
ATTCAGGCTCTGGATGAAGTCATATTTTCCTTGGAAACTTATGACATTACAACAGTTCGT
GCTTCAGTAGGTATGTATTTAATTTCCAAGTATATTCGGAAGAACACAGATAGCGTGGTG
ATCTTCTCTGGAGAAGGATCAGATGAACTTACGCAGGGTTACATATATTTTCACAAGGCT
CCTTCTCCTGAAAAAGCCGAGGAGGAGAGTGAGAGGCTTCTGAGGGAACTCTATTTGTTT
GATGTTCTCCGCGCAGATCGAACTACTGCTGCCCATGGTCTTGAACTGAGAGTCCCATTT
CTAGATCATCGATTTTTTTCCTATTACTTGTCTCTGCCACCAGAAATGAGAATTCCAAAG
AATGGGATAGAAAAACATCTCCTGAGAGAGACGTTTGAGGATTCCAATCTGATACCCAAA
GAGATTCTCTGGCGACCAAAAGAAGCCTTCAGTGATGGAATAACTTCAGTTAAGAATTCC
TGGTTTAAGATTTTACAGGAATACGTTGAACATCAGGTTGATGATGCAATGATGGCAAAT
GCAGCCCAGAAATTTCCCTTCAATACTCCTAAAACCAAAGAAGGATATTACTACCGTCAA
GTCTTTGAACGCCATTACCCAGGCCGGGCTGACTGGCTGAGCCATTACTGGATGCCCAAG
TGGATCAATGCCACTGACCCTTCTGCCCGCACGCTGACCCACTACAAGTCAGCTGTCAAA
GCTTAG
|
| Enzyme 60 GenBank Gene ID |
M27396 |
| Enzyme 60 GeneCard ID |
ASNS |
| Enzyme 60 GenAtlas ID |
ASNS |
| Enzyme 60 HGNC ID |
HGNC:753 |
| Enzyme 60 Chromosome Location |
7 |
| Enzyme 60 Locus |
7q21.3 |
| Enzyme 60 SNPs |
SNPJam Report |
| Enzyme 60 General References |
- Andrulis IL, Chen J, Ray PN: Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells. Mol Cell Biol. 1987 Jul;7(7):2435-43. [PubMed ]
- Zhang YP, Lambert MA, Cairney AE, Wills D, Ray PN, Andrulis IL: Molecular structure of the human asparagine synthetase gene. Genomics. 1989 Apr;4(3):259-65. [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 ]
- 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 ]
- Greco A, Ittmann M, Basilico C: Molecular cloning of a gene that is necessary for G1 progression in mammalian cells. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1565-9. [PubMed ]
- Greco A, Gong SS, Ittmann M, Basilico C: Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase. Mol Cell Biol. 1989 Jun;9(6):2350-9. [PubMed ]
- Van Heeke G, Schuster SM: Expression of human asparagine synthetase in Escherichia coli. J Biol Chem. 1989 Apr 5;264(10):5503-9. [PubMed ]
- Van Heeke G, Schuster SM: The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity. J Biol Chem. 1989 Nov 25;264(33):19475-7. [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 ]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
5856 |
| Enzyme 61 Name |
Ubiquitin-conjugating enzyme E2 E2 |
| Enzyme 61 Synonyms |
- UbcH8
- Ubiquitin carrier protein E2
- Ubiquitin-protein ligase E2
|
| Enzyme 61 Gene Name |
UBE2E2 |
| Enzyme 61 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 E2
MSTEAQRVDDSPSTSGGSSDGDQRESVQQEPEREQVQPKKKEGKISSKTAAKLSTSAKRI
QKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSPDYPFKPPK
VTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQ
YMTNRAEHDRMARQWTKRYAT
|
| Enzyme 61 Number of Residues |
201 |
| Enzyme 61 Molecular Weight |
22254.9 |
| Enzyme 61 Theoretical pI |
7.84 |
| Enzyme 61 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 61 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 61 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination |
| Enzyme 61 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 61 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
16553859 |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
Q96LR5 |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
UB2E2_HUMAN |
| Enzyme 61 PDB ID |
1Y6L |
| Enzyme 61 PDB File |
Show |
| Enzyme 61 3D Structure |
|
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>606 bp
ATGTCCACTGAGGCACAAAGAGTTGATGACAGTCCAAGCACTAGTGGAGGAAGTTCCGAT
GGAGATCAACGTGAAAGTGTTCAGCAAGAACCAGAAAGAGAACAAGTTCAGCCCAAGAAA
AAGGAGGGAAAAATATCCAGCAAAACCGCTGCTAAATTGTCAACTAGTGCTAAAAGAATT
CAGAAGGAACTTGCAGAAATCACATTGGACCCTCCTCCCAACTGTAGTGCTGGACCCAAA
GGAGACAACATTTATGAATGGAGGTCAACTATATTGGGACCCCCAGGATCTGTCTATGAA
GGAGGGGTGTTCTTTCTTGACATTACCTTTTCACCAGACTATCCGTTTAAACCCCCTAAG
GTTACCTTCCGAACAAGAATCTATCACTGTAATATTAACAGCCAAGGTGTGATCTGTCTG
GACATCTTAAAGGACAACTGGAGTCCGGCTTTAACTATTTCTAAAGTTCTCCTCTCCATC
TGCTCACTTCTTACAGATTGCAACCCTGCTGACCCTCTGGTGGGCAGCATCGCCACACAG
TACATGACCAACAGAGCAGAGCATGACCGGATGGCCAGACAGTGGACCAAGCGGTACGCC
ACATAG
|
| Enzyme 61 GenBank Gene ID |
AK057886 |
| Enzyme 61 GeneCard ID |
UBE2E2 |
| Enzyme 61 GenAtlas ID |
UBE2E2 |
| Enzyme 61 HGNC ID |
HGNC:12478 |
| Enzyme 61 Chromosome Location |
3 |
| Enzyme 61 Locus |
3p24.2 |
| Enzyme 61 SNPs |
SNPJam Report |
| Enzyme 61 General References |
- Kimura M, Hattori T, Matsuda Y, Yoshioka T, Sumi N, Umeda Y, Nakashima S, Okano Y: cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme. Cytogenet Cell Genet. 1997;78(2):107-11. [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 ]
- 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 ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
5858 |
| Enzyme 62 Name |
Adenylate kinase isoenzyme 4, mitochondrial |
| Enzyme 62 Synonyms |
- ATP-AMP transphosphorylase
- Adenylate kinase 3-like
|
| Enzyme 62 Gene Name |
AK4 |
| Enzyme 62 Protein Sequence |
>Adenylate kinase isoenzyme 4, mitochondrial
MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEK
SLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLK
DRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKP
VIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY
|
| Enzyme 62 Number of Residues |
223 |
| Enzyme 62 Molecular Weight |
25267.8 |
| Enzyme 62 Theoretical pI |
8.66 |
| Enzyme 62 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- nucleotide kinase activity
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 62 General Function |
Involved in ATP binding |
| Enzyme 62 Specific Function |
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. May also be active with GTP |
| Enzyme 62 Pathways |
|
| Enzyme 62 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
189069342 |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
P27144 |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
KAD4_HUMAN |
| Enzyme 62 PDB ID |
Not Available |
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>672 bp
ATGGCTTCCAAACTCCTGCGCGCGGTCATCCTCGGGCCGCCCGGCTCGGGCAAGGGCACC
GTGTGCCAGAGGATCGCCCAGAACTTTGGTCTCCAGCATCTCTCCAGCGGCCACTTCTTG
CGGGAGAACATCAAGGCCAGCACCGAAGTTGGTGAGATGGCAAAGCAGTATATAGAGAAA
AGTCTTTTGGTTCCAGACCATGTGATCACACGCCTAATGATGTCCGAGTTGGAGAACAGG
CGTGGCCAGCACTGGCTCCTTGATGGTTTTCCTAGGACATTAGGACAAGCCGAAGCCCTG
GACAAAATCTGTGAAGTGGATCTAGTGATCAGTTTGAATATTCCATTTGAAACACTTAAA
GATCGTCTCAGCCGCCGTTGGATTCACCCTCCTAGCGGAAGGGTATATAACCTGGACTTC
AATCCACCTCATGTACATGGTATTGATGACGTCACTGGTGAACCATTAGTCCAGCAGGAG
GATGATAAACCCGAAGCAGTTGCTGCCAGGCTAAGACAGTACAAAGACGTGGCAAAGCCA
GTCATTGAATTATACAAGAGCCGAGGAGTGCTCCACCAATTTTCCGGAACGGAGACGAAC
AAAATCTGGCCCTACGTTTACACACTTTTCTCAAACAAGATCACACCTATTCAGTCCAAA
GAAGCATATTGA
|
| Enzyme 62 GenBank Gene ID |
AK313611 |
| Enzyme 62 GeneCard ID |
AK4 |
| Enzyme 62 GenAtlas ID |
AK4 |
| Enzyme 62 HGNC ID |
HGNC:363 |
| Enzyme 62 Chromosome Location |
1 |
| Enzyme 62 Locus |
1p31.3 |
| Enzyme 62 SNPs |
SNPJam Report |
| Enzyme 62 General References |
- Xu G, O'Connell P, Stevens J, White R: Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene. Genomics. 1992 Jul;13(3):537-42. [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 ]
- 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 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
5859 |
| Enzyme 63 Name |
Ubiquitin-conjugating enzyme E2 D2 |
| Enzyme 63 Synonyms |
- Ubiquitin carrier protein D2
- Ubiquitin-conjugating enzyme E2(17)KB 2
- Ubiquitin-conjugating enzyme E2-17 kDa 2
- Ubiquitin-protein ligase D2
|
| Enzyme 63 Gene Name |
UBE2D2 |
| Enzyme 63 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 D2
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDREKYNRIAREWTQKYAM
|
| Enzyme 63 Number of Residues |
147 |
| Enzyme 63 Molecular Weight |
16735.1 |
| Enzyme 63 Theoretical pI |
7.96 |
| Enzyme 63 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 63 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 63 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP- induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of CHIP and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of TP53/p53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3 |
| Enzyme 63 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 63 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
Not Available |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
P62837 |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
UB2D2_HUMAN |
| Enzyme 63 PDB ID |
1UR6 |
| Enzyme 63 PDB File |
Show |
| Enzyme 63 3D Structure |
|
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>444 bp
ATGGCTCTGAAGAGAATCCACAAGGAATTGAATGATCTGGCACGGGACCCTCCAGCACAG
TGTTCAGCAGGTCCTGTTGGAGATGATATGTTCCATTGGCAAGCTACAATAATGGGGCCA
AATGACAGTCCCTATCAGGGTGGAGTATTTTTCTTGACAATTCATTTCCCAACAGATTAC
CCCTTCAAACCACCTAAGGTTGCATTTACAACAAGAATTTATCATCCAAATATTAACAGT
AATGGCAGCATTTGTCTTGATATTCTACGATCACAGTGGTCTCCAGCACTAACTATTTCA
AAAGTACTCTTGTCCATCTGTTCTCTGTTGTGTGATCCCAATCCAGATGATCCTTTAGTG
CCTGAGATTGCTCGGATCTACAAAACAGATAGAGAAAAGTACAACAGAATAGCTCGGGAA
TGGACTCAGAAGTATGCGATGTAA
|
| Enzyme 63 GenBank Gene ID |
U39317 |
| Enzyme 63 GeneCard ID |
UBE2D2 |
| Enzyme 63 GenAtlas ID |
UBE2D2 |
| Enzyme 63 HGNC ID |
HGNC:12475 |
| Enzyme 63 Chromosome Location |
5 |
| Enzyme 63 Locus |
5q31.2 |
| Enzyme 63 SNPs |
SNPJam Report |
| Enzyme 63 General References |
- Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM: Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem. 1995 Dec 22;270(51):30408-14. [PubMed ]
- Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, Draetta G: Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3264-8. [PubMed ]
- Guinn BA, Bland EA, Lodi U, Liggins AP, Tobal K, Petters S, Wells JW, Banham AH, Mufti GJ: Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia. Biochem Biophys Res Commun. 2005 Oct 7;335(4):1293-304. [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 ]
- Gonen H, Bercovich B, Orian A, Carrano A, Takizawa C, Yamanaka K, Pagano M, Iwai K, Ciechanover A: Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. J Biol Chem. 1999 May 21;274(21):14823-30. [PubMed ]
- Strack P, Caligiuri M, Pelletier M, Boisclair M, Theodoras A, Beer-Romero P, Glass S, Parsons T, Copeland RA, Auger KR, Benfield P, Brizuela L, Rolfe M: SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4. Oncogene. 2000 Jul 20;19(31):3529-36. [PubMed ]
- Saville MK, Sparks A, Xirodimas DP, Wardrop J, Stevenson LF, Bourdon JC, Woods YL, Lane DP: Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo. J Biol Chem. 2004 Oct 1;279(40):42169-81. Epub 2004 Jul 26. [PubMed ]
- Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT: An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair. J Mol Biol. 2004 Mar 12;337(1):157-65. [PubMed ]
- Windheim M, Peggie M, Cohen P: Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology. Biochem J. 2008 Feb 1;409(3):723-9. [PubMed ]
- Chiang MH, Chen LF, Chen H: Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation. Biol Reprod. 2008 Nov;79(5):914-20. Epub 2008 Aug 13. [PubMed ]
- Grou CP, Carvalho AF, Pinto MP, Wiese S, Piechura H, Meyer HE, Warscheid B, Sa-Miranda C, Azevedo JE: Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor. J Biol Chem. 2008 May 23;283(21):14190-7. Epub 2008 Mar 22. [PubMed ]
- Zeng W, Xu M, Liu S, Sun L, Chen ZJ: Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol Cell. 2009 Oct 23;36(2):315-25. [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 ]
- Zeng W, Sun L, Jiang X, Chen X, Hou F, Adhikari A, Xu M, Chen ZJ: Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell. 2010 Apr 16;141(2):315-30. [PubMed ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
- Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R: Solution structure of the ubiquitin-conjugating enzyme UbcH5B. J Mol Biol. 2004 Nov 19;344(2):513-26. [PubMed ]
- Sakata E, Satoh T, Yamamoto S, Yamaguchi Y, Yagi-Utsumi M, Kurimoto E, Tanaka K, Wakatsuki S, Kato K: Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates. Structure. 2010 Jan 13;18(1):138-47. [PubMed ]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
5860 |
| Enzyme 64 Name |
DNA ligase 4 |
| Enzyme 64 Synonyms |
- DNA ligase IV
- Polydeoxyribonucleotide synthase [ATP] 4
|
| Enzyme 64 Gene Name |
LIG4 |
| Enzyme 64 Protein Sequence |
>DNA ligase 4
MAASQTSQTVASHVPFADLCSTLERIQKSKGRAEKIRHFREFLDSWRKFHDALHKNHKDV
TDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPRDGKDALKLLNYRTPTGTHG
DAGDFAMIAYFVLKPRCLQKGSLTIQQVNDLLDSIASNNSAKRKDLIKKSLLQLITQSSA
LEQKWLIRMIIKDLKLGVSQQTIFSVFHNDAAELHNVTTDLEKVCRQLHDPSVGLSDISI
TLFSAFKPMLAAIADIEHIEKDMKHQSFYIETKLDGERMQMHKDGDVYKYFSRNGYNYTD
QFGASPTEGSLTPFIHNAFKADIQICILDGEMMAYNPNTQTFMQKGTKFDIKRMVEDSDL
QTCYCVFDVLMVNNKKLGHETLRKRYEILSSIFTPIPGRIEIVQKTQAHTKNEVIDALNE
AIDKREEGIMVKQPLSIYKPDKRGEGWLKIKPEYVSGLMDELDILIVGGYWGKGSRGGMM
SHFLCAVAEKPPPGEKPSVFHTLSRVGSGCTMKELYDLGLKLAKYWKPFHRKAPPSSILC
GTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGCTLRFPRIEKIRDDKEWHECMTLDDLE
QLRGKASGKLASKHLYIGGDDEPQEKKRKAAPKMKKVIGIIEHLKAPNLTNVNKISNIFE
DVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIRVKNIILSNKHDV
VKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSG
IKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVINDLSTKNEGTRLAI
KALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKILKESWVTDSIDK
CELQEENQYLI
|
| Enzyme 64 Number of Residues |
911 |
| Enzyme 64 Molecular Weight |
103969.9 |
| Enzyme 64 Theoretical pI |
8.04 |
| Enzyme 64 GO Classification |
| Function |
- ATP binding
- DNA binding
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleic acid binding
- nucleoside binding
- purine nucleoside binding
|
| Process |
- DNA ligation
- DNA ligation involved in DNA repair
- DNA metabolic process
- DNA recombination
- DNA repair
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
|
|
| Enzyme 64 General Function |
Involved in DNA ligase (ATP) activity |
| Enzyme 64 Specific Function |
Efficiently joins single-strand breaks in a double- stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA- dependent protein kinase complex DNA-PK to these DNA ends |
| Enzyme 64 Pathways |
Not Available |
| Enzyme 64 Reactions |
- ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m [RN:R00381]
|
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
148539894 |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
P49917 |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
DNLI4_HUMAN |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>2736 bp
ATGGCTGCCTCACAAACTTCACAAACTGTTGCATCTCACGTTCCTTTTGCAGATTTGTGT
TCAACTTTAGAACGAATACAGAAAAGTAAAGGACGTGCAGAAAAAATCAGACACTTCAGG
GAATTTTTAGATTCTTGGAGAAAATTTCATGATGCTCTTCATAAGAACCACAAAGATGTC
ACAGACTCTTTTTATCCAGCAATGAGACTAATTCTTCCTCAGCTAGAAAGAGAGAGAATG
GCCTATGGAATTAAAGAAACTATGCTTGCTAAGCTTTATATTGAGTTGCTTAATTTACCT
AGAGATGGAAAAGATGCCCTCAAACTTTTAAACTACAGAACACCCACTGGAACTCATGGA
GATGCTGGAGACTTTGCAATGATTGCATATTTTGTGTTGAAGCCAAGATGTTTACAGAAA
GGAAGTTTAACCATACAGCAAGTAAACGACCTTTTAGACTCAATTGCCAGCAATAATTCT
GCTAAAAGAAAAGACCTAATAAAAAAGAGCCTTCTTCAACTTATAACTCAGAGTTCAGCA
CTTGAGCAAAAGTGGCTTATACGGATGATCATAAAGGATTTAAAGCTTGGTGTTAGTCAG
CAAACTATCTTTTCTGTTTTTCATAATGATGCTGCTGAGTTGCATAATGTCACTACAGAT
CTGGAAAAAGTCTGTAGGCAACTGCATGATCCTTCTGTAGGACTCAGTGATATTTCTATC
ACTTTATTTTCTGCATTTAAACCAATGCTAGCTGCTATTGCAGATATTGAGCACATTGAG
AAGGATATGAAACATCAGAGTTTCTACATAGAAACCAAGCTAGATGGTGAACGTATGCAA
ATGCACAAAGATGGAGATGTATATAAATACTTCTCTCGAAATGGATATAACTACACTGAT
CAGTTTGGTGCTTCTCCTACTGAAGGTTCTCTTACCCCATTCATTCATAATGCATTCAAA
GCAGATATACAAATCTGTATTCTTGATGGTGAGATGATGGCCTATAATCCTAATACACAA
ACTTTCATGCAAAAGGGAACTAAGTTTGATATTAAAAGAATGGTAGAGGATTCTGATCTG
CAAACTTGTTATTGTGTTTTTGATGTATTGATGGTTAATAATAAAAAGCTAGGGCATGAG
ACTCTGAGAAAGAGGTATGAGATTCTTAGTAGTATTTTTACACCAATTCCAGGTAGAATA
GAAATAGTGCAGAAAACACAAGCTCATACTAAGAATGAAGTAATTGATGCATTGAATGAA
GCAATAGATAAAAGAGAAGAGGGAATTATGGTAAAACAACCTCTATCCATCTACAAGCCA
GACAAAAGAGGTGAAGGGTGGTTAAAAATTAAACCAGAGTATGTCAGTGGACTAATGGAT
GAATTGGACATTTTAATTGTTGGAGGATATTGGGGTAAAGGATCACGGGGTGGAATGATG
TCTCATTTTCTGTGTGCAGTAGCAGAGAAGCCCCCTCCTGGTGAGAAGCCATCTGTGTTT
CATACTCTCTCTCGTGTTGGGTCTGGCTGCACCATGAAAGAACTGTATGATCTGGGTTTG
AAATTGGCCAAGTATTGGAAGCCTTTTCATAGAAAAGCTCCACCAAGCAGCATTTTATGT
GGAACAGAGAAGCCAGAAGTATACATTGAACCTTGTAATTCTGTCATTGTTCAGATTAAA
GCAGCAGAGATCGTACCCAGTGATATGTATAAAACTGGCTGCACCTTGCGTTTTCCACGA
ATTGAAAAGATAAGAGATGACAAGGAGTGGCATGAGTGCATGACCCTGGACGACCTAGAA
CAACTTAGGGGGAAGGCATCTGGTAAGCTCGCATCTAAACACCTTTATATAGGTGGTGAT
GATGAACCACAAGAAAAAAAGCGGAAAGCTGCCCCAAAGATGAAGAAAGTTATTGGAATT
ATTGAGCACTTAAAAGCACCTAACCTTACTAACGTTAACAAAATTTCTAATATATTTGAA
GATGTAGAGTTTTGTGTTATGAGTGGAACAGATAGCCAGCCAAAGCCTGACCTGGAGAAC
AGAATTGCAGAATTTGGTGGTTATATAGTACAAAATCCAGGCCCAGACACGTACTGTGTA
ATTGCAGGGTCTGAGAACATCAGAGTGAAAAACATAATTTTGTCAAATAAACATGATGTT
GTCAAGCCTGCATGGCTTTTAGAATGTTTTAAGACCAAAAGCTTTGTACCATGGCAGCCT
CGCTTTATGATTCATATGTGCCCATCAACCAAAGAACATTTTGCCCGTGAATATGATTGC
TATGGTGATAGTTATTTCATTGATACAGACTTGAACCAACTGAAGGAAGTATTCTCAGGA
ATTAAAAATTCTAACGAGCAGACTCCTGAAGAAATGGCTTCTCTGATTGCTGATTTAGAA
TATCGGTATTCCTGGGATTGCTCTCCTCTCAGTATGTTTCGACGCCACACCGTTTATTTG
GACTCGTATGCTGTTATTAATGACCTGAGTACCAAAAATGAGGGGACAAGGTTAGCTATT
AAAGCCTTGGAGCTTCGGTTTCATGGAGCAAAAGTAGTTTCTTGTTTAGCTGAGGGAGTG
TCTCATGTAATAATTGGGGAAGATCATAGTCGTGTTGCAGATTTTAAAGCTTTTAGAAGA
ACTTTTAAGAGAAAGTTTAAAATCCTAAAAGAAAGTTGGGTAACTGATTCAATAGACAAG
TGTGAATTACAAGAAGAAAACCAGTATTTGATTTAA
|
| Enzyme 64 GenBank Gene ID |
NM_001098268.1 |
| Enzyme 64 GeneCard ID |
LIG4 |
| Enzyme 64 GenAtlas ID |
LIG4 |
| Enzyme 64 HGNC ID |
HGNC:6601 |
| Enzyme 64 Chromosome Location |
1 |
| Enzyme 64 Locus |
13q33-q34 |
| Enzyme 64 SNPs |
SNPJam Report |
| Enzyme 64 General References |
- Wei YF, Robins P, Carter K, Caldecott K, Pappin DJ, Yu GL, Wang RP, Shell BK, Nash RA, Schar P, et al.: Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol Cell Biol. 1995 Jun;15(6):3206-16. [PubMed ]
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [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 ]
- Robins P, Lindahl T: DNA ligase IV from HeLa cell nuclei. J Biol Chem. 1996 Sep 27;271(39):24257-61. [PubMed ]
- Grawunder U, Zimmer D, Fugmann S, Schwarz K, Lieber MR: DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes. Mol Cell. 1998 Oct;2(4):477-84. [PubMed ]
- Critchlow SE, Bowater RP, Jackson SP: Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. Curr Biol. 1997 Aug 1;7(8):588-98. [PubMed ]
- Chen L, Trujillo K, Sung P, Tomkinson AE: Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem. 2000 Aug 25;275(34):26196-205. [PubMed ]
- Calsou P, Delteil C, Frit P, Drouet J, Salles B: Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment. J Mol Biol. 2003 Feb 7;326(1):93-103. [PubMed ]
- Kanno S, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A: A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007 Apr 18;26(8):2094-103. Epub 2007 Mar 29. [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 ]
- Sibanda BL, Critchlow SE, Begun J, Pei XY, Jackson SP, Blundell TL, Pellegrini L: Crystal structure of an Xrcc4-DNA ligase IV complex. Nat Struct Biol. 2001 Dec;8(12):1015-9. [PubMed ]
- Riballo E, Critchlow SE, Teo SH, Doherty AJ, Priestley A, Broughton B, Kysela B, Beamish H, Plowman N, Arlett CF, Lehmann AR, Jackson SP, Jeggo PA: Identification of a defect in DNA ligase IV in a radiosensitive leukaemia patient. Curr Biol. 1999 Jul 1;9(13):699-702. [PubMed ]
- Riballo E, Doherty AJ, Dai Y, Stiff T, Oettinger MA, Jeggo PA, Kysela B: Cellular and biochemical impact of a mutation in DNA ligase IV conferring clinical radiosensitivity. J Biol Chem. 2001 Aug 17;276(33):31124-32. Epub 2001 May 10. [PubMed ]
- O'Driscoll M, Cerosaletti KM, Girard PM, Dai Y, Stumm M, Kysela B, Hirsch B, Gennery A, Palmer SE, Seidel J, Gatti RA, Varon R, Oettinger MA, Neitzel H, Jeggo PA, Concannon P: DNA ligase IV mutations identified in patients exhibiting developmental delay and immunodeficiency. Mol Cell. 2001 Dec;8(6):1175-85. [PubMed ]
- Roddam PL, Rollinson S, O'Driscoll M, Jeggo PA, Jack A, Morgan GJ: Genetic variants of NHEJ DNA ligase IV can affect the risk of developing multiple myeloma, a tumour characterised by aberrant class switch recombination. J Med Genet. 2002 Dec;39(12):900-5. [PubMed ]
- van der Burg M, van Veelen LR, Verkaik NS, Wiegant WW, Hartwig NG, Barendregt BH, Brugmans L, Raams A, Jaspers NG, Zdzienicka MZ, van Dongen JJ, van Gent DC: A new type of radiosensitive T-B-NK+ severe combined immunodeficiency caused by a LIG4 mutation. J Clin Invest. 2006 Jan;116(1):137-45. Epub 2005 Dec 15. [PubMed ]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
5863 |
| Enzyme 65 Name |
Arginyl-tRNA synthetase, cytoplasmic |
| Enzyme 65 Synonyms |
- Arginine--tRNA ligase
- ArgRS
|
| Enzyme 65 Gene Name |
RARS |
| Enzyme 65 Protein Sequence |
>Arginyl-tRNA synthetase, cytoplasmic
MDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQEENLKLKYRLNILRK
SLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMG
ISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSEQLTSLLV
NGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGD
WGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGK
NPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDG
RKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIF
AAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEK
ERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTR
IRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDY
IYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRM
|
| Enzyme 65 Number of Residues |
660 |
| Enzyme 65 Molecular Weight |
75378.3 |
| Enzyme 65 Theoretical pI |
6.65 |
| Enzyme 65 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- arginine-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- arginyl-tRNA aminoacylation
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 65 General Function |
Involved in nucleotide binding |
| Enzyme 65 Specific Function |
Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 |
| Enzyme 65 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 65 Reactions |
- ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg [RN:R03646]
|
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
62897153 |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
P54136 |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
SYRC_HUMAN |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>1983 bp
ATGGACGTACTGGTGTCTGAGTGCTCCGCGCGGCTGCTGCAGCAGGAAGAAGAGATTAAA
TCTCTGACTGCTGAAATTGACCGGTTGAAAAACTGTGGCTGTTTAGGAGCTTCTCCAAAT
TTGGAGCAGTTACAAGAAGAAAATTTAAAATTAAAGTATCGACTGAATATTCTTCGAAAG
AGTCTTCAGGCAGAAAGGAACAAACCAACTAAAAATATGATTAACATTATTAGCCGCCTA
CAAGAGGTCTTTGGTCATGCAATTAAGGCTGCATATCCAGATTTGGAAAATCCTCCTCTG
CTAGTGACACCAAGTCAGCAGGCCAAGTTTGGGGACTATCAGTGTAATAGTGCTATGGGT
ATTTCTCAGATGCTCAAAACCAAGGAACAGAAAGTTAATCCAAGAGAAATTGCTGAAAAC
ATTACCAAACACCTCCCAGACAATGAATGTATTGAAAAAGTTGAAATTGCTGGTCCTGGT
TTTATTAATGTCCACTTAAGAAAGGATTTTGTATCAGAACAATTGACCAGTCTTCTAGTG
AATGGAGTTCAACTACCTGCTCTGGGAGAGAATAAAAAGGTTATAGTTGACTTTTCCTCC
CCTAATATAGCTAAAGAGATGCATGTAGGCCACCTGAGGTCAACTATCATAGGAGAGAGT
ATAAGCCGCCTCTTTGAATTTGCAGGGTATGACGTGCTCAGGTTAAATCATGTAGGAGAC
TGGGGGACCCAGTTTGGCATGCTCATCGCTCACCTGCAAGACAAATTTCCAGATTATCTA
ACAGTTTCACCTCCTATTGGGGATCTTCAGGTCTTTTATAAGGAATCTAAGAAGAGGTTT
GATACTGAGGAGGAATTTAAGAAGCGAGCATATCAGTGTGTAGTTCTGCTCCAGGGTAAA
AACCCAGATATTACAAAAGCTTGGAAGCTTATCTGTGATGTCTCCCGCCAAGAGTTAAAT
AAAATCTATGATGCATTGGACGTCTCTTTAATAGAGAGAGGGGAATCCTTCTATCAAGAT
GGGATGAATGATATTGTAAAGGAATTTGAAGATAGAGGATTTGTGCAGGTGGATGATGGC
AGAAAGATTGTATTTGTCCCAGGGTGTTCCATACCATTAACCATAGTAAAATCAGATGGA
GGTTATACCTATGATACATCTGACCTGGCTGCTATTAAACAAAGACTATTTGAGGAAAAA
GCAGATATGATTATCTATGTTGTGGACAATGGACAATCTGTGCACTTCCAGACAATATTT
GCTGCTGCTCAAATGATTGGTTGGTATGACCCTAAAGTAACTCGAGTCTTCCATGCTGGA
TTTGGTGTGGTGCTAGGGGAAGACAAGAAAAAGTTTAAAACACGTTCGGGTGAAACAGTG
CGCCTCATGGATCTTCTGGGAGAAGGACTAAAACGATCCATGGACAAGTTGAAGGAAAAA
GAAAGAGACAAGGTCTTAGCTGCAGAGGAATTGAATGCTGCTCAGACATCCGTTGCGTAT
GGCTGCATCAAATATGCTGACCTTTCCCATAACCGGTTGAATGACTACATCTTCTCCTTT
GACAAAATGCTAGATGACAGAGGAAATACAGCTGCTTACTTGTTGTATGCCTTCACTAGA
ATCAGGTCTATTGCACGTCTGGCCAATATTGATGAAGAAATGCTCCAAAAAGCTGCTCGA
GAAACCAAGATTCTTTTGGATCATGAGAAGGAATGGAAACTAGGCCGGTGCATTTTACGG
TTCCCTGAGATTCTGCAAAAGATTTTAGATGACTTATTTCTCCACACTCTCTGTGATTAT
ATATATGAGCTGGCAACTGCTTTCACAGAGTTCTATGATAGCTGCTACTGTGTGGAGAAA
GATAGACAGACTGGAAAAATATTGAAGGTGAACATGTGGCGTATGCTGCTATGTGAAGCA
GTAGCTGCTGTCATGGCCAAGGGGTTTGATATCCTGGGAATAAAACCTGTCCAAAGGATG
TAA
|
| Enzyme 65 GenBank Gene ID |
AK222797 |
| Enzyme 65 GeneCard ID |
RARS |
| Enzyme 65 GenAtlas ID |
RARS |
| Enzyme 65 HGNC ID |
HGNC:9870 |
| Enzyme 65 Chromosome Location |
5 |
| Enzyme 65 Locus |
5q35.1 |
| Enzyme 65 SNPs |
SNPJam Report |
| Enzyme 65 General References |
- Girjes AA, Hobson K, Chen P, Lavin MF: Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase. Gene. 1995 Oct 27;164(2):347-50. [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 ]
- 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 ]
- Park SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K: Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. J Biol Chem. 1999 Jun 11;274(24):16673-6. [PubMed ]
- Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED: The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. J Biol Chem. 2005 Oct 14;280(41):34755-63. Epub 2005 Jul 29. [PubMed ]
- Zheng YG, Wei H, Ling C, Xu MG, Wang ED: Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA. Biochemistry. 2006 Jan 31;45(4):1338-44. [PubMed ]
- Bottoni A, Vignali C, Piccin D, Tagliati F, Luchin A, Zatelli MC, Uberti EC: Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. J Cell Physiol. 2007 Aug;212(2):293-7. [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 ]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
5865 |
| Enzyme 66 Name |
Ubiquitin-conjugating enzyme E2 E3 |
| Enzyme 66 Synonyms |
- UbcH9
- Ubiquitin carrier protein E3
- Ubiquitin-conjugating enzyme E2-23 kDa
- Ubiquitin-protein ligase E3
|
| Enzyme 66 Gene Name |
UBE2E3 |
| Enzyme 66 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 E3
MSSDRQRSDDESPSTSSGSSDADQRDPAAPEPEEQEERKPSATQQKKNTKLSSKTTAKLS
TSAKRIQKELAEITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFSSDY
PFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLV
GSIATQYLTNRAEHDRIARQWTKRYAT
|
| Enzyme 66 Number of Residues |
207 |
| Enzyme 66 Molecular Weight |
22912.3 |
| Enzyme 66 Theoretical pI |
7.25 |
| Enzyme 66 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 66 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 66 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest |
| Enzyme 66 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 66 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 66 Pfam Domain Function |
|
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
Not Available |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q969T4 |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
UB2E3_HUMAN |
| Enzyme 66 PDB ID |
1Y6L |
| Enzyme 66 PDB File |
Show |
| Enzyme 66 3D Structure |
|
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>624 bp
ATGTCCAGTGATAGGCAAAGGTCCGATGATGAGAGCCCCAGCACCAGCAGTGGCAGTTCA
GATGCGGACCAGCGAGACCCAGCCGCTCCAGAGCCTGAAGAACAAGAGGAAAGAAAACCT
TCTGCCACCCAGCAGAAGAAAAACACCAAACTCTCTAGCAAAACCACTGCTAAGTTATCC
ACTAGTGCTAAAAGAATTCAGAAGGAGCTAGCTGAAATAACCCTTGATCCTCCTCCTAAT
TGCAGTGCTGGGCCTAAAGGAGATAACATTTATGAATGGAGATCAACTATACTTGGTCCA
CCGGGTTCTGTATATGAAGGTGGTGTGTTTTTTCTGGATATCACATTTTCATCAGATTAT
CCATTTAAGCCACCAAAGGTTACTTTCCGCACCAGAATCTATCACTGCAACATCAACAGT
CAGGGAGTCATCTGTCTGGACATCCTTAAAGACAACTGGAGTCCCGCTTTGACTATTTCA
AAGGTTTTGCTGTCTATTTGTTCCCTTTTGACAGACTGCAACCCTGCGGATCCTCTGGTT
GGAAGCATAGCCACTCAGTATTTGACCAACAGAGCAGAACACGACAGGATAGCCAGACAG
TGGACCAAGAGATACGCAACATAA
|
| Enzyme 66 GenBank Gene ID |
AB017644 |
| Enzyme 66 GeneCard ID |
UBE2E3 |
| Enzyme 66 GenAtlas ID |
UBE2E3 |
| Enzyme 66 HGNC ID |
HGNC:12479 |
| Enzyme 66 Chromosome Location |
2 |
| Enzyme 66 Locus |
2q32.1 |
| Enzyme 66 SNPs |
SNPJam Report |
| Enzyme 66 General References |
- Ito K, Kato S, Matsuda Y, Kimura M, Okano Y: cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme. Cytogenet Cell Genet. 1999;84(1-2):99-104. [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 ]
- Plafker SM, Plafker KS, Weissman AM, Macara IG: Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import. J Cell Biol. 2004 Nov 22;167(4):649-59. Epub 2004 Nov 15. [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 ]
- 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 ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
5867 |
| Enzyme 67 Name |
Ubiquitin-conjugating enzyme E2 B |
| Enzyme 67 Synonyms |
- RAD6 homolog B
- HR6B
- hHR6B
- Ubiquitin carrier protein B
- Ubiquitin-conjugating enzyme E2-17 kDa
- Ubiquitin-protein ligase B
|
| Enzyme 67 Gene Name |
UBE2B |
| Enzyme 67 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 B
MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFS
EEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWNDS
|
| Enzyme 67 Number of Residues |
152 |
| Enzyme 67 Molecular Weight |
17312.2 |
| Enzyme 67 Theoretical pI |
4.64 |
| Enzyme 67 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 67 General Function |
Involved in ATP binding |
| Enzyme 67 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth |
| Enzyme 67 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 67 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| 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 |
P63146 |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
UBE2B_HUMAN |
| Enzyme 67 PDB ID |
1JAS |
| Enzyme 67 PDB File |
Show |
| Enzyme 67 3D Structure |
|
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>459 bp
ATGTCGACCCCGGCCCGGAGGAGGCTCATGCGGGATTTCAAGCGGTTACAAGAGGACCCA
CCTGTGGGTGTCAGTGGCGCACCATCTGAAAACAACATCATGCAGTGGAATGCAGTTATA
TTTGGACCAGAAGGGACACCTTTTGAAGATGGTACTTTTAAACTAGTAATAGAATTTTCT
GAAGAATATCCAAATAAACCACCAACTGTTAGGTTTTTATCCAAAATGTTTCATCCAAAT
GTGTATGCTGATGGTAGCATATGTTTAGATATCCTTCAGAATCGATGGAGTCCAACATAT
GATGTATCTTCTATCTTAACATCAATTCAGTCTCTGCTGGATGAACCGAATCCTAACAGT
CCAGCCAATAGCCAGGCAGCACAGCTTTATCAGGAAAACAAACGAGAATATGAGAAAAGA
GTTTCGGCCATTGTTGAACAAAGCTGGAATGATTCATAA
|
| Enzyme 67 GenBank Gene ID |
M74525 |
| Enzyme 67 GeneCard ID |
UBE2B |
| Enzyme 67 GenAtlas ID |
UBE2B |
| Enzyme 67 HGNC ID |
HGNC:12473 |
| Enzyme 67 Chromosome Location |
5 |
| Enzyme 67 Locus |
5q31.1 |
| Enzyme 67 SNPs |
SNPJam Report |
| Enzyme 67 General References |
- Schneider R, Eckerskorn C, Lottspeich F, Schweiger M: The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6. EMBO J. 1990 May;9(5):1431-5. [PubMed ]
- Woffendin C, Chen ZY, Staskus K, Retzel EF, Plagemann PG: Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6. Biochim Biophys Acta. 1991 Aug 27;1090(1):81-5. [PubMed ]
- Koken MH, Reynolds P, Jaspers-Dekker I, Prakash L, Prakash S, Bootsma D, Hoeijmakers JH: Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8865-9. [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 ]
- 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 ]
- Xin H, Lin W, Sumanasekera W, Zhang Y, Wu X, Wang Z: The human RAD18 gene product interacts with HHR6A and HHR6B. Nucleic Acids Res. 2000 Jul 15;28(14):2847-54. [PubMed ]
- Motegi A, Sood R, Moinova H, Markowitz SD, Liu PP, Myung K: Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination. J Cell Biol. 2006 Dec 4;175(5):703-8. Epub 2006 Nov 27. [PubMed ]
- Unk I, Hajdu I, Fatyol K, Szakal B, Blastyak A, Bermudez V, Hurwitz J, Prakash L, Prakash S, Haracska L: Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18107-12. Epub 2006 Nov 15. [PubMed ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
- Miura T, Klaus W, Ross A, Guntert P, Senn H: The NMR structure of the class I human ubiquitin-conjugating enzyme 2b. J Biomol NMR. 2002 Jan;22(1):89-92. [PubMed ]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
5868 |
| Enzyme 68 Name |
Probable leucyl-tRNA synthetase, mitochondrial |
| Enzyme 68 Synonyms |
- Leucine--tRNA ligase
- LeuRS
|
| Enzyme 68 Gene Name |
LARS2 |
| Enzyme 68 Protein Sequence |
>Probable leucyl-tRNA synthetase, mitochondrial
MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVE
KWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGM
QVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPD
YYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQ
WFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYT
ATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVI
LAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQ
DAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVT
LPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPH
SPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIK
GQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGID
TIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNK
EKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDA
LCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQ
MAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFL
VQD
|
| Enzyme 68 Number of Residues |
903 |
| Enzyme 68 Molecular Weight |
101975.4 |
| Enzyme 68 Theoretical pI |
8.32 |
| Enzyme 68 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- leucine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- leucyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 68 General Function |
Involved in nucleotide binding |
| Enzyme 68 Specific Function |
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) |
| Enzyme 68 Pathways |
|
| Enzyme 68 Reactions |
- ATP + L-leucine + tRNALeu = AMP + diphosphate + L-leucyl-tRNALeu [RN:R03657]
|
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
19683964 |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
Q15031 |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
SYLM_HUMAN |
| Enzyme 68 PDB ID |
Not Available |
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>2712 bp
ATGGCTTCTGTTTGGCAGAGATTGGGTTTTTATGCCTCTCTTCTGAAAAGACAGCTAAAT
GGTGGGCCAGATGTCATCAAGTGGGAAAGGAGAGTAATTCCCGGATGTACCAGAAGCATC
TACAGTGCCACGGGAAAGTGGACAAAAGAGTATACATTGCAGACAAGAAAGGATGTTGAG
AAATGGTGGCATCAACGAATAAAAGAACAGGCCTCCAAAATTTCAGAAGCTGATAAATCG
AAGCCAAAATTTTACGTGCTTTCCATGTTCCCTTATCCTTCTGGTAAGCTGCACATGGGC
CATGTGCGTGTCTACACCATCAGCGACACCATAGCACGGTTCCAGAAGATGAGAGGGATG
CAGGTCATCAACCCCATGGGATGGGATGCTTTTGGATTGCCTGCTGAAAATGCCGCAGTC
GAGAGGAATCTACATCCACAAAGTTGGACACAAAGTAATATTAAACACATGAGGAAACAG
CTTGATCGTCTGGGCCTGTGTTTCAGCTGGGATAGGGAAATAACTACGTGTTTGCCAGAT
TACTACAAGTGGACTCAGTATCTCTTTATTAAACTGTATGAGGCTGGGCTGGCCTATCAA
AAGGAGGCCCTGGTTAACTGGGACCCAGTGGATCAAACAGTGCTTGCCAATGAGCAGGTG
GATGAACATGGCTGTTCATGGCGTTCTGGAGCAAAGGTGGAACAGAAGTACCTCAGACAA
TGGTTTATTAAGACAACCGCTTATGCAAAGGCCATGCAGGACGCGTTGGCAGACCTTCCA
GAATGGTATGGAATAAAAGGCATGCAAGCCCACTGGATTGGGGACTGTGTGGGCTGCCAC
CTGGACTTCACATTAAAGGTTCATGGGCAAGCCACGGGCGAAAAGCTGACTGCCTATACG
GCCACCCCTGAAGCCATTTATGGCACCTCCCACGTGGCCATCTCGCCCAGCCACAGACTC
CTACATGGGCACAGCTCTCTGAAGGAAGCCTTGAGGATGGCCCTTGTCCCTGGCAAAGAT
TGCCTCACGCCTGTAATGGCTGTGAACATGCTCACCCAGCAGGAGGTCCCTGTCGTTATT
TTGGCCAAAGCTGACTTGGAAGGCTCTCTGGATTCAAAAATAGGAATTCCCAGTACTAGC
TCAGAGGACACCATCTTAGCCCAAACCCTGGGCCTGGCCTACTCTGAAGTCATTGAAACT
TTGCCAGATGGCACAGAGAGACTGAGCAGCTCTGCTGAGTTCACAGGTATGACCCGGCAG
GATGCTTTTCTAGCCCTGACTCAGAAAGCCCGGGGGAAGAGAGTGGGTGGAGACGTGACA
AGTGATAAACTGAAAGACTGGCTGATTTCACGGCAGCGGTACTGGGGCACACCAATCCCC
ATTGTCCACTGCCCAGTCTGTGGCCCCACACCTGTGCCCCTGGAGGACTTGCCTGTGACC
CTGCCCAACATCGCATCTTTCACTGGCAAGGGAGGCCCCCCACTGGCCATGGCTTCAGAG
TGGGTGAACTGCTCCTGCCCAAGGTGCAAGGGAGCAGCCAAGAGAGAGACAGACACGATG
GATACCTTTGTTGATTCTGCTTGGTACTACTTCAGATACACTGACCCTCATAATCCACAC
AGCCCTTTTAACACAGCAGTGGCCGATTACTGGATGCCTGTGGATTTGTACATTGGAGGG
AAAGAACATGCCGTCATGCACTTGTTCTATGCAAGATTCTTTAGTCATTTTTGCCATGAT
CAAAAAATGGTTAAACATAGGGAGCCTTTTCATAAGCTGCTGGCCCAAGGCCTTATCAAG
GGGCAGACATTCCGCCTACCATCTGGACAGTATCTACAGAGAGAGGAAGTGGATCTCACA
GGTTCCGTTCCTGTTCATGCAAAAACGAAAGAGAAGTTAGAGGTGACGTGGGAGAAGATG
AGTAAGTCCAAACACAACGGGGTGGACCCAGAGGAAGTTGTGGAGCAGTATGGGATCGAC
ACGATTCGGCTCTACATCCTTTTTGCTGCCCCTCCTGAGAAGGATATCTTGTGGGATGTG
AAAACTGATGCTCTCCCTGGGGTGCTGAGATGGCAACAACGACTGTGGACCTTGACAACT
CGGTTTATTGAGGCCAGGGCTTCTGGGAAGTCTCCCCAGCCTCAGCTGCTGAGTAACAAG
GAGAAAGCCGAGGCCAGGAAGCTCTGGGAGTACAAGAACTCCGTCATCTCTCAGGTGACC
ACCCATTTCACAGAGGACTTCTCACTGAATTCTGCAATTTCTCAGCTGATGGGACTCAGC
AATGCCCTCTCGCAAGCCTCTCAGAGCGTCATTCTCCACAGCCCCGAGTTTGAGGATGCT
TTGTGTGCCCTGATGGTGATGGCTGCTCCACTGGCCCCTCATGTAACCTCAGAGATCTGG
GCAGGCCTGGCGCTGGTGCCGAGGAAGCTCTGTGCCCACTACACTTGGGATGCCAGTGTG
CTGCTCCAGGCATGGCCTGCTGTGGACCCGGAGTTCCTGCAGCAGCCTGAGGTTGTCCAG
ATGGCAGTTCTGATCAACAATAAAGCTTGTGGCAAAATTCCTGTGCCCCAACAAGTTGCC
CGGGACCAGGACAAAGTCCACGAATTTGTTCTTCAAAGCGAGCTGGGTGTCAGGCTTTTG
CAAGGACGAAGCATCAAGAAGTCCTTCCTTTCCCCGAGAACTGCCCTCATCAACTTCCTG
GTGCAAGATTGA
|
| Enzyme 68 GenBank Gene ID |
BC025989 |
| Enzyme 68 GeneCard ID |
LARS2 |
| Enzyme 68 GenAtlas ID |
LARS2 |
| Enzyme 68 HGNC ID |
HGNC:17095 |
| Enzyme 68 Chromosome Location |
3 |
| Enzyme 68 Locus |
3p21.3 |
| Enzyme 68 SNPs |
SNPJam Report |
| Enzyme 68 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [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 ]
- 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 |
5870 |
| Enzyme 69 Name |
Ubiquitin-conjugating enzyme E2 J2 |
| Enzyme 69 Synonyms |
- Non-canonical ubiquitin-conjugating enzyme 2
- NCUBE-2
|
| Enzyme 69 Gene Name |
UBE2J2 |
| Enzyme 69 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 J2
MSSTSSKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGY
YHGKLIFPREFPFKPPSIYMITPNGRFKCNTRLCLSITDFHPDTWNPAWSVSTILTGLLS
FMVEKGPTLGSIETSDFTKRQLAVQSLAFNLKDKVFCELFPEVVEEIKQKQKAQDELSSR
PQTLPLPDVVPDGETHLVQNGIQLLNGHAPGAVPNLAGLQQANRHHGLLGGALANLFVIV
GFAAFAYTVKYVLRSIAQE
|
| Enzyme 69 Number of Residues |
259 |
| Enzyme 69 Molecular Weight |
28898.1 |
| Enzyme 69 Theoretical pI |
8.59 |
| Enzyme 69 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 69 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 69 Specific Function |
Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) |
| Enzyme 69 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 69 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
37577124 |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
Q8N2K1 |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
UB2J2_HUMAN |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>780 bp
ATGAGCAGCACCAGCAGTAAGAGGGCTCCGACCACGGCAACCCAGAGGCTGAAGCAGGAC
TACCTTCGCATTAAGAAAGACCCGGTGCCTTACATCTGTGCCGAGCCCCTCCCTTCGAAT
ATTCTCGAGTGGCACTATGTCGTCCGAGGCCCAGAGATGACCCCTTATGAAGGTGGCTAT
TATCATGGAAAACTAATTTTTCCCAGAGAATTTCCTTTCAAACCTCCCAGTATCTATATG
ATCACTCCCAACGGGAGGTTTAAGTGCAACACCAGGCTGTGTCTTTCTATCACGGATTTC
CACCCGGACACGTGGAACCCGGCCTGGTCTGTCTCCACCATCCTGACTGGGCTCCTGAGC
TTCATGGTGGAGAAGGGCCCCACCCTGGGCAGTATAGAGACGTCGGACTTCACGAAAAGA
CAACTGGCAGTGCAGAGTTTAGCATTTAATTTGAAAGATAAAGTCTTTTGTGAATTATTT
CCTGAAGTCGTGGAGGAGATTAAACAAAAACAGAAAGCACAAGACGAACTCAGTAGCAGA
CCCCAGACTCTCCCCTTGCCAGACGTGGTTCCAGACGGGGAGACGCACCTCGTCCAGAAC
GGGATTCAGCTGCTCAACGGGCATGCGCCGGGGGCCGTCCCAAACCTCGCAGGGCTCCAG
CAGGCCAACCGGCACCACGGACTCCTGGGTGGCGCCCTGGCGAACTTGTTTGTGATAGTT
GGGTTTGCAGCCTTTGCTTACACGGTCAAGTACGTGCTGAGGAGCATCGCGCAGGAGTGA
|
| Enzyme 69 GenBank Gene ID |
NM_058167.2 |
| Enzyme 69 GeneCard ID |
UBE2J2 |
| Enzyme 69 GenAtlas ID |
UBE2J2 |
| Enzyme 69 HGNC ID |
HGNC:19268 |
| Enzyme 69 Chromosome Location |
1 |
| Enzyme 69 Locus |
1p36.33 |
| Enzyme 69 SNPs |
SNPJam Report |
| Enzyme 69 General References |
- Tiwari S, Weissman AM: Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J Biol Chem. 2001 May 11;276(19):16193-200. Epub 2001 Feb 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 ]
- 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 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
5873 |
| Enzyme 70 Name |
Ubiquitin-conjugating enzyme E2 L3 |
| Enzyme 70 Synonyms |
- L-UBC
- UbcH7
- Ubiquitin carrier protein L3
- Ubiquitin-conjugating enzyme E2-F1
- Ubiquitin-protein ligase L3
|
| Enzyme 70 Gene Name |
UBE2L3 |
| Enzyme 70 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 L3
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAE
YPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHP
LRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD
|
| Enzyme 70 Number of Residues |
154 |
| Enzyme 70 Molecular Weight |
17861.4 |
| Enzyme 70 Theoretical pI |
8.79 |
| Enzyme 70 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 70 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 70 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis |
| Enzyme 70 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 70 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
Not Available |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
P68036 |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
UB2L3_HUMAN |
| Enzyme 70 PDB ID |
1FBV |
| Enzyme 70 PDB File |
Show |
| Enzyme 70 3D Structure |
|
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
>465 bp
ATGGCGGCCAGCAGGAGGCTGATGAAGGAGCTTGAAGAAATCCGCAAATGTGGGATGAAA
AACTTCCGTAACATCCAGGTTGATGAAGCTAATTTATTGACTTGGCAAGGGCTTATTGTT
CCTGACAACCCTCCATATGATAAGGGAGCCTTCAGAATCGAAATCAACTTTCCAGCAGAG
TACCCATTCAAACCACCGAAGATCACATTTAAAACAAAGATCTATCACCCAAACATCGAC
GAAAAGGGGCAGGTCTGTCTGCCAGTAATTAGTGCCGAAAACTGGAAGCCAGCAACCAAA
ACCGACCAAGTAATCCAGTCCCTCATAGCACTGGTGAATGACCCCCAGCCTGAGCACCCG
CTTCGGGCTGACCTAGCTGAAGAATACTCTAAGGACCGTAAAAAATTCTGTAAGAATGCT
GAAGAGTTTACAAAGAAATATGGGGAAAAGCGACCTGTGGACTAA
|
| Enzyme 70 GenBank Gene ID |
S81003 |
| Enzyme 70 GeneCard ID |
UBE2L3 |
| Enzyme 70 GenAtlas ID |
UBE2L3 |
| Enzyme 70 HGNC ID |
HGNC:12488 |
| Enzyme 70 Chromosome Location |
2 |
| Enzyme 70 Locus |
22q11.21 |
| Enzyme 70 SNPs |
SNPJam Report |
| Enzyme 70 General References |
- Robinson PA, Leek JP, Thompson J, Carr IM, Bailey A, Moynihan TP, Coletta PL, Lench NJ, Markham AF: A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3. Mamm Genome. 1995 Oct;6(10):725-31. [PubMed ]
- Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M: Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J Biol Chem. 1996 Feb 2;271(5):2795-800. [PubMed ]
- Moynihan TP, Cole CG, Dunham I, O'Neil L, Markham AF, Robinson PA: Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3. Genomics. 1998 Jul 1;51(1):124-7. [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 ]
- 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 ]
- Blumenfeld N, Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A: Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates. J Biol Chem. 1994 Apr 1;269(13):9574-81. [PubMed ]
- Ardley HC, Moynihan TP, Markham AF, Robinson PA: Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7. Biochim Biophys Acta. 2000 Apr 25;1491(1-3):57-64. [PubMed ]
- Shimura H, Hattori N, Kubo S, Mizuno Y, Asakawa S, Minoshima S, Shimizu N, Iwai K, Chiba T, Tanaka K, Suzuki T: Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet. 2000 Jul;25(3):302-5. [PubMed ]
- Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G: A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem Biophys Res Commun. 2001 Mar 2;281(3):706-13. [PubMed ]
- Ardley HC, Tan NG, Rose SA, Markham AF, Robinson PA: Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. J Biol Chem. 2001 Jun 1;276(22):19640-7. Epub 2001 Mar 13. [PubMed ]
- Toby GG, Gherraby W, Coleman TR, Golemis EA: A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels. Mol Cell Biol. 2003 Mar;23(6):2109-22. [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 ]
- Huang J, Xu LG, Liu T, Zhai Z, Shu HB: The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis. FEBS Lett. 2006 Feb 6;580(3):940-7. Epub 2006 Jan 18. [PubMed ]
- Garside H, Waters C, Berry A, Rice L, Ardley HC, White A, Robinson PA, Ray D: UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation. J Endocrinol. 2006 Sep;190(3):621-9. [PubMed ]
- Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed ]
- Marteijn JA, van der Meer LT, Smit JJ, Noordermeer SM, Wissink W, Jansen P, Swarts HG, Hibbert RG, de Witte T, Sixma TK, Jansen JH, van der Reijden BA: The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains. Leukemia. 2009 Aug;23(8):1480-9. Epub 2009 Apr 2. [PubMed ]
- Whitcomb EA, Dudek EJ, Liu Q, Taylor A: Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7. Mol Biol Cell. 2009 Jan;20(1):1-9. Epub 2008 Oct 22. [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 ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
- Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP: Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science. 1999 Nov 12;286(5443):1321-6. [PubMed ]
- Zheng N, Wang P, Jeffrey PD, Pavletich NP: Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell. 2000 Aug 18;102(4):533-9. [PubMed ]
|
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
5874 |
| Enzyme 71 Name |
RNA 3'-terminal phosphate cyclase |
| Enzyme 71 Synonyms |
- RNA cyclase
- RNA-3'-phosphate cyclase
- RNA terminal phosphate cyclase domain-containing protein 1
- RTC domain-containing protein 1
|
| Enzyme 71 Gene Name |
RTCD1 |
| Enzyme 71 Protein Sequence |
>RNA 3'-terminal phosphate cyclase
MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIR
DLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELH
LKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNP
INLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAF
GNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLI
VFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDAAKDTYIIECQGIG
MTNPNL
|
| Enzyme 71 Number of Residues |
366 |
| Enzyme 71 Molecular Weight |
39336.4 |
| Enzyme 71 Theoretical pI |
7.94 |
| Enzyme 71 GO Classification |
| Function |
- RNA-3'-phosphate cyclase activity
- catalytic activity
- cyclase activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
|
| Process |
- RNA metabolic process
- RNA processing
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 71 General Function |
Involved in ligase activity, forming phosphoric ester bonds |
| Enzyme 71 Specific Function |
Catalyzes the conversion of 3'-phosphate to a 2',3'- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps:(A) adenylation of the enzyme by ATP; (B) the enzyme acts on RNA-N3'P to produce RNA-N3'PP5'A; (C) a non catalytic nucleophilic attack by the adjacent 2'hydroxyl on the phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing |
| Enzyme 71 Pathways |
Not Available |
| Enzyme 71 Reactions |
- ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate [RN:R04274]
|
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
55665043 |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
O00442 |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
RTC1_HUMAN |
| Enzyme 71 PDB ID |
Not Available |
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>1101 bp
ATGGCGGGGCCGCGGGTGGAGGTCGATGGCAGCATCATGGAAGGGGGCGGCCAGATCCTG
AGAGTCTCTACGGCCTTGAGCTGTCTCCTAGGCCTCCCCTTGCGGGTGCAGAAGATCCGA
GCCGGCCGGAGCACGCCAGGCCTGAGGCCTCAACATTTATCTGGACTGGAAATGATTCGA
GATTTGTGTGATGGGCAACTGGAGGGGGCAGAAATTGGCTCAACAGAAATAACCTTTACA
CCAGAGAAGATCAAAGGTGGAATCCACACAGCAGATACCAAGACAGCAGGGAGTGTGTGC
CTCTTGATGCAGGTCTCAATGCCGTGTGTTCTCTTTGCTGCTTCTCCATCAGAACTTCAT
TTGAAAGGTGGAACTAATGCTGAAATGGCACCACAGATCGATTATACAGTGATGGTCTTC
AAGCCAATTGTTGAAAAATTTGGTTTCATATTTAATTGTGACATTAAAACAAGGGGATAT
TACCCAAAAGGGGGTGGTGAAGTGATTGTTCGAATGTCACCAGTTAAACAATTGAACCCT
ATAAATTTAACTGAGCGTGGCTGTGTGACTAAGATATATGGAAGAGCTTTCGTTGCTGGT
GTTTTGCCATTTAAAGTAGCAAAAGATATGGCAGCGGCAGCAGTTAGATGCATCAGAAAG
GAGATCCGGGATTTGTATGTTAACATCCAGCCTGTTCAAGAACCTAAAGACCAAGCATTT
GGCAATGGAAATGGAATAATAATTATTGCTGAGACCTCCACTGGCTGTTTGTTTGCTGGA
TCATCGCTTGGTAAACGAGGTGTAAATGCAGACAAAGTTGGAATTGAAGCTGCCGAAATG
CTATTAGCAAATCTTAGACATGGTGGTACTGTGGATGAGTATCTGCAAGACCAGCTGATT
GTTTTCATGGCATTAGCCAATGGAGTTTCCAGAATAAAAACAGGACCAGTTACACTCCAT
ACGCAAACCGCGATACATTTTGCTGAACAAATAGCAAAGGCTAAATTTATTGTGAAGAAA
TCAGAAGATGAAGAAGACGCCGCTAAAGATACTTATATTATTGAATGCCAAGGAATTGGG
ATGACAAATCCAAATCTATAG
|
| Enzyme 71 GenBank Gene ID |
AL445928 |
| Enzyme 71 GeneCard ID |
RTCD1 |
| Enzyme 71 GenAtlas ID |
RTCD1 |
| Enzyme 71 HGNC ID |
HGNC:17981 |
| Enzyme 71 Chromosome Location |
1 |
| Enzyme 71 Locus |
1p21.2 |
| Enzyme 71 SNPs |
SNPJam Report |
| Enzyme 71 General References |
- Genschik P, Billy E, Swianiewicz M, Filipowicz W: The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. EMBO J. 1997 May 15;16(10):2955-67. [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 ]
- Filipowicz W, Vicente O: RNA 3'-terminal phosphate cyclase from HeLa cells. Methods Enzymol. 1990;181:499-510. [PubMed ]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
5875 |
| Enzyme 72 Name |
Putative adenylate kinase 7 |
| Enzyme 72 Synonyms |
Not Available |
| Enzyme 72 Gene Name |
AK7 |
| Enzyme 72 Protein Sequence |
>Putative adenylate kinase 7
MAEEEETAALTEKVIRTQRVFINLLDSYSSGNIGKFLSNCVVGASLEEITEEEEEEDENK
SAMLEASSTKVKEGTFQIVGTLSKPDSPRPDFAVETYSAISREDLLMRLLECDVIIYNIT
ESSQQMEEAIWAVSALSEEVSHFEKRKLFILLSTVMTWARSKALDPEDSEVPFTEEDYRR
RKSHPNFLDHINAEKMVLKFGKKARKFAAYVVAAGLQYGAEGGMLHTFFKMAWLGEIPAL
PVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPHYLVAVDESVHTLEDIVKCISKNTGPGK
IQKIPRENAYLTKDLTQDCLDHLLVNLRMEALFVKENFNIRWAAQTGFVENINTILKEYK
QSRGLMPIKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIVAPNDVGE
GEEEVEEEEEEENVEDAQELLDGIKESMEQNAGQLDDQYIIRFMKEKLKSMPCRNQGYIL
DGFPKTYDQAKDLFNQEDEEEEDDVRGRMFPFDKLIIPEFVCALDASDEFLKERVINLPE
SIVAGTHYSQDRFLRALSNYRDINIDDETVFNYFDELEIHPIHIDVGKLEDAQNRLAIKQ
LIKEIGEPRNYGLTDEEKAEEERKAAEERLAREAAEEAEREHQEAVEMAEKIARWEEWNK
RLEEVKREERELLEAQSIPLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP
EAQ
|
| Enzyme 72 Number of Residues |
723 |
| Enzyme 72 Molecular Weight |
82657.7 |
| Enzyme 72 Theoretical pI |
4.38 |
| Enzyme 72 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
|
| Component |
| — |
|
| Enzyme 72 General Function |
Involved in ATP binding |
| Enzyme 72 Specific Function |
Play a role in maintaining ciliary structure and function |
| Enzyme 72 Pathways |
|
| Enzyme 72 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 72 Pfam Domain Function |
|
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
16553126 |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
Q96M32 |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
KAD7_HUMAN |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
>2172 bp
ATGGCTGAAGAAGAGGAAACTGCTGCTCTCACGGAGAAGGTTATCCGGACCCAGAGGGTG
TTTATAAACCTGTTGGATTCCTACAGCAGCGGAAACATCGGGAAGTTTCTATCTAACTGT
GTAGTTGGGGCTTCGCTTGAAGAAATTACAGAGGAAGAGGAAGAGGAAGATGAAAATAAG
TCAGCTATGCTGGAAGCTTCCTCAACCAAAGTGAAGGAAGGCACATTCCAGATTGTGGGC
ACGCTGTCCAAGCCTGACAGCCCGCGGCCTGACTTTGCGGTGGAGACGTACTCTGCCATC
TCTCAAGAAGACCTTCTCATGCGCCTGCTGGAGTGTGATGTTATTATTTATAACATCACT
GAGAGCTCACAGCAAATGGAGGAAGCCATCTGGGCAGTCTCTGCACTCAGTGAAGAAGTC
AGCCACTTTGAAAAGCGAAAGCTATTTATTTTACTGTCGACGGTGATGACTTGGGCGCGC
TCCAAAGCCCTGGACCCCGAGGATTCTGAGGTTCCATTCACTGAAGAAGATTATCGAAGA
AGAAAGTCTCATCCTAATTTTCTGGACCACATAAATGCTGAAAAAATGGTTCTCAAATTT
GGAAAAAAGGCCAGAAAATTTGCAGCATACGTAGTTGCTGCTGGACTCCAGTATGGAGCG
GAAGGAGGCATGTTACACACATTTTTTAAGATGGCTTGGTTGGGCGAGATTCCTGCATTA
CCAGTTTTTGGCGATGGAACAAATGTAATTCCAACAATCCATGTTCTTGATCTAGCAGGA
GTGATACAAAACGTCATAGATCACGTGCCAAAGCTTCACTACCTGGTTGCTGTGGATGAG
TCTGTTCATACCCTGGAAGACATAGTCAAGTGTATCAGTAAAAATACTGGCCCTGGGAAA
ATCCAGAAAATACCCAGAGAAAATGCATACCTAACCAAGGACTTAACGCAAGATTGTCTT
GACCATTTACTGGTCAACTTAAGAATGGAAGCGCTCTTTGTGAAGGAGAATTTTAATATT
CGATGGGCTGCCCAAACAGGATTTGTGGAAAATATCAACACTATCCTCAAGGAGTACAAG
CAAAGCAGAGGATTGATGCCAATCAAGATCTGCATTCTTGGTCCCCCTGCTGTGGGAAAA
TCCAGTATTGCTAAAGAATTGGCCAAGTACTACAAACTGCATCACATCCAACTGAAGGAT
GTCATTTCTGAAGCCATAGCAAAACTGGGGGCGATTGTTGCCCCTAACGATGTAGGGGAA
GGAGAAGAAGAAGTCGAAGAGGAAGAGGAGGAGGAGAATGTGGAAGATGCACAGGAGCTC
CTAGATGGCATCAAGGAGAGCATGGAGCAGAATGCAGGTCAACTAGACGATCAATATATA
ATTAGATTTATGAAAGAAAAGCTAAAATCAATGCCTTGCAGGAATCAAGGTTATATTTTG
GATGGATTCCCAAAGACCTATGATCAAGCAAAAGACCTGTTCAATCAGGAAGATGAGGAG
GAGGAAGATGATGTCAGAGGCAGAATGTTTCCCTTTGATAAATTAATTATACCTGAATTC
GTTTGTGCACTGGATGCTTCGGATGAGTTTCTGAAGGAGCGTGTGATAAACCTTCCTGAG
AGCATCGTGGCGGGGACCCACTACAGCCAAGACCGATTCCTCCGGGCTCTGAGCAACTAC
CGGGACATCAATATCGACGATGAGACTGTCTTCAACTATTTTGATGAACTTGAAATTCAC
CCGATACATATTGATGTAGGAAAACTTGAAGATGCTCAGAATAGACTTGCTATCAAACAG
CTCATCAAAGAGATTGGGGAGCCTCGAAATTATGGTTTAACAGACGAAGAAAAGGCAGAA
GAGGAGCGGAAGGCTGCGGAGGAGCGGCTGGCCAGGGAGGCTGCTGAGGAAGCAGAACGC
GAGCACCAGGAGGCCGTGGAGATGGCAGAGAAGATAGCTCGCTGGGAGGAGTGGAATAAA
CGACTGGAGGAAGTGAAAAGAGAAGAAAGAGAATTACTGGAGGCTCAGTCAATTCCCCTG
AGAAACTATTTAATGACCTATGTGATGCCAACTCTTATTCAGGGCCTGAATGAATGTTGC
AACGTCCGACCCGAAGACCCTGTTGATTTTCTGGCAGAATATCTCTTCAAGAACAATCCT
GAAGCACAGTGA
|
| Enzyme 72 GenBank Gene ID |
AK057426 |
| Enzyme 72 GeneCard ID |
AK7 |
| Enzyme 72 GenAtlas ID |
AK7 |
| Enzyme 72 HGNC ID |
HGNC:20091 |
| Enzyme 72 Chromosome Location |
1 |
| Enzyme 72 Locus |
14q32.2 |
| Enzyme 72 SNPs |
SNPJam Report |
| Enzyme 72 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 ]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
|
| Enzyme 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
5878 |
| Enzyme 73 Name |
Tyrosyl-tRNA synthetase, cytoplasmic |
| Enzyme 73 Synonyms |
- Tyrosyl--tRNA ligase
- TyrRS
|
| Enzyme 73 Gene Name |
YARS |
| Enzyme 73 Protein Sequence |
>Tyrosyl-tRNA synthetase, cytoplasmic
MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIA
DFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKG
TDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVD
AQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKED
VKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFA
AEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEP
EEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLV
VVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEE
LKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS
|
| Enzyme 73 Number of Residues |
528 |
| Enzyme 73 Molecular Weight |
59143.0 |
| Enzyme 73 Theoretical pI |
7.05 |
| Enzyme 73 GO Classification |
| Function |
- ATP binding
- RNA binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- tRNA binding
- tyrosine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
- tyrosyl-tRNA aminoacylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 73 General Function |
Involved in nucleotide binding |
| Enzyme 73 Specific Function |
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) |
| Enzyme 73 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Phenylalanine and Tyrosine Metabolism (map00400 )
|
| Enzyme 73 Reactions |
- ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr [RN:R02918]
|
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
193785013 |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
P54577 |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
SYYC_HUMAN |
| Enzyme 73 PDB ID |
1Q11 |
| Enzyme 73 PDB File |
Show |
| Enzyme 73 3D Structure |
|
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>1587 bp
ATGGGGGACGCTCCCAGCCCTGAAGAGAAACTGCACCTTATCACCCGGAACCTGCAGGAG
GTTCTGGGGGAAGAGAAGCTGAAGGAGATACTGAAGGAGCGGGAACTTAAAATTTACTGG
GGAACGGCAACCACGGGCAAACCACATGTGGCTTACTTTGTGCCCATGTCAAAGATTGCA
GACTTCTTAAAGGCAGGGTGTGAGGTAACAATTCTGTTTGCGGACCTCCACGCATACCTG
GATAACATGAAAGCCCCATGGGAACTTCTAGAACTCCGAGTCAGTTACTATGAGAATGTG
ATCAAAGCAATGCTGGAGAGCATTGGTGTGCCCTTGGAGAAGCTCAAGTTCATCAAAGGC
ACTGATTACCAGCTCAGCAAAGAGTACACACTAGATGTGTACAGACTCTCCTCCGTGGTC
ACACAGCACGATTCCAAGAAGGCTGGAGCTGAGGTGGTAAAGCAGGTGGAGCACCCTTTG
CTGAGTGGCCTCTTATACCCCGGACTGCAGGCTTTGGATGAAGAGTATTTAAAAGTAGAT
GCCCAATTTGGAGGCATTGATCAGAGAAAGATTTTCACCTTTGCAGAGAAGTACCTCCCT
GCACTTGGCTATTCAAAACGGGTCCATCTGATGAATCCTATGGTTCCAGGATTAACAGGC
AGCAAAATGAGCTCTTCAGAAGAGGAGTCCAAGATTGATCTCCTTGATCGGAAGGAGGAT
GTGAAGAAAAAACTGAAGAAGGCCTTCTGTGAGCCAGGAAATGTGGAGAACAATGGGGTT
CTGTCCTTCATCAAGCATGTCCTTTTTCCCCTTAAGTCCGAGTTTGTGATCCTACGAGAT
GAGAAATGGGGTGGAAACAAAACCTACACAGCTTACGTGGACCTGGAAAAGGACTTTGCT
GCTGAGGTTGTACATCCTGGAGACCTGAAGAATTCTGTTGAAGTCGCACTGAACAAGTTG
CTGGATCCAATCCGGGAAAAGTTTAATACCCCTGCCCTGAAAAAACTGGCCAGCGCTGCC
TACCCAGATCCCTCAAAGCAGAAGCCAATGGCCAAAGGCCCTGCCAAGAATTCAGAACCA
GAGGAGGTCATCCCATCCCGGCTGGATATCCGTGTGGGGAAAATCATTACTGTGGAGAAG
CACCCAGATGCAGACAGCCTGTATGTAGAGAAGATTGACGTGGGGGAAGCTGAACCACGG
ACTGTGGTGAGCGGCCTGGTACAGTTCGTGCCCAAGGAGGAACTGCAGGACAGGCTGGTA
GTGGTGCTGTGCAACCTGAAACCCCAGAAGATGAGAGGAGTCGAGTCCCAAGGCATGCTT
CTGTGTGCTTCTATAGAAGGGATAAACCGCCAGGTTGAACCTCTGGACCCTCCGGCAGGC
TCTGCTCCTGGTGAGCACGTGTTTGTGAAGGGCTATGAAAAGGGCCAACCAGATGAGGAG
CTCAAGCCCAAGAAGAAAGTCTTCGAGAAGTTGCAGGCTGACTTCAAAATTTCTGAGGAG
TGCATCGCACAGTGGAAGCAAACCAACTTCATGACCAAGCTGGGCTCCATTTCCTGTAAA
TCGCTGAAAGGGGGGAACATTAGCTAG
|
| Enzyme 73 GenBank Gene ID |
AK125213 |
| Enzyme 73 GeneCard ID |
YARS |
| Enzyme 73 GenAtlas ID |
YARS |
| Enzyme 73 HGNC ID |
HGNC:12840 |
| Enzyme 73 Chromosome Location |
1 |
| Enzyme 73 Locus |
1p35.1 |
| Enzyme 73 SNPs |
SNPJam Report |
| Enzyme 73 General References |
- Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P: Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):166-70. [PubMed ]
- Kleeman TA, Wei D, Simpson KL, First EA: Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J Biol Chem. 1997 May 30;272(22):14420-5. [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 ]
- 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 ]
- 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 ]
- Yang XL, Skene RJ, McRee DE, Schimmel P: Crystal structure of a human aminoacyl-tRNA synthetase cytokine. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. [PubMed ]
- Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L: Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15376-80. Epub 2003 Dec 11. [PubMed ]
- Jordanova A, Irobi J, Thomas FP, Van Dijck P, Meerschaert K, Dewil M, Dierick I, Jacobs A, De Vriendt E, Guergueltcheva V, Rao CV, Tournev I, Gondim FA, D'Hooghe M, Van Gerwen V, Callaerts P, Van Den Bosch L, Timmermans JP, Robberecht W, Gettemans J, Thevelein JM, De Jonghe P, Kremensky I, Timmerman V: Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy. Nat Genet. 2006 Feb;38(2):197-202. Epub 2006 Jan 22. [PubMed ]
|
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
5879 |
| Enzyme 74 Name |
DNA ligase 3 |
| Enzyme 74 Synonyms |
- DNA ligase III
- Polydeoxyribonucleotide synthase [ATP] 3
|
| Enzyme 74 Gene Name |
LIG3 |
| Enzyme 74 Protein Sequence |
>DNA ligase 3
MSLAFKIFFPQTLRALSRKELCLFRKHHWRDVRQFSQWSETDLLHGHPLFLRRKPVLSFQ
GSHLRSRATYLVFLPGLHVGLCSGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIG
KVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQITQH
IADLSSKAAGTPKKKAVVQAKLTTTGQVTSPVKGASFVTSTNPRKFSGFSAKPNNSGEAP
SSPTPKRSLSSSKCDPRHKDCLLREFRKLCAMVADNPSYNTKTQIIQDFLRKGSAGDGFH
GDVYLTVKLLLPGVIKTVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQ
SKSFPPAAKSLLTIQEVDEFLLRLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDL
KMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNAQEVEKEPGQRRALSVQASLMTP
VQPMLAEACKSVEYAMKKCPNGMFSEIKYDGERVQVHKNGDHFSYFSRSLKPVLPHKVAH
FKDYIPQAFPGGHSMILDSEVLLIDNKTGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYF
NDVSLMDRPLCERRKFLHDNMVEIPNRIMFSEMKRVTKALDLADMITRVIQEGLEGLVLK
DVKGTYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGQGSKGGMMSIFLMGCYDPGS
QKWCTVTKCAGGHDDATLARLQNELDMVKISKDPSKIPSWLKVNKIYYPDFIVPDPKKAA
VWEITGAEFSKSEAHTADGISIRFPRCTRIRDDKDWKSATNLPQLKELYQLSKEKADFTV
VAGDEGSSTTGGSSEENKGPSGSAVSRKAPSKPSASTKKAEGKLSNSNSKDGNMQTAKPS
AMKVGEKLATKSSPVKVGEKRKAADETLCQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFV
AFDGDLVQEFDMTSATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC
|
| Enzyme 74 Number of Residues |
1009 |
| Enzyme 74 Molecular Weight |
112906.0 |
| Enzyme 74 Theoretical pI |
9.43 |
| Enzyme 74 GO Classification |
| Function |
- ATP binding
- DNA binding
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- ligase activity
- ligase activity, forming phosphoric ester bonds
- metal ion binding
- nucleic acid binding
- nucleoside binding
- purine nucleoside binding
- transition metal ion binding
- zinc ion binding
|
| Process |
- DNA ligation
- DNA ligation involved in DNA repair
- DNA metabolic process
- DNA recombination
- DNA repair
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
|
|
| Enzyme 74 General Function |
Involved in DNA ligase (ATP) activity |
| Enzyme 74 Specific Function |
Interacts with DNA-repair protein XRCC1 and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents |
| Enzyme 74 Pathways |
Not Available |
| Enzyme 74 Reactions |
- ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m [RN:R00381]
|
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
73747829 |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
P49916 |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
DNLI3_HUMAN |
| Enzyme 74 PDB ID |
1UW0 |
| Enzyme 74 PDB File |
Show |
| Enzyme 74 3D Structure |
|
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>3030 bp
ATGTCTTTGGCTTTCAAGATCTTCTTTCCACAAACCCTCCGTGCACTCAGCCGAAAAGAA
CTGTGCCTATTCCGAAAACATCACTGGCGTGATGTAAGACAATTCAGCCAGTGGTCAGAA
ACAGATCTGCTTCATGGACATCCCCTCTTCCTGAGAAGAAAGCCTGTTCTATCATTCCAG
GGAAGCCATCTAAGATCACGTGCCACCTACCTTGTTTTCTTGCCAGGGTTGCATGTGGGA
CTCTGCAGTGGCCCCTGTGAGATGGCTGAGCAACGGTTCTGTGTGGACTATGCCAAGCGT
GGCACAGCTGGCTGCAAAAAATGCAAGGAAAAGATTGTGAAGGGCGTATGCCGAATTGGC
AAAGTGGTGCCCAATCCCTTCTCAGAGTCTGGGGGTGATATGAAAGAGTGGTACCACATT
AAATGCATGTTTGAGAAACTAGAGCGGGCCCGGGCCACCACAAAAAAAATCGAGGACCTC
ACAGAGCTGGAAGGCTGGGAAGAGCTGGAAGATAATGAGAAGGAACAGATAACCCAGCAC
ATTGCAGATCTGTCTTCTAAGGCAGCAGGTACACCAAAGAAGAAAGCTGTTGTCCAGGCT
AAGTTGACAACCACTGGCCAGGTGACTTCTCCAGTGAAAGGCGCCTCATTTGTCACCAGT
ACCAATCCCCGGAAATTTTCTGGCTTTTCAGCCAAGCCCAACAACTCTGGGGAAGCCCCC
TCGAGCCCCACCCCTAAGAGAAGTCTGTCTTCAAGCAAATGTGACCCCAGGCATAAGGAC
TGTCTGCTACGGGAGTTTCGAAAGTTATGCGCCATGGTGGCCGATAATCCTAGCTACAAC
ACGAAGACCCAGATCATCCAGGACTTCCTTCGGAAAGGCTCAGCAGGAGATGGTTTCCAC
GGTGATGTGTACCTAACAGTGAAGCTGCTGCTGCCAGGAGTCATTAAGACTGTTTACAAC
TTGAACGATAAGCAGATTGTGAAGCTTTTCAGTCGCATTTTTAACTGCAACCCAGATGAT
ATGGCACGGGACCTAGAGCAGGGTGACGTGTCAGAGACAATCAGAGTCTTCTTTGAGCAG
AGCAAGTCTTTCCCCCCAGCTGCCAAGAGCCTCCTTACCATCCAGGAAGTGGATGAGTTC
CTTCTGCGGCTGTCCAAGCTCACCAAGGAGGATGAGCAGCAACAGGCCCTACAGGACATT
GCCTCCAGGTGTACAGCCAATGACCTTAAATGCATCATCAGGTTGATCAAACATGATCTG
AAGATGAACTCAGGTGCAAAACATGTGTTAGACGCCCTTGACCCCAATGCCTATGAAGCC
TTCAAAGCCTCGCGCAACCTGCAGGATGTGGTGGAGCGGGTCCTTCACAACGCGCAGGAG
GTGGAGAAGGAGCCGGGCCAGAGACGAGCTCTGAGCGTCCAGGCCTCGCTGATGACACCT
GTGCAGCCCATGTTGGCGGAGGCCTGCAAGTCCGTTGAGTATGCAATGAAGAAATGTCCC
AATGGCATGTTCTCTGAGATCAAGTACGATGGAGAGCGAGTCCAGGTGCATAAGAATGGA
GACCACTTCAGCTACTTCAGCCGCAGTCTCAAGCCCGTCCTTCCTCACAAGGTGGCCCAC
TTTAAGGACTACATTCCCCAGGCTTTTCCTGGGGGCCACAGCATGATCTTGGATTCTGAA
GTGCTTCTGATTGACAACAAGACAGGCAAACCACTGCCCTTTGGGACTCTGGGAGTACAC
AAGAAAGCAGCCTTCCAGGATGCTAATGTCTGCCTGTTTGTTTTTGATTGTATCTACTTT
AATGATGTCAGCTTGATGGACAGACCTCTGTGTGAGCGGCGGAAGTTTCTTCATGACAAC
ATGGTTGAAATTCCAAACCGGATCATGTTCTCAGAAATGAAGCGAGTCACAAAAGCTTTG
GACTTGGCTGACATGATAACCCGGGTGATCCAGGAGGGATTGGAGGGGCTGGTGCTGAAG
GATGTGAAGGGTACATATGAGCCTGGGAAGCGGCACTGGCTGAAAGTGAAGAAAGACTAT
TTGAACGAGGGGGCCATGGCCGACACAGCTGACCTGGTGGTCCTTGGAGCCTTCTATGGG
CAAGGGAGCAAAGGCGGCATGATGTCAATCTTCCTCATGGGCTGCTACGACCCTGGCAGC
CAGAAGTGGTGCACAGTCACCAAGTGTGCAGGAGGCCATGATGATGCCACGCTTGCCCGC
CTGCAGAATGAACTAGACATGGTGAAGATCAGCAAGGACCCCAGCAAAATACCCAGCTGG
TTGAAGGTCAACAAGATCTACTATCCTGACTTCATCGTCCCAGACCCAAAGAAAGCTGCC
GTGTGGGAGATCACAGGGGCTGAATTCTCCAAATCGGAGGCTCATACAGCTGACGGGATC
TCCATCCGATTCCCTCGCTGCACCCGAATCCGAGATGATAAGGACTGGAAATCTGCCACT
AACCTTCCCCAACTCAAGGAACTGTACCAGTTGTCCAAGGAGAAGGCAGACTTCACTGTA
GTGGCTGGAGATGAGGGGAGCTCCACTACAGGGGGTAGCAGTGAAGAGAATAAGGGTCCC
TCAGGGTCTGCTGTGTCCCGCAAGGCCCCCAGCAAGCCCTCAGCCAGTACCAAGAAAGCA
GAAGGGAAGCTGAGTAACTCCAACAGCAAAGATGGCAACATGCAGACTGCAAAGCCTTCC
GCTATGAAGGTGGGGGAGAAGCTGGCCACAAAGTCTTCTCCAGTGAAAGTAGGGGAGAAG
CGGAAAGCTGCTGATGAGACGCTGTGCCAAACAAAGGTATTGCTGGACATCTTCACTGGG
GTGCGGCTTTACTTGCCACCCTCCACACCAGACTTCAGCCGTCTCAGACGCTACTTTGTG
GCATTCGACGGGGACCTGGTACAGGAATTTGATATGACTTCAGCCACGCACGTGCTGGGT
AGCAGGGACAAGAACCCTGCGGCCCAGCAGGTCTCCCCAGAGTGGATTTGGGCATGTATC
CGGAAACGGAGACTGGTAGCTCCCTGCTAG
|
| Enzyme 74 GenBank Gene ID |
NM_013975.3 |
| Enzyme 74 GeneCard ID |
LIG3 |
| Enzyme 74 GenAtlas ID |
LIG3 |
| Enzyme 74 HGNC ID |
HGNC:6600 |
| Enzyme 74 Chromosome Location |
1 |
| Enzyme 74 Locus |
17q11.2-q12 |
| Enzyme 74 SNPs |
SNPJam Report |
| Enzyme 74 General References |
- Wei YF, Robins P, Carter K, Caldecott K, Pappin DJ, Yu GL, Wang RP, Shell BK, Nash RA, Schar P, et al.: Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination. Mol Cell Biol. 1995 Jun;15(6):3206-16. [PubMed ]
- Chen J, Tomkinson AE, Ramos W, Mackey ZB, Danehower S, Walter CA, Schultz RA, Besterman JM, Husain I: Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination. Mol Cell Biol. 1995 Oct;15(10):5412-22. [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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- Thornton KH, Krishnan VV, West MG, Popham J, Ramirez M, Thelen MP, Cosman M: Expression, purification, and biophysical characterization of the BRCT domain of human DNA ligase IIIalpha. Protein Expr Purif. 2001 Apr;21(3):401-11. [PubMed ]
- Kulczyk AW, Yang JC, Neuhaus D: Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha. J Mol Biol. 2004 Aug 13;341(3):723-38. [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 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
5880 |
| Enzyme 75 Name |
Aspartyl-tRNA synthetase, cytoplasmic |
| Enzyme 75 Synonyms |
- Aspartate--tRNA ligase
- AspRS
- Cell proliferation-inducing gene 40 protein
|
| Enzyme 75 Gene Name |
DARS |
| Enzyme 75 Protein Sequence |
>Aspartyl-tRNA synthetase, cytoplasmic
MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVV
WVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVV
RKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRL
DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYF
KNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYH
EVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGV
EMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFM
RGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLF
LGLHNVRQTSMFPRDPKRLTP
|
| Enzyme 75 Number of Residues |
501 |
| Enzyme 75 Molecular Weight |
57135.8 |
| Enzyme 75 Theoretical pI |
6.52 |
| Enzyme 75 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- aspartate-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- aspartyl-tRNA aminoacylation
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 75 General Function |
Involved in nucleotide binding |
| Enzyme 75 Specific Function |
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction:the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA |
| Enzyme 75 Pathways |
|
| Enzyme 75 Reactions |
- ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp [RN:R05577]
|
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
62896511 |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
P14868 |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
SYDC_HUMAN |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>1506 bp
ATGCCCAGCGCCAGCGCCAGCCGCAAGAGTCAGGAGAAGCCGCGGGAGATCATGGACGCG
GCGGAAGATTATGCTAAAGAGAGATATGGAATATCTTCAATGATACAATCACACGAAAAA
CCAGATCGAGTTTTGGTTCGGGTTAGAGACTTGACAATACAAAAAGCTGATGAAGTTGTT
TGGGTACGTGCAAGAGTTCATACAAGCAGAGCTAAAGGGAAACAGTGCTTCTTAGTCCTA
CGTCAGCAGCAGTTTAATGTCCAGGCTCTTGTGGCGGTGGGAGACCATGCAAGCAAGCAG
ATGGTTAAATTTGCTGCCAACATCAACAAAGAGAGCATTGTGGATGTAGAAGGTGTTGTG
AGAAAAGTGAATCAGAAAATTGGAAGCTGTACACAGCAAGACGTTGAGTTACATGTTCAG
AAGATTTATGTGATCAGTTTGGCTGAACCCCGTCTGCCCCTGCAGCTGGATGATGCTGTT
CGGCCTGAGGCAGAAGGAGAAGAGGAAGGAAGAGCTACTGTTAACCAGGATACAAGATTA
GACAACAGAGTCATTGATCTTAGGACATCAACTAGTCAGGCAGTCTTCCGTCTCCAGTCT
GGCATCTGCCATCTCTTCCGAGAAACTTTAATTAACAAAGGTTTTGTGGAAATCCAAACT
CCTAAAATTATTTCAGCTGCCAGTGAAGGAGGAGCCAATGTTTTTACTGTGTCATATTTT
AAAAATAATGCATACCTGGCTCAGTCCCCACAGCTATATAAGCAAATGTGCATTTGTGCT
GATTTTGAGAAGGTTTTCTCTATTGGACCAGTATTCAGAGCGGAAGACTCTAATACCCAT
AGACATCTAACTGAGTTTGTTGGTTTGGACATTGAAATGGCTTTTAATTACCATTACCAC
GAAGTTATGGAAGAAATTGCTGACACCATGGTACAAATATTCAAAGGACTTCAAGAAAGG
TTTCAGACTGAAATTCAAACAGTGAATAAACAGTTCCCATGTGAGCCATTCAAATTTTTG
GAGCCAACTCTAAGACTAGAATATTGTGAAGCATTGGCTATGCTTAGGGAAGCTGGAGTC
GAAATGGGAGATGAAGACGATCTGAGCACACCAAATGAAAAGCTGTTGGGTCATTTGGTA
AAGGAAAAGTATGATACAGATTTTTATATTCTTGATAAATATCCATTGGCTGTAAGACCT
TTCTATACCATGCCTGACCCAAGAAATCCCAAACAGTCCAACTCTTACGATATGTTCATG
AGAGGAGAAGAAATATTGTCAGGAGCTCAAAGAATACATGATCCTCAACTGCTAACAGAG
AGAGCTTTACATCATGGAATTGATTTGGAGAAAATTAAGGCTTACATTGATTCCTTCCGC
TTTGGAGCCCCTCCTCATGCTGGTGGAGGCATTGGATTGGAACGAGTTACTATGCTGTTT
CTGGGATTGCATAATGTTCGTCAGACCTCCATGTTCCCTCGTGATCCCAAACGACTCACT
CCTTAA
|
| Enzyme 75 GenBank Gene ID |
AK222476 |
| Enzyme 75 GeneCard ID |
DARS |
| Enzyme 75 GenAtlas ID |
DARS |
| Enzyme 75 HGNC ID |
HGNC:2678 |
| Enzyme 75 Chromosome Location |
2 |
| Enzyme 75 Locus |
2q21.3 |
| Enzyme 75 SNPs |
SNPJam Report |
| Enzyme 75 General References |
- Jacobo-Molina A, Peterson R, Yang DC: cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J Biol Chem. 1989 Oct 5;264(28):16608-12. [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 ]
- 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 ]
- Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [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 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
5882 |
| Enzyme 76 Name |
Ubiquitin-conjugating enzyme E2 D3 |
| Enzyme 76 Synonyms |
- Ubiquitin carrier protein D3
- Ubiquitin-conjugating enzyme E2(17)KB 3
- Ubiquitin-conjugating enzyme E2-17 kDa 3
- Ubiquitin-protein ligase D3
|
| Enzyme 76 Gene Name |
UBE2D3 |
| Enzyme 76 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 D3
MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDRDKYNRISREWTQKYAM
|
| Enzyme 76 Number of Residues |
147 |
| Enzyme 76 Molecular Weight |
16687.0 |
| Enzyme 76 Theoretical pI |
7.95 |
| Enzyme 76 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 76 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 76 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA- linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML- NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction |
| Enzyme 76 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 76 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 76 Pfam Domain Function |
|
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
4507777 |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
P61077 |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
UB2D3_HUMAN |
| Enzyme 76 PDB ID |
1X23 |
| Enzyme 76 PDB File |
Show |
| Enzyme 76 3D Structure |
|
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>444 bp
ATGGCGCTGAAACGGATTAATAAGGAACTTAGTGATTTGGCCCGTGACCCTCCAGCACAA
TGTTCTGCAGGTCCAGTTGGGGATGATATGTTTCATTGGCAAGCCACAATTATGGGACCT
AATGACAGCCCATATCAAGGCGGTGTATTCTTTTTGACAATTCATTTTCCTACAGACTAC
CCCTTCAAACCACCTAAGGTTGCATTTACAACAAGAATTTATCATCCAAATATTAACAGT
AATGGCAGCATTTGTCTCGATATTCTAAGATCACAGTGGTCGCCTGCTTTAACAATTTCT
AAAGTTCTTTTATCCATTTGTTCACTGCTATGTGATCCAAACCCAGATGACCCCCTAGTG
CCAGAGATTGCACGGATCTATAAAACAGACAGAGATAAGTACAACAGAATATCTCGGGAA
TGGACTCAGAAGTATGCCATGTGA
|
| Enzyme 76 GenBank Gene ID |
NM_003340.5 |
| Enzyme 76 GeneCard ID |
UBE2D3 |
| Enzyme 76 GenAtlas ID |
UBE2D3 |
| Enzyme 76 HGNC ID |
HGNC:12476 |
| Enzyme 76 Chromosome Location |
4 |
| Enzyme 76 Locus |
4q24 |
| Enzyme 76 SNPs |
SNPJam Report |
| Enzyme 76 General References |
- Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM: Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem. 1995 Dec 22;270(51):30408-14. [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 ]
- 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 ]
- Gonen H, Bercovich B, Orian A, Carrano A, Takizawa C, Yamanaka K, Pagano M, Iwai K, Ciechanover A: Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. J Biol Chem. 1999 May 21;274(21):14823-30. [PubMed ]
- Murata S, Minami Y, Minami M, Chiba T, Tanaka K: CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2001 Dec;2(12):1133-8. Epub 2001 Nov 21. [PubMed ]
- Yogosawa S, Miyauchi Y, Honda R, Tanaka H, Yasuda H: Mammalian Numb is a target protein of Mdm2, ubiquitin ligase. Biochem Biophys Res Commun. 2003 Mar 21;302(4):869-72. [PubMed ]
- Rajendra R, Malegaonkar D, Pungaliya P, Marshall H, Rasheed Z, Brownell J, Liu LF, Lutzker S, Saleem A, Rubin EH: Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53. J Biol Chem. 2004 Aug 27;279(35):36440-4. Epub 2004 Jul 9. [PubMed ]
- Saville MK, Sparks A, Xirodimas DP, Wardrop J, Stevenson LF, Bourdon JC, Woods YL, Lane DP: Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo. J Biol Chem. 2004 Oct 1;279(40):42169-81. Epub 2004 Jul 26. [PubMed ]
- Huang J, Huang Q, Zhou X, Shen MM, Yen A, Yu SX, Dong G, Qu K, Huang P, Anderson EM, Daniel-Issakani S, Buller RM, Payan DG, Lu HH: The poxvirus p28 virulence factor is an E3 ubiquitin ligase. J Biol Chem. 2004 Dec 24;279(52):54110-6. Epub 2004 Oct 20. [PubMed ]
- Polanowska J, Martin JS, Garcia-Muse T, Petalcorin MI, Boulton SJ: A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites. EMBO J. 2006 May 17;25(10):2178-88. Epub 2006 Apr 20. [PubMed ]
- Ohbayashi N, Okada K, Kawakami S, Togi S, Sato N, Ikeda O, Kamitani S, Muromoto R, Sekine Y, Kawai T, Akira S, Matsuda T: Physical and functional interactions between ZIP kinase and UbcH5. Biochem Biophys Res Commun. 2008 Aug 8;372(4):708-12. Epub 2008 Jun 2. [PubMed ]
- Zhang S, Chea J, Meng X, Zhou Y, Lee EY, Lee MY: PCNA is ubiquitinated by RNF8. Cell Cycle. 2008 Nov 1;7(21):3399-404. [PubMed ]
- Umebayashi K, Stenmark H, Yoshimori T: Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation. Mol Biol Cell. 2008 Aug;19(8):3454-62. Epub 2008 May 28. [PubMed ]
- Saha A, Deshaies RJ: Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol Cell. 2008 Oct 10;32(1):21-31. [PubMed ]
- Kubori T, Hyakutake A, Nagai H: Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions. Mol Microbiol. 2008 Mar;67(6):1307-19. Epub 2008 Feb 13. [PubMed ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
- Wu K, Kovacev J, Pan ZQ: Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate. Mol Cell. 2010 Mar 26;37(6):784-96. [PubMed ]
- Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE: A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol Cell. 2006 Mar 17;21(6):873-80. [PubMed ]
|
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
5883 |
| Enzyme 77 Name |
Asparaginyl-tRNA synthetase, cytoplasmic |
| Enzyme 77 Synonyms |
- Asparagine--tRNA ligase
- AsnRS
|
| Enzyme 77 Gene Name |
NARS |
| Enzyme 77 Protein Sequence |
>Asparaginyl-tRNA synthetase, cytoplasmic
MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISK
SQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGAL
EGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVA
VYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGE
NMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSS
QLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCD
VVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIP
EAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIF
DSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP
RFVQRCTP
|
| Enzyme 77 Number of Residues |
548 |
| Enzyme 77 Molecular Weight |
62942.4 |
| Enzyme 77 Theoretical pI |
6.17 |
| Enzyme 77 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- asparagine-tRNA ligase activity
- aspartate-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- asparaginyl-tRNA aminoacylation
- aspartyl-tRNA aminoacylation
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 77 General Function |
Involved in nucleotide binding |
| Enzyme 77 Specific Function |
ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn) |
| Enzyme 77 Pathways |
|
| Enzyme 77 Reactions |
- ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn [RN:R03648]
|
| Enzyme 77 Pfam Domain Function |
|
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
2764505 |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
O43776 |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
SYNC_HUMAN |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>1647 bp
ATGGTGCTAGCAGAGCTGTACGTCTCTGACCGAGAGGGAAGCGATGCCACGGGAGATGGA
ACCAAGGAGAAACCATTTAAAACAGGTCTAAAGGCTTTGATGACAGTAGGGAAAGAACCA
TTTCCTACCATTTACGTAGATTCACAAAAAGAAAATGAGAGGTGGAATGTTATTTCTAAA
TCACAGTTGAAGAACATTAAAAAGATGTGGCATAGGGAACAAATGAAGAGTGAATCCCGG
GAAAAGAAAGAGGCAGAAGATAGTTTACGAAGAGAAAAGAACCTGGAAGAAGCAAAGAAG
ATTACCATTAAAAATGATCCAAGTCTCCCAGAGCCAAAATGTGTGAAGATTGGTGCGTTA
GAAGGATATAGAGGCCAAAGAGTAAAGGTGTTTGGCTGGGTCCACAGGCTGCGCAGGCAA
GGAAAGAATTTAATGTTTCTGGTGTTGCGAGATGGTACAGGTTATCTTCAGTGTGTCTTG
GCGGATGAGTTGTGTCAGTGCTACAATGGAGTTCTCTTGTCCACGGAGAGCAGTGTTGCA
GTGTATGGAATGCTAAATCTTACCCCAAAGGGCAAGCAGGCTCCAGGTGGCCATGAGCTG
AGTTGTGACTTCTGGGAACTAATTGGGTTGGCCCCTGCTGGAGGAGCTGACAACCTGATC
AATGAGGAGTCTGACGTTGATGTCCAGCTCAACAACAGACACATGATGATCCGAGGAGAA
AACATGTCCAAAATCCTAAAAGCACGATCCATGGTCACCAGGTGCTTTAGAGATCACTTC
TTTGATAGGGGGTACTATGAAGTTACTCCTCCAACATTAGTGCAAACACAAGTAGAAGGT
GGTGCCACACTCTTCAAGCTTGACTATTTTGGGGAAGAGGCATTTTTGACTCAATCCTCT
CAGTTGTACTTGGAGACCTGCCTCCCAGCCCTGGGAGATGTTTTTTGTATTGCTCAGTCA
TACCGGGCAGAGCAGTCCAGAACACGAAGGCACCTGGCTGAGTACACTCACGTGGAAGCT
GAGTGTCCTTTCCTGACTTTTGACGACCTCCTGAACCGGTTGGAGGACTTGGTTTGTGAT
GTGGTAGATCGAATATTGAAGTCACCTGCAGGGAGCATAGTGCATGAGCTCAACCCGAAC
TTTCAGCCCCCCAAACGGCCTTTCAAACGGATGAACTATTCAGATGCTATCGTTTGGCTA
AAAGAACATGATGTAAAGAAAGAAGATGGAACTTTCTATGAATTTGGAGAAGATATCCCA
GAAGCTCCTGAGAGACTGATGACAGACACCATTAATGAACCAATCTTGCTGTGTCGATTT
CCTGTGGAGATCAAGTCCTTCTACATGCAGCGATGTCCTGAGGATTCCCGTCTTACTGAA
TCTGTCGACGTGTTGATGCCCAATGTTGGTGAGATTGTGGGAGGCTCAATGCGTATCTTT
GATAGTGAAGAAATACTGGCAGGTTATAAAAGGGAAGGGATTGACCCCACTCCCTATTAC
TGGTATACGGATCAGAGAAAATACGGTACATGTCCCCATGGAGGATATGGCTTGGGCTTG
GAACGATTCTTAACGTGGATTCTGAATAGGTATCACATCCGAGACGTGTGCTTATACCCT
CGATTTGTCCAGCGTTGCACGCCATAA
|
| Enzyme 77 GenBank Gene ID |
AJ000334 |
| Enzyme 77 GeneCard ID |
NARS |
| Enzyme 77 GenAtlas ID |
NARS |
| Enzyme 77 HGNC ID |
HGNC:7643 |
| Enzyme 77 Chromosome Location |
1 |
| Enzyme 77 Locus |
18q21.31 |
| Enzyme 77 SNPs |
SNPJam Report |
| Enzyme 77 General References |
- Beaulande M, Tarbouriech N, Hartlein M: Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen. Nucleic Acids Res. 1998 Jan 15;26(2):521-4. [PubMed ]
- Shiba K, Motegi H, Yoshida M, Noda T: Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family. Nucleic Acids Res. 1998 Nov 15;26(22):5045-51. [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 ]
- 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 ]
- 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 ]
|
| Enzyme 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
5885 |
| Enzyme 78 Name |
Lysyl-tRNA synthetase |
| Enzyme 78 Synonyms |
- Lysine--tRNA ligase
- LysRS
|
| Enzyme 78 Gene Name |
KARS |
| Enzyme 78 Protein Sequence |
>Lysyl-tRNA synthetase
MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTT
DNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH
LTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGD
IIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAP
ELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSG
MVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETR
KILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYG
LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
|
| Enzyme 78 Number of Residues |
597 |
| Enzyme 78 Molecular Weight |
68047.5 |
| Enzyme 78 Theoretical pI |
6.31 |
| Enzyme 78 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- lysine-tRNA ligase activity
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- lysyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 78 General Function |
Involved in nucleotide binding |
| Enzyme 78 Specific Function |
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction:the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation |
| Enzyme 78 Pathways |
|
| Enzyme 78 Reactions |
- ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys [RN:R03658]
|
| Enzyme 78 Pfam Domain Function |
|
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
5031815 |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
Q15046 |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
SYK_HUMAN |
| Enzyme 78 PDB ID |
Not Available |
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>1794 bp
ATGGCGGCCGTGCAGGCGGCCGAGGTGAAAGTGGATGGCAGCGAGCCGAAACTGAGCAAG
AATGAGCTGAAGAGACGCCTGAAAGCTGAGAAGAAAGTAGCAGAGAAGGAGGCCAAACAG
AAAGAGCTCAGTGAGAAACAGCTAAGCCAAGCCACTGCTGCTGCCACCAACCACACCACT
GATAATGGTGTGGGTCCTGAGGAAGAGAGCGTGGACCCAAATCAATACTACAAAATCCGC
AGTCAAGCAATTCATCAGCTGAAGGTCAATGGGGAAGACCCATACCCACACAAGTTCCAT
GTAGACATCTCACTCACTGACTTCATCCAAAAATATAGTCACCTGCAGCCTGGGGATCAC
CTGACTGACATCACCTTAAAGGTGGCAGGTAGGATCCATGCCAAAAGAGCTTCTGGGGGA
AAGCTCATCTTCTATGATCTTCGAGGAGAGGGGGTGAAGTTGCAAGTCATGGCCAATTCC
AGAAATTATAAATCAGAAGAAGAATTTATTCATATTAATAACAAACTGCGTCGGGGAGAC
ATAATTGGAGTTCAGGGGAATCCTGGTAAAACCAAGAAGGGTGAGCTGAGCATCATTCCG
TATGAGATCACACTGCTGTCTCCCTGTTTGCATATGTTACCTCATCTTCACTTTGGCCTC
AAAGACAAGGAAACAAGGTATCGCCAGAGATACTTGGACTTGATCCTGAATGACTTTGTG
AGGCAGAAATTTATCATCCGCTCTAAGATCATCACATATATAAGAAGTTTCTTAGATGAG
CTGGGATTCCTAGAGATTGAAACTCCCATGATGAACATCATCCCAGGGGGAGCCGTGGCC
AAGCCTTTCATCACTTATCACAACGAGCTGGACATGAACTTATATATGAGAATTGCTCCA
GAACTCTATCATAAGATGCTTGTGGTTGGTGGCATCGACCGGGTTTATGAAATTGGACGC
CAGTTCCGGAATGAGGGGATTGATTTGACGCACAATCCTGAGTTCACCACCTGTGAGTTC
TACATGGCCTATGCAGACTATCACGATCTCATGGAAATCACGGAGAAGATGGTTTCAGGG
ATGGTGAAGCATATTACAGGCAGTTACAAGGTCACCTACCACCCAGATGGCCCAGAGGGC
CAAGCCTACGATGTTGACTTCACCCCACCCTTCCGGCGAATCAACATGGTAGAAGAGCTT
GAGAAAGCCCTGGGGATGAAGCTGCCAGAAACGAACCTCTTTGAAACTGAAGAAACTCGC
AAAATTCTTGATGATATCTGTGTGGCAAAAGCTGTTGAATGCCCTCCACCTCGGACCACA
GCCAGGCTCCTTGACAAGCTTGTTGGGGAGTTCCTGGAAGTGACTTGCATCAATCCTACA
TTCATCTGTGATCACCCACAGATAATGAGCCCTTTGGCTAAATGGCACCGCTCTAAAGAG
GGTCTGACTGAGCGCTTTGAGCTGTTTGTCATGAAGAAAGAGATATGCAATGCGTATACT
GAGCTGAATGATCCCATGCGGCAGCGGCAGCTTTTTGAAGAACAGGCCAAGGCCAAGGCT
GCAGGTGATGATGAGGCCATGTTCATAGATGAAAACTTCTGTACTGCCCTGGAATATGGG
CTGCCCCCCACAGCTGGCTGGGGCATGGGCATTGATCGAGTCGCCATGTTTCTCACGGAC
TCCAACAACATCAAGGAAGTACTTCTGTTTCCTGCCATGAAACCCGAAGACAAGAAGGAG
AATGTAGCAACCACTGATACACTGGAAAGCACAACAGTTGGCACTTCTGTCTAG
|
| Enzyme 78 GenBank Gene ID |
NM_005548.2 |
| Enzyme 78 GeneCard ID |
KARS |
| Enzyme 78 GenAtlas ID |
KARS |
| Enzyme 78 HGNC ID |
HGNC:6215 |
| Enzyme 78 Chromosome Location |
1 |
| Enzyme 78 Locus |
16q23.1 |
| Enzyme 78 SNPs |
SNPJam Report |
| Enzyme 78 General References |
- Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P: Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. J Biol Chem. 1997 Sep 5;272(36):22809-16. [PubMed ]
- Tolkunova E, Park H, Xia J, King MP, Davidson E: The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript. J Biol Chem. 2000 Nov 10;275(45):35063-9. [PubMed ]
- Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [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 ]
- Zamecnik PC, Stephenson ML, Janeway CM, Randerath K: Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun. 1966 Jul 6;24(1):91-7. [PubMed ]
- Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M: Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J Mol Biol. 1999 Jan 8;285(1):183-95. [PubMed ]
- Tan M, Wei C, Price CM: The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes. Gene. 2003 Dec 24;323:1-10. [PubMed ]
- Lee YN, Nechushtan H, Figov N, Razin E: The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Immunity. 2004 Feb;20(2):145-51. [PubMed ]
- Javanbakht H, Halwani R, Cen S, Saadatmand J, Musier-Forsyth K, Gottlinger H, Kleiman L: The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly. J Biol Chem. 2003 Jul 25;278(30):27644-51. Epub 2003 May 19. [PubMed ]
- Halwani R, Cen S, Javanbakht H, Saadatmand J, Kim S, Shiba K, Kleiman L: Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly. J Virol. 2004 Jul;78(14):7553-64. [PubMed ]
- Park SG, Kim HJ, Min YH, Choi EC, Shin YK, Park BJ, Lee SW, Kim S: Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Proc Natl Acad Sci U S A. 2005 May 3;102(18):6356-61. Epub 2005 Apr 25. [PubMed ]
- Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [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 ]
- Guo M, Ignatov M, Musier-Forsyth K, Schimmel P, Yang XL: Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation. Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2331-6. Epub 2008 Feb 13. [PubMed ]
|
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
5886 |
| Enzyme 79 Name |
Isoleucyl-tRNA synthetase, cytoplasmic |
| Enzyme 79 Synonyms |
- Isoleucine--tRNA ligase
- IRS
- IleRS
|
| Enzyme 79 Gene Name |
IARS |
| Enzyme 79 Protein Sequence |
>Isoleucyl-tRNA synthetase, cytoplasmic
MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHIL
AGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQC
RAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMP
FSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNP
EMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCK
ENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTT
EVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVE
NMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVC
IGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHY
PFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQK
MSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAY
RFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVV
PRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELM
YQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKT
IPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMV
LGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQ
FEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGT
YLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPAC
AYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQN
QTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPL
GQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTA
DF
|
| Enzyme 79 Number of Residues |
1262 |
| Enzyme 79 Molecular Weight |
144496.9 |
| Enzyme 79 Theoretical pI |
6.03 |
| Enzyme 79 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- isoleucine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- isoleucyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 79 General Function |
Involved in nucleotide binding |
| Enzyme 79 Specific Function |
ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile) |
| Enzyme 79 Pathways |
|
| Enzyme 79 Reactions |
- ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle [RN:R03656]
|
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
158259489 |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
P41252 |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
SYIC_HUMAN |
| Enzyme 79 PDB ID |
Not Available |
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
>3789 bp
ATGCTTCAACAAGTTCCAGAAAACATAAATTTTCCTGCTGAAGAAGAGAAAATCTTGGAG
TTTTGGACTGAATTTAATTGTTTTCAGGAATGCTTAAAGCAATCAAAACATAAACCAAAA
TTTACCTTCTATGATGGTCCTCCTTTTGCAACTGGACTGCCTCACTATGGACATATACTT
GCGGGTACAATTAAAGATATAGTTACAAGATATGCTCACCAGAGTGGGTTTCATGTTGAC
AGAAGATTTGGATGGGATTGCCATGGCTTACCTGTGGAATATGAAATTGATAAGACACTG
GGAATCAGAGGACCAGAGGATGTGGCCAAAATGGGGATTACAGAGTATAACAATCAGTGC
CGAGCAATTGTGATGAGATATTCTGCTGAGTGGAAGTCTACTGTTAGCAGACTTGGCCGA
TGGATTGACTTTGACAATGACTATAAAACTCTGTATCCACAATTCATGGAATCAGTCTGG
TGGGTCTTCAAACAACTCTATGATAAAGGCCTTGTTTATAGAGGTGTGAAAGTCATGCCC
TTCTCTACGGCATGTAACACTCCACTTTCCAACTTCGAGTCACACCAGAATTATAAGGAT
GTTCAAGATCCTTCAGTATTTGTAACTTTCCCTTTGGAAGAAGATGAAACTGTATCTTTA
GTTGCTTGGACAACCACTCCCTGGACTCTACCTAGTAACCTTGCTGTGTGTGTTAATCCA
GAAATGCAATATGTGAAAATTAAAGATGTTGCCAGAGGACGATTACTCATTTTAATGGAA
GCCAGATTGTCAGCCCTCTATAAATTGGAGAGTGACTATGAGATCCTTGAAAGATTTCCT
GGTGCCTATCTTAAAGGCAAGAAGTACAGGCCCCTGTTTGACTATTTCCTGAAGTGTAAA
GAGAATGGCGCTTTCACTGTGCTTGTTGACAACTATGTGAAGGAAGAAGAAGGCACAGGG
GTTGTCCACCAAGCTCCTTACTTCGGTGCTGAGGACTATCGGGTCTGTATGGACTTTAAC
ATTATTCGGAAAGACTCACTCCCTGTTTGCCCTGTGGATGCTTCAGGCTGCTTCACAACG
GAGGTGACAGATTTCGCAGGACAGTATGTGAAGGATGCTGACAAAAGTATCATCAGGACT
TTGAAGGAACAAGGCCGACTTCTGGTTGCCACCACCTTCACTCACAGCTACCCTTTTTGC
TGGAGATCAGACACTCCTCTAATTTACAAAGCAGTGCCCAGCTGGTTTGTGCGAGTGGAG
AACATGGTGGACCAGCTCCTAAGGAACAATGACCTGTGCTACTGGGTCCCAGAGTTGGTA
CGAGAAAAACGATTTGGAAATTGGCTGAAAGATGCACGTGACTGGACAATTTCCAGAAAC
AGATACTGGGGCACCCCCATCCCACTGTGGGTCAGCGATGACTTTGAGGAGGTGGTATGC
ATTGGGTCAGTGGCGGAACTTGAAGAACTGTCAGGAGCAAAGATCTCAGATCTCCACAGA
GAGAGTGTTGACCACCTGACCATTCCTTCACGCTGTGGGAAGGGATCCTTGCACCGCATC
TCTGAAGTGTTTGACTGTTGGTTTGAGAGTGGCAGCATGCCCTATGCTCAGGTTCATTAC
CCGTTTGAAAACAAGAGGGAGTTTGAGGATGCTTTTCCTGCAGATTTCATTGCCGAGGGC
ATCGACCAAACCAGAGGATGGTTTTATACCCTGCTGGTGCTGGCCACGGCCCTCTTTGGA
CAACCGCCTTTCAAGAACGTAATTGTGAATGGGCTTGTCCTGGCAAGTGATGGCCAAAAA
ATGAGCAAACGGAAAAAGAATTATCCAGATCCAGTTTCCATCATCCAGAAGTATGGTGCT
GATGCCCTCAGATTATATCTGATTAACTCCCCTGTGGTGAGAGCAGAAAACCTCCGCTTT
AAAGAAGAGGGTGTGCGGGACGTCCTTAAGGATGTACTGCTCCCATGGTACAATGCCTAT
CGCTTCTTAATCCAGAACGTTCTGAGGCTCCAGAAGGAGGAAGAAATAGAATTTCTCTAC
AATGAGAACACGGTTAGAGAAAGCCCCAACATTACAGACCGGTGGATCCTGTCCTTCATG
CAGTCTCTCATTGGCTTCTTTGAGACTGAAATGGCAGCTTATAGGCTTTATACTGTGGTG
CCTCGCCTGGTCAAGTTTGTAGATATTCTGACCAATTGGTATGTTAGAATGAACCGCAGA
AGATTAAAGGGTGAAAATGGGATGGAGGATTGTGTCATGGCCCTAGAAACCTTGTTTAGT
GTTCTGCTTTCTCTTTGCAGACTTATGGCTCCCTACACACCTTTTCTCACTGAATTGATG
TACCAGAATCTAAAGGTGCTGATTGACCCTGTTTCTGTTCAGGACAAGGACACACTCAGC
ATTCACTACCTCATGCTGCCCCGTGTTCGAGAAGAATTGATTGACAAGAAAACAGAGAGT
GCAGTATCTCAGATGCAGTCTGTGATTGAACTTGGAAGAGTGATCAGAGACCGAAAAACT
ATTCCCATAAAGTATCCTTTGAAAGAAATTGTGGTTATCCATCAAGATCCAGAAGCTCTT
AAAGATATCAAGTCTTTGGAGAAGTATATCATTGAGGAACTCAATGTTCGAAAAGTTACA
CTGTCTACAGATAAAAACAAGTATGGCATTCGGCTAAGGGCAGAACCAGATCACATGGTC
CTGGGGAAGCGTCTGAAGGGAGCCTTTAAGGCAGTGATGACGTCCATCAAGCAGTTGAGC
AGTGAGGAGCTGGAGCAGTTCCAGAAGACTGGGACCATTGTTGTGGAAGGCCATGAATTG
CACGATGAAGACATCCGCCTCATGTACACCTTTGATCAGGCCACAGGTGGGACTGCGCAA
TTTGAAGCACACTCAGATGCTCAGGCTTTGGTCCTCTTAGATGTCACTCCTGACCAGTCA
ATGGTAGATGAAGGAATGGCTCGGGAAGTCATCAATCGCATACAGAAACTTCGCAAAAAG
TGCAATCTGGTTCCAACTGATGAAATCACAGTGTACTATAAAGCAAAGTCTGAAGGAACA
TATCTGAATAGTGTTATTGAAAGCCACACAGAGTTCATATTTACCACCATAAAGGCTCCC
TTGAAACCATATCCAGTTTCTCCATCGGATAAAGTCCTTATTCAAGAAAAAACACAGTTG
AAGGGATCTGAACTGGAAATTACACTCACCAGAGGATCTTCCCTTCCTGGTCCTGCTTGT
GCATATGTCAATCTTAACATTTGTGCAAATGGCAGTGAACAAGGTGGAGTATTGCTCCTG
GAAAATCCAAAAGGTGACAATAGGTTGGACCTTTTAAAGCTGAAGAGTGTTGTCACTAGC
ATTTTTGGTGTGAAAAATACAGAGCTGGCTGTCTTCCATGATGAAACAGAAATACAAAAC
CAAACTGACTTACTGAGTCTTAGTGGAAAAACACTTTGTGTGACTGCAGGATCGGCTCCC
TCTCTGATCAACAGTTCTAGTACTCTTCTTTGTCAGTATATCAACCTACAGCTCCTGAAT
GCAAAGCCACAAGAGTGTTTAATGGGGACAGTGGGCACTCTCCTGCTTGAAAACCCACTT
GGGCAGAATGGGCTCACCCACCAAGGTCTTCTGTATGAAGCAGCCAAGGTGTTTGGCCTT
CGGAGCAGGAAGCTAAAGCTGTTTCTGAATGAGACCCAAACGCAGGAAATTACAGAAGAC
ATCCCCGTGAAGACTTTGAATATGAAGACTGTGTATGTTTCTGTGTTACCAACAACAGCA
GACTTCTAG
|
| Enzyme 79 GenBank Gene ID |
AK293014 |
| Enzyme 79 GeneCard ID |
IARS |
| Enzyme 79 GenAtlas ID |
IARS |
| Enzyme 79 HGNC ID |
HGNC:5330 |
| Enzyme 79 Chromosome Location |
9 |
| Enzyme 79 Locus |
9q21 |
| Enzyme 79 SNPs |
SNPJam Report |
| Enzyme 79 General References |
- Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T: Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7435-9. [PubMed ]
- Nichols RC, Raben N, Boerkoel CF, Plotz PH: Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension. Gene. 1995 Apr 3;155(2):299-304. [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 ]
- 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 ]
- 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 ]
- 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 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
5890 |
| Enzyme 80 Name |
Ubiquitin-like modifier-activating enzyme 1 |
| Enzyme 80 Synonyms |
- Protein A1S9
- Ubiquitin-activating enzyme E1
|
| Enzyme 80 Gene Name |
UBA1 |
| Enzyme 80 Protein Sequence |
>Ubiquitin-like modifier-activating enzyme 1
MSSSPLSKKRRVSGPDPKPGSNCSPAQSVLSEVPSVPTNGMAKNGSEADIDEGLYSRQLY
VLGHEAMKRLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTAQWADLSSQFYLRE
EDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNTPLEDQLRVGEFCH
NRGIKLVVADTRGLFGQLFCDFGEEMILTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARH
GFESGDFVSFSEVQGMVELNGNQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKK
ISFKSLVASLAEPDFVVTDFAKFSRPAQLHIGFQALHQFCAQHGRPPRPRNEEDAAELVA
LAQAVNARALPAVQQNNLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPI
MQWLYFDALECLPEDKEVLTEDKCLQRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIG
CELLKNFAMIGLGCGEGGEIIVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMN
PHIRVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGT
LGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPA
ENVNQYLTDPKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWADCVTWACHHWHTQYSN
NIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNPLHLDYVMAAANLFAQTYGLTG
SQDRAAVATFLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLP
GFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDIPSADRHKSKLIAGKIIPAIATTTAA
VVGLVCLELYKVVQGHRQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEV
QGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVS
RVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
|
| Enzyme 80 Number of Residues |
1058 |
| Enzyme 80 Molecular Weight |
117848.1 |
| Enzyme 80 Theoretical pI |
5.50 |
| Enzyme 80 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- purine nucleoside binding
- small protein activating enzyme activity
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein modification process
|
| Component |
| — |
|
| Enzyme 80 General Function |
Involved in catalytic activity |
| Enzyme 80 Specific Function |
Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP |
| 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 |
35830 |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
P22314 |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
UBA1_HUMAN |
| Enzyme 80 PDB ID |
1Z7L |
| Enzyme 80 PDB File |
Show |
| Enzyme 80 3D Structure |
|
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
>3177 bp
ATGTCCAGCTCGCCGCTGTCCAAGAAACGTCGCGTGTCCGGGCCTGATCCAAAGCCGGGT
TCTAACTGCTCCCCTGCCCAGTCCGTGTTGTCCGAAGTGCCCTCGGTGCCAACCAACGGA
ATGGCCAAGAACGGCAGTGAAGCAGACATAGACGAGGGCCTTTACTCCCGGCAGCTGTAT
GTGTTGGGCCATGAGGCAATGAAGCGGCTCCAGACATCCAGTGTCCTGGTATCAGGCCTG
CGGGGCCTGGGCGTGGAGATCGCTAAGAACATCATCCTTGGTGGGGTCAAGGCTGTTACC
CTACATGACCAGGGCACTGCCCAGTGGGCTGATCTTTCCTCCCAGTTCTACCTGCGGGAG
GAGGACATCGGTAAAAACCGGGCCGAGGTATCACAGCCCCGCCTCGCTGAGCTCAACAGC
TATGTGCCTGTCACTGCCTACACTGGACCCCTCGTTGAGGACTTCCTTAGTGGTTTCCAG
GTGGTGGTGCTCACCAACACCCCCCTGGAGGACCAGCTGCGAGTGGGTGAGTTCTGTCAC
AACCGTGGCATCAAGCTGGTGGTGGCAGGCACGCGGGGCCTGTTTGGGCAGCTCTTCTGT
GACTTTGGAGAGGAAATGATCCTCACAGATTCCAATGGGGAGCAGCCACTCAGTGCTATG
GTTTCTATGGTTACCAAGGACAACCCCGGTGTGGTTACCTGCCTGGATGAGGCCCGACAC
GGGTTTGAGAGCGGGGACTTTGTCTCCTTTTCAGAAGTACAGGGCATGGTTGAACTCAAC
GGAAATCAGCCCATGGAGATCAAAGTCCTGGGTCCTTATACCTTTAGCATCTGTGACACC
TCCAACTTCTCCGACTACATCCGTGGAGGCATCGTCAGTCAGGTCAAAGTACCTAAGAAG
ATTAGCTTTAAATCCTTGGTGGCCTCACTGGCAGAACCTGACTTTGTGGTGACGGACTTC
GCCAAGTTTTCTCGCCCTGCCCAGCTGCACATTGGCTTCCAGGCCCTGCACCAGTTCTGT
GCTCAGCATGGCCGGCCACCTCGGCCCCGCAATGAGGAGGATGCAGCAGAACTGGTAGCC
TTAGCACAGGCTGTGAATGCTCGAGCCCTGCCAGCAGTGCAGCAAAATAACCTGGACGAG
GACCTCATCCGGAAGCTGGCATATGTGGCTGCTGGGGATCTGGCACCCATAAACGCCTTC
ATTGGGGGCCTGGCTGCCCAGGAAGTCATGAAGGCCTGCTCCGGGAAGTTCATGCCCATC
ATGCAGTGGCTATACTTTGATGCCCTTGAGTGTCTCCCTCAGGACAAAGAGGTCCTCACA
GAGGACAAGTGCCTCCAGCGCCAGAACCGTTATGACGGGCAAGTGGCTGTGTTTGGCTCA
GACCTGCAAGAGAAGCTGGGCAAGCAGAAGTATTTCCTGGTGGGTGCGGGGGCCATTGGC
TGTGAGCTGCTCAAGAACTTTGCCATGATTGGGCTGGGCTGCGGGGAGGGTGGAGAAATC
ATCGTTACAGACATGGACACCATTGAGAAGTCAAATCTGAATCGACAGTTTCTTTTCCGG
CCCTGGGATGTCACGAAGTTAAAGTCTGACACGGCTGCTGCAGCTGTGCGCCAAATGAAT
CCACATATCCGGGTGACAAGCCACCAGAACCGTGTGGGTCCTGACACGGAGCGCATCTAT
GATGACGATTTTTTCCAAAACCTAGATGGCGTGGCCAATGCCCTGGACAACGTGGATGCC
CGCATGTACATGGACCGCCGCTGTGTCTACTACCGGAAGCCACTGCTGGAGTCAGGCACA
CTGGGCACCAAAGGCAATGTGCAGGTGGTGATCCCCTTCCTGACAGAGTCGTACAGTTCC
AGCCAGGACCCACCTGAGAAGTCCATCCCCATCTGTACCCTGAAGAACTTCCCTAATGCC
ATCGAGCACACCCTGCAGTGGGCTCGGGATGAGTTTGAAGGCCTCTTCAAGCAGCCAGCA
GAAAATGTCAACCAGTACCTCACAGACCCCAAGTTTGTGGAGCGAACACTGCGGCTGGCA
GGCACTCAGCCCTTGGAGGTGCTGGAGGCTGTGCAGCGCAGCCTGGTGCTGCAGCGACCA
CAGACCTGGGCTGACTGCGTGACCTGGGCCTGCCACCACTGGCACACCCAGTACTCGAAC
AACATCCGGCAGCTGCTGCACAACTTCCCTCCTGACCAGCTCACAAGCTCAGGAGCGCCG
TTCTGGTCTGGGCCCAAACGCTGTCCACACCCGCTCACCTTTGATGTCAACAATCCCCTG
CATCTGGACTATGTGATGGCTGCTGCCAACCTGTTTGCCCAGACCTACGGGCTGACAGGC
TCTCAGGACCGAGCTGCTGTGGCCACATTCCTGCAGTCTGTGCAGGTCCCCGAATTCACC
CCCAAGTCTGGCGTCAAGATCCATGTTTCTGACCAGGAGCTGCAGAGCGCCAATGCCTCT
GTTGATGACAGTCGTCTAGAGGAGCTCAAAGCCACTCTGCCCAGCCCAGACAAGCTCCCT
GGATTCAAGATGTACCCCATTGACTTTGAGAAGGATGATGACAGCAACTTTCATATGGAT
TTCATCGTGGCTGCATCCAACCTCCGGGCAGAAAACTATGACATTCCTTCTGCAGACCGG
CACAAGAGCAAGCTGATTGCAGGGAAGATCATCCCAGCCATTGCCACGACCACAGCAGCC
GTGGTTGGCCTTGTGTGTCTGGAGCTGTACAAGGTTGTGCAGGGGCACCGACAGCTTGAC
TCCTACAAGAATGGTTTCCTCAACTTGGCCCTGCCTTTCTTTGGTTTCTCTGAACCCCTT
GCCGCACCACGTCACCAGTACTATAACCAAGAGTGGACATTGTGGGATCGCTTTGAGGTA
CAAGGGCTGCAGCCTAATGGTGAGGAGATGACCCTCAAACAGTTCCTCGACTATTTTAAG
ACAGAGCACAAATTAGAGATCACCATGCTGTCCCAGGGCGTGTCCATGCTCTATTCCTTC
TTCATGCCAGCTGCCAAGCTCAAGGAACGGTTGGATCAGCCGATGACAGAGATTGTGAGC
CGTGTGTCGAAGCGAAAGCTGGGCCGCCACGTGCGGGCGCTGGTGCTTGAGCTGTGCTGT
AACGACGAGAGCGGCGAGGATGTCGAGGTTCCCTATGTCCGATACACCATCCGCTGA
|
| Enzyme 80 GenBank Gene ID |
X56976 |
| Enzyme 80 GeneCard ID |
UBA1 |
| Enzyme 80 GenAtlas ID |
UBA1 |
| Enzyme 80 HGNC ID |
HGNC:12469 |
| Enzyme 80 Chromosome Location |
Not Available |
| Enzyme 80 Locus |
Not Available |
| Enzyme 80 SNPs |
SNPJam Report |
| Enzyme 80 General References |
- Ayusawa D, Kaneda S, Itoh Y, Yasuda H, Murakami Y, Sugasawa K, Hanaoka F, Seno T: Complementation by a cloned human ubiquitin-activating enzyme E1 of the S-phase-arrested mouse FM3A cell mutant with thermolabile E1. Cell Struct Funct. 1992 Apr;17(2):113-22. [PubMed ]
- Handley PM, Mueckler M, Siegel NR, Ciechanover A, Schwartz AL: Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):258-62. [PubMed ]
- Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7456. [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 ]
- Zacksenhaus E, Sheinin R: Molecular cloning, primary structure and expression of the human X linked A1S9 gene cDNA which complements the ts A1S9 mouse L cell defect in DNA replication. EMBO J. 1990 Sep;9(9):2923-9. [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 ]
- Allen E, Ding J, Wang W, Pramanik S, Chou J, Yau V, Yang Y: Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival. Nature. 2005 Nov 10;438(7065):224-8. Epub 2005 Oct 16. [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 ]
- 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 ]
- Ramser J, Ahearn ME, Lenski C, Yariz KO, Hellebrand H, von Rhein M, Clark RD, Schmutzler RK, Lichtner P, Hoffman EP, Meindl A, Baumbach-Reardon L: Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy. Am J Hum Genet. 2008 Jan;82(1):188-93. [PubMed ]
|
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
5891 |
| Enzyme 81 Name |
Tyrosyl-tRNA synthetase, mitochondrial |
| Enzyme 81 Synonyms |
- Tyrosine--tRNA ligase
- TyrRS
|
| Enzyme 81 Gene Name |
YARS2 |
| Enzyme 81 Protein Sequence |
>Tyrosyl-tRNA synthetase, mitochondrial
MAAPILRSFSWGRWSGTLNLSVLLPLGLRKAHSGAQGLLAAQKARGLFKDFFPETGTKIE
LPELFDRGTASFPQTIYCGFDPTADSLHVGHLLALLGLFHLQRAGHNVIALVGGATARLG
DPSGRTKEREALETERVRANARALRLGLEALAANHQQLFTDGRSWGSFTVLDNSAWYQKQ
HLVDFLAAVGGHFRMGTLLSRQSVQLRLKSPEGMSLAEFFYQVLQAYDFYYLFQRYGCRV
QLGGSDQLGNIMSGYEFINKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNRDKTSPF
ELYQFFVRQPDDSVERYLKLFTFLPLPEIDHIMQLHVKEPERRGPQKRLAAEVTKLVHGR
EGLDSAKRCTQALYHSSIDALEVMSDQELKELFKEAPFSEFFLDPGTSVLDTCRKANAIP
DGPRGYRMITEGGVSINHQQVTNPESVLIVGQHILKNGLSLLKIGKRNFYIIKWLQL
|
| Enzyme 81 Number of Residues |
477 |
| Enzyme 81 Molecular Weight |
53198.6 |
| Enzyme 81 Theoretical pI |
9.34 |
| Enzyme 81 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- tyrosine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
- tyrosyl-tRNA aminoacylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 81 General Function |
Involved in nucleotide binding |
| Enzyme 81 Specific Function |
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction:tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) |
| Enzyme 81 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Phenylalanine and Tyrosine Metabolism (map00400 )
|
| Enzyme 81 Reactions |
- ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr [RN:R02918]
|
| Enzyme 81 Pfam Domain Function |
|
| Enzyme 81 Signals |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
94681057 |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
Q9Y2Z4 |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
SYYM_HUMAN |
| Enzyme 81 PDB ID |
Not Available |
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
>1434 bp
ATGGCGGCGCCCATCTTGCGGTCCTTTTCCTGGGGCCGGTGGTCTGGTACCCTAAATCTC
TCAGTATTGTTGCCCTTGGGGCTGCGTAAGGCCCACTCGGGCGCTCAGGGGTTACTGGCA
GCGCAGAAGGCTCGAGGTCTGTTCAAGGACTTCTTCCCGGAGACGGGGACGAAAATAGAG
CTCCCAGAGCTCTTCGACCGTGGCACGGCGAGTTTTCCCCAAACCATTTACTGTGGCTTC
GACCCCACGGCAGACTCGCTTCATGTGGGTCATCTACTTGCGCTGCTGGGCCTGTTTCAT
TTGCAGCGAGCGGGCCACAACGTGATCGCGCTGGTGGGAGGCGCCACGGCGCGCCTGGGA
GACCCGAGCGGCCGTACCAAGGAACGCGAGGCGCTGGAGACAGAGCGCGTGCGAGCCAAC
GCGCGAGCTCTGCGCCTAGGGCTTGAGGCCCTGGCGGCTAATCACCAGCAGCTTTTCACT
GATGGGCGCTCCTGGGGCAGCTTCACTGTGCTGGACAACTCGGCCTGGTACCAGAAGCAG
CACCTGGTGGACTTCCTGGCGGCAGTGGGGGGTCACTTCCGCATGGGGACGCTGCTGAGC
CGGCAGAGCGTGCAGCTGCGGCTCAAGAGCCCCGAGGGCATGAGCTTGGCCGAGTTCTTT
TACCAGGTGCTCCAGGCCTATGACTTCTATTACCTCTTCCAGCGTTATGGATGCAGGGTC
CAGCTGGGCGGATCTGATCAACTAGGCAACATCATGTCCGGATATGAGTTCATCAACAAG
TTGACTGGAGAAGATGTATTTGGAATCACCGTTCCTCTAATTACAAGTACAACTGGAGCA
AAGCTGGGAAAGTCTGCTGGCAACGCTGTTTGGCTAAACAGAGATAAGACATCTCCATTT
GAATTGTATCAATTCTTTGTCAGGCAACCGGACGATTCAGTGGAAAGGTACCTGAAGCTG
TTCACTTTCCTGCCCCTTCCAGAGATTGATCATATCATGCAGCTGCATGTCAAAGAGCCA
GAAAGGCGGGGTCCTCAGAAACGACTGGCAGCAGAAGTAACAAAGCTTGTTCATGGACGA
GAAGGATTGGATTCTGCTAAAAGGTGTACACAAGCCCTTTATCACAGTAGCATAGATGCA
CTGGAGGTCATGTCTGATCAGGAGTTAAAAGAGTTGTTTAAAGAAGCTCCATTTTCTGAA
TTTTTTCTCGATCCTGGAACAAGTGTCCTAGATACTTGCCGCAAAGCAAATGCCATTCCA
GATGGTCCCCGAGGGTATCGAATGATAACAGAAGGCGGAGTCAGCATAAATCACCAACAA
GTAACAAATCCTGAGAGTGTTTTAATTGTTGGACAACATATTCTCAAGAATGGACTTTCC
TTACTTAAAATAGGAAAAAGAAATTTCTACATTATAAAATGGCTTCAGTTGTGA
|
| Enzyme 81 GenBank Gene ID |
NM_001040436.1 |
| Enzyme 81 GeneCard ID |
YARS2 |
| Enzyme 81 GenAtlas ID |
YARS2 |
| Enzyme 81 HGNC ID |
HGNC:24249 |
| Enzyme 81 Chromosome Location |
1 |
| Enzyme 81 Locus |
12p11.21 |
| Enzyme 81 SNPs |
SNPJam Report |
| Enzyme 81 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 ]
- 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 ]
- Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [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 ]
- 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 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
5892 |
| Enzyme 82 Name |
Ubiquitin-conjugating enzyme E2 E1 |
| Enzyme 82 Synonyms |
- UbcH6
- Ubiquitin carrier protein E1
- Ubiquitin-protein ligase E1
|
| Enzyme 82 Gene Name |
UBE2E1 |
| Enzyme 82 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 E1
MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAKRIQKELADIT
LDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFTPEYPFKPPKVTFRTRIY
HCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEH
DRMARQWTKRYAT
|
| Enzyme 82 Number of Residues |
193 |
| Enzyme 82 Molecular Weight |
21403.9 |
| Enzyme 82 Theoretical pI |
8.71 |
| Enzyme 82 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 82 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 82 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination |
| Enzyme 82 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 82 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 82 Pfam Domain Function |
|
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
189054583 |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
P51965 |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
UB2E1_HUMAN |
| Enzyme 82 PDB ID |
1Y6L |
| Enzyme 82 PDB File |
Show |
| Enzyme 82 3D Structure |
|
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>582 bp
ATGTCGGATGACGATTCGAGGGCCAGCACCAGCTCCTCCTCATCTTCGTCTTCCAACCAG
CAAACCGAGAAAGAAACAAACACCCCCAAGAAGAAGGAGAGTAAAGTCAGCATGAGCAAA
AACTCCAAACTCCTCTCCACCAGCGCCAAGAGAATTCAGAAGGAGCTGGCGGACATCACT
TTAGACCCTCCACCTAATTGCAGTGCTGGTCCCAAAGGCGATAACATCTATGAATGGAGA
TCAACCATTCTAGGGCCTCCAGGATCCGTGTATGAGGGTGGTGTATTCTTTCTCGATATC
ACTTTTACACCAGAATATCCCTTCAAGCCTCCAAAGGTTACATTTCGGACAAGAATCTAT
CATTGTAATATTAACAGTCAAGGTGTTATTTGCTTGGACATATTGAAAGATAATTGGAGT
CCAGCACTAACCATTTCTAAAGTCCTCCTTTCTATCTGCTCACTTCTTACAGACTGTAAT
CCTGCCGACCCCTTGGTGGGAAGTATTGCCACTCAGTATATGACCAACAGAGCAGAACAT
GACAGAATGGCCAGACAGTGGACCAAGAGATACGCTACATAA
|
| Enzyme 82 GenBank Gene ID |
AK314854 |
| Enzyme 82 GeneCard ID |
UBE2E1 |
| Enzyme 82 GenAtlas ID |
UBE2E1 |
| Enzyme 82 HGNC ID |
HGNC:12477 |
| Enzyme 82 Chromosome Location |
3 |
| Enzyme 82 Locus |
3p24.2 |
| Enzyme 82 SNPs |
SNPJam Report |
| Enzyme 82 General References |
- Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M: Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J Biol Chem. 1996 Feb 2;271(5):2795-800. [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 ]
- Takeuchi T, Iwahara S, Saeki Y, Sasajima H, Yokosawa H: Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme. J Biochem. 2005 Dec;138(6):711-9. [PubMed ]
- Espinosa A, Oke V, Elfving A, Nyberg F, Covacu R, Wahren-Herlenius M: The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide. Exp Cell Res. 2008 Dec 10;314(20):3605-13. Epub 2008 Sep 25. [PubMed ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [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 ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
|
| Enzyme 82 Metabolite References |
Not Available |
|
Enzyme 83
[top]
|
| Enzyme 83 ID |
5893 |
| Enzyme 83 Name |
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] |
| Enzyme 83 Synonyms |
- Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
- Ap4A hydrolase
- Ap4Aase
- Diadenosine tetraphosphatase
- Nucleoside diphosphate-linked moiety X motif 2
- Nudix motif 2
|
| Enzyme 83 Gene Name |
NUDT2 |
| Enzyme 83 Protein Sequence |
>Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
|
| Enzyme 83 Number of Residues |
147 |
| Enzyme 83 Molecular Weight |
16829.1 |
| Enzyme 83 Theoretical pI |
5.06 |
| Enzyme 83 GO Classification |
| Function |
- bis(5'-nucleosyl)-tetraphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- nucleotide diphosphatase activity
- pyrophosphatase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 83 General Function |
Involved in hydrolase activity |
| Enzyme 83 Specific Function |
Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis |
| Enzyme 83 Pathways |
|
| Enzyme 83 Reactions |
- P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]
|
| Enzyme 83 Pfam Domain Function |
|
| Enzyme 83 Signals |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
55958893 |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
P50583 |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
AP4A_HUMAN |
| Enzyme 83 PDB ID |
1XSC |
| Enzyme 83 PDB File |
Show |
| Enzyme 83 3D Structure |
|
| Enzyme 83 Cellular Location |
Not Available |
| Enzyme 83 Gene Sequence |
>444 bp
ATGGCCTTGAGAGCATGTGGCTTGATCATCTTCCGAAGATGCCTCATTCCCAAAGTGGAC
AACAATGCAATTGAGTTTTTACTGCTGCAGGCATCAGATGGCATTCATCACTGGACTCCT
CCCAAAGGCCATGTGGAACCAGGAGAGGATGACTTGGAAACAGCCCTGAGGGAGACCCAA
GAGGAAGCAGGCATAGAAGCAGGCCAGCTGACCATTATTGAGGGGTTCAAAAGGGAACTC
AATTATGTGGCCAGGAACAAGCCTAAAACAGTCATTTACTGGCTGGCGGAGGTGAAGGAC
TATGACGTGGAGATCCGCCTCTCCCATGAGCACCAAGCCTACCGCTGGCTGGGGCTGGAG
GAGGCCTGCCAGTTGGCTCAGTTCAAGGAGATGAAGGCAGCGCTCCAAGAAGGACACCAG
TTTCTTTGCTCCATAGAGGCCTGA
|
| Enzyme 83 GenBank Gene ID |
AL356494 |
| Enzyme 83 GeneCard ID |
NUDT2 |
| Enzyme 83 GenAtlas ID |
NUDT2 |
| Enzyme 83 HGNC ID |
HGNC:8049 |
| Enzyme 83 Chromosome Location |
9 |
| Enzyme 83 Locus |
9p13 |
| Enzyme 83 SNPs |
SNPJam Report |
| Enzyme 83 General References |
- Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG: Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases. Biochem J. 1995 Nov 1;311 ( Pt 3):717-21. [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 ]
- Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR: Structure and substrate-binding mechanism of human Ap4A hydrolase. J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. [PubMed ]
|
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
5894 |
| Enzyme 84 Name |
Long-chain-fatty-acid--CoA ligase 6 |
| Enzyme 84 Synonyms |
- Long-chain acyl-CoA synthetase 6
- LACS 6
|
| Enzyme 84 Gene Name |
ACSL6 |
| Enzyme 84 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 6
MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
|
| Enzyme 84 Number of Residues |
697 |
| Enzyme 84 Molecular Weight |
77751.3 |
| Enzyme 84 Theoretical pI |
7.46 |
| Enzyme 84 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 84 General Function |
Involved in catalytic activity |
| Enzyme 84 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 84 Pathways |
|
| Enzyme 84 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 84 Pfam Domain Function |
|
| Enzyme 84 Signals |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
5702202 |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
Q9UKU0 |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
ACSL6_HUMAN |
| Enzyme 84 PDB ID |
Not Available |
| Enzyme 84 Cellular Location |
Not Available |
| Enzyme 84 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 84 GenBank Gene ID |
AF129166 |
| Enzyme 84 GeneCard ID |
ACSL6 |
| Enzyme 84 GenAtlas ID |
ACSL6 |
| Enzyme 84 HGNC ID |
HGNC:16496 |
| Enzyme 84 Chromosome Location |
5 |
| Enzyme 84 Locus |
5q31 |
| Enzyme 84 SNPs |
SNPJam Report |
| Enzyme 84 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 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
5895 |
| Enzyme 85 Name |
Methionyl-tRNA synthetase, cytoplasmic |
| Enzyme 85 Synonyms |
- Methionine--tRNA ligase
- MetRS
|
| Enzyme 85 Gene Name |
MARS |
| Enzyme 85 Protein Sequence |
>Methionyl-tRNA synthetase, cytoplasmic
MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLF
STSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRA
LTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQE
PCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAW
EKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRL
RQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTP
QQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDK
CGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQF
ITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWW
KNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGV
GVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMF
VSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ
VNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSI
LLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQ
QIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK
|
| Enzyme 85 Number of Residues |
900 |
| Enzyme 85 Molecular Weight |
101114.9 |
| Enzyme 85 Theoretical pI |
6.05 |
| Enzyme 85 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- methionine-tRNA ligase activity
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- methionyl-tRNA aminoacylation
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 85 General Function |
Involved in nucleotide binding |
| Enzyme 85 Specific Function |
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) |
| Enzyme 85 Pathways |
|
| Enzyme 85 Reactions |
- ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet [RN:R03659]
|
| Enzyme 85 Pfam Domain Function |
|
| Enzyme 85 Signals |
|
| Enzyme 85 Transmembrane Regions |
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
1702932 |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
P56192 |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
SYMC_HUMAN |
| Enzyme 85 PDB ID |
Not Available |
| Enzyme 85 Cellular Location |
Not Available |
| Enzyme 85 Gene Sequence |
>2703 bp
ATGAGACTGTTCGTGAGTGATGGCGTCCCGGGTTGCTTGCCGGTGCTGGCCGCCGCCGGG
AGAGCCCGGGGCAGAGCAGAGGTGCTGATCAGCACTGTAGGCCCGGAAGATTGTGTGGTC
CCGTTCCTGACCCGGCCTAAGGTCCCTGTCTTGCAGGTGGATAGCGGCAACTACCTCTTC
TCCACTAGTGCAATCTGCCGATATTTTTTTTTGTTATCTGGCTGGGAGCAAGATGACCTC
ACTAACCAGTGGCTGGAATGGGAAGCGACAGAGCTGCAGCCAGCTTTGTCTGCTCCCCTG
TACTATTTAGTGGTCCAAGGCAAGAAGGGGGAAGATGTTCTTGGTTCAGTGCGGAGAGCC
CTGACTCACATTGACCACAGCTTGAGTCGTCAGAACTGTCCTTTCCTGGCTGGGGAGACA
GAATCTCTAGCCGACATTGTTTTGTGGGGAGCCCAATACCCATTACTGCAAGATCCCGCC
TACCTCCCTGAGGAGCTGAGTGCCCTGCACAGCTGGTTCCAGACACTGAGTACCCAGGAA
CCATGTCAGCGAGCTGCAGAGACTGTACTGAAACAGCAAGGTGTCCTGGCTCTCCGGCCT
TACCTCCAAAAGCAGCCCCAGCCCAGCCCCGCTGAGGGAAGGGCTGTCACCAATGAGCCT
GAGGAGGAGGAGCTGGCTACCCTATCTGAGGAGGAGATTGCTATGGCTGTTACTGCTTGG
GAGAAGGGCCTAGAAAGTTTGCCCCCGCTGCGGCCCCAGCAGAATCCAGTGTTGCCTGTG
GCTGGAGAAAGGAATGTGCTCATCACCAGTGCCCTCCCTTACGTCAACAATGTCCCCCAC
CTTGGGAACATCATTGGTTGTGTGCTCAGTGCCGATGTCTTTGCCAGGTACTCTCGCCTC
CGCCAGTGGAACACCCTCTATCTGTGTGGGACAGATGAGTATGGTACAGCAACAGAGACC
AAGGCTCTGGAGGAGGGACTAACCCCCCAGGAGATCTGCGACAAGTACCACATCATCCAT
GCTGACATCTACCGCTGGTTTAACATTTCGTTTGATATTTTTGGTCGCACCACCACTCCA
CAGCAGACCAAAATCACCCAGGACATTTTCCAGCAGTTGCTGAAACGAGGTTTTGTGCTG
CAAGATACTGTGGAGCAACTGCGATGTGAGCACTGTGCTCGCTTCCTGGCTGACCGCTTC
GTGGAGGGCGTGTGTCCCTTCTGTGGCTATGAGGAGGCTCGGGGTGACCAGTGTGACAAG
TGTGGCAAGCTCATCAATGCTGTCGAGCTTAAGAAGCCTCAGTGTAAAGTCTGCCGATCA
TGCCCTGTGGTGCAGTCGAGCCAGCACCTGTTTCTGGACCTGCCTAAGCTGGAGAAGCGA
CTGGAGGAGTGGTTGGGGAGGACATTGCCTGGCAGTGACTGGACACCCAATGCCCAGTTT
ATCACCCGTTCTTGGCTTCGGGATGGCCTCAAGCCACGCTGCATAACCCGAGACCTCAAA
TGGGGAACCCCTGTACCCTTAGAAGGTTTTGAAGACAAGGTATTCTATGTCTGGTTTGAT
GCCACTATTGGCTATCTGTCCATCACAGCCAACTACACAGACCAGTGGGAGAGATGGTGG
AAGAACCCAGAGCAAGTGGACCTGTATCAGTTCATGGCCAAAGACAATGTTCCTTTCCAT
AGCTTAGTCTTTCCTTGCTCAGCCCTAGGAGCTGAGGATAACTATACCTTGGTCAGCCAC
CTCATTGCTACAGAGTACCTGAACTATGAGGATGGGAAATTCTCTAAGAGCCGCGGTGTG
GGAGTGTTTGGGGACATGGCCCAGGACACGGGGATCCCTGCTGACATCTGGCGCTTCTAT
CTGCTGTACATTCGGCCTGAGGGCCAGGACAGTGCTTTCTCCTGGACGGACCTGCTGCTG
AAGAATAATTCTGAGCTGCTTAACAACCTGGGCAACTTCATCAACAGAGCTGGGATGTTT
GTGTCTAAGTTCTTTGGGGGCTATGTGCCTGAGATGGTGCTCACCCCTGATGATCAGCGC
CTGCTGGGCCATGTCACCCTGGAGCTCCAGCACTATCACCAGCTACTTGAGAAGGTTCGG
ATCCGGGATGCCTTGCGCAGTATCCTCACCATATCTCGACATGGCAACCAATATATTCAG
GTGAATGAGCCCTGGAAGCGGATTAAAGGCAGTGAGGCTGACAGGCAACGGGCAGGAACA
GTGACTGGCTTGGCAGTGAATATAGCTGCCTTGCTCTCTGTCATGCTTCAGCCTTACATG
CCCACGGTTAGTGCCACAATCCAGGCCCAGCTGCAGCTCCCACCTCCAGCCTGCAGTATC
CTGCTGACAAACTTCCTGTGTACCTTACCAGCAGGACACCAGATTGGCACAGTCAGTCCC
TTGTTCCAAAAATTGGAAAATGACCAGATTGAAAGTTTAAGGCAGCGCTTTGGAGGGGGC
CAGGCAAAAACGTCCCCGAAGCCAGCAGTTGTAGAGACTGTTACAACAGCCAAGCCACAG
CAGATACAAGCGCTGATGGATGAAGTGACAAAACAAGGAAACATTGTCCGAGAACTGAAA
GCACAAAAGGCAGACAAGAACGAGGTTGCTGCGGAGGTGGCGAAACTCTTGGATCTAAAG
AAACAGTTGGCTGTAGCTGAGGGGAAACCCCCTGAAGCCCCTAAAGGCAAGAAGAAAAAG
TAA
|
| Enzyme 85 GenBank Gene ID |
X94754 |
| Enzyme 85 GeneCard ID |
MARS |
| Enzyme 85 GenAtlas ID |
MARS |
| Enzyme 85 HGNC ID |
HGNC:6898 |
| Enzyme 85 Chromosome Location |
1 |
| Enzyme 85 Locus |
12q13.2 |
| Enzyme 85 SNPs |
SNPJam Report |
| Enzyme 85 General References |
- Lage H, Dietel M: Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene. 1996 Oct 31;178(1-2):187-9. [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 ]
- 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 85 Metabolite References |
Not Available |
|
Enzyme 86
[top]
|
| Enzyme 86 ID |
5897 |
| Enzyme 86 Name |
Alanyl-tRNA synthetase, cytoplasmic |
| Enzyme 86 Synonyms |
- Alanine--tRNA ligase
- AlaRS
- Renal carcinoma antigen NY-REN-42
|
| Enzyme 86 Gene Name |
AARS |
| Enzyme 86 Protein Sequence |
>Alanyl-tRNA synthetase, cytoplasmic
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPS
HPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALE
LLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGD
TGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDT
GMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLAD
HARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDA
FPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGF
PVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEV
TDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGG
QIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRP
IMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMI
EAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSV
EFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAK
VKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKR
VLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKIT
CLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQ
LRLGDVKN
|
| Enzyme 86 Number of Residues |
968 |
| Enzyme 86 Molecular Weight |
106809.5 |
| Enzyme 86 Theoretical pI |
5.18 |
| Enzyme 86 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- alanine-tRNA ligase activity
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- alanyl-tRNA aminoacylation
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 86 General Function |
Involved in nucleotide binding |
| Enzyme 86 Specific Function |
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction:alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain |
| Enzyme 86 Pathways |
|
| Enzyme 86 Reactions |
- ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla [RN:R03038]
|
| Enzyme 86 Pfam Domain Function |
|
| Enzyme 86 Signals |
|
| Enzyme 86 Transmembrane Regions |
|
| Enzyme 86 Essentiality |
Not Available |
| Enzyme 86 GenBank ID Protein |
109148542 |
| Enzyme 86 UniProtKB/Swiss-Prot ID |
P49588 |
| Enzyme 86 UniProtKB/Swiss-Prot Entry Name |
SYAC_HUMAN |
| Enzyme 86 PDB ID |
Not Available |
| Enzyme 86 Cellular Location |
Not Available |
| Enzyme 86 Gene Sequence |
>2907 bp
ATGGACTCTACTCTAACAGCAAGTGAAATCCGGCAGCGATTTATAGATTTCTTCAAGAGG
AACGAGCATACGTATGTTCACTCGTCTGCCACCATCCCATTGGATGACCCCACTTTGCTC
TTTGCCAATGCAGGCATGAACCAGTTTAAACCCATTTTCCTGAACACAATTGACCCATCT
CACCCCATGGCAAAGCTGAGCAGAGCTGCCAATACCCAGAAGTGCATCCGGGCTGGGGGC
AAACATAATGACCTGGACGATGTGGGCAAGGATGTCTATCATCACACCTTCTTCGAGATG
CTGGGCTCTTGGTCTTTTGGAGATTACTTTAAGGAATTGGCATGTAAGATGGCTCTGGAA
CTCCTCACCCAAGAGTTTGGCATTCCCATTGAAAGACTTTATGTTACTTACTTTGGCGGG
GATGAAGCAGCTGGCTTAGAAGCAGATCTGGAATGCAAACAGATCTGGCAAAATTTGGGG
CTGGATGACACCAAAATCCTCCCAGGCAACATGAAGGATAACTTCTGGGAGATGGGTGAC
ACGGGCCCCTGTGGTCCTTGCAGTGAGATCCACTACGACCGGATTGGTGGTCGGGACGCC
GCACATCTTGTCAACCAGGACGACCCTAATGTGCTGGAGATCTGGAACCTTGTGTTCATC
CAGTATAACAGGGAAGCTGATGGCATTCTGAAACCTCTTCCCAAGAAAAGCATTGACACA
GGGATGGGCCTGGAACGACTGGTATCTGTGCTGCAGAATAAGATGTCCAACTATGACACT
GACCTTTTTGTCCCTTACTTTGAAGCCATTCAGAAGGGCACAGGTGCCCGACCATACACT
GGGAAAGTTGGTGCTGAGGATGCCGATGGGATTGACATGGCCTACCGGGTGCTGGCTGAC
CACGCTCGGACCATCACTGTGGCACTGGCTGATGGTGGCCGGCCTGACAACACAGGGCGT
GGATATGTGTTGAGACGGATTCTCCGCCGAGCTGTCCGATACGCCCATGAAAAGCTCAAT
GCCAGCAGGGGCTTCTTTGCTACGTTAGTGGATGTTGTCGTCCAGTCCCTGGGAGATGCA
TTTCCTGAGCTGAAGAAGGACCCAGACATGGTGAAGGACATCATTAATGAAGAAGAGGTG
CAGTTTCTCAAGACTCTCAGCAGAGGGCGTCGCATCCTGGACAGGAAAATTCAGAGCCTG
GGAGACAGCAAGACCATTCCCGGAGACACTGCTTGGCTCCTCTATGACACCTATGGGTTT
CCAGTGGATCTGACTGGACTGATTGCTGAAGAGAAGGGCCTGGTGGTAGACATGGATGGC
TTTGAAGAGGAGAGGAAACTGGCCCAGCTGAAATCACAGGGCAAGGGAGCTGGTGGGGAA
GACCTCATTATGCTGGACATTTACGCTATCGAAGAGCTCCGGGCACGGGGTCTGGAGGTC
ACAGATGATTCCCCAAAGTACAATTACCATTTGGACTCCAGTGGTAGCTATGTATTTGAG
AACACAGTGGCTACGGTGATGGCTCTGCGCAGGGAGAAGATGTTCGTGGAAGAGGTGTCC
ACAGGCCAGGAGTGTGGAGTGGTGCTGGACAAGACCTGTTTCTATGCTGAGCAAGGAGGC
CAGATCTATGACGAAGGCTACCTGGTGAAGGTGGATGACAGCAGTGAAGATAAAACAGAG
TTTACAGTGAAGAATGCTCAGGTCCGAGGAGGGTATGTGCTACACATTGGAACCATCTAC
GGTGACCTGAAAGTGGGGGATCAGGTCTGGCTGTTTATTGATGAGCCCCGACGAAGACCC
ATCATGAGCAACCACACAGCTACGCACATTCTGAACTTCGCCCTGCGCTCAGTGCTTGGG
GAAGCTGACCAGAAAGGCTCATTGGTTGCTCCTGACCGCCTCAGATTTGACTTTACTGCC
AAGGGAGCCATGTCCACCCAACAGATCAAGAAGGCTGAAGAGATTGCTAATGAGATGATT
GAGGCAGCCAAGGCCGTCTATACCCAGGATTGCCCCCTGGCAGCAGCGAAAGCCATCCAG
GGCCTACGGGCTGTGTTTGATGAGACCTATCCTGACCCTGTGCGAGTCGTCTCCATTGGG
GTCCCGGTGTCCGAGTTGCTGGATGACCCCTCTGGGCCTGCTGGCTCCCTGACTTCTGTT
GAGTTCTGTGGGGGAACGCACCTGCGGAACTCGAGTCATGCAGGAGCTTTTGTGATCGTG
ACGGAAGAAGCCATTGCCAAGGGTATCCGGAGGATTGTGGCTGTCACAGGTGCCGAGGCC
CAGAAGGCCCTCAGGAAAGCAGAGAGCTTGAAGAAATGTCTCTCTGTCATGGAAGCCAAA
GTGAAGGCTCAGACTGCTCCAAACAAGGATGTGCAGAGGGAGATCGCTGACCTTGGAGAG
GCCCTGGCCACTGCAGTCATCCCCCAGTGGCAGAAGGATGAATTGCGGGAGACTCTCAAA
TCCCTAAAGAAGGTCATGGATGACTTGGACCGAGCCAGCAAAGCCGATGTCCAGAAACGA
GTGTTAGAGAAGACGAAGCAGTTCATCGACAGCAACCCCAACCAGCCTCTTGTCATCCTG
GAGATGGAGAGCGGCGCCTCAGCCAAGGCCCTGAATGAAGCCTTGAAGCTCTTCAAGATG
CACTCCCCTCAGACTTCTGCCATGCTCTTCACGGTGGACAATGAGGCTGGCAAGATCACG
TGCCTGTGTCAAGTTCCCCAGAATGCAGCCAATCGGGGCTTAAAAGCCAGCGAGTGGGTG
CAGCAGGTGTCAGGCTTGATGGACGGTAAAGGTGGTGGCAAGGATGTGTCTGCACAGGCC
ACAGGCAAGAACGTTGGCTGCCTGCAGGAGGCGCTGCAGCTGGCCACTTCCTTCGCCCAG
CTGCGCCTCGGGGATGTAAAGAACTGA
|
| Enzyme 86 GenBank Gene ID |
NM_001605.2 |
| Enzyme 86 GeneCard ID |
AARS |
| Enzyme 86 GenAtlas ID |
AARS |
| Enzyme 86 HGNC ID |
HGNC:20 |
| Enzyme 86 Chromosome Location |
1 |
| Enzyme 86 Locus |
16q22 |
| Enzyme 86 SNPs |
SNPJam Report |
| Enzyme 86 General References |
- Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P: Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition. Biochemistry. 1995 Aug 22;34(33):10340-9. [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 ]
- 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 ]
- 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 ]
- 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 ]
- Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P: The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. [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 ]
- Latour P, Thauvin-Robinet C, Baudelet-Mery C, Soichot P, Cusin V, Faivre L, Locatelli MC, Mayencon M, Sarcey A, Broussolle E, Camu W, David A, Rousson R: A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. Am J Hum Genet. 2010 Jan;86(1):77-82. Epub 2009 Dec 31. [PubMed ]
|
| Enzyme 86 Metabolite References |
Not Available |
|
Enzyme 87
[top]
|
| Enzyme 87 ID |
5898 |
| Enzyme 87 Name |
Tryptophanyl-tRNA synthetase, mitochondrial |
| Enzyme 87 Synonyms |
- (Mt)TrpRS
- Tryptophan--tRNA ligase
- TrpRS
|
| Enzyme 87 Gene Name |
WARS2 |
| Enzyme 87 Protein Sequence |
>Tryptophanyl-tRNA synthetase, mitochondrial
MALHSMRKARERWSFIRALHKGSAAAPALQKDSKKRVFSGIQPTGILHLGNYLGAIESWV
RLQDEYDSVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQQSQVSEH
TQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGE
DQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDKLATVRI
TDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTA
RYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL
|
| Enzyme 87 Number of Residues |
360 |
| Enzyme 87 Molecular Weight |
40146.3 |
| Enzyme 87 Theoretical pI |
9.82 |
| Enzyme 87 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- tryptophan-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
- tryptophanyl-tRNA aminoacylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 87 General Function |
Involved in nucleotide binding |
| Enzyme 87 Specific Function |
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp) |
| Enzyme 87 Pathways |
|
| Enzyme 87 Reactions |
- ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp [RN:R03664]
|
| Enzyme 87 Pfam Domain Function |
|
| Enzyme 87 Signals |
|
| Enzyme 87 Transmembrane Regions |
|
| Enzyme 87 Essentiality |
Not Available |
| Enzyme 87 GenBank ID Protein |
6572289 |
| Enzyme 87 UniProtKB/Swiss-Prot ID |
Q9UGM6 |
| Enzyme 87 UniProtKB/Swiss-Prot Entry Name |
SYWM_HUMAN |
| Enzyme 87 PDB ID |
Not Available |
| Enzyme 87 Cellular Location |
Not Available |
| Enzyme 87 Gene Sequence |
>1083 bp
ATGGCGCTGCACTCAATGCGGAAAGCGCGTGAGCGCTGGAGCTTCATCCGGGCACTTCAT
AAGGGATCCGCAGCTGCTCCCGCTCTCCAGAAAGACAGCAAGAAGCGAGTATTTTCCGGC
ATTCAACCTACAGGAATCCTCCACCTGGGCAATTACCTGGGAGCCATTGAGAGCTGGGTG
AGGTTACAGGATGAATATGACTCTGTATTATACAGCATTGTTGACCTCCACTCCATTACT
GTCCCCCAAGACCCAGCTGTCCTTCGGCAGAGCATCCTGGACATGACTGCTGTTCTTCTT
GCCTGTGGCATAAACCCGGAAAAAAGCATCCTTTTCCAACAATCTCAGGTGTCTGAACAC
ACACAATTAAGTTGGATCCTTTCCTGCATGGTCAGACTACCTCGATTACAACATTTACAT
CAGTGGAAGGCAAAGACTACCAAGCAGAAGCACGATGGCACGGTGGGCCTGCTCACATAC
CCAGTACTCCAGGCAGCCGACATTCTGTTGTACAAGTCCACACACGTTCCTGTTGGGGAG
GATCAAGTCCAGCACATGGAACTAGTTCAGGATCTAGCACAAGGTTTCAACAAGAAGTAT
GGGGAGTTCTTTCCAGTGCCCGAGTCCATTCTCACATCCATGAAGAAGGTAAAATCCCTA
CGTGATCCTTCTGCCAAAATGTCGAAATCAGACCCTGACAAACTGGCCACCGTCCGAATA
ACAGACAGCCCAGAGGAGATAGTGCAGAAATTCCGCAAGGCTGTGACAGACTTCACCTCG
GAGGTCACCTATGACCCGGCTGGCCGCGCTGGCGTGTCCAACATAGTGGCGGTGCATGCC
GCGGTGACGGGGCTCTCCGTGGAGGAAGTGGTGCGCCGCAGCGCGGGCATGAACACTGCT
CGCTACAAGCTGGCCGTGGCAGATGCTGTGATTGAGAAGTTTGCCCCAATTAAGCGTGAA
ATTGAAAAACTGAAGCTGGACAAGGACCATTTAGAGAAGGTTTTACAAATTGGATCAGCA
AAAGCCAAAGAATTAGCATACACTGTGTGCCAGGAGGTGAAGAAATTGGTGGGTTTTCTA
TAG
|
| Enzyme 87 GenBank Gene ID |
AJ242739 |
| Enzyme 87 GeneCard ID |
WARS2 |
| Enzyme 87 GenAtlas ID |
WARS2 |
| Enzyme 87 HGNC ID |
HGNC:12730 |
| Enzyme 87 Chromosome Location |
1 |
| Enzyme 87 Locus |
1p12 |
| Enzyme 87 SNPs |
SNPJam Report |
| Enzyme 87 General References |
- Jorgensen R, Sogaard TM, Rossing AB, Martensen PM, Justesen J: Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase. J Biol Chem. 2000 Jun 2;275(22):16820-6. [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 87 Metabolite References |
Not Available |
|
Enzyme 88
[top]
|
| Enzyme 88 ID |
5900 |
| Enzyme 88 Name |
Ribose-phosphate pyrophosphokinase 1 |
| Enzyme 88 Synonyms |
- PPRibP
- Phosphoribosyl pyrophosphate synthase I
- PRS-I
|
| Enzyme 88 Gene Name |
PRPS1 |
| Enzyme 88 Protein Sequence |
>Ribose-phosphate pyrophosphokinase 1
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGC
GEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTS
IADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL
|
| Enzyme 88 Number of Residues |
318 |
| Enzyme 88 Molecular Weight |
34833.9 |
| Enzyme 88 Theoretical pI |
6.98 |
| Enzyme 88 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- diphosphotransferase activity
- ion binding
- magnesium ion binding
- metal ion binding
- ribose phosphate diphosphokinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular biosynthetic 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 metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide biosynthetic process
- nucleotide metabolic process
- ribonucleoside monophosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 88 General Function |
Involved in magnesium ion binding |
| Enzyme 88 Specific Function |
Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis |
| Enzyme 88 Pathways |
|
| Enzyme 88 Reactions |
- ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01049]
|
| Enzyme 88 Pfam Domain Function |
|
| Enzyme 88 Signals |
|
| Enzyme 88 Transmembrane Regions |
|
| Enzyme 88 Essentiality |
Not Available |
| Enzyme 88 GenBank ID Protein |
57208781 |
| Enzyme 88 UniProtKB/Swiss-Prot ID |
P60891 |
| Enzyme 88 UniProtKB/Swiss-Prot Entry Name |
PRPS1_HUMAN |
| Enzyme 88 PDB ID |
Not Available |
| Enzyme 88 Cellular Location |
Not Available |
| Enzyme 88 Gene Sequence |
>957 bp
ATGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCTCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGTGTGGAAATTGGTGAAAGTGTACGTGGAGAGGATGTCTACATTGTTCAGAGTGGTTGT
GGCGAAATCAATGACAATTTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCCAGCCGGGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGGCAGGATAAGAAA
GATAAGAGCCGGGCGCCAATCTCAGCCAAGCTTGTTGCAAATATGCTATCTGTAGCAGGT
GCAGATCATATTATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAATTTGTATGCAGAGCCGGCTGTCCTAAAGTGGATAAGGGAGAATATCTCT
GAGTGGAGGAACTGCACTATTGTCTCACCTGATGCTGGTGGAGCTAAGAGAGTGACCTCC
ATTGCAGACAGGCTGAATGTGGACTTTGCCTTGATTCACAAAGAACGGAAGAAGGCCAAT
GAAGTGGACCGCATGGTGCTTGTGGGAGATGTGAAGGATCGGGTGGCCATCCTTGTGGAT
GACATGGCTGACACTTGTGGCACAATCTGCCATGCAGCTGACAAACTTCTCTCAGCTGGC
GCCACCAGAGTTTATGCCATCTTGACTCATGGAATCTTCTCCGGTCCTGCTATTTCTCGC
ATCAACAACGCATGCTTTGAGGCAGTAGTAGTCACCAATACCATACCTCAGGAGGACAAG
ATGAAGCATTGCTCCAAAATACAGGTGATTGACATCTCTATGATCCTTGCAGAAGCCATC
AGGAGAACTCACAATGGAGAATCCGTTTCTTACCTATTCAGCCATGTCCCTTTATAA
|
| Enzyme 88 GenBank Gene ID |
AL137787 |
| Enzyme 88 GeneCard ID |
PRPS1 |
| Enzyme 88 GenAtlas ID |
PRPS1 |
| Enzyme 88 HGNC ID |
HGNC:9462 |
| Enzyme 88 Chromosome Location |
Not Available |
| Enzyme 88 Locus |
Not Available |
| Enzyme 88 SNPs |
SNPJam Report |
| Enzyme 88 General References |
- Roessler BJ, Bell G, Heidler S, Seino S, Becker M, Palella TD: Cloning of two distinct copies of human phosphoribosylpyrophosphate synthetase cDNA. Nucleic Acids Res. 1990 Jan 11;18(1):193. [PubMed ]
- Sonoda T, Taira M, Ishijima S, Ishizuka T, Iizasa T, Tatibana M: Complete nucleotide sequence of human phosphoribosyl pyrophosphate synthetase subunit I (PRS I) cDNA and a comparison with human and rat PRPS gene families. J Biochem (Tokyo). 1991 Feb;109(2):361-4. [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 ]
- Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed ]
- Li S, Lu Y, Peng B, Ding J: Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site. Biochem J. 2007 Jan 1;401(1):39-47. [PubMed ]
- Becker MA, Smith PR, Taylor W, Mustafi R, Switzer RL: The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity. J Clin Invest. 1995 Nov;96(5):2133-41. [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 ]
- de Brouwer AP, Williams KL, Duley JA, van Kuilenburg AB, Nabuurs SB, Egmont-Petersen M, Lugtenberg D, Zoetekouw L, Banning MJ, Roeffen M, Hamel BC, Weaving L, Ouvrier RA, Donald JA, Wevers RA, Christodoulou J, van Bokhoven H: Arts syndrome is caused by loss-of-function mutations in PRPS1. Am J Hum Genet. 2007 Sep;81(3):507-18. Epub 2007 Aug 3. [PubMed ]
- Kim HJ, Sohn KM, Shy ME, Krajewski KM, Hwang M, Park JH, Jang SY, Won HH, Choi BO, Hong SH, Kim BJ, Suh YL, Ki CS, Lee SY, Kim SH, Kim JW: Mutations in PRPS1, which encodes the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis, cause hereditary peripheral neuropathy with hearing loss and optic neuropathy (cmtx5). Am J Hum Genet. 2007 Sep;81(3):552-8. Epub 2007 Jun 29. [PubMed ]
- Liu X, Han D, Li J, Han B, Ouyang X, Cheng J, Li X, Jin Z, Wang Y, Bitner-Glindzicz M, Kong X, Xu H, Kantardzhieva A, Eavey RD, Seidman CE, Seidman JG, Du LL, Chen ZY, Dai P, Teng M, Yan D, Yuan H: Loss-of-function mutations in the PRPS1 gene cause a type of nonsyndromic X-linked sensorineural deafness, DFN2. Am J Hum Genet. 2010 Jan;86(1):65-71. [PubMed ]
|
| Enzyme 88 Metabolite References |
Not Available |
|
Enzyme 89
[top]
|
| Enzyme 89 ID |
5901 |
| Enzyme 89 Name |
Seryl-tRNA synthetase, mitochondrial |
| Enzyme 89 Synonyms |
- SerRSmt
- Serine--tRNA ligase
- SerRS
- Seryl-tRNA(Ser/Sec) synthetase
|
| Enzyme 89 Gene Name |
SARS2 |
| Enzyme 89 Protein Sequence |
>Seryl-tRNA synthetase, mitochondrial
MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDI
ERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRAL
LANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPV
GDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQH
GLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTA
EVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPG
LEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVT
SASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPA
LQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS
|
| Enzyme 89 Number of Residues |
518 |
| Enzyme 89 Molecular Weight |
58282.1 |
| Enzyme 89 Theoretical pI |
8.22 |
| Enzyme 89 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- serine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- seryl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 89 General Function |
Involved in nucleotide binding |
| Enzyme 89 Specific Function |
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) |
| Enzyme 89 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 89 Reactions |
- ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer [RN:R03662]
|
| Enzyme 89 Pfam Domain Function |
|
| Enzyme 89 Signals |
|
| Enzyme 89 Transmembrane Regions |
|
| Enzyme 89 Essentiality |
Not Available |
| Enzyme 89 GenBank ID Protein |
9188535 |
| Enzyme 89 UniProtKB/Swiss-Prot ID |
Q9NP81 |
| Enzyme 89 UniProtKB/Swiss-Prot Entry Name |
SYSM_HUMAN |
| Enzyme 89 PDB ID |
Not Available |
| Enzyme 89 Cellular Location |
Not Available |
| Enzyme 89 Gene Sequence |
>1557 bp
ATGGCTGCGTCCATGGCGCGGCGCTTGTGGCCTTTGCTGACTCGTCGGGGGTTCCGGCCC
CGGGGAGGCTGCATCTCCAACGATAGTCCAAGGAGAAGTTTCACTACAGAGAAACGAAAC
CGGAACCTCCTGTACGAGTATGCGCGCGAGGGCTACAGCGCACTCCCTCAGCTGGACATA
GAGCGGTTCTGCGCATGCCCAGAAGAGGCCGCACACGCCCTGGAGCTCCGCAAGGGGGAG
CTGCGCTCGGCGGACCTGCCCGCGATCATCTCGACATGGCAGGAGCTGAGGCAGCTGCAG
GAGCAGATCCGGAGCCTGGAGGAAGAGAAGGCAGCTGTGACTGAGGCAGTGCGGGCCCTG
CTGGCAAACCAGGACAGTGGTGAAGTGCAGCAGGACCCCAAGTACCAGGGTCTGCGGGCA
CGTGGCCGGGAGATCCGGAAGGAGCTTGTTCACCTGTACCCCAGGGAGGCCCAGCTTGAG
GAGCAGTTCTACCTGCAGGCGCTGAAGCTGCCCAACCAGACCCACCCAGACGTGCCCGTC
GGGGATGAGAGCCAGGCTCGAGTGCTCCACATGGTCGGAGACAAGCCAGTTTTCTCCTTC
CAACCTCGGGGCCACCTGGAAATTGGCGAGAAACTCGACATCATCCGTCAGAAGCGCCTG
TCCCACGTGTCTGGCCACCGGTCCTATTACCTGCGCGGGGCTGGAGCCCTCCTGCAGCAC
GGCCTGGTCAACTTCACATTCAACAAGCTTCTCCGCCGGGGCTTCACCCCCATGACGGTG
CCAGACCTTCTCCGCGGAGCAGTGTTTGAAGGCTGTGGGATGACACCAAATGCCAACCCA
TCCCAAATTTACAACATCGACCCTGCCCGCTTCAAAGATCTCAACCTGGCTGGAACAGCG
GAGGTGGGGCTTGCAGGCTACTTCATGGACCACACCGTGGCCTTCAGGGACCTGCCAGTC
AGGATGGTTTGCTCCAGCACCTGCTACCGGGCAGAGACAAACACGGGACAGGAACCCCGG
GGGCTGTATCGAGTACACCACTTCACCAAGGTGGAGATGTTTGGGGTGACAGGCCCTGGG
CTGGAGCAGAGCTCACAGCTGCTGGAGGAGTTCCTGTCCCTTCAGATGGAGATCTTGACA
GAGCTGGGCTTGCACTTCCGGGTCCTGGATATGCCCACCCAAGAACTGGGCCTCCCCGCC
TACCGCAAGTTTGACATTGAGGCCTGGATGCCAGGCCGAGGCCGCTTTGGAGAGGTCACC
AGTGCTTCCAACTGCACAGACTTCCAGAGCCGCCGCCTCCACATCATGTTCCAGACCGAG
GCTGGGGAGCTGCAGTTTGCCCACACGGTGAACGCCACCGCCTGTGCTGTCCCCCGCCTT
CTCATCGCGCTCCTGGAGAGTAACCAGCAGAAGGACGGCTCAGTGCTCGTGCCCCCTGCC
CTCCAGTCCTACCTCGGCACTGATCGGATCACAGCCCCTACCCACGTGCCTCTCCAGTAC
ATCGGCCCCAACCAGCCCCGGAAGCCTGGGCTGCCTGGCCAGCCTGCTGTAAGCTAA
|
| Enzyme 89 GenBank Gene ID |
AB029948 |
| Enzyme 89 GeneCard ID |
SARS2 |
| Enzyme 89 GenAtlas ID |
SARS2 |
| Enzyme 89 HGNC ID |
HGNC:17697 |
| Enzyme 89 Chromosome Location |
1 |
| Enzyme 89 Locus |
19q13.2 |
| Enzyme 89 SNPs |
SNPJam Report |
| Enzyme 89 General References |
- Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K: Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem. 2000 Jun 30;275(26):19913-20. [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 ]
- 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 ]
|
| Enzyme 89 Metabolite References |
Not Available |
|
Enzyme 90
[top]
|
| Enzyme 90 ID |
5904 |
| Enzyme 90 Name |
Ribose-phosphate pyrophosphokinase 2 |
| Enzyme 90 Synonyms |
- PPRibP
- Phosphoribosyl pyrophosphate synthase II
- PRS-II
|
| Enzyme 90 Gene Name |
PRPS2 |
| Enzyme 90 Protein Sequence |
>Ribose-phosphate pyrophosphokinase 2
MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGC
GEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRVTS
IADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCTKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL
|
| Enzyme 90 Number of Residues |
318 |
| Enzyme 90 Molecular Weight |
34768.8 |
| Enzyme 90 Theoretical pI |
6.60 |
| Enzyme 90 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- diphosphotransferase activity
- ion binding
- magnesium ion binding
- metal ion binding
- ribose phosphate diphosphokinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular biosynthetic 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 metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide biosynthetic process
- nucleotide metabolic process
- ribonucleoside monophosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 90 General Function |
Involved in magnesium ion binding |
| Enzyme 90 Specific Function |
Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis |
| Enzyme 90 Pathways |
|
| Enzyme 90 Reactions |
- ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01049]
|
| Enzyme 90 Pfam Domain Function |
|
| Enzyme 90 Signals |
|
| Enzyme 90 Transmembrane Regions |
|
| Enzyme 90 Essentiality |
Not Available |
| Enzyme 90 GenBank ID Protein |
4506129 |
| Enzyme 90 UniProtKB/Swiss-Prot ID |
P11908 |
| Enzyme 90 UniProtKB/Swiss-Prot Entry Name |
PRPS2_HUMAN |
| Enzyme 90 PDB ID |
Not Available |
| Enzyme 90 Cellular Location |
Not Available |
| Enzyme 90 Gene Sequence |
>957 bp
ATGCCCAACATCGTGCTGTTCAGCGGCAGCTCGCATCAGGACCTGTCCCAGCGCGTGGCC
GACCGCCTGGGCCTGGAGCTGGGCAAGGTGGTCACGAAGAAGTTCAGCAACCAGGAGACC
AGCGTGGAGATTGGTGAAAGCGTGAGAGGGGAAGATGTCTACATCATCCAGAGCGGCTGC
GGGGAAATTAACGACAACCTGATGGAACTCCTCATCATGATCAATGCCTGCAAGATTGCG
TCATCATCCAGAGTAACTGCCGTGATCCCGTGTTTCCCATACGCCCGACAAGATAAAAAG
GACAAGAGTCGTGCCCCAATTTCTGCAAAACTTGTGGCCAATATGCTGTCGGTGGCTGGG
GCGGATCACATCATCACCATGGACCTGCATGCTTCTCAGATACAGGGATTCTTTGATATT
CCTGTGGATAATTTGTATGCGGAGCCCGCAGTCCTGCAGTGGATTCGGGAAAACATTGCC
GAGTGGAAGAACTGTATCATTGTTTCACCTGACGCAGGGGGAGCCAAAAGGGTTACATCA
ATTGCAGACAGGTTGAATGTGGAATTTGCTTTGATCCACAAAGAGAGGAAGAAGGCGAAT
GAAGTGGACCGGATGGTCCTGGTGGGCGACGTGAAGGACCGTGTGGCCATCCTCGTGGAT
GACATGGCTGACACTTGCGGCACCATCTGCCATGCTGCGGACAAGCTGCTGTCAGCTGGA
GCCACCAAAGTGTATGCTATCCTTACCCATGGGATCTTCTCTGGACCAGCTATTTCCAGA
ATAAATAATGCCGCCTTTGAGGCTGTTGTCGTCACAAACACAATTCCGCAAGAGGACAAA
ATGAAACACTGCACCAAGATTCAGGTCATTGACATTTCCATGATCTTGGCCGAAGCAATC
CGAAGGACACACAATGGGGAATCCGTGTCCTACCTGTTCAGCCATGTCCCGCTATAA
|
| Enzyme 90 GenBank Gene ID |
NM_002765.4 |
| Enzyme 90 GeneCard ID |
PRPS2 |
| Enzyme 90 GenAtlas ID |
PRPS2 |
| Enzyme 90 HGNC ID |
HGNC:9465 |
| Enzyme 90 Chromosome Location |
Not Available |
| Enzyme 90 Locus |
Not Available |
| Enzyme 90 SNPs |
SNPJam Report |
| Enzyme 90 General References |
- Iizasa T, Taira M, Shimada H, Ishijima S, Tatibana M: Molecular cloning and sequencing of human cDNA for phosphoribosyl pyrophosphate synthetase subunit II. FEBS Lett. 1989 Feb 13;244(1):47-50. [PubMed ]
- Iizasa T, Taira M, Shimada H, Tatibana M: Deduced amino acid sequence from human phosphoribosylpyrophosphate synthetase subunit II cDNA. Adv Exp Med Biol. 1989;253A:519-23. [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 T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed ]
|
| Enzyme 90 Metabolite References |
Not Available |
|
Enzyme 91
[top]
|
| Enzyme 91 ID |
5907 |
| Enzyme 91 Name |
SUMO-conjugating enzyme UBC9 |
| Enzyme 91 Synonyms |
- SUMO-protein ligase
- Ubiquitin carrier protein 9
- Ubiquitin carrier protein I
- Ubiquitin-conjugating enzyme E2 I
- Ubiquitin-protein ligase I
- p18
|
| Enzyme 91 Gene Name |
UBE2I |
| Enzyme 91 Protein Sequence |
>SUMO-conjugating enzyme UBC9
MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKL
RMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELL
NEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
|
| Enzyme 91 Number of Residues |
158 |
| Enzyme 91 Molecular Weight |
18006.7 |
| Enzyme 91 Theoretical pI |
8.90 |
| Enzyme 91 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 91 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 91 Specific Function |
Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation |
| 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 |
4507785 |
| Enzyme 91 UniProtKB/Swiss-Prot ID |
P63279 |
| Enzyme 91 UniProtKB/Swiss-Prot Entry Name |
UBC9_HUMAN |
| Enzyme 91 PDB ID |
1KPS |
| Enzyme 91 PDB File |
Show |
| Enzyme 91 3D Structure |
|
| Enzyme 91 Cellular Location |
Not Available |
| Enzyme 91 Gene Sequence |
>477 bp
ATGTCGGGGATCGCCCTCAGCAGACTCGCCCAGGAGAGGAAAGCATGGAGGAAAGACCAC
CCATTTGGTTTCGTGGCTGTCCCAACAAAAAATCCCGATGGCACGATGAACCTCATGAAC
TGGGAGTGCGCCATTCCAGGAAAGAAAGGGACTCCGTGGGAAGGAGGCTTGTTTAAACTA
CGGATGCTTTTCAAAGATGATTATCCATCTTCGCCACCAAAATGTAAATTCGAACCACCA
TTATTTCACCCGAATGTGTACCCTTCGGGGACAGTGTGCCTGTCCATCTTAGAGGAGGAC
AAGGACTGGAGGCCAGCCATCACAATCAAACAGATCCTATTAGGAATACAGGAACTTCTA
AATGAACCAAATATCCAAGACCCAGCTCAAGCAGAGGCCTACACGATTTACTGCCAAAAC
AGAGTGGAGTACGAGAAAAGGGTCCGAGCACAAGCCAAGAAGTTTGCGCCCTCATAA
|
| Enzyme 91 GenBank Gene ID |
NM_003345.3 |
| Enzyme 91 GeneCard ID |
UBE2I |
| Enzyme 91 GenAtlas ID |
UBE2I |
| Enzyme 91 HGNC ID |
HGNC:12485 |
| Enzyme 91 Chromosome Location |
1 |
| Enzyme 91 Locus |
16p13.3 |
| Enzyme 91 SNPs |
SNPJam Report |
| Enzyme 91 General References |
- Yasugi T, Howley PM: Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9. Nucleic Acids Res. 1996 Jun 1;24(11):2005-10. [PubMed ]
- Tachibana M, Iwata N, Watanabe A, Nobukuni Y, Ploplis B, Kajigaya S: Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization. Cytogenet Cell Genet. 1996;75(4):222-3. [PubMed ]
- Watanabe TK, Fujiwara T, Kawai A, Shimizu F, Takami S, Hirano H, Okuno S, Ozaki K, Takeda S, Shimada Y, Nagata M, Takaichi A, Takahashi E, Nakamura Y, Shin S: Cloning, expression, and mapping of UBE2I, a novel gene encoding a human homologue of yeast ubiquitin-conjugating enzymes which are critical for regulating the cell cycle. Cytogenet Cell Genet. 1996;72(1):86-9. [PubMed ]
- Masson M, Menissier-de Murcia J, Mattei MG, de Murcia G, Niedergang CP: Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9. Gene. 1997 May 6;190(2):287-96. [PubMed ]
- Kovalenko OV, Plug AW, Haaf T, Gonda DK, Ashley T, Ward DC, Radding CM, Golub EI: Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2958-63. [PubMed ]
- Jiang W, Koltin Y: Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae. Mol Gen Genet. 1996 May 23;251(2):153-60. [PubMed ]
- Wang ZY, Qiu QQ, Seufert W, Taguchi T, Testa JR, Whitmore SA, Callen DF, Welsh D, Shenk T, Deuel TF: Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9. J Biol Chem. 1996 Oct 4;271(40):24811-6. [PubMed ]
- Hahn SL, Wasylyk B, Criqui-Filipe P: Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme. Oncogene. 1997 Sep 18;15(12):1489-95. [PubMed ]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [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 ]
- Hateboer G, Hijmans EM, Nooij JB, Schlenker S, Jentsch S, Bernards R: mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect. J Biol Chem. 1996 Oct 18;271(42):25906-11. [PubMed ]
- Hu G, Zhang S, Vidal M, Baer JL, Xu T, Fearon ER: Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway. Genes Dev. 1997 Oct 15;11(20):2701-14. [PubMed ]
- Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Janne OA: Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. J Biol Chem. 1999 Jul 2;274(27):19441-6. [PubMed ]
- Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, Naismith JH, Hay RT: Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem. 2001 Sep 21;276(38):35368-74. Epub 2001 Jul 12. [PubMed ]
- Eloranta JJ, Hurst HC: Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. J Biol Chem. 2002 Aug 23;277(34):30798-804. Epub 2002 Jun 18. [PubMed ]
- Tatham MH, Chen Y, Hay RT: Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex. Biochemistry. 2003 Mar 25;42(11):3168-79. [PubMed ]
- Tatham MH, Kim S, Yu B, Jaffray E, Song J, Zheng J, Rodriguez MS, Hay RT, Chen Y: Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation. Biochemistry. 2003 Aug 26;42(33):9959-69. [PubMed ]
- Pichler A, Knipscheer P, Saitoh H, Sixma TK, Melchior F: The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. Nat Struct Mol Biol. 2004 Oct;11(10):984-91. Epub 2004 Sep 19. [PubMed ]
- Tatham MH, Kim S, Jaffray E, Song J, Chen Y, Hay RT: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat Struct Mol Biol. 2005 Jan;12(1):67-74. Epub 2004 Dec 19. [PubMed ]
- Li T, Santockyte R, Shen RF, Tekle E, Wang G, Yang DC, Chock PB: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers. Arch Biochem Biophys. 2006 Sep 1;453(1):70-4. Epub 2006 Mar 20. [PubMed ]
- Pan X, Li H, Zhang P, Jin B, Man J, Tian L, Su G, Zhao J, Li W, Liu H, Gong W, Zhou T, Zhang X: Ubc9 interacts with SOX4 and represses its transcriptional activity. Biochem Biophys Res Commun. 2006 Jun 9;344(3):727-34. Epub 2006 Apr 17. [PubMed ]
- Tomoiu A, Gravel A, Tanguay RM, Flamand L: Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation. J Virol. 2006 Oct;80(20):10218-28. [PubMed ]
- Carbia-Nagashima A, Gerez J, Perez-Castro C, Paez-Pereda M, Silberstein S, Stalla GK, Holsboer F, Arzt E: RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia. Cell. 2007 Oct 19;131(2):309-23. [PubMed ]
- Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [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 ]
- Lee B, Muller MT: SUMOylation enhances DNA methyltransferase 1 activity. Biochem J. 2009 Jul 15;421(3):449-61. [PubMed ]
- Kuo FT, Bentsi-Barnes IK, Barlow GM, Bae J, Pisarska MD: Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the Steroidogenic Acute Regulatory gene. Cell Signal. 2009 Dec;21(12):1935-44. Epub 2009 Sep 8. [PubMed ]
- Figueroa-Romero C, Iniguez-Lluhi JA, Stadler J, Chang CR, Arnoult D, Keller PJ, Hong Y, Blackstone C, Feldman EL: SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle. FASEB J. 2009 Nov;23(11):3917-27. Epub 2009 Jul 28. [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 ]
- Yousef AF, Fonseca GJ, Pelka P, Ablack JN, Walsh C, Dick FA, Bazett-Jones DP, Shaw GS, Mymryk JS: Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation. Oncogene. 2010 Aug 19;29(33):4693-704. Epub 2010 Jun 14. [PubMed ]
- Tong H, Hateboer G, Perrakis A, Bernards R, Sixma TK: Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. J Biol Chem. 1997 Aug 22;272(34):21381-7. [PubMed ]
- Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD: Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell. 2002 Feb 8;108(3):345-56. [PubMed ]
- Reverter D, Lima CD: Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature. 2005 Jun 2;435(7042):687-92. [PubMed ]
- Yunus AA, Lima CD: Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Nat Struct Mol Biol. 2006 Jun;13(6):491-9. Epub 2006 May 28. [PubMed ]
|
| Enzyme 91 Metabolite References |
Not Available |
|
Enzyme 92
[top]
|
| Enzyme 92 ID |
5912 |
| Enzyme 92 Name |
Adenosine kinase |
| Enzyme 92 Synonyms |
- AK
- Adenosine 5'-phosphotransferase
|
| Enzyme 92 Gene Name |
ADK |
| Enzyme 92 Protein Sequence |
>Adenosine kinase
MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAED
KHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKA
AEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKAR
VCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGN
ETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFA
VLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPD
FH
|
| Enzyme 92 Number of Residues |
362 |
| Enzyme 92 Molecular Weight |
40545.1 |
| Enzyme 92 Theoretical pI |
6.67 |
| Enzyme 92 GO Classification |
| Function |
- adenosine kinase activity
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- purine ribonucleoside salvage
- purine salvage
|
| Component |
| — |
|
| Enzyme 92 General Function |
Involved in adenosine kinase activity |
| Enzyme 92 Specific Function |
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides |
| Enzyme 92 Pathways |
|
| Enzyme 92 Reactions |
- ATP + adenosine = ADP + AMP [RN:R00185]
|
| Enzyme 92 Pfam Domain Function |
|
| Enzyme 92 Signals |
|
| Enzyme 92 Transmembrane Regions |
|
| Enzyme 92 Essentiality |
Not Available |
| Enzyme 92 GenBank ID Protein |
32484975 |
| Enzyme 92 UniProtKB/Swiss-Prot ID |
P55263 |
| Enzyme 92 UniProtKB/Swiss-Prot Entry Name |
ADK_HUMAN |
| Enzyme 92 PDB ID |
1BX4 |
| Enzyme 92 PDB File |
Show |
| Enzyme 92 3D Structure |
|
| Enzyme 92 Cellular Location |
Not Available |
| Enzyme 92 Gene Sequence |
>1089 bp
ATGGCAGCTGCTGAGGAGGAGCCGAAGCCCAAAAAGCTGAAGGTGGAGGCGCCGCAAGCG
CTGAGAGAAAATATTCTCTTTGGAATGGGAAATCCTCTGCTTGACATCTCTGCTGTAGTG
GACAAAGATTTCCTTGATAAGTATTCTCTGAAACCAAATGACCAAATCTTGGCTGAAGAC
AAACACAAGGAACTGTTTGATGAACTTGTGAAAAAATTCAAAGTCGAATATCATGCTGGT
GGCTCTACCCAGAATTCAATTAAAGTGGCTCAGTGGATGATTCAACAGCCACACAAAGCA
GCAACATTTTTTGGATGCATTGGGATAGATAAATTTGGGGAGATCCTGAAGAGAAAAGCT
GCTGAAGCCCATGTGGATGCTCATTACTACGAGCAGAATGAGCAGCCAACAGGAACTTGT
GCTGCATGCATCACTGGTGACAACAGGTCCCTCATAGCTAATCTTGCTGCTGCCAATTGT
TATAAAAAGGAAAAACATCTTGATCTGGAGAAAAACTGGATGTTGGTAGAAAAAGCAAGA
GTTTGTTATATAGCAGGCTTTTTTCTTACAGTTTCCCCAGAGTCAGTATTAAAGGTGGCT
CACCATGCTTCTGAAAACAACAGGATTTTCACTTTGAATCTATCTGCACCGTTTATTAGC
CAGTTCTACAAGGAATCATTGATGAAAGTTATGCCTTATGTTGATATACTTTTTGGAAAT
GAGACAGAAGCTGCCACTTTTGCTAGAGAGCAAGGCTTTGAGACTAAAGACATTAAAGAG
ATAGCCAAAAAGACACAAGCCCTGCCAAAGATGAACTCAAAGAGGCAGCGAATCGTGATC
TTCACCCAAGGGAGAGATGACACTATAATGGCTACAGAAAGTGAAGTCACTGCTTTTGCT
GTCTTGGATCAAGACCAGAAAGAAATTATTGATACCAATGGAGCTGGAGATGCATTTGTT
GGAGGTTTTCTGTCTCAACTGGTCTCTGACAAGCCTCTGACTGAATGTATCCGTGCTGGC
CACTATGCAGCAAGCATCATAATTAGACGGACTGGCTGCACCTTTCCTGAGAAGCCAGAC
TTCCACTGA
|
| Enzyme 92 GenBank Gene ID |
NM_006721 |
| Enzyme 92 GeneCard ID |
ADK |
| Enzyme 92 GenAtlas ID |
ADK |
| Enzyme 92 HGNC ID |
HGNC:257 |
| Enzyme 92 Chromosome Location |
1 |
| Enzyme 92 Locus |
10q22|10q11-q24 |
| Enzyme 92 SNPs |
SNPJam Report |
| Enzyme 92 General References |
- Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1232-7. [PubMed ]
- Singh B, Hao W, Wu Z, Eigl B, Gupta RS: Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene. Eur J Biochem. 1996 Oct 15;241(2):564-71. [PubMed ]
- McNally T, Helfrich RJ, Cowart M, Dorwin SA, Meuth JL, Idler KB, Klute KA, Simmer RL, Kowaluk EA, Halbert DN: Cloning and expression of the adenosine kinase gene from rat and human tissues. Biochem Biophys Res Commun. 1997 Feb 24;231(3):645-50. [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 ]
- 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 ]
- Mathews II, Erion MD, Ealick SE: Structure of human adenosine kinase at 1.5 A resolution. Biochemistry. 1998 Nov 10;37(45):15607-20. [PubMed ]
- Maguire PB, Wynne KJ, Harney DF, O'Donoghue NM, Stephens G, Fitzgerald DJ: Identification of the phosphotyrosine proteome from thrombin activated platelets. Proteomics. 2002 Jun;2(6):642-8. [PubMed ]
|
| Enzyme 92 Metabolite References |
Not Available |
|
Enzyme 93
[top]
|
| Enzyme 93 ID |
5914 |
| Enzyme 93 Name |
Probable histidyl-tRNA synthetase, mitochondrial |
| Enzyme 93 Synonyms |
- Histidine--tRNA ligase
- HisRS
- Histidine--tRNA ligase-like
|
| Enzyme 93 Gene Name |
HARS2 |
| Enzyme 93 Protein Sequence |
>Probable histidyl-tRNA synthetase, mitochondrial
MPLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAHQEKPNFIIKTP
KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKD
QGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIA
GQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSID
KLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGL
GDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQAGEEPLNVGSVAA
GGRYDGLVGMFDPKGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKN
FLQERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIR
SVASREEVAIKRENFVAEIQKRLSES
|
| Enzyme 93 Number of Residues |
506 |
| Enzyme 93 Molecular Weight |
56887.9 |
| Enzyme 93 Theoretical pI |
8.35 |
| Enzyme 93 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- histidine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- histidyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 93 General Function |
Involved in nucleotide binding |
| Enzyme 93 Specific Function |
ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His) |
| Enzyme 93 Pathways |
|
| Enzyme 93 Reactions |
- ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis [RN:R03655]
|
| Enzyme 93 Pfam Domain Function |
|
| Enzyme 93 Signals |
|
| Enzyme 93 Transmembrane Regions |
|
| Enzyme 93 Essentiality |
Not Available |
| Enzyme 93 GenBank ID Protein |
Not Available |
| Enzyme 93 UniProtKB/Swiss-Prot ID |
P49590 |
| Enzyme 93 UniProtKB/Swiss-Prot Entry Name |
SYHM_HUMAN |
| Enzyme 93 PDB ID |
Not Available |
| Enzyme 93 Cellular Location |
Not Available |
| Enzyme 93 Gene Sequence |
>1521 bp
ATGCCCCTGCTCGGACTTCTTCCCAGGAGGGCCTGGGCTTCGCTGCTCAGCCAGCTCCTG
CGACCGCCCTGCGCTTCGTGCACCGGGGCGGTCCGTTGCCAAAGCCAGGTTGCAGAGGCA
GTGTTAACATCCCAACTGAAAGCACATCAAGAGAAACCAAATTTTATTATCAAGACCCCA
AAGGGTACCAGGGATCTTAGTCCTCAGCATATGGTTGTGAGGGAGAAAATTCTTGATTTG
GTTATCAGCTGCTTTAAACGTCATGGAGCAAAGGGGATGGACACCCCAGCATTTGAGCTG
AAGGAAACCCTGACTGAGAAGTATGGAGAGGACTCTGGGCTCATGTATGATCTGAAGGAT
CAAGGTGGAGAGCTGTTGTCCCTCCGCTATGACCTTACTGTTCCCTTTGCTCGTTATCTG
GCCATGAATAAGGTGAAGAAGATGAAACGTTATCATGTTGGAAAGGTGTGGCGGCGAGAG
AGCCCAACCATAGTCCAAGGCCGTTATAGGGAGTTCTGCCAGTGTGATTTTGACATTGCT
GGTCAGTTTGACCCTATGATCCCCGATGCAGAGTGTTTGAAGATCATGTGTGAAATCCTA
AGTGGATTGCAGTTGGGAGACTTTCTCATTAAGGTAAATGACCGGCGGATTGTGGATGGG
ATGTTTGCTGTCTGTGGTGTTCCTGAAAGCAAGTTCCGTGCCATCTGCTCCTCCATAGAT
AAACTAGACAAGATGGCTTGGAAAGATGTGAGACATGAGATGGTGGTGAAGAAAGGCCTG
GCTCCTGAGGTGGCTGATCGAATTGGGGACTATGTCCAGTGTCATGGTGGGGTATCCCTA
GTAGAGCAAATGTTTCAGGATCCCAGACTATCCCAGAACAAGCAGGCCCTGGAGGGCCTG
GGAGACCTAAAGCTGCTATTTGAATACCTGACTTTATTTGGAATTGCTGATAAGATCTCC
TTTGACCTCAGCCTGGCTCGGGGCCTAGACTACTATACAGGAGTGATCTATGAAGCAGTG
CTGCTGCAGACCCCAACTCAGGCTGGGGAGGAGCCCCTGAATGTGGGCAGTGTGGCTGCT
GGTGGGCGCTATGATGGGCTGGTGGGCATGTTTGACCCCAAGGGCCACAAGGTGCCATGT
GTGGGACTCAGCATTGGGGTTGAGCGAATCTTCTACATTGTGGAGCAGAGGATGAAGACC
AAAGGTGAGAAGGTGCGGACTACAGAGACTCAAGTGTTTGTGGCCACACCACAGAAGAAC
TTTCTCCAAGAACGGTTGAAGCTTATTGCAGAGCTTTGGGATTCTGGAATCAAGGCAGAG
ATGCTATACAAGAACAACCCCAAACTATTAACCCAGCTGCACTATTGTGAGAGCACAGGC
ATTCCACTGGTGGTCATTATTGGTGAGCAAGAACTGAAAGAAGGGGTCATCAAGATCCGT
TCAGTGGCCAGCAGAGAGGAGGTGGCCATTAAACGGGAAAATTTTGTGGCTGAAATTCAG
AAGCGACTGTCTGAGTCTTGA
|
| Enzyme 93 GenBank Gene ID |
U18937 |
| Enzyme 93 GeneCard ID |
HARS2 |
| Enzyme 93 GenAtlas ID |
HARS2 |
| Enzyme 93 HGNC ID |
HGNC:4817 |
| Enzyme 93 Chromosome Location |
5 |
| Enzyme 93 Locus |
5q31.3 |
| Enzyme 93 SNPs |
SNPJam Report |
| Enzyme 93 General References |
- O'Hanlon TP, Raben N, Miller FW: A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. Biochem Biophys Res Commun. 1995 May 16;210(2):556-66. [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 ]
- 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 93 Metabolite References |
Not Available |
|
Enzyme 94
[top]
|
| Enzyme 94 ID |
5915 |
| Enzyme 94 Name |
Ubiquitin-conjugating enzyme E2 J1 |
| Enzyme 94 Synonyms |
- Non-canonical ubiquitin-conjugating enzyme 1
- NCUBE-1
- Yeast ubiquitin-conjugating enzyme UBC6 homolog E
- HsUBC6e
|
| Enzyme 94 Gene Name |
UBE2J1 |
| Enzyme 94 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 J1
METRYNLKSPAVKRLMKEAAELKDPTDHYHAQPLEDNLFEWHFTVRGPPDSDFDGGVYHG
RIVLPPEYPMKPPSIILLTANGRFEVGKKICLSISGHHPETWQPSWSIRTALLAIIGFMP
TKGEGAIGSLDYTPEERRALAKKSQDFCCEGCGSAMKDVLLPLKSGSDSSQADQEAKELA
RQISFKAEVNSSGKTISESDLNHSFSLTDLQDDIPTTFQGATASTSYGLQNSSAASFHQP
TQPVAKNTSMSPRQRRAQQQSQRRLSTSPDVIQGHQPRDNHTDHGGSAVLIVILTLALAA
LIFRRIYLANEYIFDFEL
|
| Enzyme 94 Number of Residues |
318 |
| Enzyme 94 Molecular Weight |
35198.3 |
| Enzyme 94 Theoretical pI |
6.74 |
| Enzyme 94 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 94 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 94 Specific Function |
Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum |
| Enzyme 94 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 94 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 94 Pfam Domain Function |
|
| Enzyme 94 Signals |
|
| Enzyme 94 Transmembrane Regions |
|
| Enzyme 94 Essentiality |
Not Available |
| Enzyme 94 GenBank ID Protein |
37577122 |
| Enzyme 94 UniProtKB/Swiss-Prot ID |
Q9Y385 |
| Enzyme 94 UniProtKB/Swiss-Prot Entry Name |
UB2J1_HUMAN |
| Enzyme 94 PDB ID |
Not Available |
| Enzyme 94 Cellular Location |
Not Available |
| Enzyme 94 Gene Sequence |
>957 bp
ATGGAGACCCGCTACAACCTGAAGAGTCCGGCTGTTAAACGTTTAATGAAAGAAGCGGCA
GAATTGAAAGATCCAACAGATCATTACCATGCGCAGCCTTTAGAGGATAACCTTTTTGAA
TGGCACTTCACGGTTAGAGGGCCCCCAGACTCCGATTTTGATGGAGGAGTTTATCACGGG
CGGATAGTACTGCCACCAGAGTATCCCATGAAACCACCAAGCATTATTCTCCTAACGGCT
AATGGTCGATTTGAAGTGGGCAAGAAAATCTGTTTGAGCATCTCAGGCCATCATCCTGAA
ACTTGGCAGCCTTCGTGGAGTATAAGGACAGCATTATTAGCCATCATTGGGTTTATGCCA
ACAAAAGGAGAGGGAGCCATAGGTTCTCTAGATTACACTCCTGAGGAAAGAAGAGCACTT
GCCAAAAAATCACAAGATTTCTGTTGTGAAGGATGTGGCTCTGCCATGAAGGATGTCCTG
TTGCCTTTAAAATCTGGAAGCGATTCAAGCCAAGCTGACCAAGAAGCCAAAGAACTGGCT
AGGCAAATAAGCTTTAAGGCAGAAGTCAATTCATCTGGAAAGACTATCTCTGAGTCAGAC
TTAAACCACTCTTTTTCACTAACTGATTTACAAGATGATATACCTACAACATTCCAGGGT
GCTACGGCCAGTACATCGTACGGACTCCAGAATTCCTCAGCAGCATCCTTTCATCAACCT
ACCCAACCTGTAGCTAAGAATACCTCCATGAGCCCTCGACAGCGCCGGGCCCAGCAGCAG
AGTCAGAGAAGGTTGTCTACTTCACCAGATGTAATCCAGGGCCACCAGCCAAGAGACAAC
CACACTGATCATGGTGGGTCAGCTGTACTGATTGTCATCCTGACTTTGGCATTGGCAGCT
CTTATATTCCGACGAATATATCTGGCAAACGAATACATATTTGACTTTGAGTTATAA
|
| Enzyme 94 GenBank Gene ID |
NM_016021.2 |
| Enzyme 94 GeneCard ID |
UBE2J1 |
| Enzyme 94 GenAtlas ID |
UBE2J1 |
| Enzyme 94 HGNC ID |
HGNC:17598 |
| Enzyme 94 Chromosome Location |
6 |
| Enzyme 94 Locus |
6q15 |
| Enzyme 94 SNPs |
SNPJam Report |
| Enzyme 94 General References |
- Lester D, Farquharson C, Russell G, Houston B: Identification of a family of noncanonical ubiquitin-conjugating enzymes structurally related to yeast UBC6. Biochem Biophys Res Commun. 2000 Mar 16;269(2):474-80. [PubMed ]
- Lenk U, Yu H, Walter J, Gelman MS, Hartmann E, Kopito RR, Sommer T: A role for mammalian Ubc6 homologues in ER-associated protein degradation. J Cell Sci. 2002 Jul 15;115(Pt 14):3007-14. [PubMed ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 94 Metabolite References |
Not Available |
|
Enzyme 95
[top]
|
| Enzyme 95 ID |
5916 |
| Enzyme 95 Name |
Long-chain-fatty-acid--CoA ligase 5 |
| Enzyme 95 Synonyms |
- Long-chain acyl-CoA synthetase 5
- LACS 5
|
| Enzyme 95 Gene Name |
ACSL5 |
| Enzyme 95 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 5
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD
|
| Enzyme 95 Number of Residues |
683 |
| Enzyme 95 Molecular Weight |
75990.1 |
| Enzyme 95 Theoretical pI |
6.91 |
| Enzyme 95 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 95 General Function |
Involved in catalytic activity |
| Enzyme 95 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 95 Pathways |
|
| Enzyme 95 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 95 Pfam Domain Function |
|
| Enzyme 95 Signals |
|
| Enzyme 95 Transmembrane Regions |
|
| Enzyme 95 Essentiality |
Not Available |
| Enzyme 95 GenBank ID Protein |
6174680 |
| Enzyme 95 UniProtKB/Swiss-Prot ID |
Q9ULC5 |
| Enzyme 95 UniProtKB/Swiss-Prot Entry Name |
ACSL5_HUMAN |
| Enzyme 95 PDB ID |
Not Available |
| Enzyme 95 Cellular Location |
Not Available |
| Enzyme 95 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 95 GenBank Gene ID |
AB033899 |
| Enzyme 95 GeneCard ID |
ACSL5 |
| Enzyme 95 GenAtlas ID |
ACSL5 |
| Enzyme 95 HGNC ID |
HGNC:16526 |
| Enzyme 95 Chromosome Location |
1 |
| Enzyme 95 Locus |
10q25.1-q25.2 |
| Enzyme 95 SNPs |
SNPJam Report |
| Enzyme 95 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 95 Metabolite References |
Not Available |
|
Enzyme 96
[top]
|
| Enzyme 96 ID |
5917 |
| Enzyme 96 Name |
Histidyl-tRNA synthetase, cytoplasmic |
| Enzyme 96 Synonyms |
- Histidine--tRNA ligase
- HisRS
|
| Enzyme 96 Gene Name |
HARS |
| Enzyme 96 Protein Sequence |
>Histidyl-tRNA synthetase, cytoplasmic
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPK
GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQ
GGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAG
NFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDK
LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLG
DLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAG
GRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKL
LEERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRS
VTSREEVDVRREDLVEEIKRRTGQPLCIC
|
| Enzyme 96 Number of Residues |
509 |
| Enzyme 96 Molecular Weight |
57410.0 |
| Enzyme 96 Theoretical pI |
5.56 |
| Enzyme 96 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- histidine-tRNA ligase activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- histidyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 96 General Function |
Involved in nucleotide binding |
| Enzyme 96 Specific Function |
ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His) |
| Enzyme 96 Pathways |
|
| Enzyme 96 Reactions |
- ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis [RN:R03655]
|
| Enzyme 96 Pfam Domain Function |
|
| Enzyme 96 Signals |
|
| Enzyme 96 Transmembrane Regions |
|
| Enzyme 96 Essentiality |
Not Available |
| Enzyme 96 GenBank ID Protein |
32460 |
| Enzyme 96 UniProtKB/Swiss-Prot ID |
P12081 |
| Enzyme 96 UniProtKB/Swiss-Prot Entry Name |
SYHC_HUMAN |
| Enzyme 96 PDB ID |
Not Available |
| Enzyme 96 Cellular Location |
Not Available |
| Enzyme 96 Gene Sequence |
>1530 bp
ATGGCAGAGCGTGCGGCGCTGGAGGAGCTGGTGAAACTTCAGGGAGAGCGCGTGCGAGGC
CTCAAGCAGCAGAAGGCCAGCGCCGAGCTGATCGAGGAGGAGGTGGCGAAACTCCTGAAA
CTGAAGGCACAGCTGGGTCCTGATGAAAGCAAACAGAAATTTGTGCTCAAAACCCCCAAG
GGCACAAGAGACTATAGTCCCCGGCAGATGGCAGTTCGCGAGAAGGTGTTTGACGTAATC
ATCCGTTGCTTCAAGCGCCACGGTGCAGAAGTCATTGATACACCTGTATTTGAACTAAAG
GAAACACTGATGGGAAAGTATGGGGAAGACTCCAAGCTTATCTATGACCTGAAGGACCAG
GGCGGGGAGCTCCTGTCCCTTCGCTATGACCTCACTGTTCCTTTTGCTCGGTATTTGGCA
ATGAATAAACTGACCAACATTAAACGCTACCACATAGCAAAGGTATATCGGCGGGATAAC
CCAGCCATGACCCGTGGCCGATACCGGGAATTCTACCAGTGTGATTTTGACATTGCTGGG
AACTTTGATCCCATGATCCCTGATGCAGAGTGCCTGAAGATCATGTGCGAGATCCTGAGT
TCACTTCAGATAGGCGACTTCCTGGTCAAGGTAAACGATCGACGCATTCTAGATGGGATG
TTTGCTATCTGTGGTGTTTCTGACAGCAAGTTCCGTACCATCTGCTCCTCAGTAGACAAG
CTGGACAAGGTGTCCTGGGAAGAGGTGAAGAATGAGATGGTGGGAGAGAAGGGCCTTGCA
CCTGAGGTGGCTGACCGCATTGGGGACTATGTCCAGCAACATGGTGGGGTATCCCTGGTG
GAACAGCTGCTCCAGGATCCTAAACTATCCCAAAACAAGCAGGCCTTGGAGGGCCTGGGA
GACCTGAAGTTGCTCTTTGAGTACCTGACCCTATTTGGCATTGATGACAAAATCTCCTTT
GACCTGAGCCTTGCTCGAGGGCTGGATTACTACACTGGGGTGATCTATGAGGCAGTGCTG
CTACAGACCCCAGCCCAGGCAGGGGAAGAGCCCCTGGGTGTGGGCAGTGTGGCTGCTGGA
GGACGCTATGATGGGCTAGTGGGCATGTTCGACCCCAAAGGGCGCAAGGTGCCATGTGTG
GGGCTCAGCATTGGGGTGGAGCGGATTTTCTCCATCGTGGAACAGAGACTAGAGGCTTTG
GAGGAGAAGATACGGACCACGGAGACACAGGTGCTTGTGGCATCTGCACAGAAGAAGCTG
CTAGAGGAAAGACTAAAGCTTGTCTCAGAACTGTGGGATGCTGGGATCAAGGCTGAGCTG
CTGTACAAGAAGAACCCAAAGCTACTGAACCAGTTACAGTACTGTGAGGAGGCAGGCATC
CCACTGGTGGCTATCATCGGCGAGCAGGAACTCAAGGATGGGGTCATCAAGCTCCGTTCA
GTGACGAGCAGGGAAGAGGTGGATGTCCGAAGAGAAGACCTTGTGGAGGAAATCAAAAGG
AGAACAGGCCAGCCCCTCTGCATCTGCTGA
|
| Enzyme 96 GenBank Gene ID |
Z11518 |
| Enzyme 96 GeneCard ID |
HARS |
| Enzyme 96 GenAtlas ID |
HARS |
| Enzyme 96 HGNC ID |
HGNC:4816 |
| Enzyme 96 Chromosome Location |
5 |
| Enzyme 96 Locus |
5q31.3 |
| Enzyme 96 SNPs |
SNPJam Report |
| Enzyme 96 General References |
- Raben N, Borriello F, Amin J, Horwitz R, Fraser D, Plotz P: Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases. Nucleic Acids Res. 1992 Mar 11;20(5):1075-81. [PubMed ]
- Tsui FW, Siminovitch L: Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase. Nucleic Acids Res. 1987 Apr 24;15(8):3349-67. [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 ]
- Tsui HW, Mok S, de Souza L, Martin A, Tsui FW: Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element. Gene. 1993 Sep 15;131(2):201-8. [PubMed ]
- O'Hanlon TP, Raben N, Miller FW: A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. Biochem Biophys Res Commun. 1995 May 16;210(2):556-66. [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 96 Metabolite References |
Not Available |
|
Enzyme 97
[top]
|
| Enzyme 97 ID |
5918 |
| Enzyme 97 Name |
Seryl-tRNA synthetase, cytoplasmic |
| Enzyme 97 Synonyms |
- Serine--tRNA ligase
- SerRS
- Seryl-tRNA(Ser/Sec) synthetase
|
| Enzyme 97 Gene Name |
SARS |
| Enzyme 97 Protein Sequence |
>Seryl-tRNA synthetase, cytoplasmic
MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLC
SKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAE
RIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGF
EGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQL
SQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTC
FRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYH
IVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKV
EFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEP
SKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA
|
| Enzyme 97 Number of Residues |
514 |
| Enzyme 97 Molecular Weight |
58776.8 |
| Enzyme 97 Theoretical pI |
6.38 |
| Enzyme 97 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- serine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- seryl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 97 General Function |
Involved in nucleotide binding |
| Enzyme 97 Specific Function |
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) |
| Enzyme 97 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970 )
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 97 Reactions |
- ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer [RN:R03662]
|
| Enzyme 97 Pfam Domain Function |
|
| Enzyme 97 Signals |
|
| Enzyme 97 Transmembrane Regions |
|
| Enzyme 97 Essentiality |
Not Available |
| Enzyme 97 GenBank ID Protein |
1050527 |
| Enzyme 97 UniProtKB/Swiss-Prot ID |
P49591 |
| Enzyme 97 UniProtKB/Swiss-Prot Entry Name |
SYSC_HUMAN |
| Enzyme 97 PDB ID |
Not Available |
| Enzyme 97 Cellular Location |
Not Available |
| Enzyme 97 Gene Sequence |
>1545 bp
ATGGTGCTGGATCTGGATTTGTTTCGGGTGGATAAAGGAGGGGACCCAGCCCTCATCCGA
GAGACGCAGGAGAAGCGCTTCAAGGACCCGGGACTAGTGGACCAGCTGGTGAAGGCAGAC
AGCGAGTGGCGACGATGTAGATTTCGGGCAGACAACTTGAGCAAGCTGAAGAACCTATGC
AGCAAGACAATCGGAGAGAAAATGAAGAAAAAAGAGCCAGTGGGAGATGATGAGTCTGTC
CCAGAGAATGTGCTGAGTTTCGATGACCTTACTGCAGACGCTTTAGCTAACCTGAAAGTC
TCACAAATCAAAAAAGTCCGACTCCTCATTGATGAAGCCATCCTGAAGTGTGACGCGGAG
CGGATAAAGTTGGAAGCAGAGCGGTTTGAGAACCTCCGAGAGATTGGGAACCTTCTGCAC
CCTTCTGTACCCATCAGTAACGATGAGGATGTGGACAACAAAGTAGAGAGGATTTGGGGC
GATTGTACAGTCAGGAAGAAGTACTCTCATGTGGACCTGGTGGTGATGGTAGATGGCTTT
GAAGGCGAAAAGGGGGCCGTGGTGGCTGGGAGTCGAGGGTACTTCTTGAAGGGGGTCCTG
GTGTTCCTGGAACAGGCTCTCATCCAGTATGCCCTTCGCACCTTGGGAAGTCGGGGCTAC
ATTCCCATTTATACCCCCTTTTTCATGAGGAAGGAGGTCATGCAGGAGGTGGCACAGCTC
AGCCAGTTTGATGAAGAACTTTATAAGGTGATTGGCAAAGGCAGTGAAAAGTCTGATGAC
AACTCCTATGATGAGAAGTACCTGATTGCCACCTCAGAGCAGCCCATTGCTGCCCTGCAC
CGGGATGAGTGGCTCCGGCCGGAGGACCTGCCCATCAAGTATGCTGGCCTGTCTACCTGC
TTCCGTCAGGAGGTGGGCTCCCATGGCCGTGACACCCGTGGCATCTTCCGAGTCCATCAG
TTTGAGAAGATTGAACAGTTTGTGTACTCATCACCCCATGACAACAAGTCATGGGAGATG
TTTGAAGAGATGATTACCACCGCAGAGGAGTTCTACCAGTCCCTGGGGATTCCTTACCAC
ATTGTGAATATTGTCTCAGGTTCTTTGAATCATGCTGCCAGTAAGAAGCTTGACCTGGAG
GCCTGGTTTCCGGGCTCAGGAGCCTTCCGTGAGTTGGTCTCCTGTTCTAATTGCACGGAT
TACCAGGCTCGCCGGCTTCGAATCCGATATGGGCAAACCAAGAAGATGATGGACAAGGTG
GAGTTTGTCCATATGCTCAATGCTACCATGTGCGCCACTACCCGTACCATCTGCGCCATC
CTGGAGAACTACCAGACAGAGAAGGGCATCACTGTGCCTGAGAAATTGAAGGAGTTCATG
CCGCCAGGACTGCAAGAACTGATCCCCTTTGTGAAGCCTGCGCCCATTGAGCAGGAGCCA
TCAAAGAAGCAGAAGAAGCAACATGAGGGCAGCAAAAAGAAAGCAGCAGCAAGAGACGTC
ACCCTAGAAAACAGGCTGCAGAACATGGAGGTCACCGATGCTTGA
|
| Enzyme 97 GenBank Gene ID |
X91257 |
| Enzyme 97 GeneCard ID |
SARS |
| Enzyme 97 GenAtlas ID |
SARS |
| Enzyme 97 HGNC ID |
HGNC:10537 |
| Enzyme 97 Chromosome Location |
1 |
| Enzyme 97 Locus |
1p13.3 |
| Enzyme 97 SNPs |
SNPJam Report |
| Enzyme 97 General References |
- Vincent C, Tarbouriech N, Hartlein M: Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase. Eur J Biochem. 1997 Nov 15;250(1):77-84. [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 ]
- 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 ]
- 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 97 Metabolite References |
Not Available |
|
Enzyme 98
[top]
|
| Enzyme 98 ID |
5919 |
| Enzyme 98 Name |
Long-chain-fatty-acid--CoA ligase 3 |
| Enzyme 98 Synonyms |
- Long-chain acyl-CoA synthetase 3
- LACS 3
|
| Enzyme 98 Gene Name |
ACSL3 |
| Enzyme 98 Protein Sequence |
>Long-chain-fatty-acid--CoA ligase 3
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
|
| Enzyme 98 Number of Residues |
720 |
| Enzyme 98 Molecular Weight |
80419.4 |
| Enzyme 98 Theoretical pI |
8.51 |
| Enzyme 98 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 98 General Function |
Involved in catalytic activity |
| Enzyme 98 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 98 Pathways |
|
| Enzyme 98 Reactions |
- ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
|
| Enzyme 98 Pfam Domain Function |
|
| Enzyme 98 Signals |
|
| Enzyme 98 Transmembrane Regions |
|
| Enzyme 98 Essentiality |
Not Available |
| Enzyme 98 GenBank ID Protein |
17026088 |
| Enzyme 98 UniProtKB/Swiss-Prot ID |
O95573 |
| Enzyme 98 UniProtKB/Swiss-Prot Entry Name |
ACSL3_HUMAN |
| Enzyme 98 PDB ID |
Not Available |
| Enzyme 98 Cellular Location |
Not Available |
| Enzyme 98 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 98 GenBank Gene ID |
AB061436 |
| Enzyme 98 GeneCard ID |
ACSL3 |
| Enzyme 98 GenAtlas ID |
ACSL3 |
| Enzyme 98 HGNC ID |
HGNC:3570 |
| Enzyme 98 Chromosome Location |
2 |
| Enzyme 98 Locus |
2q34-q35 |
| Enzyme 98 SNPs |
SNPJam Report |
| Enzyme 98 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 98 Metabolite References |
Not Available |
|
Enzyme 99
[top]
|
| Enzyme 99 ID |
5921 |
| Enzyme 99 Name |
Ubiquitin-conjugating enzyme E2 C |
| Enzyme 99 Synonyms |
- UbcH10
- Ubiquitin carrier protein C
- Ubiquitin-protein ligase C
|
| Enzyme 99 Gene Name |
UBE2C |
| Enzyme 99 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 C
MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLF
KWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKE
KWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP
|
| Enzyme 99 Number of Residues |
179 |
| Enzyme 99 Molecular Weight |
19652.1 |
| Enzyme 99 Theoretical pI |
7.50 |
| Enzyme 99 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
- small conjugating protein ligase activity
- ubiquitin-protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification by small protein conjugation
- protein modification by small protein conjugation or removal
- protein modification process
- protein ubiquitination
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 99 General Function |
Involved in ubiquitin-protein ligase activity |
| Enzyme 99 Specific Function |
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit |
| Enzyme 99 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 99 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 99 Pfam Domain Function |
|
| Enzyme 99 Signals |
|
| Enzyme 99 Transmembrane Regions |
|
| Enzyme 99 Essentiality |
Not Available |
| Enzyme 99 GenBank ID Protein |
5902146 |
| Enzyme 99 UniProtKB/Swiss-Prot ID |
O00762 |
| Enzyme 99 UniProtKB/Swiss-Prot Entry Name |
UBE2C_HUMAN |
| Enzyme 99 PDB ID |
1I7K |
| Enzyme 99 PDB File |
Show |
| Enzyme 99 3D Structure |
|
| Enzyme 99 Cellular Location |
Not Available |
| Enzyme 99 Gene Sequence |
>540 bp
ATGGCTTCCCAAAACCGCGACCCAGCCGCCACTAGCGTCGCCGCCGCCCGTAAAGGAGCT
GAGCCGAGCGGGGGCGCCGCCCGGGGTCCGGTGGGCAAAAGGCTACAGCAGGAGCTGATG
ACCCTCATGATGTCTGGCGATAAAGGGATTTCTGCCTTCCCTGAATCAGACAACCTTTTC
AAATGGGTAGGGACCATCCATGGAGCAGCTGGAACAGTATATGAAGACCTGAGGTATAAG
CTCTCGCTAGAGTTCCCCAGTGGCTACCCTTACAATGCGCCCACAGTGAAGTTCCTCACG
CCCTGCTATCACCCCAACGTGGACACCCAGGGTAACATATGCCTGGACATCCTGAAGGAA
AAGTGGTCTGCCCTGTATGATGTCAGGACCATTCTGCTCTCCATCCAGAGCCTTCTAGGA
GAACCCAACATTGATAGTCCCTTGAACACACATGCTGCCGAGCTCTGGAAAAACCCCACA
GCTTTTAAGAAGTACCTGCAAGAAACCTACTCAAAGCAGGTCACCAGCCAGGAGCCCTGA
|
| Enzyme 99 GenBank Gene ID |
NM_007019.2 |
| Enzyme 99 GeneCard ID |
UBE2C |
| Enzyme 99 GenAtlas ID |
UBE2C |
| Enzyme 99 HGNC ID |
HGNC:15937 |
| Enzyme 99 Chromosome Location |
2 |
| Enzyme 99 Locus |
20q13.12 |
| Enzyme 99 SNPs |
SNPJam Report |
| Enzyme 99 General References |
- Townsley FM, Aristarkhov A, Beck S, Hershko A, Ruderman JV: Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase. Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2362-7. [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 ]
- Rape M, Kirschner MW: Autonomous regulation of the anaphase-promoting complex couples mitosis to S-phase entry. Nature. 2004 Dec 2;432(7017):588-95. Epub 2004 Nov 21. [PubMed ]
- Jin L, Williamson A, Banerjee S, Philipp I, Rape M: Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell. 2008 May 16;133(4):653-65. [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 ]
- Garnett MJ, Mansfeld J, Godwin C, Matsusaka T, Wu J, Russell P, Pines J, Venkitaraman AR: UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit. Nat Cell Biol. 2009 Nov;11(11):1363-9. Epub 2009 Oct 11. [PubMed ]
- Williamson A, Wickliffe KE, Mellone BG, Song L, Karpen GH, Rape M: Identification of a physiological E2 module for the human anaphase-promoting complex. Proc Natl Acad Sci U S A. 2009 Oct 27;106(43):18213-8. Epub 2009 Oct 12. [PubMed ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
- Lin Y, Hwang WC, Basavappa R: Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10. J Biol Chem. 2002 Jun 14;277(24):21913-21. Epub 2002 Apr 1. [PubMed ]
|
| Enzyme 99 Metabolite References |
Not Available |
|
Enzyme 100
[top]
|
| Enzyme 100 ID |
5923 |
| Enzyme 100 Name |
Valyl-tRNA synthetase |
| Enzyme 100 Synonyms |
- Protein G7a
- Valine--tRNA ligase
- ValRS
|
| Enzyme 100 Gene Name |
VARS |
| Enzyme 100 Protein Sequence |
>Valyl-tRNA synthetase
MSTLYVSPHPDAFPSLRALIAARYGEAGEGPGWGGAHPRICLQPPPTSRTPFPPPRLPAL
EQGPGGLWVWGATAVAQLLWPAGLGGPGGSRAAVLVQQWVSYADTELIPAACGATLPALG
LRSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRYVLDPPA
RRIWNNVTRWFVTCVRQPEFRAVLGEVVLYSGARPLSHQPGPEAPALPKTAAQLKKEAKK
REKLEKFQQKQKIQQQQPPPGEKKPKPEKREKRDPGVITYDLPTPPGEKKDVSGPMPDSY
SPRYVEAAWYPWWEQQGFFKPEYGRPNVSAANPRGVFMMCIPPPNVTGSLHLGHALTNAI
QDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWK
EEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCT
LNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYKVQGSDSDEEVVVATTRIET
MLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQND
YEVGQRHGLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVV
PLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHAWMDNIREWC
ISRQLWWGHRIPAYFVTVSDPAVPPGEDPDGRYWVSGRNEAEAREKAAKEFGVSPDKISL
QQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKL
TGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVE
KAKEGQKADFPAGIPECGTDALRFGLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFA
LRGLGKGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLY
ELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMP
QAPPSLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRIRPDCFLEVAD
EATGALASAVSGYVQALASAGVVAVLALGAPAPQGCAVALASDRCSIHLQLQGLVDPARE
LGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAELRKVDEAIALF
QKML
|
| Enzyme 100 Number of Residues |
1264 |
| Enzyme 100 Molecular Weight |
140474.8 |
| Enzyme 100 Theoretical pI |
7.63 |
| Enzyme 100 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
- valine-tRNA ligase activity
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
- valyl-tRNA aminoacylation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 100 General Function |
Involved in nucleotide binding |
| Enzyme 100 Specific Function |
ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val) |
| Enzyme 100 Pathways |
|
| Enzyme 100 Reactions |
- ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal [RN:R03665]
|
| Enzyme 100 Pfam Domain Function |
|
| Enzyme 100 Signals |
|
| Enzyme 100 Transmembrane Regions |
|
| Enzyme 100 Essentiality |
Not Available |
| Enzyme 100 GenBank ID Protein |
4529896 |
| Enzyme 100 UniProtKB/Swiss-Prot ID |
P26640 |
| Enzyme 100 UniProtKB/Swiss-Prot Entry Name |
SYVC_HUMAN |
| Enzyme 100 PDB ID |
Not Available |
| Enzyme 100 Cellular Location |
Not Available |
| Enzyme 100 Gene Sequence |
>3795 bp
ATGTCCACCCTCTACGTCTCCCCTCACCCAGATGCCTTCCCCAGCCTCCGAGCCCTCATA
GCCGCTCGCTATGGGGAGGCTGGGGAGGGTCCCGGATGGGGAGGAGCCCACCCCCGCATC
TGTCTCCAGCCACCCCCGACTAGCAGGACTCCCTTTCCCCCACCCCGCCTGCCGGCCCTG
GAGCAGGGGCCCGGTGGGCTCTGGGTGTGGGGGGCCACGGCTGTGGCCCAGCTGCTGTGG
CCAGCAGGCCTGGGGGGCCCAGGGGGCAGCCGGGCGGCTGTCCTTGTCCAACAGTGGGTC
AGTTACGCCGACACGGAGTTAATACCAGCTGCCTGTGGAGCAACGCTGCCGGCCCTGGGA
CTCCGAAGCTCGGCCCAGGACCCCCAGGCTGTGCTGGGGGCCCTGGGCAGGGCCCTGAGC
CCCTTGGAGGAGTGGCTTCGGCTGCACACCTACTTGGCCGGGGAGGCCCCCACTCTGGCT
GACCTGGCGGCTGTCACAGCCTTGCTGCTGCCTTTCCGATACGTCCTAGACCCACCTGCC
CGCCGGATCTGGAATAATGTGACTCGCTGGTTTGTCACGTGTGTCCGGCAGCCAGAATTC
CGAGCCGTGCTAGGAGAAGTGGTTCTATACTCAGGAGCCAGGCCTCTCTCTCATCAGCCA
GGCCCCGAGGCTCCTGCCCTCCCAAAGACAGCTGCTCAGCTCAAGAAAGAGGCAAAGAAA
CGGGAGAAGCTAGAGAAATTCCAACAGAAGCAGAAGATCCAACAGCAGCAGCCACCTCCA
GGGGAGAAGAAACCAAAACCAGAGAAGAGGGAGAAACGGGATCCTGGGGTCATTACCTAT
GACCTCCCAACCCCACCCGGGGAAAAGAAAGATGTCAGTGGCCCCATGCCCGACTCCTAC
AGCCCTCGGTATGTGGAGGCTGCCTGGTACCCTTGGTGGGAGCAGCAGGGCTTCTTCAAG
CCAGAGTATGGGCGTCCTAATGTGTCAGCAGCAAATCCCCGAGGTGTCTTCATGATGTGC
ATCCCACCCCCCAATGTGACAGGCTCCCTGCACCTGGGCCATGCACTCACCAACGCCATC
CAGGACTCCCTGACTCGATGGCACCGCATGCGTGGGGAGACCACCCTGTGGAACCCTGGC
TGTGACCATGCAGGTATTGCCACCCAGGTGGTGGTGGAGAAGAAGCTATGGCGTGAGCAG
GGACTGAGCCGGCACCAGCTGGGCCGCGAGGCCTTTCTACAGGAAGTCTGGAAGTGGAAG
GAGGAGAAAGGTGACCGGATTTACCACCAGTTGAAGAAGCTTGGCAGCTCCTTGGACTGG
GATCGAGCCTGTTTCACCATGGACCCTAAACTCTCAGCAGCTGTGACAGAGGCCTTTGTC
CGGCTTCACGAGGAAGGCATCATCTATCGCAGTACCCGCCTTGTTAACTGGTCCTGCACC
CTCAACTCCGCCATCTCTGACATTGAGGTGGATAAGAAGGAGCTGACAGGTCGCACCCTG
CTCTCCGTGCCTGGCTACAAGGAGAAGGTGGAGTTCGGGGTCCTCGTGTCCTTTGCCTAT
AAGGTCCAAGGCTCAGATAGCGACGAGGAGGTGGTGGTGGCAACAACTCGGATCGAGACA
ATGCTGGGAGATGTGGCTGTAGCTGTGCACCCCAAAGATACCAGATACCAGCACCTGAAG
GGGAAGAACGTGATCCACCCATTCCTGTCTCGGAGCCTTCCCATTGTCTTCGATGAATTT
GTGGACATGGACTTTGGCACAGGTGCTGTGAAGATCACCCCCGCACATGACCAAAATGAC
TATGAAGTTGGGCAGCGGCACGGGCTGGAGGCCATCAGCATCATGGACTCCCGGGGGGCC
CTCATCAATGTGCCTCCGCCTTTCCTGGGCCTGCCCAGGTTTGAGGCCAGGAAAGCGGTG
CTGGTGGCGCTGAAGGAGCGGGGACTGTTCCGTGGCATTGAGGACAACCCCATGGTGGTG
CCACTTTGCAACCGGTCGAAGGACGTGGTAGAGCCTCTGCTGCGGCCGCAGTGGTACGTT
CGCTGCGGGGAGATGGCCCAGGCTGCCAGCGCCGCTGTGACTCGGGGTGACCTCCGCATC
CTGCCTGAGGCCCATCAGCGCACATGGCATGCCTGGATGGACAACATCCGGGAGTGGTGC
ATTTCCAGGCAGCTGTGGTGGGGCCATCGCATCCCAGCCTACTTTGTCACTGTCAGTGAC
CCAGCGGTGCCCCCTGGGGAGGACCCTGATGGGCGGTACTGGGTGAGTGGACGCAATGAG
GCGGAGGCCCGGGAGAAGGCAGCCAAGGAGTTCGGAGTGTCCCCTGACAAGATCAGTCTC
CAGCAAGATGAGGATGTATTGGATACCTGGTTCTCCTCTGGCCTCTTCCCCTTATCCATT
TTGGGCTGGCCCAACCAGTCAGAAGACCTGAGTGTGTTCTACCCCGGGACACTGCTGGAG
ACCGGTCATGACATCCTCTTCTTCTGGGTGGCCCGGATGGTCATGCTGGGCCTGAAGCTC
ACGGGCAGGCTGCCCTTTAGAGAGGTCTACCTCCATGCCATCGTGCGAGATGCTCACGGC
CGGAAGATGAGCAAGTCTCTAGGCAATGTCATCGATCCCCTGGATGTCATCTATGGAATC
TCCCTGCAGGGCCTCCACAACCAGCTGCTGAACAGCAACCTGGATCCCAGCGAGGTGGAG
AAGGCCAAAGAAGGGCAGAAAGCTGACTTCCCAGCGGGGATTCCTGAATGTGGCACCGAT
GCTCTCCGGTTTGGATTATGTGCCTACATGTCCCAGGGTCGTGACATCAACCTGGATGTG
AACCGGATACTGGGTTACCGCCACTTCTGCAACAAGCTCTGGAATGCCACCAAGTTTGCC
CTTCGTGGCCTTGGGAAGGGTTTTGTGCCCTCACCCACCTCCCAGCCCGGAGGCCATGAG
AGCCTGGTGGACCGCTGGATCCGCAGCCGCCTGACAGAGGCTGTGAGGCTCAGCAATCAA
GGCTTCCAGGCCTACGACTTCCCGGCCGTCACCACTGCCCAGTACAGCTTCTGGCTCTAT
GAGCTCTGTGATGTCTACTTGGAGTGCCTGAAACCTGTACTGAATGGGGTGGACCAGGTG
GCAGCTGAGTGTGCCCGCCAGACCCTGTACACTTGCCTGGACGTTGGCCTGCGGCTGCTC
TCACCCTTCATGCCCTTCGTGACGGAGGAGCTGTTCCAGAGGCTGCCCCGGAGGATGCCG
CAAGCTCCCCCTAGCCTCTGTGTTACCCCCTACCCGGAGCCCTCAGAGTGCTCCTGGAAG
GACCCCGAGGCAGAAGCCGCCCTTGAGCTGGCGCTAAGCATCACGCGAGCCGTGCGCTCC
CTGCGGGCCGACTACAACCTCACCCGGATCCGGCCTGACTGTTTCCTGGAAGTGGCGGAT
GAGGCCACGGGCGCCCTGGCATCGGCGGTGTCGGGCTACGTGCAGGCCCTGGCCAGCGCA
GGTGTGGTGGCTGTTCTGGCCCTGGGGGCTCCCGCCCCCCAGGGTTGCGCTGTGGCTCTG
GCTTCTGATCGCTGCTCCATCCACCTGCAGCTTCAGGGGCTGGTGGACCCTGCACGGGAG
CTGGGCAAGCTGCAAGCCAAGCGAGTTGAGGCCCAGCGGCAGGCCCAGCGTCTGCGGGAA
CGCCGTGCTGCCTCGGGCTATCCTGTCAAGGTGCCGCTCGAAGTCCAGGAGGCAGATGAA
GCCAAGCTCCAACAGACAGAAGCAGAGCTCAGGAAGGTGGATGAGGCCATCGCCCTATTC
CAGAAGATGCTGTGA
|
| Enzyme 100 GenBank Gene ID |
AF134726 |
| Enzyme 100 GeneCard ID |
VARS |
| Enzyme 100 GenAtlas ID |
VARS |
| Enzyme 100 HGNC ID |
HGNC:12651 |
| Enzyme 100 Chromosome Location |
6 |
| Enzyme 100 Locus |
6p21.3 |
| Enzyme 100 SNPs |
SNPJam Report |
| Enzyme 100 General References |
- Hsieh SL, Campbell RD: Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase. Biochem J. 1991 Sep 15;278 ( Pt 3):809-16. [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 ]
- Vilalta A, Donovan D, Wood L, Vogeli G, Yang DC: Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase. Gene. 1993 Jan 30;123(2):181-6. [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 ]
|
| Enzyme 100 Metabolite References |
Not Available |
|
Enzyme 101
[top]
|
| Enzyme 101 ID |
5924 |
| Enzyme 101 Name |
Adenylate kinase isoenzyme 5 |
| Enzyme 101 Synonyms |
- AK 5
- ATP-AMP transphosphorylase 5
|
| Enzyme 101 Gene Name |
AK5 |
| Enzyme 101 Protein Sequence |
>Adenylate kinase isoenzyme 5
MNTNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFV
SQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIE
EYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKW
SLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVIDGFPRDVAQALSFEDQICTPDLV
VFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDA
DRDEDEVFYDISMAVDNKLFPNKEAAAGSSDLDPSMILDTGEIIDTGSDYEDQGDDQLNV
FGEDTMGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESE
RSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDP
QLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHK
INAEGTPEDVFLQLCTAIDSIF
|
| Enzyme 101 Number of Residues |
562 |
| Enzyme 101 Molecular Weight |
63332.4 |
| Enzyme 101 Theoretical pI |
4.69 |
| Enzyme 101 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- adenylate kinase activity
- binding
- catalytic activity
- kinase activity
- nucleobase, nucleoside, nucleotide kinase activity
- nucleoside binding
- phosphotransferase activity, phosphate group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- ATP metabolic 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 phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside triphosphate metabolic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 101 General Function |
Involved in ATP binding |
| Enzyme 101 Specific Function |
Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP |
| Enzyme 101 Pathways |
|
| Enzyme 101 Reactions |
- ATP + AMP = 2 ADP [RN:R00127]
|
| Enzyme 101 Pfam Domain Function |
|
| Enzyme 101 Signals |
|
| Enzyme 101 Transmembrane Regions |
|
| Enzyme 101 Essentiality |
Not Available |
| Enzyme 101 GenBank ID Protein |
28144897 |
| Enzyme 101 UniProtKB/Swiss-Prot ID |
Q9Y6K8 |
| Enzyme 101 UniProtKB/Swiss-Prot Entry Name |
KAD5_HUMAN |
| Enzyme 101 PDB ID |
Not Available |
| Enzyme 101 Cellular Location |
Not Available |
| Enzyme 101 Gene Sequence |
>1689 bp
ATGAACACCAACGATGCCAAGGAGTATCTGGCCCGGAGGGAAATCCCTCAGCTTTTTGAG
AGCCTTTTGAATGGACTGATGTGTTCTAAGCCCGAAGATCCAGTAGAATACTTGGAAAGT
TGTTTACAAAAAGTAAAGGAACTGGGTGGCTGTGACAAGGTGAAATGGGATACATTTGTA
AGCCAGGAAAAGAAGACCTTACCTCCACTAAATGGAGGACAGTCACGGAGATCCTTTCTA
AGAAATGTAATGCCTGAAAACTCAAACTTTCCATATCGGCGGTATGACCGGCTCCCTCCA
ATCCATCAATTCTCCATAGAAAGTGACACGGATCTCTCTGAGACTGCAGAGTTGATTGAG
GAGTATGAGGTTTTTGATCCTACCAGACCTCGACCAAAAATCATTCTTGTTATAGGTGGT
CCAGGAAGTGGAAAGGGTACTCAGAGTTTGAAAATTGCAGAACGATATGGATTCCAATAC
ATTTCTGTGGGAGAATTATTAAGAAAGAAGATCCACAGTACCAGCAGCAATAGGAAATGG
AGTCTTATTGCCAAGATAATTACAACTGGAGAATTGGCCCCACAGGAAACAACAATTACA
GAGATAAAACAAAAATTGATGCAAATACCTGATGAAGAGGGCATTGTTATTGATGGATTT
CCAAGAGATGTTGCCCAGGCTCTATCTTTTGAGGACCAAATCTGTACCCCCGATTTGGTG
GTATTCCTGGCTTGTGCTAATCAGAGACTCAAAGAAAGATTACTGAAGCGTGCAGAACAG
CAGGGCCGACCAGACGACAATGTAAAAGCTACCCAAAGGAGACTAATGAACTTCAAGCAG
AATGCTGCTCCATTGGTTAAATACTTCCAGGAAAAGGGGCTCATCATGACATTTGATGCC
GACCGCGATGAGGATGAGGTGTTCTATGACATCAGCATGGCAGTTGACAACAAGTTATTT
CCAAACAAAGAGGCTGCAGCAGGTTCAAGTGACCTTGATCCTTCGATGATATTGGACACT
GGAGAGATCATTGATACAGGATCTGATTATGAAGATCAGGGTGATGACCAGTTAAATGTA
TTTGGAGAGGACACTATGGGAGGTTTCATGGAAGATTTGAGAAAGTGTAAAATTATTTTC
ATAATTGGTGGTCCTGGCTCTGGCAAAGGCACACAGTGTGAAAAGCTGGTGGAAAAATAT
GGATTTACACATCTCTCAACTGGCGAGCTCCTGCGTGAGGAACTGGCATCAGAATCTGAA
AGAAGCAAATTGATCAGAGACATTATGGAACGTGGAGACCTGGTGCCCTCAGGCATCGTT
TTGGAGCTCCTGAAGGAGGCCATGGTGGCCAGCCTCGGGGACACCAGGGGCTTCCTGATT
GACGGCTATCCTCGGGAGGTGAAGCAAGGGGAAGAGTTCGGACGCAGGATTGGAGACCCA
CAGTTGGTGATCTGTATGGACTGCTCGGCAGACACCATGACCAACCGCCTTCTCCAAAGG
AGCCGGAGCAGCCTGCCTGTGGACGACACCACCAAGACCATCGCCAAGCGCCTAGAAGCC
TACTACCGAGCGTCCATCCCCGTGATCGCCTACTACGAGACAAAAACACAGCTACACAAG
ATAAATGCAGAGGGAACACCAGAGGACGTTTTTCTTCAACTCTGCACAGCTATTGACTCT
ATTTTCTGA
|
| Enzyme 101 GenBank Gene ID |
NM_174858.1 |
| Enzyme 101 GeneCard ID |
AK5 |
| Enzyme 101 GenAtlas ID |
AK5 |
| Enzyme 101 HGNC ID |
HGNC:365 |
| Enzyme 101 Chromosome Location |
1 |
| Enzyme 101 Locus |
1p31 |
| Enzyme 101 SNPs |
SNPJam Report |
| Enzyme 101 General References |
- Van Rompay AR, Johansson M, Karlsson A: Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur J Biochem. 1999 Apr;261(2):509-17. [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 |
5925 |
| Enzyme 102 Name |
Selenide, water dikinase 1 |
| Enzyme 102 Synonyms |
- Selenium donor protein 1
- Selenophosphate synthase 1
|
| Enzyme 102 Gene Name |
SEPHS1 |
| Enzyme 102 Protein Sequence |
>Selenide, water dikinase 1
MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAV
MPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECD
NMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVC
QPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMA
AVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKG
NRTARIIDKPRIIEVAPQVATQNVNPTPGATS
|
| Enzyme 102 Number of Residues |
392 |
| Enzyme 102 Molecular Weight |
42910.3 |
| Enzyme 102 Theoretical pI |
5.84 |
| Enzyme 102 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- purine nucleoside binding
- selenide, water dikinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 102 General Function |
Involved in catalytic activity |
| Enzyme 102 Specific Function |
Synthesizes selenophosphate from selenide and ATP |
| Enzyme 102 Pathways |
|
| Enzyme 102 Reactions |
- ATP + selenide + H2O = AMP + selenophosphate + phosphate [RN:R03595]
|
| Enzyme 102 Pfam Domain Function |
|
| Enzyme 102 Signals |
|
| Enzyme 102 Transmembrane Regions |
|
| Enzyme 102 Essentiality |
Not Available |
| Enzyme 102 GenBank ID Protein |
55957750 |
| Enzyme 102 UniProtKB/Swiss-Prot ID |
P49903 |
| Enzyme 102 UniProtKB/Swiss-Prot Entry Name |
SPS1_HUMAN |
| Enzyme 102 PDB ID |
Not Available |
| Enzyme 102 Cellular Location |
Not Available |
| Enzyme 102 Gene Sequence |
>1179 bp
ATGTCTACGCGGGAGTCCTTTAACCCGGAAAGTTACGAATTGGACAAAAGCTTCCGGCTA
ACCAGATTCACTGAACTGAAGGGCACAGGCTGCAAAGTGCCCCAAGATGTCCTGCAAAAA
TTGCTGGAATCTTTACAGGAGAACCACTTCCAAGAAGATGAGCAGTTTCTGGGAGCCGTT
ATGCCAAGGCTTGGCATTGGAATGGATACTTGTGTCATTCCTTTGAGGCACGGTGGGCTT
TCCTTGGTTCAAACCACAGATTACATTTACCCGATCGTAGACGACCCTTACATGATGGGC
AGGATAGCGTGTGCCAATGTCCTCAGTGACCTCTATGCAATGGGGGTCACGGAATGTGAC
AATATGCTGATGCTCCTTGGAGTCAGTAATAAAATGACCGACAGGGAAAGGGATAAAGTG
ATGCCTCTGATTATCCAAGGTTTTAAAGACGCAGCTGAGGAAGCAGGAACATCTGTAACA
GGCGGCCAAACAGTACTAAACCCCTGGATTGTCCTGGGAGGAGTGGCTACCACTGTCTGC
CAACCCAATGAATTTATCATGCCAGACAATGCAGTGCCAGGGGACGTGCTGGTGCTGACA
AAACCCCTGGGGACACAGGTGGCAGTGGCTGTGCACCAGTGGCTGGATATCCCTGAGAAA
TGGAATAAGATTAAACTAGTGGTCACCCAAGAAGATGTAGAGCTGGCCTACCAGGAGGCG
ATGATGAACATGGCGAGGCTCAACAGGACAGCTGCAGGACTCATGCACACGTTCAATGCC
CACGCCGCCACTGACATCACGGGCTTCGGGATTTTGGGCCATGCGCAGAACCTGGCCAAG
CAGCAGAGGAACGAGGTGTCGTTTGTAATTCACAACCTCCCGGTGCTGGCCAAGATGGCT
GCGGTGAGCAAGGCCTGCGGAAACATGTTCGGCCTCATGCACGGGACCTGCCCGGAGACT
TCAGGCGGCCTTCTGATCTGTTTACCACGTGAGCAAGCAGCTCGGTTCTGTGCAGAGATA
AAGTCCCCCAAATATGGTGAAGGCCACCAAGCATGGATTATTGGGATTGTAGAGAAGGGC
AACCGCACAGCCAGAATCATAGACAAACCCCGGATCATCGAGGTCGCACCACAAGTGGCC
ACTCAAAATGTGAATCCCACACCCGGGGCCACCTCTTAA
|
| Enzyme 102 GenBank Gene ID |
AL138764 |
| Enzyme 102 GeneCard ID |
SEPHS1 |
| Enzyme 102 GenAtlas ID |
SEPHS1 |
| Enzyme 102 HGNC ID |
HGNC:19685 |
| Enzyme 102 Chromosome Location |
1 |
| Enzyme 102 Locus |
10p14 |
| Enzyme 102 SNPs |
SNPJam Report |
| Enzyme 102 General References |
- Low SC, Harney JW, Berry MJ: Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J Biol Chem. 1995 Sep 15;270(37):21659-64. [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 ]
- 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 ]
- Wang KT, Wang J, Li LF, Su XD: Crystal structures of catalytic intermediates of human selenophosphate synthetase 1. J Mol Biol. 2009 Jul 24;390(4):747-59. Epub 2009 May 25. [PubMed ]
|
| Enzyme 102 Metabolite References |
Not Available |
|
Enzyme 103
[top]
|
| Enzyme 103 ID |
5926 |
| Enzyme 103 Name |
Ubiquitin-conjugating enzyme E2 N |
| Enzyme 103 Synonyms |
- Bendless-like ubiquitin-conjugating enzyme
- Ubc13
- Ubiquitin carrier protein N
- Ubiquitin-protein ligase N
|
| Enzyme 103 Gene Name |
UBE2N |
| Enzyme 103 Protein Sequence |
>Ubiquitin-conjugating enzyme E2 N
MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPE
EYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDP
LANDVAEQWKTNEAQAIETARAWTRLYAMNNI
|
| Enzyme 103 Number of Residues |
152 |
| Enzyme 103 Molecular Weight |
17137.6 |
| Enzyme 103 Theoretical pI |
6.53 |
| Enzyme 103 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- small conjugating protein ligase activity
|
| Process |
- biological regulation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein modification process
- regulation of biological process
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of protein metabolic process
|
| Component |
| — |
|
| Enzyme 103 General Function |
Involved in acid-amino acid ligase activity |
| Enzyme 103 Specific Function |
The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD |
| Enzyme 103 Pathways |
- Ubiquitin mediated proteolysis (map04120 )
|
| Enzyme 103 Reactions |
- ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine [RN:R03876]
|
| Enzyme 103 Pfam Domain Function |
|
| Enzyme 103 Signals |
|
| Enzyme 103 Transmembrane Regions |
|
| Enzyme 103 Essentiality |
Not Available |
| Enzyme 103 GenBank ID Protein |
12653255 |
| Enzyme 103 UniProtKB/Swiss-Prot ID |
P61088 |
| Enzyme 103 UniProtKB/Swiss-Prot Entry Name |
UBE2N_HUMAN |
| Enzyme 103 PDB ID |
1J7D |
| Enzyme 103 PDB File |
Show |
| Enzyme 103 3D Structure |
|
| Enzyme 103 Cellular Location |
Not Available |
| Enzyme 103 Gene Sequence |
>459 bp
ATGGCCGGGCTGCCCCGCAGGATCATCAAGGAAACCCAGCGTTTGCTGGCAGAACCAGTT
CCTGGCATCAAAGCCGAACCAGATGAGAGCAACGCCCGTTATTTTCATGTGGTCATTGCT
GGCCCTCAGGATTCCCCCTTTGAGGGAGGGACTTTTAAACTTGAACTATTCCTTCCAGAA
GAATACCCAATGGCAGCCCCTAAAGTACGTTTCATGACCAAAATTTATCATCCTAATGTA
GACAAGTTGGGAAGAATATGTTTAGATATTTTGAAAGATAAGTGGTCCCCAGCACTGCAG
ATCCGCACAGTTCTGCTATCGATCCAGGCCTTGTTAAGTGCTCCCAATCCAGATGATCCA
TTAGCAAATGATGTAGCGGAGCAGTGGAAGACCAACGAAGCCCAAGCCATAGAAACAGCT
AGAGCATGGACTAGGCTATATGCCATGAATAATATTTAA
|
| Enzyme 103 GenBank Gene ID |
BC000396 |
| Enzyme 103 GeneCard ID |
UBE2N |
| Enzyme 103 GenAtlas ID |
UBE2N |
| Enzyme 103 HGNC ID |
HGNC:12492 |
| Enzyme 103 Chromosome Location |
1 |
| Enzyme 103 Locus |
12q22 |
| Enzyme 103 SNPs |
SNPJam Report |
| Enzyme 103 General References |
- Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S: Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product. J Biochem (Tokyo). 1996 Sep;120(3):494-97. [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 ]
- Zou W, Papov V, Malakhova O, Kim KI, Dao C, Li J, Zhang DE: ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin. Biochem Biophys Res Commun. 2005 Oct 14;336(1):61-8. [PubMed ]
- Hofmann RM, Pickart CM: Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 1999 Mar 5;96(5):645-53. [PubMed ]
- Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD: The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains. Oncogene. 2003 Oct 16;22(46):7101-7. [PubMed ]
- Takeuchi T, Yokosawa H: ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity. Biochem Biophys Res Commun. 2005 Oct 14;336(1):9-13. [PubMed ]
- Motegi A, Sood R, Moinova H, Markowitz SD, Liu PP, Myung K: Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination. J Cell Biol. 2006 Dec 4;175(5):703-8. Epub 2006 Nov 27. [PubMed ]
- Plans V, Scheper J, Soler M, Loukili N, Okano Y, Thomson TM: The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation. J Cell Biochem. 2006 Feb 15;97(3):572-82. [PubMed ]
- Unk I, Hajdu I, Fatyol K, Szakal B, Blastyak A, Bermudez V, Hurwitz J, Prakash L, Prakash S, Haracska L: Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18107-12. Epub 2006 Nov 15. [PubMed ]
- Lamothe B, Besse A, Campos AD, Webster WK, Wu H, Darnay BG: Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation. J Biol Chem. 2007 Feb 9;282(6):4102-12. Epub 2006 Nov 29. [PubMed ]
- Unk I, Hajdu I, Fatyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L: Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination. Proc Natl Acad Sci U S A. 2008 Mar 11;105(10):3768-73. Epub 2008 Mar 3. [PubMed ]
- Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung K: Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks. Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12411-6. Epub 2008 Aug 21. [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 ]
- Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES, Nakada S, Ylanko J, Olivarius S, Mendez M, Oldreive C, Wildenhain J, Tagliaferro A, Pelletier L, Taubenheim N, Durandy A, Byrd PJ, Stankovic T, Taylor AM, Durocher D: The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell. 2009 Feb 6;136(3):420-34. [PubMed ]
- Tcherpakov M, Delaunay A, Toth J, Kadoya T, Petroski MD, Ronai ZA: Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP). J Biol Chem. 2009 May 1;284(18):12099-109. Epub 2009 Mar 6. [PubMed ]
- Marteijn JA, van der Meer LT, Smit JJ, Noordermeer SM, Wissink W, Jansen P, Swarts HG, Hibbert RG, de Witte T, Sixma TK, Jansen JH, van der Reijden BA: The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains. Leukemia. 2009 Aug;23(8):1480-9. Epub 2009 Apr 2. [PubMed ]
- Scheper J, Oliva B, Villa-Freixa J, Thomson TM: Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes. Proteins. 2009 Jan;74(1):92-103. [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 ]
- David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. Epub 2010 Jan 8. [PubMed ]
- Moraes TF, Edwards RA, McKenna S, Pastushok L, Xiao W, Glover JN, Ellison MJ: Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. Nat Struct Biol. 2001 Aug;8(8):669-73. [PubMed ]
|
| Enzyme 103 Metabolite References |
Not Available |
|
Enzyme 104
[top]
|
| Enzyme 104 ID |
5928 |
| Enzyme 104 Name |
Argininosuccinate synthase |
| Enzyme 104 Synonyms |
- Citrulline--aspartate ligase
|
| Enzyme 104 Gene Name |
ASS1 |
| Enzyme 104 Protein Sequence |
>Argininosuccinate synthase
MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVF
IEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATG
KGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWS
MDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKD
GTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAF
TMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYI
LGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK
|
| Enzyme 104 Number of Residues |
412 |
| Enzyme 104 Molecular Weight |
46530.1 |
| Enzyme 104 Theoretical pI |
8.18 |
| Enzyme 104 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- argininosuccinate synthase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- arginine biosynthetic process
- arginine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 104 General Function |
Involved in argininosuccinate synthase activity |
| Enzyme 104 Specific Function |
ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate |
| Enzyme 104 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 104 Reactions |
- ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate [RN:R01954]
|
| Enzyme 104 Pfam Domain Function |
|
| Enzyme 104 Signals |
|
| Enzyme 104 Transmembrane Regions |
|
| Enzyme 104 Essentiality |
Not Available |
| Enzyme 104 GenBank ID Protein |
28872 |
| Enzyme 104 UniProtKB/Swiss-Prot ID |
P00966 |
| Enzyme 104 UniProtKB/Swiss-Prot Entry Name |
ASSY_HUMAN |
| Enzyme 104 PDB ID |
Not Available |
| Enzyme 104 Cellular Location |
Not Available |
| Enzyme 104 Gene Sequence |
>1239 bp
ATGTCCAGCAAAGGCTCCGTGGTTCTGGCCTACAGTGGCGGCCTGGACACCTCGTGCATC
CTCGTGTGGCTGAAGGAACAAGGCTATGACGTCATTGCCTATCTGGCCAACATTGGCCAG
AAGGAAGACTTCGAGGAAGCCAGGAAGAAGGCACTGAAGCTTGGGGCCAAAAAGGTGTTC
ATTGAGGATGTCAGCAGGGAGTTTGTGGAGGAGTTCATCTGGCCGGCCATCCAGTCCAGC
GCACTGTATGAGGACCGCTACCTCCTGGGCACCTCTCTTGCCAGGCCCTGCATCGCCCGC
AAACAAGTGGAAATCGCCCAGCGGGAGGGGGCCAAGTATGTGTCCCACGGCGCCACAGGA
AAGGGGAACGATCAGGTCCGGTTTGAGCTCAGCTGCTACTCACTGGCCCCCCAGATAAAG
GTCATTGCTCCCTGGAGGATGCCTGAATTCTACAACCGGTTCAAGGGCCGCAATGACCTG
ATGGAGTACGCAAAGCAACACGGGATTCCCATCCCGGTCACTCCCAAGAACCCGTGGAGC
ATGGATGAGAACCTCATGCACATCAGCTACGAGGCTGGAATCCTGGAGAACCCCAAGAAC
CAAGCGCCTCCAGGTCTCTACACGAAGACCCAGGACCCAGCCAAAGCCCCCAACACCCCT
GACATTCTCGAGATCGAGTTCAAAAAAGGGGTCCCTGTGAAGGTGACCAACGTCAAGGAT
GGCACCACCCACCAGACCTCCTTGGAGCTCTTCATGTACCTGAACGAAGTCGCGGGCAAG
CATGGCGTGGGCCGTATTGACATCGTGGAGAACCGCTTCATTGGAATGAAGTCCCGAGGT
ATCTACGAGACCCCAGCAGGCACCATCCTTTACCATGCTCATTTAGACATCGAGGCCTTC
ACCATGGACCGGGAAGTGCGCAAAATCAAACAAGGCCTGGGCTTGAAATTTGCTGAGCTG
GTGTATACCGGTTTACGGCCTAGCCCTGAGTGTGAATTTGTCCGCCACTGCATCGCCAAG
TCCCAGGAGCGAGTGGAAGGGAAAGTGCAGGTGTCCGTCCTCAAGGGCCAGGTGTACATC
CTCGGCCGGGAGTCCCCACTGTCTCTCTACAATGAGGAGCTGGTGAGCATGAACGTGCAG
GGTGATTATGAGCCAACTGATGCCACCGGGTTCATCAACATCAATTCCCTCAGGCTGAAG
GAATATCATCGTCTCCAGAGCAAGGTCACTGCCAAATAG
|
| Enzyme 104 GenBank Gene ID |
X01630 |
| Enzyme 104 GeneCard ID |
ASS1 |
| Enzyme 104 GenAtlas ID |
ASS1 |
| Enzyme 104 HGNC ID |
HGNC:758 |
| Enzyme 104 Chromosome Location |
9 |
| Enzyme 104 Locus |
9q34.1 |
| Enzyme 104 SNPs |
SNPJam Report |
| Enzyme 104 General References |
- Bock HG, Su TS, O'Brien WE, Beaudet AL: Sequence for human argininosuccinate synthetase cDNA. Nucleic Acids Res. 1983 Sep 24;11(18):6505-12. [PubMed ]
- Freytag SO, Bock HG, Beaudet AL, O'Brien WE: Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications. J Biol Chem. 1984 Mar 10;259(5):3160-6. [PubMed ]
- Haberle J, Pauli S, Linnebank M, Kleijer WJ, Bakker HD, Wanders RJ, Harms E, Koch HG: Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia. Hum Genet. 2002 Apr;110(4):327-33. Epub 2002 Mar 1. [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 ]
- Jinno Y, Nomiyama H, Matuo S, Shimada K, Matsuda I, Saheki T: Structure of the 5' end region of the human argininosuccinate synthetase gene. J Inherit Metab Dis. 1985;8(3):157-9. [PubMed ]
- Isashiki Y, Noda T, Kobayashi K, Sase M, Saheki T, Titani K: Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase. Protein Seq Data Anal. 1989 Jul;2(4):283-7. [PubMed ]
- Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed ]
- Zheng X, Dai X, Zhao Y, Chen Q, Lu F, Yao D, Yu Q, Liu X, Zhang C, Gu X, Luo M: Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein. Proc Natl Acad Sci U S A. 2007 May 22;104(21):8809-14. Epub 2007 May 11. [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 ]
- 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 ]
- Engel K, Hohne W, Haberle J: Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene. Hum Mutat. 2009 Mar;30(3):300-7. [PubMed ]
- Kobayashi K, Jackson MJ, Tick DB, O'Brien WE, Beaudet AL: Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia. J Biol Chem. 1990 Jul 5;265(19):11361-7. [PubMed ]
- Kobayashi K, Rosenbloom C, Beaudet AL, O'Brien WE: Additional mutations in argininosuccinate synthetase causing citrullinemia. Mol Biol Med. 1991 Feb;8(1):95-100. [PubMed ]
- Kobayashi K, Shaheen N, Terazono H, Saheki T: Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia. Am J Hum Genet. 1994 Dec;55(6):1103-12. [PubMed ]
- Shaheen N, Kobayashi K, Terazono H, Fukushige T, Horiuchi M, Saheki T: Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells. Enzyme Protein. 1994-1995;48(5-6):251-64. [PubMed ]
- Vilaseca MA, Kobayashi K, Briones P, Lambruschini N, Campistol J, Tabata A, Alomar A, Rodes M, Lluch M, Saheki T: Phenotype and genotype heterogeneity in Mediterranean citrullinemia. Mol Genet Metab. 2001 Nov;74(3):396-8. [PubMed ]
- Gao HZ, Kobayashi K, Tabata A, Tsuge H, Iijima M, Yasuda T, Kalkanoglu HS, Dursun A, Tokatli A, Coskun T, Trefz FK, Skladal D, Mandel H, Seidel J, Kodama S, Shirane S, Ichida T, Makino S, Yoshino M, Kang JH, Mizuguchi M, Barshop BA, Fuchinoue S, Seneca S, Zeesman S, Knerr I, Rodes M, Wasant P, Yoshida I, De Meirleir L, Abdul Jalil M, Begum L, Horiuchi M, Katunuma N, Nakagawa S, Saheki T: Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients. Hum Mutat. 2003 Jul;22(1):24-34. [PubMed ]
- Haberle J, Pauli S, Schmidt E, Schulze-Eilfing B, Berning C, Koch HG: Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1). Mol Genet Metab. 2003 Nov;80(3):302-6. [PubMed ]
- Kleijer WJ, Garritsen VH, van der Sterre ML, Berning C, Haberle J, Huijmans JG: Prenatal diagnosis of citrullinemia and argininosuccinic aciduria: evidence for a transmission ratio distortion in citrullinemia. Prenat Diagn. 2006 Mar;26(3):242-7. [PubMed ]
|
| Enzyme 104 Metabolite References |
Not Available |
|
Enzyme 105
[top]
|
| Enzyme 105 ID |
5930 |
| Enzyme 105 Name |
Selenide, water dikinase 2 |
| Enzyme 105 Synonyms |
- Selenium donor protein 2
- Selenophosphate synthase 2
|
| Enzyme 105 Gene Name |
SEPHS2 |
| Enzyme 105 Protein Sequence |
>Selenide, water dikinase 2
MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGU
GCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMD
SCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVS
QSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPD
SAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNR
TAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRF
GLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKP
RVIEVLPRGATAAVLAPDSSNASSEPSS
|
| Enzyme 105 Number of Residues |
448 |
| Enzyme 105 Molecular Weight |
47304.7 |
| Enzyme 105 Theoretical pI |
5.69 |
| Enzyme 105 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- purine nucleoside binding
- selenide, water dikinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 105 General Function |
Involved in catalytic activity |
| Enzyme 105 Specific Function |
Synthesizes selenophosphate from selenide and ATP |
| Enzyme 105 Pathways |
|
| Enzyme 105 Reactions |
- ATP + selenide + H2O = AMP + selenophosphate + phosphate [RN:R03595]
|
| Enzyme 105 Pfam Domain Function |
|
| Enzyme 105 Signals |
|
| Enzyme 105 Transmembrane Regions |
|
| Enzyme 105 Essentiality |
Not Available |
| Enzyme 105 GenBank ID Protein |
Not Available |
| Enzyme 105 UniProtKB/Swiss-Prot ID |
Q99611 |
| Enzyme 105 UniProtKB/Swiss-Prot Entry Name |
SPS2_HUMAN |
| Enzyme 105 PDB ID |
Not Available |
| Enzyme 105 Cellular Location |
Not Available |
| Enzyme 105 Gene Sequence |
>1347 bp
ATGGCGGAAGCCTCGGCGACGGGCGCCTGCGGAGAGGCGATGGCAGCGGCGGAAGGCTCC
TCGGGCCCGGCGGGCTTGACTCTGGGCCGGAGCTTCTCGAACTACCGGCCCTTCGAGCCC
CAGGCGTTGGGCCTCAGCCCGAGCTGGCGGCTGACGGGCTTCTCCGGCATGAAGGGCTGA
GGCTGCAAGGTCCCGCAGGAGGCGCTGCTCAAACTCCTGGCGGGACTGACGCGGCCGGAC
GTGCGGCCCCCGCTGGGCCGGGGCCTGGTGGGTGGCCAGGAAGAGGCGTCCCAGGAAGCC
GGCCTGCCGGCAGGAGCGGGCCCCAGCCCCACCTTTCCAGCCCTGGGCATCGGGATGGAC
TCCTGCGTCATCCCCCTGAGGCACGGGGGCCTGTCACTGGTGCAGACCACGGACTTCTTT
TACCCCTTGGTAGAAGATCCCTACATGATGGGGCGCATAGCTTGTGCCAACGTGCTGAGT
GACCTCTACGCCATGGGGATTACTGAGTGTGACAACATGTTGATGTTACTCAGCGTCAGC
CAGAGTATGAGTGAGGAGGAACGCGAAAAGGTAACGCCACTCATGGTCAAAGGCTTTCGG
GATGCGGCTGAGGAAGGAGGGACGGCAGTGACCGGTGGGCAAACGGTGGTCAACCCTTGG
ATTATAATCGGTGGAGTTGCCACTGTAGTATGCCAACCAAATGAGTTCATAATGCCGGAC
AGCGCCGTCGTTGGGGACGTGCTGGTGTTAACCAAACCGTTAGGAACCCAGGTTGCTGTC
AATGCCCACCAATGGCTGGATAATCCTGAAAGATGGAATAAAGTAAAGATGGTGGTCTCC
AGAGAAGAGGTGGAGCTGGCCTATCAGGAAGCCATGTTCAATATGGCTACCCTCAACAGA
ACTGCTGCAGGTTTAATGCACACATTTAATGCCCATGCGGCCACAGATATCACAGGCTTT
GGCATTCTAGGACACTCCCAGAACCTTGCAAAACAACAAAGAAATGAAGTGTCCTTTGTT
ATTCATAATCTGCCAATAATTGCCAAGATGGCTGCCGTCAGCAAGGCCAGTGGACGGTTT
GGGCTTCTTCAAGGAACCTCAGCTGAAACCTCTGGGGGATTACTGATTTGTCTGCCAAGA
GAACAGGCGGCTCGCTTTTGTTCTGAAATCAAATCCTCCAAGTACGGAGAGGGTCACCAA
GCGTGGATCGTTGGCATTGTGGAAAAGGGAAACCGAACGGCCCGGATCATTGACAAGCCG
CGAGTTATTGAAGTCCTGCCTCGTGGGGCCACAGCTGCTGTTCTTGCTCCTGACAGTTCA
AATGCCTCCTCTGAGCCTAGCTCGTGA
|
| Enzyme 105 GenBank Gene ID |
U43286 |
| Enzyme 105 GeneCard ID |
SEPHS2 |
| Enzyme 105 GenAtlas ID |
SEPHS2 |
| Enzyme 105 HGNC ID |
HGNC:19686 |
| Enzyme 105 Chromosome Location |
1 |
| Enzyme 105 Locus |
16p11.2 |
| Enzyme 105 SNPs |
SNPJam Report |
| Enzyme 105 General References |
- Guimaraes MJ, Bazan JF, Zlotnik A, Wiles MV, Grimaldi JC, Lee F, McClanahan T: A new approach to the study of haematopoietic development in the yolk sac and embryoid bodies. Development. 1995 Oct;121(10):3335-46. [PubMed ]
- Guimaraes MJ, Peterson D, Vicari A, Cocks BG, Copeland NG, Gilbert DJ, Jenkins NA, Ferrick DA, Kastelein RA, Bazan JF, Zlotnik A: Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism? Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15086-91. [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 ]
- 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 105 Metabolite References |
Not Available |
|
Enzyme 106
[top]
|
| Enzyme 106 ID |
5932 |
| Enzyme 106 Name |
DNA ligase 1 |
| Enzyme 106 Synonyms |
- DNA ligase I
- Polydeoxyribonucleotide synthase [ATP] 1
|
| Enzyme 106 Gene Name |
LIG1 |
| Enzyme 106 Protein Sequence |
>DNA ligase 1
MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKA
ARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPK
RRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQ
PTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVK
KEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIE
EVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQ
ATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSAST
AKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAM
VDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPL
KPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPD
IISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAF
DLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCE
GLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLL
ASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSA
VWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQ
SQIQNQQGEDSGSDPEDTY
|
| Enzyme 106 Number of Residues |
919 |
| Enzyme 106 Molecular Weight |
101735.1 |
| Enzyme 106 Theoretical pI |
5.30 |
| Enzyme 106 GO Classification |
| Function |
- ATP binding
- DNA binding
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase (ATP) activity
- DNA ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleic acid binding
- nucleoside binding
- purine nucleoside binding
|
| Process |
- DNA ligation
- DNA ligation involved in DNA repair
- DNA metabolic process
- DNA recombination
- DNA repair
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 106 General Function |
Involved in DNA ligase (ATP) activity |
| Enzyme 106 Specific Function |
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair |
| Enzyme 106 Pathways |
Not Available |
| Enzyme 106 Reactions |
- ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP + diphosphate + (deoxyribonucleotide)n+m [RN:R00381]
|
| Enzyme 106 Pfam Domain Function |
|
| Enzyme 106 Signals |
|
| Enzyme 106 Transmembrane Regions |
|
| Enzyme 106 Essentiality |
Not Available |
| Enzyme 106 GenBank ID Protein |
187143 |
| Enzyme 106 UniProtKB/Swiss-Prot ID |
P18858 |
| Enzyme 106 UniProtKB/Swiss-Prot Entry Name |
DNLI1_HUMAN |
| Enzyme 106 PDB ID |
1X9N |
| Enzyme 106 PDB File |
Show |
| Enzyme 106 3D Structure |
|
| Enzyme 106 Cellular Location |
Not Available |
| Enzyme 106 Gene Sequence |
>2760 bp
ATGCAGCGAAGTATCATGTCATTTTTCCACCCCAAGAAAGAGGGTAAAGCAAAGAAGCCT
GAGAAGGAGGCATCCAATAGCAGCAGAGAGACGGAGCCCCCTCCAAAGGCGGCACTGAAG
GAGTGGAATGGAGTGGTGTCCGAGAGTGACTCTCCGGTGAAGAGGCCAGGGAGGAAGGCG
GCCCGGGTCCTGGGCAGCGAAGGGGAAGAGGAGGATGAAGCCCTTAGCCCTGCTAAAGGC
CAGAAGCCTGCCCTGGACTGCTCACAGGTCTCCCCGCCCCGTCCTGCCACATCTCCTGAG
AACAATGCTTCCCTCTCTGACACCTCTCCCATGGACAGTTCCCCATCAGGGATTCCGAAG
CGTCGCACAGCTCGGAAGCAGCTCCCGAAACGGACCATTCAGGAAGTCCTGGAAGAGCAG
AGTGAGGACGAGGACAGAGAAGCCAAGAGGAAGAAGGAGGAGGAAGAAGAGGAGACCCCG
AAAGAAAGCCTCACAGAGGCTGAAGTGGCAACAGAGAAGGAAGGAGAAGACGGGGACCAG
CCCACCACGCCTCCCAAGCCCCTAAAGACCTCCAAAGCAGAGACCCCGACGGAAAGCGTT
TCAGAGCCTGAGGTGGCCACGAAGCAGGAACTGCAGGAGGAGGAAGAGCAGACCAAGCCT
CCCCGCAGAGCTCCCAAGACGCTCAGCAGCTTCTTCACCCCCCGGAAGCCAGCAGTCAAA
AAAGAAGTGAAGGAAGAGGAGCCAGGGGCTCCAGGAAAGGAGGGAGCTGCTGAGGGACCC
CTGGATCCATCTGGTTACAATCCTGCCAAGAACAACTATCATCCCGTGGAAGATGCCTGC
TGGAAACCGGGCCAGAAGGTTCCTTACCTGGCTGTGGCCCGGACGTTTGAGAAGATCGAG
GAGGTGTCTGCTCGGCTCCGGATGGTGGAGACGCTGAGCAACTTGCTGCGCTCCGTGGTG
GCCCTGTCGCCTCCAGACCTCCTCCCTGTCCTCTACCTCAGCCTCAACCACCTTGGGCCA
CCCCAGCAGGGCCTGGAGCTTGGCGTGGGTGATGGTGTCCTTCTCAAGGCAGTGGCCCAG
GCCACAGGTCGGCAGCTGGAGTCCGTCCGGGCTGAGGCAGCCGAGAAAGGCGACGTGGGG
CTGGTGGCCGAGAACAGCCGCAGCACCCAGAGGCTCATGCTGCCACCACCTCCGCTCACT
GCCTCCGGGGTCTTCAGCAAGTTCCGCGACATCGCCAGGCTCACTGGCAGTGCTTCCACA
GCCAAGAAGATAGACATCATCAAAGGCCTCTTTGTGGCCTGCCGCCACTCAGAAGCCCGG
TTCATCGCTAGGTCCCTGAGCGGACGGCTGCGCCTTGGGCTGGCAGAGCAGTCGGTGCTG
GCTGCCCTCTCCCAGGCAGTGAGCCTCACGCCCCCGGGCCAAGAATTCCCACCAGCCATG
GTGGATGCTGGGAAGGGCAAGACAGCAGAGGCCAGAAAGACGTGGCTGGAGGAGCAAGGC
ATGATCCTGAAGCAGACGTTCTGCGAGGTTCCCGACCTGGACCGAATTATCCCCGTGCTG
CTGGAGCACGGCCTGGAACGTCTCCCGGAGCACTGCAAGCTGAGCCCAGGGATTCCCCTG
AAACCAATGTTGGCCCATCCCACCCGGGGCATCAGCGAGGTCCTGAAACGCTTTGAGGAG
GCAGCTTTCACCTGCGAATACAAATATGACGGGCAGAGGGCACAGATCCACGCCCTGGAA
GGCGGGGAGGTGAAGATCTTCAGCAGGAATCAGGAAGACAACACTGGGAAGTACCCGGAC
ATCATCAGCCGCATCCCCAAGATTAAACTCCCATCGGTCACATCCTTCATCCTGGACACC
GAAGCCGTGGCTTGGGACCGGGAAAAGAAGCAGATCCAGCCATTCCAAGTGCTCACCACC
CGCAAACGCAAGGAGGTGGATGCGTCTGAGATCCAGGTGCAGGTGTGTTTGTACGCCTTC
GACCTCATCTACCTCAATGGAGAGTCCCTGGTACGTGAGCCCCTTTCCCGGCGCCGGCAG
CTGCTCCGGGAGAACTTTGTGGAGACAGAGGGCGAGTTTGTCTTCGCCACCTCCCTGGAC
ACCAAGGACATCGAGCAGATCGCCGAGTTCCTGGAGCAGTCAGTGAAAGACTCCTGCGAG
GGGCTGATGGTGAAGACCCTGGATGTTGATGCCACCTACGAGATCGCCAAGAGATCGCAC
AACTGGCTCAAGCTGAAGAAGGACTACCTTGATGGCGTGGGTGACACCCTGGACCTGGTG
GTGATCGGCGCCTACCTGGGCCGGGGGAAGCGGGCCGGCCGGTACGGGGGCTTCCTGCTG
GCCTCCTACGACGAGGACAGTGAGGAGCTGCAGGCCATATGCAAGCTTGGAACTGGCTTC
AGTGATGAGGAGCTGGAGGAGCATCACCAGAGCCTCAAGGCGCTGGTGCTGCCCAGCCCA
CGCCCTTACGTGCGGATAGATGGCGCTGTGATTCCCGACCACTGGCTGGACCCCAGCGCT
GTGTGGGAGGTGAAGTGCGCTGACCTCTCCCTCTCTCCCATCTACCCTGCTGCGCGGGGC
CTGGTGGATAGTGACAAGGGCATCTCCCTTCGCTTCCCTCGGTTTATTCGAGTCCGTGAA
GACAAGCAGCCGGAGCAGGCCACCACCAGTGCTCAGGTGGCCTGTTTGTACCGGAAGCAA
AGTCAGATTCAGAACCAACAAGGCGAGGACTCAGGCTCTGACCCTGAAGATACCTACTAA
|
| Enzyme 106 GenBank Gene ID |
M36067 |
| Enzyme 106 GeneCard ID |
LIG1 |
| Enzyme 106 GenAtlas ID |
LIG1 |
| Enzyme 106 HGNC ID |
HGNC:6598 |
| Enzyme 106 Chromosome Location |
1 |
| Enzyme 106 Locus |
19q13.2-q13.3 |
| Enzyme 106 SNPs |
SNPJam Report |
| Enzyme 106 General References |
- Barnes DE, Johnston LH, Kodama K, Tomkinson AE, Lasko DD, Lindahl T: Human DNA ligase I cDNA: cloning and functional expression in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6679-83. [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 ]
- Petrini JH, Huwiler KG, Weaver DT: A wild-type DNA ligase I gene is expressed in Bloom's syndrome cells. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7615-9. [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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
- Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L, Gong Y, Xu BE, Wu J, Luo Y, Qiang B, Yuan J, Sun X, Peng X: Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells. Proteomics. 2008 Jul;8(14):2885-96. [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 ]
- Pascal JM, O'Brien PJ, Tomkinson AE, Ellenberger T: Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature. 2004 Nov 25;432(7016):473-8. [PubMed ]
- Barnes DE, Tomkinson AE, Lehmann AR, Webster AD, Lindahl T: Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents. Cell. 1992 May 1;69(3):495-503. [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 106 Metabolite References |
Not Available |
|
Enzyme 107
[top]
|
| Enzyme 107 ID |
5949 |
| Enzyme 107 Name |
CTP synthase 1 |
| Enzyme 107 Synonyms |
- CTP synthetase 1
- UTP--ammonia ligase 1
|
| Enzyme 107 Gene Name |
CTPS |
| Enzyme 107 Protein Sequence |
>CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
|
| Enzyme 107 Number of Residues |
591 |
| Enzyme 107 Molecular Weight |
66689.9 |
| Enzyme 107 Theoretical pI |
6.42 |
| Enzyme 107 GO Classification |
| Function |
- CTP synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| 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 phosphate metabolic process
- nucleotide metabolic process
- pyrimidine nucleotide biosynthetic process
- pyrimidine nucleotide metabolic process
|
| Component |
| — |
|
| Enzyme 107 General Function |
Involved in CTP synthase activity |
| Enzyme 107 Specific Function |
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen |
| Enzyme 107 Pathways |
|
| Enzyme 107 Reactions |
- ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
|
| Enzyme 107 Pfam Domain Function |
|
| Enzyme 107 Signals |
|
| Enzyme 107 Transmembrane Regions |
|
| Enzyme 107 Essentiality |
Not Available |
| Enzyme 107 GenBank ID Protein |
30293 |
| Enzyme 107 UniProtKB/Swiss-Prot ID |
P17812 |
| Enzyme 107 UniProtKB/Swiss-Prot Entry Name |
PYRG1_HUMAN |
| Enzyme 107 PDB ID |
Not Available |
| Enzyme 107 Cellular Location |
Not Available |
| Enzyme 107 Gene Sequence |
>1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
|
| Enzyme 107 GenBank Gene ID |
X52142 |
| Enzyme 107 GeneCard ID |
CTPS |
| Enzyme 107 GenAtlas ID |
CTPS |
| Enzyme 107 HGNC ID |
HGNC:2519 |
| Enzyme 107 Chromosome Location |
1 |
| Enzyme 107 Locus |
1p34.1 |
| Enzyme 107 SNPs |
SNPJam Report |
| Enzyme 107 General References |
- Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [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 ]
- 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 ]
- Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [PubMed ]
- Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed ]
- Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [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 ]
- 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 ]
- 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 ]
|
| Enzyme 107 Metabolite References |
Not Available |
|
Enzyme 108
[top]
|
| Enzyme 108 ID |
5977 |
| Enzyme 108 Name |
Adenylate cyclase type 7 |
| Enzyme 108 Synonyms |
- ATP pyrophosphate-lyase 7
- Adenylate cyclase type VII
- Adenylyl cyclase 7
|
| Enzyme 108 Gene Name |
ADCY7 |
| Enzyme 108 Protein Sequence |
>Adenylate cyclase type 7
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPS
RHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAA
CAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQL
LANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAH
ISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKEL
VVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQ
VREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEAT
LKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRA
SVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRS
EDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACA
SLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISER
VETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLP
YYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKP
NGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFET
MENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKE
GLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAH
IGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVAS
RMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
|
| Enzyme 108 Number of Residues |
1080 |
| Enzyme 108 Molecular Weight |
120307.2 |
| Enzyme 108 Theoretical pI |
8.16 |
| Enzyme 108 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 108 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 108 Specific Function |
This is a membrane-bound, calcium-inhibitable adenylyl cyclase |
| Enzyme 108 Pathways |
|
| Enzyme 108 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 108 Pfam Domain Function |
|
| Enzyme 108 Signals |
|
| Enzyme 108 Transmembrane Regions |
- 34-54
63-83
95-117
122-142
147-167
176-196
595-615
620-640
669-688
718-737
746-773
794-814
|
| Enzyme 108 Essentiality |
Not Available |
| Enzyme 108 GenBank ID Protein |
116496681 |
| Enzyme 108 UniProtKB/Swiss-Prot ID |
P51828 |
| Enzyme 108 UniProtKB/Swiss-Prot Entry Name |
ADCY7_HUMAN |
| Enzyme 108 PDB ID |
Not Available |
| Enzyme 108 Cellular Location |
Not Available |
| Enzyme 108 Gene Sequence |
>3243 bp
ATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGCGAGGAGGGCCCTGACCAAGATGCG
CTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGGCCGCTGCTGCTCACGCTCCTGCTG
GTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATTGCCTTCAGCCAGGGGGACCCCTCC
AGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTGCTGGCGGTGTTTGCGGCCCTCTCT
GTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGGCTCAGGGCCTTGGCGCTGCTCACC
TGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTGTTCGACGCATGGACAAAGGCGGCC
TGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATTGTCTTCGTGGTGTACACACTACTG
CCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCCGTCTCCACTGCCTCCCACCTCCTG
GTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCCAGTGTCCGGGTGGGGCTGCAGCTG
CTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTGACAGGCGCCTTCCACAAGCACCAA
ATGCAGGATGCGTCCCGGGACCTCTTCACCTACACTGTGAAGTGCATCCAGATCCGCCGG
AAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTGCTGCTGTCAGTGCTTCCGGCCCAC
ATCTCCATGGGCATGAAGCTGGCCATCATCGAACGGCTCAAGGAGCATGGTGACCGTCGC
TGCATGCCTGACAACAACTTCCACAGCCTCTACGTCAAGAGGCACCAGAATGTCAGCATC
CTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCCAGCGACTGTTCTCCCAAGGAGCTG
GTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGACCAGATCGCCAAGGCCAACGAGTGC
ATGCGAATCAAGATCCTCGGCGACTGCTACTACTGTGTATCGGGCCTGCCCGTGTCGCTG
CCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTGGACATGTGCCAGGCCATCAAGCAG
GTGCGGGAGGCCACGGGCGTGGACATCAACATGCGTGTGGGCATACACTCGGGGAATGTG
CTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTATGACGTGTGGTCCCACGACGTGTCC
CTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGCCGGGTGCACATCACGGAGGCCACG
CTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGATGGGCACGGGCAGCAGCGGGACCCC
TACCTCAAGGAGATGAACATCCGCACCTACCTGGTCATCGACCCCCGGAGCCAGCAGCCA
CCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGGGACGCGGCCCTGAAGATGCGGGCG
TCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGGGCGGCACGGCCCTTTGCACATCTC
AACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCACGTCCCCAACGGGCGGAGGCCTAAG
AGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGAAGCATGTCCCCCAAGGGGCGGTCG
GAGGATGACTCGTACGATGACGAGATGCTGTCAGCCATTGAGGGGCTCAGCTCCACGAGG
CCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTTGGGTCCATCTTCCTGGAGAAGGGC
TTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGGGCCCGCCACGACTTTGCCTGCGCC
AGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTCCTGCTCATGCCCAGGACGGCGGCA
CTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTGGGGCTGGTGCTGGGCCTGTGCTTT
GCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGGACGCTCTGCACTATCTCTGAGAGG
GTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCCGTCCTGACCATCGGCAGCCTGCTC
ACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTCCAAGTTCCAGAGCTGCCTGTTGGC
AATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACAAGAGCCCTGTGTGAGCCCCTCCCG
TACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCCTGCTCGGTCTTCCTGAGGATGAGC
CTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTGGTGGCCTACCTGGTGCTCTTCAAC
CTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAAGGCCTGGGCAACCTCACCAAGCCC
AACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGGAAGGACCTGAAGACCATGACCAAT
TTCTACCTGGTCCTGTTCTACATCACCCTGCTTACACTCTCCAGACAGATTGACTATTAC
TGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAGAAGGAGCACGAGGAGTTTGAGACC
ATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTCCTGCCAGCCCACGTGGCTGCCCAC
TTTATCGGTGACAAGTTAAACGAGGACTGGTACCATCAGTCCTATGACTGCGTCTGTGTC
ATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTACACAGAGTGCGATGTCAACAAAGAA
GGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATTGCCGACTTCGACGAGCTCCTACTG
AAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACCATCGGCAGCACGTACATGGCAGCT
GCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAGGAGCTGGAGCGGCAGCATGCCCAC
ATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATGAGTAAGCTGGACGGCATCAACAGG
CACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATAAACCATGGGCCTGTGATTGCTGGA
GTGATTGGGGCCCGAAAACCTCAGTATGACATCTGGGGAAACACTGTCAATGTGGCCAGC
CGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAGGTTACCGAGGAGACCTGCACCATC
CTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGCCTGATCAACGTCAAAGGCAAAGGC
GAGCTGAGGACTTACTTTGTCTGTACGGACACTGCCAAGTTTCAGGGGCTGGGGCTGAAC
TGA
|
| Enzyme 108 GenBank Gene ID |
BC126271 |
| Enzyme 108 GeneCard ID |
ADCY7 |
| Enzyme 108 GenAtlas ID |
ADCY7 |
| Enzyme 108 HGNC ID |
HGNC:238 |
| Enzyme 108 Chromosome Location |
1 |
| Enzyme 108 Locus |
16q12.1 |
| Enzyme 108 SNPs |
SNPJam Report |
| Enzyme 108 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [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 ]
|
| Enzyme 108 Metabolite References |
Not Available |
|
Enzyme 109
[top]
|
| Enzyme 109 ID |
5978 |
| Enzyme 109 Name |
Adenylate cyclase type 4 |
| Enzyme 109 Synonyms |
- ATP pyrophosphate-lyase 4
- Adenylate cyclase type IV
- Adenylyl cyclase 4
|
| Enzyme 109 Gene Name |
ADCY4 |
| Enzyme 109 Protein Sequence |
>Adenylate cyclase type 4
MARLFSPRPPPSEDLFYETYYSLSQQYPLLLLLLGIVLCALAALLAVAWASGRELTSDPS
FLTTVLCALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQV
SYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVLGLYLGPQPDSRPALLPQLAANAVL
FLCGNVAGVYHKALMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMK
AEIMARLQAGQGSRPESTNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNE
LFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKLRAATG
VDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAG
AYAVEDAGMEHRDPYLRELGEPTYLVIDPRAEEEDEKGTAGGLLSSLEGLKMRPSLLMTR
YLESWGAAKPFAHLSHGDSPVSTSTPLPEKTLASFSTQWSLDRSRTPRGLDDELDTGDAK
FFQVIEQLNSQKQWKQSKDFNPLTLYFREKEMEKEYRLSAIPAFKYYEACTFLVFLSNFI
IQMLVTNRPPALAITYSITFLLFLLILFVCFSEDLMRCVLKGPKMLHWLPALSGLVATRP
GLRIALGTATILLVFAMAITSLFFFPTSSDCPFQAPNVSSMISNLSWELPGSLPLISVPY
SMHCCTLGFLSCSLFLHMSFELKLLLLLLWLAASCSLFLHSHAWLSECLIVRLYLGPLDS
RPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRL
LLENVLPAHVAPQFIGQNRRNEDLYHQSYECVCVLFASVPDFKEFYSESNINHEGLECLR
LLNEIIADFDELLSKPKFSGVEKIKTIGSTYMAATGLNATSGQDAQQDAERSCSHLGTMV
EFAVALGSKLDVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMEST
GVLGKIQVTEETAWALQSLGYTCYSRGVIKVKGKGQLCTYFLNTDLTRTGPPSATLG
|
| Enzyme 109 Number of Residues |
1077 |
| Enzyme 109 Molecular Weight |
119792.9 |
| Enzyme 109 Theoretical pI |
7.50 |
| Enzyme 109 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 109 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 109 Specific Function |
This is a membrane-bound, calmodulin-insensitive adenylyl cyclase |
| Enzyme 109 Pathways |
|
| Enzyme 109 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 109 Pfam Domain Function |
|
| Enzyme 109 Signals |
|
| Enzyme 109 Transmembrane Regions |
- 29-50
61-80
94-117
120-138
141-162
170-190
586-607
611-633
664-687
715-736
744-764
791-807
|
| Enzyme 109 Essentiality |
Not Available |
| Enzyme 109 GenBank ID Protein |
22212709 |
| Enzyme 109 UniProtKB/Swiss-Prot ID |
Q8NFM4 |
| Enzyme 109 UniProtKB/Swiss-Prot Entry Name |
ADCY4_HUMAN |
| Enzyme 109 PDB ID |
Not Available |
| Enzyme 109 Cellular Location |
Not Available |
| Enzyme 109 Gene Sequence |
>3234 bp
ATGGCCCGCCTCTTCAGCCCCCGGCCGCCCCCCAGCGAAGACCTCTTCTACGAGACCTAC
TACAGCCTGAGCCAGCAGTACCCGCTGCTGCTGCTGCTGCTGGGGATCGTGCTCTGTGCG
CTCGCGGCGCTGCTCGCAGTGGCCTGGGCCAGCGGCAGGGAGCTGACCTCAGACCCGAGC
TTCCTGACCACTGTGCTGTGCGCGCTGGGCGGCTTCTCGCTGCTGCTGGGCCTCGCTTCC
CGGGAGCAGCGACTGCAGCGCTGGACGCGTCCCCTGTCCGGCTTGGTATGGGTCGCGCTG
CTAGCGCTAGGCCACGCCTTCCTGTTCACCGGGGGCGTGGTGAGCGCCTGGGACCAGGTG
TCCTATTTTCTCTTCGTCATCTTCACGGCGTATGCCATGCTGCCCTTGGGCATGCGGGAC
GCCGCCGTCGCGGGCCTCGCCTCCTCACTCTCGCATCTGCTGGTCCTCGGGCTGTATCTT
GGGCCACAGCCGGACTCACGGCCTGCACTGCTGCCGCAGTTGGCAGCAAACGCAGTGCTG
TTCCTGTGCGGGAACGTGGCAGGAGTGTACCACAAGGCGCTGATGGAGCGCGCCCTGCGG
GCCACGTTCCGGGAGGCACTCAGCTCCCTGCACTCACGCCGGCGGCTGGACACCGAGAAG
AAGCACCAGGAACACCTTCTCTTGTCCATCCTTCCTGCCTACCTGGCCCGAGAGATGAAG
GCAGAGATCATGGCACGGCTGCAGGCAGGACAGGGGTCACGGCCAGAGAGCACTAACAAT
TTCCACAGCCTCTATGTCAAGAGGCACCAGGGAGTCAGCGTGCTGTATGCTGACATCGTG
GGCTTCACGCGGCTGGCCAGCGAGTGTTCCCCTAAGGAGCTGGTGCTCATGCTCAATGAG
CTCTTTGGCAAGTTCGACCAGATTGCCAAGGAGCATGAATGCATGCGGATCAAGATCCTG
GGGGACTGTTACTACTGTGTCTCTGGGCTGCCACTCTCACTGCCAGACCATGCCATCAAC
TGCGTGCGCATGGGCCTGGACATGTGCCGGGCCATCAGGAAACTGCGGGCAGCCACTGGC
GTGGACATCAACATGCGTGTGGGCGTGCACTCAGGCAGCGTACTGTGTGGAGTCATCGGG
CTGCAGAAGTGGCAGTACGACGTTTGGTCACATGATGTCACACTGGCTAACCACATGGAG
GCAGGCGGTGTACCAGGGCGAGTGCACATCACAGGGGCTACCCTGGCCCTGCTGGCAGGG
GCTTATGCTGTGGAGGACGCAGGCATGGAGCATCGGGACCCCTACCTTCGGGAGCTAGGG
GAGCCTACCTATCTGGTCATCGATCCACGGGCAGAGGAGGAGGATGAGAAGGGCACTGCA
GGAGGCTTGCTGTCCTCGCTTGAGGGCCTCAAGATGCGTCCATCACTGCTGATGACCCGT
TACCTGGAGTCCTGGGGCGCAGCCAAGCCTTTTGCCCACCTGAGCCACGGAGACAGCCCT
GTGTCCACCTCCACCCCTCTCCCGGAGAAGACCCTGGCTTCCTTCAGCACCCAGTGGAGC
CTGGATCGGAGCCGTACCCCCCGGGGACTAGATGATGAACTGGACACCGGGGATGCCAAG
TTCTTCCAGGTCATTGAGCAGCTCAACTCGCAGAAACAGTGGAAGCAGTCGAAGGACTTC
AACCCACTGACACTGTACTTCAGAGAGAAGGAGATGGAGAAAGAGTACCGACTCTCTGCA
ATCCCCGCCTTCAAATACTATGAAGCCTGCACCTTCCTGGTTTTTCTCTCCAACTTCATC
ATCCAGATGCTAGTGACAAACAGGCCCCCAGCTCTGGCCATCACGTATAGCATCACCTTC
CTCCTCTTCCTCCTCATCCTTTTTGTCTGCTTCTCAGAGGACCTGATGAGGTGTGTCCTG
AAAGGCCCCAAGATGCTGCACTGGCTGCCTGCACTGTCTGGCCTGGTGGCCACACGACCA
GGACTGAGAATAGCCTTGGGCACCGCCACCATCCTCCTTGTCTTTGCCATGGCCATTACC
AGCCTGTTCTTCTTCCCAACATCATCAGACTGCCCTTTCCAAGCTCCCAATGTGTCCTCC
ATGATTTCCAACCTCTCCTGGGAGCTCCCTGGGTCTCTGCCTCTCATCAGTGTCCCATAC
TCCATGCACTGCTGCACGCTGGGCTTCCTCTCCTGCTCCCTCTTTCTGCACATGAGCTTC
GAGCTGAAGCTGCTGCTGCTCCTGCTGTGGCTGGCGGCATCCTGCTCCCTCTTCCTGCAC
TCCCATGCCTGGCTGTCGGAATGCCTCATCGTCCGCCTCTATCTGGGCCCCTTGGACTCC
AGGCCCGGAGTGCTGAAGGAGCCCAAACTGATGGGTGCTATCTCCTTCTTCATCTTCTTC
TTCACCCTCCTTGTCCTGGCTCGCCAGAATGAGTACTACTGCCGCCTGGACTTCCTGTGG
AAGAAGAAGCTGAGGCAGGAGAGGGAGGAGACAGAGACGATGGAGAACCTGACTCGGCTG
CTCTTGGAGAACGTGCTCCCTGCACACGTGGCCCCCCAGTTCATTGGCCAGAACCGGCGC
AACGAGGATCTCTACCACCAGTCCTATGAATGCGTTTGTGTCCTCTTCGCCTCAGTCCCA
GACTTCAAGGAGTTCTACTCTGAATCCAACATCAATCATGAGGGCCTAGAGTGTCTGAGG
CTGCTCAATGAGATAATTGCTGATTTTGATGAGCTGCTCTCCAAGCCCAAGTTCAGTGGG
GTGGAGAAGATCAAGACCATCGGCAGCACCTACATGGCAGCCACAGGCTTAAATGCCACC
TCTGGACAGGATGCACAACAGGATGCTGAACGGAGCTGCAGCCACCTTGGCACTATGGTG
GAATTTGCCGTGGCCCTGGGGTCTAAGCTGGACGTCATCAACAAGCATTCATTCAACAAC
TTCCGCCTGCGAGTGGGGTTGAACCATGGACCCGTAGTAGCTGGAGTTATTGGGGCCCAG
AAGCCGCAATATGACATTTGGGGCAACACAGTGAACGTGGCCAGCCGCATGGAGAGTACA
GGAGTCCTTGGCAAAATCCAAGTGACTGAGGAGACAGCATGGGCCCTACAGTCCCTGGGC
TACACCTGCTACAGCCGGGGTGTCATCAAGGTGAAAGGCAAAGGGCAGCTCTGCACCTAC
TTCCTGAACACAGACTTGACACGAACTGGACCTCCTTCAGCTACCCTAGGCTGA
|
| Enzyme 109 GenBank Gene ID |
AF497516 |
| Enzyme 109 GeneCard ID |
ADCY4 |
| Enzyme 109 GenAtlas ID |
ADCY4 |
| Enzyme 109 HGNC ID |
HGNC:235 |
| Enzyme 109 Chromosome Location |
1 |
| Enzyme 109 Locus |
14q12 |
| Enzyme 109 SNPs |
SNPJam Report |
| Enzyme 109 General References |
- Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [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 109 Metabolite References |
Not Available |
|
Enzyme 110
[top]
|
| Enzyme 110 ID |
5979 |
| Enzyme 110 Name |
Adenylate cyclase type 6 |
| Enzyme 110 Synonyms |
- ATP pyrophosphate-lyase 6
- Adenylate cyclase type VI
- Adenylyl cyclase 6
- Ca(2+)-inhibitable adenylyl cyclase
|
| Enzyme 110 Gene Name |
ADCY6 |
| Enzyme 110 Protein Sequence |
>Adenylate cyclase type 6
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGP
PRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWR
RLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAY
VALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLW
CPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTN
VIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINT
KKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHC
LRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRV
HCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNA
YLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFR
QMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKK
YSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSC
GSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLT
PADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLA
MIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPV
ILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHF
LARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIIS
EERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNN
FQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKG
YQLECRGVVKVKGKGEMTTYFLNGGPSS
|
| Enzyme 110 Number of Residues |
1168 |
| Enzyme 110 Molecular Weight |
130614.1 |
| Enzyme 110 Theoretical pI |
8.27 |
| Enzyme 110 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 110 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 110 Specific Function |
Membrane-bound, calcium-inhibitable adenylyl cyclase |
| Enzyme 110 Pathways |
|
| Enzyme 110 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 110 Pfam Domain Function |
|
| Enzyme 110 Signals |
|
| Enzyme 110 Transmembrane Regions |
- 152-168
181-197
214-230
239-255
259-275
289-305
674-691
702-718
743-759
820-836
839-855
897-913
|
| Enzyme 110 Essentiality |
Not Available |
| Enzyme 110 GenBank ID Protein |
Not Available |
| Enzyme 110 UniProtKB/Swiss-Prot ID |
O43306 |
| Enzyme 110 UniProtKB/Swiss-Prot Entry Name |
ADCY6_HUMAN |
| Enzyme 110 PDB ID |
1U0H |
| Enzyme 110 PDB File |
Show |
| Enzyme 110 3D Structure |
|
| Enzyme 110 Cellular Location |
Not Available |
| Enzyme 110 Gene Sequence |
>3507 bp
ATGTCATGGTTTAGTGGCCTCCTGGTCCCTAAAGTGGATGAACGGAAAACAGCCTGGGGC
GAACGCAATGGGCAGAAGCGTTCGCGGCGCCGTGGCACTCGGGCAGGTGGCTTCTGCACG
CCCCGCTATATGAGCTGCCTCCGGGATGCAGAGCCACCCAGCCCCACCCCTGCCGGCCCC
CCTCGGTGCCCCTGGCAGGATGACGCCTTCATCCGGAGGGGCGGCCCAGGCAAGGGCAAG
GAGCTGGGGCTGCGGGCAGTGGCCCTGGGCTTCGAGGATACCGAGGTGACAACGACAGCG
GGCGGGACGGCTGAGGTGGCGCCCGACGCGGTGCCCAGGAGTGGGCGATCCTGCTGGCGC
CGTCTGGTGCAGGTGTTCCAGTCGAAGCAGTTCCGTTCGGCCAAGCTGGAGCGCCTGTAC
CAGCGGTACTTCTTCCAGATGAACCAGAGCAGCCTGACGCTGCTGATGGCGGTGCTGGTG
CTGCTCACAGCGGTGCTGCTGGCTTTCCACGCCGCACCCGCCCGCCCTCAGCCTGCCTAT
GTGGCACTGTTGGCCTGTGCCGCCGCCCTGTTCGTGGGGCTCATGGTGGTGTGTAACCGG
CATAGCTTCCGCCAGGACTCCATGTGGGTGGTGAGCTACGTGGTGCTGGGCATCCTGGCG
GCAGTGCAGGTCGGGGGCGCTCTCGCAGCAGACCCGCGCAGCCCCTCTGCGGGCCTCTGG
TGCCCTGTGTTCTTTGTCTACATCGCCTACACGCTCCTCCCCATCCGCATGCGGGCTGCC
GTCCTCAGCGGCCTGGGCCTCTCCACCTTGCATTTGATCTTGGCCTGGCAACTTAACCGT
GGTGATGCCTTCCTCTGGAAGCAGCTCGGTGCCAATGTGCTGCTGTTCCTCTGCACCAAC
GTCATTGGCATCTGCACACACTATCCAGCAGAGGTGTCTCAGCGCCAGGCCTTTCAGGAG
ACCCGCGGTTACATCCAGGCCCGGCTCCACCTGCAGCATGAGAATCGGCAGCAGGAGCGG
CTGCTGCTGTCGGTATTGCCCCAGCACGTTGCCATGGAGATGAAAGAAGACATCAACACA
AAAAAAGAAGACATGATGTTCCACAAGATCTACATACAGAAGCATGACAATGTCAGCATC
CTGTTTGCAGACATTGAGGGCTTCACCAGCCTGGCATCCCAGTGCACTGCGCAGGAGCTG
GTCATGACCCTGAATGAGCTCTTTGCCCGGTTTGACAAGCTGGCTGCGGAGAATCACTGC
CTGAGGATCAAGATCTTGGGGGACTGTTACTACTGTGTGTCAGGGCTGCCGGAGGCCCGG
GCCGACCATGCCCACTGCTGTGTGGAGATGGGGGTAGACATGATTGAGGCCATCTCGCTG
GTACGTGAGGTGACAGGTGTGAATGTGAACATGCGCGTGGGCATCCACAGCGGGCGCGTG
CACTGCGGCGTCCTTGGCTTGCGGAAATGGCAGTTCGATGTGTGGTCCAATGATGTGACC
CTGGCCAACCACATGGAGGCAGGAGGCCGGGCTGGCCGCATCCACATCACTCGGGCAACA
CTGCAGTACCTGAACGGGGACTACGAGGTGGAGCCAGGCCGTGGTGGCGAGCGCAACGCG
TACCTCAAGGAGCAGCACATTGAGACTTTCCTCATCCTGGGCGCCAGCCAGAAACGGAAA
GAGGAGAAGGCCATGCTGGCCAAGCTGCAGCGGACTCGGGCCAACTCCATGGAAGGGCTG
ATGCCGCGCTGGGTTCCTGATCGTGCCTTCTCCCGGACCAAGGACTCCAAGGCCTTCCGC
CAGATGGGCATTGATGATTCCAGCAAAGACAACCGGGGCACCCAAGATGCCCTGAACCCT
GAGGATGAGGTGGATGAGTTCCTGAGCCGTGCCATCGATGCCCGCAGCATTGATCAGCTG
CGGAAGGACCATGTGCGCCGGTTTCTGCTCACCTTCCAGAGAGAGGATCTTGAGAAGAAG
TACTCCCGGAAGGTGGATCCCCGCTTCGGAGCCTACGTTGCCTGTGCCCTGTTGGTCTTC
TGCTTCATCTGCTTCATCCAGCTTCTCATCTTCCCACACTCCACCCTGATGCTTGGGATC
TATGCCAGCATCTTCCTGCTGCTGCTAATCACCGTGCTGATCTGTGCTGTGTACTCCTGT
GGTTCTCTGTTCCCTAAGGCCCTGCAACGTCTGTCCCGCAGCATTGTCCGCTCACGGGCA
CATAGCACCGCAGTTGGCATCTTTTCCGTCCTGCTTGTGTTTACTTCTGCCATTGCCAAC
ATGTTCACCTGTAACCACACCCCCATACGGAGCTGTGCAGCCCGGATGCTGAATTTAACA
CCTGCTGACATCACTGCCTGCCACCTGCAGCAGCTCAATTACTCTCTGGGCCTGGATGCT
CCCCTGTGTGAGGGCACCATGCCCACCTGCAGCTTTCCTGAGTACTTCATCGGGAACATG
CTGCTGAGTCTCTTGGCCAGCTCTGTCTTCCTGCACATCAGCAGCATCGGGAAGTTGGCC
ATGATCTTTGTCTTGGGGCTCATCTATTTGGTGCTGCTTCTGCTGGGTCCCCCAGCCACC
ATCTTTGACAACTATGACCTACTGCTTGGCGTCCATGGCTTGGCTTCTTCCAATGAGACC
TTTGATGGGCTGGACTGTCCAGCTGCAGGGAGGGTGGCCCTCAAATATATGACCCCTGTG
ATTCTGCTGGTGTTTGCGCTGGCGCTGTATCTGCATGCTCAGCAGGTGGAGTCGACTGCC
CGCCTAGACTTCCTCTGGAAACTACAGGCAACAGGGGAGAAGGAGGAGATGGAGGAGCTA
CAGGCATACAACCGGAGGCTGCTGCATAACATTCTGCCCAAGGACGTGGCGGCCCACTTC
CTGGCCCGGGAGCGCCGCAATGATGAACTCTACTATCAGTCGTGTGAGTGTGTGGCTGTT
ATGTTTGCCTCCATTGCCAACTTCTCTGAGTTCTATGTGGAGCTGGAGGCAAACAATGAG
GGTGTCGAGTGCCTGCGGCTGCTCAACGAGATCATCGCTGACTTTGATGAGATTATCAGC
GAGGAGCGGTTCCGGCAGCTGGAAAAGATCAAGACGATTGGTAGCACCTACATGGCTGCC
TCAGGGCTGAACGCCAGCACCTACGATCAGGTGGGCCGCTCCCACATCACTGCCCTGGCT
GACTACGCCATGCGGCTCATGGAGCAGATGAAGCACATCAATGAGCACTCCTTCAACAAT
TTCCAGATGAAGATTGGGCTGAACATGGGCCCAGTCGTGGCAGGTGTCATCGGGGCTCGG
AAGCCACAGTATGACATCTGGGGGAACACAGTGAATGTCTCTAGTCGTATGGACAGCACG
GGGGTCCCCGACCGAATCCAGGTGACCACGGACCTGTACCAGGTTCTAGCTGCCAAGGGC
TACCAGCTGGAGTGTCGAGGGGTGGTCAAGGTGAAGGGCAAGGGGGAGATGACCACCTAC
TTCCTCAATGGGGGCCCCAGCAGTTAA
|
| Enzyme 110 GenBank Gene ID |
AF250226 |
| Enzyme 110 GeneCard ID |
ADCY6 |
| Enzyme 110 GenAtlas ID |
ADCY6 |
| Enzyme 110 HGNC ID |
HGNC:237 |
| Enzyme 110 Chromosome Location |
1 |
| Enzyme 110 Locus |
12q12-q13 |
| Enzyme 110 SNPs |
SNPJam Report |
| Enzyme 110 General References |
- Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed ]
- Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [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 ]
- Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [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 ]
- 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 ]
|
| Enzyme 110 Metabolite References |
Not Available |
|
Enzyme 111
[top]
|
| Enzyme 111 ID |
5980 |
| Enzyme 111 Name |
Adenylate cyclase type 5 |
| Enzyme 111 Synonyms |
- ATP pyrophosphate-lyase 5
- Adenylate cyclase type V
- Adenylyl cyclase 5
|
| Enzyme 111 Gene Name |
ADCY5 |
| Enzyme 111 Protein Sequence |
>Adenylate cyclase type 5
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGA
VTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRR
GAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEG
GEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS
SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGL
ACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSAL
HLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH
SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTS
LASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEM
GMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGK
AGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMN
RQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFL
GRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQI
TIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVF
TITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSP
WPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADL
LVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKL
QATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANF
SEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTY
DKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWG
NTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPL
S
|
| Enzyme 111 Number of Residues |
1261 |
| Enzyme 111 Molecular Weight |
138906.4 |
| Enzyme 111 Theoretical pI |
7.25 |
| Enzyme 111 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 111 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 111 Specific Function |
This is a membrane-bound, calcium-inhibitable adenylyl cyclase |
| Enzyme 111 Pathways |
|
| Enzyme 111 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 111 Pfam Domain Function |
|
| Enzyme 111 Signals |
|
| Enzyme 111 Transmembrane Regions |
- 196-216
242-262
268-288
299-319
325-345
374-394
770-790
792-812
836-856
910-930
935-955
984-1004
|
| Enzyme 111 Essentiality |
Not Available |
| Enzyme 111 GenBank ID Protein |
34486092 |
| Enzyme 111 UniProtKB/Swiss-Prot ID |
O95622 |
| Enzyme 111 UniProtKB/Swiss-Prot Entry Name |
ADCY5_HUMAN |
| Enzyme 111 PDB ID |
1U0H |
| Enzyme 111 PDB File |
Show |
| Enzyme 111 3D Structure |
|
| Enzyme 111 Cellular Location |
Not Available |
| Enzyme 111 Gene Sequence |
>3786 bp
ATGTCCGGCTCCAAAAGCGTGAGCCCCCCGGGCTACGCGGCGCAGAAGACTGCGGCGCCG
GCGCCCCGGGGAGGCCCCGAACACCGCTCTGCGTGGGGCGAGGCCGATTCCCGCGCGAAT
GGCTACCCCCATGCCCCCGGGGGCTCTGCCCGCGGCTCCACCAAGAAACCCGGGGGGGCG
GTGACCCCGCAGCAGCAGCAGCGCCTGGCCAGCCGCTGGCGCAGCGACGACGACGACGAT
CCTCCGCTGAGCGGTGACGACCCCCTGGCCGGGGGCTTCGGCTTCAGCTTCCGCTCCAAG
TCCGCCTGGCAGGAGCGCGGCGGCGACGACTGCGGTCGCGGCAGCCGCCGGCAGCGGCGG
GGCGCGGCCAGCGGGGGCAGCACCCGGGCGCCCCCTGCGGGCGGCGGCGGCGGCTCGGCG
GCGGCGGCTGCCTCGGCGGGCGGGACGGAGGTGCGCCCTCGCTCGGTGGAGGTGGGTCTG
GAGGAGCGGCGGGGCAAGGGGCGCGCGGCCGACGAGCTGGAGGCCGGCGCCGTCGAGGGC
GGCGAGGGGTCCGGGGATGGCGGCAGCTCGGCGGACTCGGGCTCGGGCGCGGGGCCCGGC
GCGGTGCTGTCCCTGGGCGCCTGCTGCCTGGCGTTGCTGCAGATATTCCGCTCCAAGAAG
TTCCCGTCGGACAAACTGGAGCGGCTGTACCAGCGCTACTTCTTCCGCCTGAACCAGAGC
AGCCTCACCATGCTCATGGCCGTGCTGGTGCTCGTGTGCCTGGTCATGTTGGCCTTCCAC
GCGGCGCGGCCCCCGCTCCAGCTGCCCTACCTGGCCGTGCTGGCGGCCGCCGTCGGCGTG
ATCCTCATCATGGCTGTGCTTTGCAACCGCGCCGCCTTCCACCAGGACCACATGGGCCTG
GCCTGCTATGCGCTCATCGCCGTGGTGCTGGCCGTCCAGGTGGTGGGCCTGCTGCTGCCG
CAGCCACGCAGCGCCTCTGAGGGCATCTGGTGGACCGTGTTCTTCATCTACACCATCTAC
ACGCTGCTGCCCGTGCGCATGCGGGCCGCAGTGCTCAGCGGGGTGCTCCTGTCCGCCCTC
CACCTGGCCATCGCCCTGCGCACCAACGCCCAGGACCAGTTCCTGCTGAAGCAGCTTGTC
TCCAATGTTCTCATTTTCTCCTGCACCAACATCGTGGGTGTCTGCACCCACTATCCGGCT
GAGGTCTCCCAGAGACAGGCTTTCCAGGAGACCCGAGAGTGCATCCAGGCGCGGCTCCAC
TCGCAGCGGGAGAACCAGCAGCAGGAACGGCTCCTGCTGTCTGTCCTTCCCCGTCATGTT
GCCATGGAGATGAAAGCAGACATCAACGCCAAGCAGGAGGATATGATGTTCCATAAGATT
TACATCCAGAAACATGACAACGTGAGCATCCTGTTTGCTGACATCGAGGGCTTCACCAGC
CTGGCGTCCCAGTGCACTGCACAGGAACTGGTCATGACCCTCAACGAGCTCTTCGCCCGC
TTTGACAAGCTGGCCGCAGAGAATCACTGTTTACGTATTAAGATCCTTGGGGATTGTTAT
TACTGCGTCTCGGGGCTGCCTGAAGCAAGGGCTGACCACGCCCACTGCTGTGTGGAGATG
GGCATGGACATGATCGAGGCCATCTCGTTGGTCCGGGAGGTGACAGGGGTGAACGTGAAC
ATGCGTGTGGGAATTCACAGCGGGCGAGTACACTGCGGTGTCCTTGGTCTCAGGAAGTGG
CAGTTCGACGTCTGGTCTAACGATGTCACGCTAGCCAACCACATGGAGGCTGGCGGCAAG
GCAGGACGCATCCACATCACCAAGGCTACACTCAACTACCTGAATGGGGACTACGAGGTG
GAGCCAGGCTGTGGGGGCGAGCGCAACGCCTACCTCAAGGAGCACAGTATCGAGACCTTC
CTCATCCTGCGCTGCACCCAGAAGCGGAAAGAAGAGAAGGCCATGATCGCCAAGATGAAC
CGCCAGAGAACCAACTCCATCGGGCACAACCCACCACACTGGGGGGCTGAGCGCCCCTTC
TACAACCACCTGGGTGGCAACCAGGTGTCCAAGGAGATGAAGCGGATGGGCTTTGAAGAC
CCCAAGGACAAGAACGCCCAGGAGAGTGCGAACCCTGAGGATGAAGTGGATGAGTTTCTG
GGCCGTGCCATTGACGCCAGGAGCATTGATAGGCTTCGGTCTGAGCACGTCCGCAAGTTC
CTCCTGACCTTCAGGGAGCCTGACTTAGAGAAGAAGTACTCCAAGCAGGTAGACGACCGA
TTTGGTGCCTATGTGGCGTGTGCCTCGCTCGTCTTCCTCTTCATCTGCTTTGTCCAGATC
ACCATCGTGCCCCACTCCATATTCATGCTCAGCTTCTACCTGACCTGTTCCCTGCTGCTG
ACCTTGGTGGTGTTTGTGTCTGTGATCTACTCCTGCGTAAAGCTCTTCCCCTCCCCACTG
CAGACCCTCTCCAGGAAGATCGTGCGGTCCAAGATGAACAGCACCCTGGTTGGGGTGTTC
ACCATCACCCTGGTGTTCCTGGCGGCTTTTGTCAACATGTTCACGTGCAACTCCAGGGAC
CTGCTGGGCTGCTTGGCACAGGAGCACAACATCAGCGCGAGCCAGGTCAACGCGTGTCAC
GTGGCGGAGTCGGCCGTCAACTACAGCCTGGGCGATGAGCAGGGCTTCTGTGGCAGCCCC
TGGCCCAACTGCAACTTCCCCGAGTACTTCACCTACAGCGTGCTGCTCAGCCTGCTGGCC
TGCTCCGTGTTCCTGCAGATCAGCTGCATCGGGAAGCTGGTGCTCATGCTGGCCATCGAG
CTCATCTACGTGCTCATCGTGGAGGTGCCAGGTGTCACGCTCTTCGACAACGCCGACCTG
CTGGTCACCGCCAACGCCATAGACTTCTTCAACAACGGGACCTCCCAGTGCCCTGAGCAT
GCAACCAAGGTGGCATTGAAGGTGGTGACGCCCATCATCATCTCAGTCTTTGTGCTGGCC
CTGTACCTGCACGCCCAGCAGGTGGAGTCCACTGCCCGCCTCGACTTCCTCTGGAAACTG
CAGGCCACAGAGGAGAAAGAGGAGATGGAGGAGCTGCAGGCCTACAACCGGCGGCTGCTG
CACAACATCCTGCCCAAGGACGTGGCCGCTCACTTCCTGGCCCGCGAGCGGCGCAATGAT
GAGCTCTACTATCAGTCCTGTGAGTGTGTGGCGGTCATGTTCGCCTCCATCGCCAACTTC
TCCGAGTTCTACGTTGAGCTGGAGGCCAACAACGAGGGTGTCGAGTGCCTGCGGCTACTC
AATGAGATCATCGCTGACTTTGATGAGATCATCAGCGAGGATCGGTTCCGGCAGCTGGAG
AAGATCAAGACCATCGGCAGCACCTACATGGCTGCCTCCGGCCTCAACGACTCTACCTAC
GACAAGGTGGGCAAGACCCACATCAAGGCACTGGCCGACTTTGCCATGAAGCTGATGGAC
CAGATGAAGTACATCAATGAGCACTCCTTCAACAACTTCCAGATGAAGATCGGGCTCAAC
ATCGGCCCCGTGGTGGCCGGGGTGATAGGGGCACGAAAGCCTCAGTACGACATCTGGGGC
AATACCGTGAACGTGGCCAGCCGCATGGACAGCACCGGTGTACCCGACCGCATCCAGGTC
ACCACAGACATGTACCAGGTGCTGGCTGCCAACACGTACCAGCTGGAGTGCCGGGGCGTG
GTCAAGGTCAAGGGCAAAGGCGAGATGATGACCTACTTCCTCAATGGAGGGCCCCCGCTC
AGTTAG
|
| Enzyme 111 GenBank Gene ID |
NM_183357.1 |
| Enzyme 111 GeneCard ID |
ADCY5 |
| Enzyme 111 GenAtlas ID |
ADCY5 |
| Enzyme 111 HGNC ID |
HGNC:236 |
| Enzyme 111 Chromosome Location |
3 |
| Enzyme 111 Locus |
3q13.2-q21 |
| Enzyme 111 SNPs |
SNPJam Report |
| Enzyme 111 General References |
- 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 ]
- Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed ]
- Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed ]
|
| Enzyme 111 Metabolite References |
Not Available |
|
Enzyme 112
[top]
|
| Enzyme 112 ID |
5981 |
| Enzyme 112 Name |
Adenylate cyclase type 8 |
| Enzyme 112 Synonyms |
- ATP pyrophosphate-lyase 8
- Adenylate cyclase type VIII
- Adenylyl cyclase 8
- Ca(2+)/calmodulin-activated adenylyl cyclase
|
| Enzyme 112 Gene Name |
ADCY8 |
| Enzyme 112 Protein Sequence |
>Adenylate cyclase type 8
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
|
| Enzyme 112 Number of Residues |
1251 |
| Enzyme 112 Molecular Weight |
140120.8 |
| Enzyme 112 Theoretical pI |
6.99 |
| Enzyme 112 GO Classification |
| Function |
- adenylate cyclase activity
- catalytic activity
- cyclase activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 112 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 112 Specific Function |
This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence |
| Enzyme 112 Pathways |
|
| Enzyme 112 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 112 Pfam Domain Function |
|
| Enzyme 112 Signals |
|
| Enzyme 112 Transmembrane Regions |
- 183-203
212-232
247-267
274-294
296-316
321-341
716-736
738-758
787-807
831-851
861-881
894-914
|
| Enzyme 112 Essentiality |
Not Available |
| Enzyme 112 GenBank ID Protein |
516263 |
| Enzyme 112 UniProtKB/Swiss-Prot ID |
P40145 |
| Enzyme 112 UniProtKB/Swiss-Prot Entry Name |
ADCY8_HUMAN |
| Enzyme 112 PDB ID |
Not Available |
| Enzyme 112 Cellular Location |
Not Available |
| Enzyme 112 Gene Sequence |
>3756 bp
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTACGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCCGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
|
| Enzyme 112 GenBank Gene ID |
Z35309 |
| Enzyme 112 GeneCard ID |
ADCY8 |
| Enzyme 112 GenAtlas ID |
ADCY8 |
| Enzyme 112 HGNC ID |
HGNC:239 |
| Enzyme 112 Chromosome Location |
8 |
| Enzyme 112 Locus |
8q24 |
| Enzyme 112 SNPs |
SNPJam Report |
| Enzyme 112 General References |
- Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed ]
- Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [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 112 Metabolite References |
Not Available |
|
Enzyme 113
[top]
|
| Enzyme 113 ID |
5983 |
| Enzyme 113 Name |
Adenylate cyclase type 3 |
| Enzyme 113 Synonyms |
- ATP pyrophosphate-lyase 3
- Adenylate cyclase type III
- AC-III
- Adenylate cyclase, olfactive type
- Adenylyl cyclase 3
- AC3
|
| Enzyme 113 Gene Name |
ADCY3 |
| Enzyme 113 Protein Sequence |
>Adenylate cyclase type 3
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPE
SLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDII
LFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFF
ITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVG
IMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDES
QKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQ
LRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTV
LGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCD
YLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHS
SGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESA
QVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTN
YVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMAN
VVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLM
LLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKY
SMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHV
ARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFD
SLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFA
LAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVM
GNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQV
VDNS
|
| Enzyme 113 Number of Residues |
1144 |
| Enzyme 113 Molecular Weight |
128958.9 |
| Enzyme 113 Theoretical pI |
6.55 |
| Enzyme 113 GO Classification |
| Function |
- catalytic activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 113 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 113 Specific Function |
Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration |
| Enzyme 113 Pathways |
|
| Enzyme 113 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 113 Pfam Domain Function |
|
| Enzyme 113 Signals |
|
| Enzyme 113 Transmembrane Regions |
- 80-100
105-125
139-159
173-193
226-246
381-401
633-653
664-684
708-728
754-774
775-795
833-853
|
| Enzyme 113 Essentiality |
Not Available |
| Enzyme 113 GenBank ID Protein |
148536830 |
| Enzyme 113 UniProtKB/Swiss-Prot ID |
O60266 |
| Enzyme 113 UniProtKB/Swiss-Prot Entry Name |
ADCY3_HUMAN |
| Enzyme 113 PDB ID |
Not Available |
| Enzyme 113 Cellular Location |
Not Available |
| Enzyme 113 Gene Sequence |
>3435 bp
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTTCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCCGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAAACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
|
| Enzyme 113 GenBank Gene ID |
NM_004036.3 |
| Enzyme 113 GeneCard ID |
ADCY3 |
| Enzyme 113 GenAtlas ID |
ADCY3 |
| Enzyme 113 HGNC ID |
HGNC:234 |
| Enzyme 113 Chromosome Location |
2 |
| Enzyme 113 Locus |
2p23.3 |
| Enzyme 113 SNPs |
SNPJam Report |
| Enzyme 113 General References |
- Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [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 ]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed ]
- Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed ]
|
| Enzyme 113 Metabolite References |
Not Available |
|
Enzyme 114
[top]
|
| Enzyme 114 ID |
5984 |
| Enzyme 114 Name |
Adenylate cyclase type 1 |
| Enzyme 114 Synonyms |
- ATP pyrophosphate-lyase 1
- Adenylate cyclase type I
- Adenylyl cyclase 1
- Ca(2+)/calmodulin-activated adenylyl cyclase
|
| Enzyme 114 Gene Name |
ADCY1 |
| Enzyme 114 Protein Sequence |
>Adenylate cyclase type 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
|
| Enzyme 114 Number of Residues |
1119 |
| Enzyme 114 Molecular Weight |
123438.8 |
| Enzyme 114 Theoretical pI |
8.49 |
| Enzyme 114 GO Classification |
| Function |
- catalytic activity
- lyase activity
- phosphorus-oxygen lyase activity
|
| Process |
- cellular nitrogen compound metabolic process
- cyclic nucleotide biosynthetic process
- intracellular signaling pathway
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside monophosphate biosynthetic process
- nucleoside monophosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 114 General Function |
Involved in phosphorus-oxygen lyase activity |
| Enzyme 114 Specific Function |
This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning |
| Enzyme 114 Pathways |
|
| Enzyme 114 Reactions |
- ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
|
| Enzyme 114 Pfam Domain Function |
|
| Enzyme 114 Signals |
|
| Enzyme 114 Transmembrane Regions |
- 64-84
88-108
125-145
158-178
183-203
214-234
611-631
635-655
674-694
725-745
753-773
775-794
|
| Enzyme 114 Essentiality |
Not Available |
| Enzyme 114 GenBank ID Protein |
31083193 |
| Enzyme 114 UniProtKB/Swiss-Prot ID |
Q08828 |
| Enzyme 114 UniProtKB/Swiss-Prot Entry Name |
ADCY1_HUMAN |
| Enzyme 114 PDB ID |
Not Available |
| Enzyme 114 Cellular Location |
Not Available |
| Enzyme 114 Gene Sequence |
>3360 bp
ATGGCGGGGGCGCCGCGCGGCGGAGGCGGCGGCGGAGGCGGCGCGGGCGAGCCCGGGGGC
GCCGAGCGGGCGGCCGGGACAAGCCGCCGGCGCGGGCTCCGGGCGTGCGACGAGGAGTTC
GCTTGCCCAGAGCTGGAGGCGCTGTTCCGCGGCTACACGCTGCGGCTGGAGCAGGCGGCC
ACGCTGAAGGCGCTGGCCGTTCTCAGCCTGCTGGCGGGCGCGCTGGCGCTGGCCGAGCTG
CTGGGCGCGCCGGGGCCCGCGCCCGGCCTGGCCAAGGGCTCACACCCGGTGCACTGCGTC
CTCTTCCTGGCGCTGCTCGTGGTAACCAACGTCCGGTCCCTGCAGGTGCCCCAGCTGCAG
CAGGTCGGCCAGCTGGCGCTGCTCTTCAGCCTCACCTTCGCGCTGCTCTGCTGTCCTTTC
GCGCTGGGCGGCCCCGCCCGGGGTTCCGCCGGGGCCGCTGGGGGGCCAGCGACCGCCGAA
CAAGGGGTTTGGCAGCTCCTTTTGGTCACCTTCGTGTCCTATGCCTTGCTGCCCGTGCGC
AGCCTGCTGGCCATAGGCTTTGGGCTCGTGGTGGCTGCGTCGCACTTGCTGGTCACAGCC
ACCTTGGTCCCCGCCAAGCGCCCACGTCTCTGGAGGACGCTCGGTGCCAATGCCTTGCTC
TTCGTCGGTGTGAACATGTATGGGGTCTTTGTGCGGATTCTGACTGAGCGTTCACAGAGG
AAGGCGTTCCTGCAGGCCCGGAGCTGCATTGAGGACCGACTGAGGCTGGAGGATGAGAAC
GAGAAGCAGGAGCGGCTCCTCATGAGCCTCCTGCCCCGGAACGTTGCCATGGAGATGAAG
GAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGGCACGAC
AATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAGTGCACA
GCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTAGCCACG
GAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCGGGCCTC
ACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATGATTGAT
ACCATCACATCTGTGGCTGAAGCCACCGAGGTGGATCTGAACATGCGTGTGGGTCTGCAC
ACGGGCAGGGTCCTCTGTGGTGTCCTGGGCTTGCGCAAGTGGCAGTACGACGTGTGGTCC
AATGATGTGACCTTGGCCAATGTCATGGAAGCCGCTGGCCTGCCAGGGAAGGTTCATATC
ACAAAGACGACCCTAGCGTGCTTGAATGGGGACTACGAGGTAGAACCGGGTTACGGACAT
GAGAGGAACAGTTTCTTGAAAACTCATAACATCGAAACCTTTTTTATTGTGCCATCCCAT
CGCCGAAAGATATTTCCAGGCCTGATTCTCTCAGATATAAAACCGGCCAAAAGGATGAAG
TTCAAGACTGTCTGCTACCTGCTGGTGCAGCTCATGCACTGCCGGAAAATGTTCAAGGCC
GAGATCCCCTTCTCCAATGTCATGACCTGCGAGGACGATGACAAGCGGAGGGCATTAAGA
ACAGCCTCGGAAAAACTCAGAAACCGCTCATCTTTTTCTACCAACGTTGTCTACACCACC
CCGGGCACTCGCGTCAACAGGTACATCAGCCGCCTCTTAGAAGCCCGCCAGACAGAGCTG
GAGATGGCAGACCTGAACTTCTTTACCCTGAAGTACAAACATGTCGAACGGGAGCAAAAG
TACCACCAGCTTCAGGACGAGTATTTCACCAGCGCCGTTGTCCTCACCCTCATCCTGGCT
GCCTTATTTGGCCTTGTCTACCTTCTAATATTCCCACAGAGTGTGGTCGTCCTGCTCCTG
CTAGTATTCTGCATCTGCTTCCTGGTGGCCTGTGTCCTGTACCTGCACATCACCCGGGTC
CAGTGTTTTCCAGGGTGCCTGACGATTCAGATTCGCACTGTCCTGTGTATTTTCATAGTG
GTCTTAATCTACTCAGTAGCCCAAGGTTGTGTGGTGGGCTGCCTGCCTTGGGCCTGGAGC
TCCAAGCCCAACAGTTCCCTGGTGGTCCTTTCGTCTGGGGGCCAGCGCACAGCCCTGCCC
ACCCTGCCCTGCGAGTCTACACACCATGCCCTGCTCTGCTGCCTGGTGGGCACCCTCCCG
CTAGCCATATTTTTCCGGGTGTCCTCCTTGCCAAAAATGATCCTGCTCTCCGGGCTCACC
ACGTCCTACATCCTCGTTCTGGAGCTCAGCGGATACACCAGGACTGGGGGTGGTGCCGTC
TCCGGGCGCAGCTACGAGCCGATTGTGGCCATCCTGCTCTTCTCCTGTGCGCTGGCCCTG
CATGCCAGGCAGGTGGACATCAGGCTGAGGCTGGACTACCTCTGGGCCGCACAGGCAGAG
GAGGAGCGAGAGGACATGGAGAAGGTGAAGCTGGACAACAGGCGCATCCTCTTCAACCTC
CTGCCGGCCCACGTCGCCCAGCACTTCCTCATGTCCAACCCTCGGAACATGGACCTCTAC
TACCAGTCCTACTCCCAGGTGGGCGTCATGTTTGCCTCCATCCCCAACTTCAATGACTTC
TACATCGAGCTGGACGGCAACAACATGGGGGTGGAGTGTCTGCGGCTTCTCAACGAGATC
ATCGCCGACTTTGACGAGCTCATGGAAAAAGACTTTTACAAGGACATAGAGAAGATCAAG
ACCATCGGGAGCACCTACATGGCCGCTGTGGGGCTAGCGCCCACCTCGGGGACCAAGGCT
AAGAAGTCCATCTCCTCCCACCTGAGCACGCTGGCGGACTTTGCCATTGAGATGTTTGAC
GTTCTGGATGAAATCAACTACCAGTCTTACAACGACTTTGTCCTCCGAGTTGGCATCAAT
GTTGGCCCTGTGGTGGCTGGAGTGATTGGCGCTCGCAGGCCCCAGTACGACATCTGGGGA
AACACAGTCAACGTGGCCAGTCGGATGGATAGCACAGGGGTCCAGGGCAGAATCCAGGTG
ACTGAGGAAGTCCACCGGCTGCTGAGAAGGTGCCCCTACCACTTTGTGTGCCGAGGCAAA
GTCAGTGTCAAGGGCAAAGGCGAGATGTTGACATACTTTCTAGAAGGCAGGACTGATGGA
AACGGCTCCCAAATCAGGTCCCTGGGCTTGGATCGGAAAATGTGTCCATTTGGGAGAGCT
GGCCTTCAGGGCAGACGTCCCCCCGTGTGCCCCATGCCTGGCGTCTCAGTCAGGGCTGGG
CTCCCTCCACACTCCCCAGGCCAGTACCTGCCCTCTGCAGCAGCTGGGAAGGAGGCTTAG
|
| Enzyme 114 GenBank Gene ID |
NM_021116.2 |
| Enzyme 114 GeneCard ID |
ADCY1 |
| Enzyme 114 GenAtlas ID |
ADCY1 |
| Enzyme 114 HGNC ID |
HGNC:232 |
| Enzyme 114 Chromosome Location |
7 |
| Enzyme 114 Locus |
7p13-p12 |
| Enzyme 114 SNPs |
SNPJam Report |
| Enzyme 114 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 ]
- 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 ]
- Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed ]
|
| Enzyme 114 Metabolite References |
Not Available |
|
Enzyme 115
[top]
|
| Enzyme 115 ID |
5993 |
| Enzyme 115 Name |
Creatine kinase S-type, mitochondrial |
| Enzyme 115 Synonyms |
- Basic-type mitochondrial creatine kinase
- Mib-CK
- Sarcomeric mitochondrial creatine kinase
- S-MtCK
|
| Enzyme 115 Gene Name |
CKMT2 |
| Enzyme 115 Protein Sequence |
>Creatine kinase S-type, mitochondrial
MASIFSKLLTGRNASLLFATMGTSVLTTGYLLNRQKVCAEVREQPRLFPPSADYPDLRKH
NNCMAECLTPAIYAKLRNKVTPNGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFA
DLFDPVIKLRHNGYDPRVMKHTTDLDASKITQGQFDEHYVLSSRVRTGRSIRGLSLPPAC
TRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAG
MARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQE
RGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVD
TAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGKK
|
| Enzyme 115 Number of Residues |
419 |
| Enzyme 115 Molecular Weight |
47504.1 |
| Enzyme 115 Theoretical pI |
8.31 |
| Enzyme 115 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 115 General Function |
Involved in kinase activity |
| Enzyme 115 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 115 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 115 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 115 Pfam Domain Function |
|
| Enzyme 115 Signals |
|
| Enzyme 115 Transmembrane Regions |
|
| Enzyme 115 Essentiality |
Not Available |
| Enzyme 115 GenBank ID Protein |
20810521 |
| Enzyme 115 UniProtKB/Swiss-Prot ID |
P17540 |
| Enzyme 115 UniProtKB/Swiss-Prot Entry Name |
KCRS_HUMAN |
| Enzyme 115 PDB ID |
1CRK |
| Enzyme 115 PDB File |
Show |
| Enzyme 115 3D Structure |
|
| Enzyme 115 Cellular Location |
Not Available |
| Enzyme 115 Gene Sequence |
>1260 bp
ATGGCCAGTATCTTTTCTAAGTTGCTAACTGGCCGCAATGCTTCTCTGCTGTTTGCTACC
ATGGGCACCAGTGTCCTGACCACCGGGTACCTGCTGAACCGGCAGAAAGTGTGTGCCGAG
GTCCGGGAGCAGCCTAGGCTATTTCCTCCAAGCGCAGACTACCCAGACCTGCGCAAGCAC
AACAACTGCATGGCCGAGTGCCTCACCCCCGCCATTTATGCCAAGCTTCGCAACAAGGTG
ACACCCAACGGCTACACGCTGGACCAGTGCATCCAGACTGGAGTGGACAACCCTGGCCAC
CCCTTCATAAAGACTGTGGGCATGGTGGCTGGTGACGAGGAGTCCTATGAGGTGTTTGCT
GACCTTTTTGACCCCGTCATCAAACTAAGACACAACGGCTATGACCCCAGGGTGATGAAG
CACACAACGGATCTGGATGCATCAAAGATCACCCAAGGGCAGTTCGACGAGCATTACGTG
CTGTCTTCTCGGGTGCGCACTGGCCGCAGCATCCGTGGGCTGAGCCTGCCTCCAGCCTGC
ACCCGGGCCGAGCGAAGGGAGGTAGAGAACGTGGCCATCACTGCCCTGGAGGGCCTCAAG
GGGGACCTGGCTGGCCGCTACTACAAGCTGTCCGAGATGACGGAGCAGGACCAGCAGCGG
CTCATCGATGACCACTTTCTGTTTGATAAGCCAGTGTCCCCTTTATTAACATGTGCTGGG
ATGGCCCGTGACTGGCCAGATGCCAGGGGAATCTGGCATAATTATGATAAGACATTTCTC
ATCTGGATAAATGAGGAGGATCACACCAGGGTAATCTCAATGGAAAAAGGAGGCAATATG
AAACGAGTATTTGAGCGATTCTGTCGTGGACTAAAAGAAGTAGAACGGTTAATCCAAGAA
CGAGGCTGGGAGTTCATGTGGAATGAGCGCCTAGGATACATTTTGACCTGTCCTTCGAAC
CTTGGAACAGGACTACGAGCTGGTGTCCACGTTAGGATCCCAAAGCTCAGCAAGGACCCA
CGCTTTTCTAAGATCCTGGAAAACCTAAGACTCCAGAAGCGTGGCACAGGTGGTGTGGAC
ACTGCCGCGGTCGCAGATGTGTACGACATTTCCAACATAGATAGAATTGGTCGATCAGAG
GTTGAGCTTGTTCAGATAGTCATCGATGGAGTCAATTACCTGGTGGATTGTGAAAAGAAG
TTGGAGAGAGGCCAAGATATTAAGGTGCCACCCCCTCTGCCTCAGTTTGGCAAAAAGTAA
|
| Enzyme 115 GenBank Gene ID |
BC029140 |
| Enzyme 115 GeneCard ID |
CKMT2 |
| Enzyme 115 GenAtlas ID |
CKMT2 |
| Enzyme 115 HGNC ID |
HGNC:1996 |
| Enzyme 115 Chromosome Location |
5 |
| Enzyme 115 Locus |
5q13.3 |
| Enzyme 115 SNPs |
SNPJam Report |
| Enzyme 115 General References |
- Haas RC, Strauss AW: Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes. J Biol Chem. 1990 Apr 25;265(12):6921-7. [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 ]
- Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [PubMed ]
|
| Enzyme 115 Metabolite References |
Not Available |
|
Enzyme 116
[top]
|
| Enzyme 116 ID |
5994 |
| Enzyme 116 Name |
Creatine kinase B-type |
| Enzyme 116 Synonyms |
- B-CK
- Creatine kinase B chain
|
| Enzyme 116 Gene Name |
CKB |
| Enzyme 116 Protein Sequence |
>Creatine kinase B-type
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTG
VDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDD
LDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMT
EAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISM
QKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLP
NLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLL
IEMEQRLEQGQAIDDLMPAQK
|
| Enzyme 116 Number of Residues |
381 |
| Enzyme 116 Molecular Weight |
42643.9 |
| Enzyme 116 Theoretical pI |
5.30 |
| Enzyme 116 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 116 General Function |
Involved in kinase activity |
| Enzyme 116 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 116 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 116 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 116 Pfam Domain Function |
|
| Enzyme 116 Signals |
|
| Enzyme 116 Transmembrane Regions |
|
| Enzyme 116 Essentiality |
Not Available |
| Enzyme 116 GenBank ID Protein |
180572 |
| Enzyme 116 UniProtKB/Swiss-Prot ID |
P12277 |
| Enzyme 116 UniProtKB/Swiss-Prot Entry Name |
KCRB_HUMAN |
| Enzyme 116 PDB ID |
1G0W |
| Enzyme 116 PDB File |
Show |
| Enzyme 116 3D Structure |
|
| Enzyme 116 Cellular Location |
Not Available |
| Enzyme 116 Gene Sequence |
>1146 bp
ATGCCCTTCTCCAACAGCCACAACGCACTGAAGCTGCGCTTCCCGGCCGAGGACGAGTTC
CCCGACCTGAGCGCCCACAACAACCACATGGCCAAGGTGCTGACCCCCGAGCTGTACGCG
GACGTGCGCGCCAAGAGCACGCCGAGCGGCTTCACGCTGGACGACGTCATCCAGACAGGC
GTGGACAACCCGGGCCACCCGTACATCATGACCGTGGGCTGCGTGGCGGGCGACGAGGAG
TCCTACGAAGTGTTCAAGGATCTCTTCGACCCCATCATCGAGGACCGGCACCGGCGCTAC
AAGCCCAGCGATGACGACAAGACCGACCTCAACCCCGACAACCTGCAGGGCGGCGACGAC
CTGGACCCCAACTACGTGCTGAGCTCGCGGGTGGCCACGGGCCGCAGCATCCGTGGCTTC
TGCCTCCCCCCGCACTGCAGCCGCGGGGAGCGCCGAGCCATCGAGAAGCTCGCGGTGGAA
GCCCTGTCCAGCCTGGACGGCGACCTGGCGGGCCGATACTACGCGCTCAAGAGCATGACG
GAGGCGGAGCAGCAGCAGCTCATCGACGACCACTTCCTCTTCGACAAGCCCGTGTCGCCC
CTGCTGCTGGCCTCGGGCATGGCCCGCGACTGGCCCGACGCCGCGCGTATCTGGCACAAT
GACAATAAGACCTTCCTGGTGTGGGTCAACGAGGAGGACCACCTGCGGGTCATCTCCATG
CAGAAGGGGGGCAACATGAAGGAGGTGTTCACCCGCTTCTGCACCGGCCTCACCCAGATT
GAAACTCTCTTCAAGTCTAAGGACTATGAGTTCATGTGGAACCCTCACCTGGGCTACATC
CTCACCTGCCCATCCAACCTGGGCACCGGGCTGCGGGCAGGTGTCGATATCAAGCTGCCC
AACCTGGGCAAGCATGAGAAGTTCTCGGAGGTGCTTAAGCGGCTGCGACTTCAGAAGCGA
GGCACAGGCGGTGTGGACACGGCTGCGGTGGGCGGGGTCTTCGACGTCTCCAACGCTGAC
CGCCTGGGCTTCTCAGAGGTGGAGCTGGTGCAGATGGTGGTGGACGGAGTGAAGCTGCTC
ATCGAGATGGAACAGCGGCTGGAGCAGGGCCAGGCCATCGACGACCTCATGCCTGCCCAG
AAATGA
|
| Enzyme 116 GenBank Gene ID |
M16451 |
| Enzyme 116 GeneCard ID |
CKB |
| Enzyme 116 GenAtlas ID |
CKB |
| Enzyme 116 HGNC ID |
HGNC:1991 |
| Enzyme 116 Chromosome Location |
1 |
| Enzyme 116 Locus |
14q32 |
| Enzyme 116 SNPs |
SNPJam Report |
| Enzyme 116 General References |
- Villarreal-Levy G, Ma TS, Kerner SA, Roberts R, Perryman MB: Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number. Biochem Biophys Res Commun. 1987 May 14;144(3):1116-27. [PubMed ]
- Mariman EC, Broers CA, Claesen CA, Tesser GI, Wieringa B: Structure and expression of the human creatine kinase B gene. Genomics. 1987 Oct;1(2):126-37. [PubMed ]
- Kaye FJ, McBride OW, Battey JF, Gazdar AF, Sausville EA: Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci. J Clin Invest. 1987 May;79(5):1412-20. [PubMed ]
- Mariman EC, Schepens JT, Wieringa B: Complete nucleotide sequence of the human creatine kinase B gene. Nucleic Acids Res. 1989 Aug 11;17(15):6385. [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 ]
- Daouk GH, Kaddurah-Daouk R, Putney S, Kingston R, Schimmel P: Isolation of a functional human gene for brain creatine kinase. J Biol Chem. 1988 Feb 15;263(5):2442-6. [PubMed ]
- Kliffen M, de Jong PT, Luider TM: Protein analysis of human maculae in relation to age-related maculopathy. Lab Invest. 1995 Aug;73(2):267-72. [PubMed ]
- Lin L, Perryman MB, Friedman D, Roberts R, Ma TS: Determination of the catalytic site of creatine kinase by site-directed mutagenesis. Biochim Biophys Acta. 1994 May 18;1206(1):97-104. [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 ]
|
| Enzyme 116 Metabolite References |
Not Available |
|
Enzyme 117
[top]
|
| Enzyme 117 ID |
5995 |
| Enzyme 117 Name |
Creatine kinase U-type, mitochondrial |
| Enzyme 117 Synonyms |
- Acidic-type mitochondrial creatine kinase
- Mia-CK
- Ubiquitous mitochondrial creatine kinase
- U-MtCK
|
| Enzyme 117 Gene Name |
CKMT1A |
| Enzyme 117 Protein Sequence |
>Creatine kinase U-type, mitochondrial
MAGPFSRLLSARPGLRLLALAGAGSLAAGFLLRPEPVRAASERRRLYPPSAEYPDLRKHN
NCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFAD
LFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACT
RAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGM
ARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQER
GWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDT
AATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDIRIPTPVIHTKH
|
| Enzyme 117 Number of Residues |
417 |
| Enzyme 117 Molecular Weight |
47036.3 |
| Enzyme 117 Theoretical pI |
8.47 |
| Enzyme 117 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 117 General Function |
Involved in kinase activity |
| Enzyme 117 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 117 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 117 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 117 Pfam Domain Function |
|
| Enzyme 117 Signals |
|
| Enzyme 117 Transmembrane Regions |
|
| Enzyme 117 Essentiality |
Not Available |
| Enzyme 117 GenBank ID Protein |
Not Available |
| Enzyme 117 UniProtKB/Swiss-Prot ID |
P12532 |
| Enzyme 117 UniProtKB/Swiss-Prot Entry Name |
KCRU_HUMAN |
| Enzyme 117 PDB ID |
1QK1 |
| Enzyme 117 PDB File |
Show |
| Enzyme 117 3D Structure |
|
| Enzyme 117 Cellular Location |
Not Available |
| Enzyme 117 Gene Sequence |
>1254 bp
ATGGCTGGTCCCTTCTCCCGTCTGCTGTCCGCCCGCCCGGGACTCAGGCTCCTGGCTTTG
GCCGGAGCGGGGTCTCTAGCCGCTGGGTTTCTGCTCCGACCGGAACCTGTACGAGCTGCC
AGTGAACGACGGAGGCTGTATCCCCCGAGCGCTGAGTACCCAGACCTCCGAAAGCACAAC
AACTGCATGGCCAGTCACCTGACCCCAGCAGTCTATGCACGGCTCTGCGACAAGACCACA
CCCACTGGTTGGACGCTAGATCAGTGTATCCAGACTGGCGTGGACAACCCTGGCCACCCC
TTCATCAAGACTGTGGGCATGGTGGCTGGAGATGAGGAGACCTATGAGGTATTTGCTGAC
CTGTTTGACCCTGTGATCCAAGAGCGACACAATGGATATGACCCCCGGACAATGAAGCAC
ACCACGGATCTAGATGCCAGTAAAATCCGTTCTGGCTACTTTGATGAGAGGTATGTATTG
TCCTCTAGAGTCAGAACTGGCCGAAGCATCCGAGGACTCAGTCTGCCTCCAGCTTGCACT
CGAGCAGAGCGACGAGAGGTGGAACGTGTTGTGGTGGATGCACTGAGTGGCCTGAAGGGT
GACCTGGCTGGACGTTACTATAGGCTCAGTGAGATGACAGAGGCTGAACAGCAGCAGCTT
ATTGATGACCACTTTCTGTTTGATAAGCCTGTGTCCCCGTTGCTGACTGCAGCAGGAATG
GCTCGAGACTGGCCAGATGCTCGTGGAATTTGGCACAACAATGAGAAGAGCTTCCTGATC
TGGGTGAATGAGGAGGATCATACACGGGTGATCTCCATGGAGAAGGGTGGTAACATGAAG
AGAGTGTTTGAAAGATTCTGCCGAGGCCTCAAAGAGGTGGAGAGACTTATCCAAGAACGT
GGCTGGGAGTTCATGTGGAATGAGCGTTTGGGATACATCTTGACCTGTCCATCTAACCTG
GGCACTGGACTTCGGGCAGGAGTGCACATCAAACTGCCCCTGCTAAGCAAAGATAGCCGC
TTCCCAAAGATCCTGGAGAACCTAAGACTCCAAAAGCGTGGTACTGGAGGAGTGGACACT
GCTGCCACAGGCGGTGTCTTTGATATTTCTAATTTGGACCGACTAGGCAAATCAGAGGTG
GAGCTGGTGCAACTGGTCATCGATGGAGTAAACTATTTGATTGATTGTGAACGGCGTCTG
GAGAGAGGCCAGGATATCCGCATCCCCACACCTGTCATCCACACCAAGCATTAG
|
| Enzyme 117 GenBank Gene ID |
BT006628 |
| Enzyme 117 GeneCard ID |
CKMT1A |
| Enzyme 117 GenAtlas ID |
CKMT1A |
| Enzyme 117 HGNC ID |
HGNC:31736 |
| Enzyme 117 Chromosome Location |
1 |
| Enzyme 117 Locus |
15q15 |
| Enzyme 117 SNPs |
SNPJam Report |
| Enzyme 117 General References |
- Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [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 ]
- 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 ]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed ]
- Eder M, Fritz-Wolf K, Kabsch W, Wallimann T, Schlattner U: Crystal structure of human ubiquitous mitochondrial creatine kinase. Proteins. 2000 May 15;39(3):216-25. [PubMed ]
|
| Enzyme 117 Metabolite References |
Not Available |
|
Enzyme 118
[top]
|
| Enzyme 118 ID |
5996 |
| Enzyme 118 Name |
Creatine kinase M-type |
| Enzyme 118 Synonyms |
- Creatine kinase M chain
- M-CK
|
| Enzyme 118 Gene Name |
CKM |
| Enzyme 118 Protein Sequence |
>Creatine kinase M-type
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTG
VDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDD
LDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMT
EKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISM
EKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLA
HLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLM
VEMEKKLEKGQSIDDMIPAQK
|
| Enzyme 118 Number of Residues |
381 |
| Enzyme 118 Molecular Weight |
43100.9 |
| Enzyme 118 Theoretical pI |
7.28 |
| Enzyme 118 GO Classification |
| Function |
- catalytic activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 118 General Function |
Involved in kinase activity |
| Enzyme 118 Specific Function |
Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa |
| Enzyme 118 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 118 Reactions |
- ATP + creatine = ADP + phosphocreatine [RN:R01881]
|
| Enzyme 118 Pfam Domain Function |
|
| Enzyme 118 Signals |
|
| Enzyme 118 Transmembrane Regions |
|
| Enzyme 118 Essentiality |
Not Available |
| Enzyme 118 GenBank ID Protein |
180576 |
| Enzyme 118 UniProtKB/Swiss-Prot ID |
P06732 |
| Enzyme 118 UniProtKB/Swiss-Prot Entry Name |
KCRM_HUMAN |
| Enzyme 118 PDB ID |
1I0E |
| Enzyme 118 PDB File |
Show |
| Enzyme 118 3D Structure |
|
| Enzyme 118 Cellular Location |
Not Available |
| Enzyme 118 Gene Sequence |
>1146 bp
ATGCCATTCGGTAACACCCACAACAAGTTCAAGCTGAATTACAAGCCTGAGGAGGAGTAC
CCCGACCTCAGCAAACATAACAACCACATGGCCAAGGTACTGACCCTTGAACTCTACAAG
AAGCTGCGGGACAAGGAGATCCCATCTGGCTTCACTGTAGACGATGTCATCCAGACAGGA
GTGGACAACCCAGGTCACCCCTTCATCATGACCGTGGGCTGCGTGGCTGGTGATGAGGAG
TCCTACGAAGTTTTCAAGGAACTCTTTGACCCCATCATCTCGGATCGCCACGGGGGCTAC
AAACCCACTGACAAGCACAAGACTGACCTCAACCATGAAAACCTCAAGGGTGGAGACGAC
CTGGACCCCAACTACGTGCTCAGCAGCCCGGTCCGCACTGGCCGCAGCATCAAGGGCTAC
ACGTTGCCCCCACACTGCTCCCGTGGCGAGCGCCGGGCGGTGGAGAAGCTCTCTGTGGAA
GCTCTCAACAGCCTGACGGGCGAGTTCAAAGGGAAGTACTACCCTCTGAAGAGCATGACG
GAGAAGGAGCAGCAGCAGCTCATCGATGACCACTTCCAGTTCGACAAGCCCGTGTCCCCG
CTGCTGCTGGCCTCAGGCATGGCCCGCCACTGGCCCGACGCCCCTGGCATCTGGCACAAT
GACAACAAGAGCTTCCTGGTGTGGGTGAACGAGGAGGATCACCTCCGGGTCATCTCCATG
GAGAAGGGGGGCAACATGAAGGAGGTTTTCCGCCGCTTCTGCGTAGGGCTGCAGAAGATT
GAGGAGATCTTTAAGAAAGCTGGCCACCCCTTCATGTGGAACCAGCACCTGGGCTACGTG
CTCACCTGCCCATCCAACCTGGGCACTGGGCTGCGTGGAGGCGTGCATGTGAAGCTGGCG
CACCTGAGCAAGCACCCCAAGTTCGAGGAGATCCTCACCCGCCTGCGTCTGCAGAAGAGG
GGTACAGGTGCGGTGGACACAGCTGCCGTGGGCTCAGTATTTGACGTGTCCAACGCTGAT
CGGCTGGGCTCGTCCGAAGTAGAACAGGTGCAGCTGGTGGTGGATGGTGTGAAGCTCATG
GTGGAAATGGAGAAGAAGTTGGAGAAAGGCCAGTCCATCGACGACATGATCCCCGCCCAG
AAGTAG
|
| Enzyme 118 GenBank Gene ID |
M14780 |
| Enzyme 118 GeneCard ID |
CKM |
| Enzyme 118 GenAtlas ID |
CKM |
| Enzyme 118 HGNC ID |
HGNC:1994 |
| Enzyme 118 Chromosome Location |
1 |
| Enzyme 118 Locus |
19q13.2-q13.3 |
| Enzyme 118 SNPs |
SNPJam Report |
| Enzyme 118 General References |
- Perryman MB, Kerner SA, Bohlmeyer TJ, Roberts R: Isolation and sequence analysis of a full-length cDNA for human M creatine kinase. Biochem Biophys Res Commun. 1986 Nov 14;140(3):981-9. [PubMed ]
- Trask RV, Strauss AW, Billadello JJ: Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene. J Biol Chem. 1988 Nov 15;263(32):17142-9. [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 ]
- Hamburg RJ, Friedman DL, Olson EN, Ma TS, Cortez MD, Goodman C, Puleo PR, Perryman MB: Muscle creatine kinase isoenzyme expression in adult human brain. J Biol Chem. 1990 Apr 15;265(11):6403-9. [PubMed ]
- Nigro JM, Schweinfest CW, Rajkovic A, Pavlovic J, Jamal S, Dottin RP, Hart JT, Kamarck ME, Rae PM, Carty MD, et al.: cDNA cloning and mapping of the human creatine kinase M gene to 19q13. Am J Hum Genet. 1987 Feb;40(2):115-25. [PubMed ]
- Tang L, Zhou HM, Lin ZJ: Crystallization and preliminary X-ray analysis of human muscle creatine kinase. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):669-70. [PubMed ]
|
| Enzyme 118 Metabolite References |
Not Available |
|
Enzyme 119
[top]
|
| Enzyme 119 ID |
6009 |
| Enzyme 119 Name |
6-phosphofructokinase type C |
| Enzyme 119 Synonyms |
- 6-phosphofructokinase, platelet type
- Phosphofructo-1-kinase isozyme C
- PFK-C
- Phosphofructokinase 1
- Phosphohexokinase
|
| Enzyme 119 Gene Name |
PFKP |
| Enzyme 119 Protein Sequence |
>6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
|
| Enzyme 119 Number of Residues |
784 |
| Enzyme 119 Molecular Weight |
85595.4 |
| Enzyme 119 Theoretical pI |
7.60 |
| Enzyme 119 GO Classification |
| Function |
- 6-phosphofructokinase activity
- catalytic activity
- phosphofructokinase activity
- phosphotransferase activity, alcohol group as acceptor
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
- 6-phosphofructokinase complex
- cell part
- cytoplasm
- intracellular part
- macromolecular complex
- protein complex
|
|
| Enzyme 119 General Function |
Involved in 6-phosphofructokinase activity |
| Enzyme 119 Specific Function |
ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate |
| Enzyme 119 Pathways |
|
| Enzyme 119 Reactions |
- ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
|
| Enzyme 119 Pfam Domain Function |
|
| Enzyme 119 Signals |
|
| Enzyme 119 Transmembrane Regions |
|
| Enzyme 119 Essentiality |
Not Available |
| Enzyme 119 GenBank ID Protein |
Not Available |
| Enzyme 119 UniProtKB/Swiss-Prot ID |
Q01813 |
| Enzyme 119 UniProtKB/Swiss-Prot Entry Name |
K6PP_HUMAN |
| Enzyme 119 PDB ID |
Not Available |
| Enzyme 119 Cellular Location |
Not Available |
| Enzyme 119 Gene Sequence |
>2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
|
| Enzyme 119 GenBank Gene ID |
D25328 |
| Enzyme 119 GeneCard ID |
PFKP |
| Enzyme 119 GenAtlas ID |
PFKP |
| Enzyme 119 HGNC ID |
HGNC:8878 |
| Enzyme 119 Chromosome Location |
1 |
| Enzyme 119 Locus |
10p15.3-p15.2 |
| Enzyme 119 SNPs |
SNPJam Report |
| Enzyme 119 General References |
- Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [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 ]
- 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 ]
- Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [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 ]
- 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 ]
- 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 ]
- 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 |
6011 |
| Enzyme 120 Name |
DNA-directed RNA polymerase III subunit RPC4 |
| Enzyme 120 Synonyms |
- RNA polymerase III subunit C4
- DNA-directed RNA polymerase III subunit D
- Protein BN51
- RNA polymerase III 47 kDa subunit
- RPC53 homolog
|
| Enzyme 120 Gene Name |
POLR3D |
| Enzyme 120 Protein Sequence |
>DNA-directed RNA polymerase III subunit RPC4
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTP
NIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKK
GNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQL
PLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAAR
KTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVL
IKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQEL
VSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
|
| Enzyme 120 Number of Residues |
398 |
| Enzyme 120 Molecular Weight |
44395.5 |
| Enzyme 120 Theoretical pI |
6.97 |
| Enzyme 120 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular macromolecule biosynthetic process
- macromolecule biosynthetic process
- metabolic process
- transcription
- transcription from RNA polymerase III promoter
- transcription, DNA-dependent
|
| Component |
- DNA-directed RNA polymerase III complex
- intracellular organelle part
- nuclear part
- nucleoplasm part
- organelle part
|
|
| Enzyme 120 General Function |
Involved in DNA binding |
| Enzyme 120 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway |
| Enzyme 120 Pathways |
|
| 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 |
55769552 |
| Enzyme 120 UniProtKB/Swiss-Prot ID |
P05423 |
| Enzyme 120 UniProtKB/Swiss-Prot Entry Name |
RPC4_HUMAN |
| Enzyme 120 PDB ID |
Not Available |
| Enzyme 120 Cellular Location |
Not Available |
| Enzyme 120 Gene Sequence |
>1197 bp
ATGTCGGAAGGAAACGCCGCCGGCGAGCCCAGCACGCCGGGAGGGCCCCGACCTCTCCTG
ACTGGGGCCCGGGGGCTCATCGGGCGGCGGCCGGCGCCTCCCCTCACCCCCGGCCGCCTT
CCCTCCATCCGTTCCAGGGACCTCACCCTCGGGGGAGTCAAGAAGAAAACCTTCACCCCA
AATATCATCAGTCGGAAGATCAAGGAAGAGCCCAAGGAAGAAGTAACTGTCAAGAAGGAG
AAGCGTGAAAGGGACAGAGACCGACAACGAGAGGGGCATGGACGAGGGCGAGGCCGTCCA
GAAGTGATCCAGTCTCACTCCATCTTTGAGCAGGGCCCAGCTGAAATGATGAAGAAAAAA
GGGAACTGGGATAAGACAGTGGATGTGTCAGACATGGGACCTTCTCATATCATCAACATC
AAAAAAGAGAAGAGAGAGACAGACGAAGAAACTAAACAGATCTTGCGTATGCTGGAGAAG
GACGATTTCCTCGATGACCCCGGCCTGAGGAACGACACTCGAAATATGCCTGTGCAGCTG
CCGCTGGCTCACTCAGGATGGCTTTTTAAGGAAGAAAATGACGAACCAGATGTTAAACCT
TGGCTGGCTGGCCCCAAGGAAGAGGACATGGAGGTGGACATACCTGCTGTGAAAGTGAAA
GAGGAGCCACGAGATGAGGAGGAAGAGGCCAAGATGAAGGCTCCTCCCAAAGCAGCCAGG
AAGACTCCAGGCCTCCCGAAGGATGTATCTGTGGCAGAGCTGCTGAGGGAGCTGAGCCTC
ACCAAGGAAGAGGAACTGCTGTTTCTGCAGCTGCCAGACACCCTCCCTGGCCAGCCACCC
ACCCAGGACATCAAGCCTATCAAGACAGAGGTGCAGGGCGAGGACGGACAGGTGGTGCTC
ATCAAGCAGGAGAAAGACCGAGAAGCCAAATTGGCAGAGAATGCTTGTACCCTGGCTGAC
CTGACAGAGGGTCAGGTTGGCAAGCTACTCATCCGCAAGTCTGGAAGGGTGCAACTCCTC
TTGGGCAAGGTGACTCTGGACGTGACCATGGGAACTGCCTGCTCCTTCCTGCAGGAGCTG
GTGTCCGTGGGCCTTGGAGACAGTAGGACAGGGGAGATGACAGTCCTGGGACACGTGAAG
CACAAACTTGTATGTTCCCCTGATTTTGAATCCCTCTTGGATCACAAACACCGGTAA
|
| Enzyme 120 GenBank Gene ID |
NM_001722.2 |
| Enzyme 120 GeneCard ID |
POLR3D |
| Enzyme 120 GenAtlas ID |
POLR3D |
| Enzyme 120 HGNC ID |
HGNC:1080 |
| Enzyme 120 Chromosome Location |
8 |
| Enzyme 120 Locus |
8q21 |
| Enzyme 120 SNPs |
SNPJam Report |
| Enzyme 120 General References |
- Ittmann M, Greco A, Basilico C: Isolation of the human gene that complements a temperature-sensitive cell cycle mutation in BHK cells. Mol Cell Biol. 1987 Oct;7(10):3386-93. [PubMed ]
- Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [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 ]
- Chong SS, Hu P, Hernandez N: Reconstitution of transcription from the human U6 small nuclear RNA promoter with eight recombinant polypeptides and a partially purified RNA polymerase III complex. J Biol Chem. 2001 Jun 8;276(23):20727-34. Epub 2001 Feb 27. [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 ]
- Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed ]
- Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 120 Metabolite References |
Not Available |
|
Enzyme 121
[top]
|
| Enzyme 121 ID |
6012 |
| Enzyme 121 Name |
DNA-directed RNA polymerase II subunit RPB2 |
| Enzyme 121 Synonyms |
- DNA-directed RNA polymerase II 140 kDa polypeptide
- DNA-directed RNA polymerase II subunit B
- RNA polymerase II subunit 2
- RNA polymerase II subunit B2
|
| Enzyme 121 Gene Name |
POLR2B |
| Enzyme 121 Protein Sequence |
>DNA-directed RNA polymerase II subunit RPB2
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVE
DAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTY
SAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLD
PGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSML
ARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEM
VKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETK
KAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQ
KFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLS
HLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSP
ILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSE
VSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASG
VVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSP
RNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIV
AIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGM
RHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSE
TGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEG
ITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGY
HLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSR
DGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGC
RNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
|
| Enzyme 121 Number of Residues |
1174 |
| Enzyme 121 Molecular Weight |
133895.4 |
| Enzyme 121 Theoretical pI |
6.87 |
| Enzyme 121 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleoside binding
- nucleotidyltransferase activity
- ribonucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular macromolecule biosynthetic process
- macromolecule biosynthetic process
- metabolic process
- transcription
|
| Component |
| — |
|
| Enzyme 121 General Function |
Involved in DNA-directed RNA polymerase activity |
| Enzyme 121 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template |
| Enzyme 121 Pathways |
|
| Enzyme 121 Reactions |
- nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
|
| Enzyme 121 Pfam Domain Function |
|
| Enzyme 121 Signals |
|
| Enzyme 121 Transmembrane Regions |
|
| Enzyme 121 Essentiality |
Not Available |
| Enzyme 121 GenBank ID Protein |
36122 |
| Enzyme 121 UniProtKB/Swiss-Prot ID |
P30876 |
| Enzyme 121 UniProtKB/Swiss-Prot Entry Name |
RPB2_HUMAN |
| Enzyme 121 PDB ID |
Not Available |
| Enzyme 121 Cellular Location |
Not Available |
| Enzyme 121 Gene Sequence |
>3525 bp
ATGTACGACGCGGATGAGGATATGCAATATGATGAGGATGATGATGAAATCACCCCGGAT
TTGTGGCAAGAAGCATGCTGGATTGTAATCAGTTCCTATTTTGACGAGAAAGGCTTGGTT
AGACAACAGCTGGATTCTTTTGATGAGTTTATTCAGATGTCTGTTCAAAGAATTGTGGAA
GACGCTCCTCCTATAGACCTACAGGCTGAAGCTCAGCATGCTAGTGGAGAAGTTGAAGAA
CCGCCACGATATTTGCTGAAGTTTGAACAAATTTATCTTTCCAAGCCTACCCATTGGGAA
AGAGATGGTGCTCCTTCACCAATGATGCCCAATGAAGCTAGATTAAGGAATCTCACGTAT
TCTGCTCCGCTTTATGTTGATATAACAAAAACAGTCATTAAAGAAGGTGAAGAACAACTT
CAGACTCAGCATCAGAAAACTTTTATAGGAAAAATTCCAATTATGTTGCGGTCAACTTAC
TGCCTTTTGAATGGCTTGACAGATCGTGATCTTTGTGAGTTAAATGAATGCCCTTTGGAT
CCTGGTGGCTATTTCATTATTAATGGATCAGAAAAGGTTCTGATTGCCCAAGAGAAAATG
GCAACAAACACAGTTTATGTGTTTGCCAAAAAGGATTCTAAATATGCCTACACAGGAGAG
TGTAGATCATGTCTTGAGAATTCTTCCCGACCCACCAGTACTATATGGGTTAGCATGCTG
GCAAGAGGAGGACAGGGTGCCAAGAAGAGTGCTATTGGTCAGCGCATTGTGGCAACTCTA
CCATATATCAAGCAAGAAGTTCCCATCATTATTGTGTTCAGAGCATTAGGTTTTGTGTCC
GACAGAGATATTTTAGAACATATTATTTATGATTTTGAAGATCCAGAGATGATGGAAATG
GTTAAACCTTCTCTCGATGAAGCTTTTGTCATCCAAGAACAGAATGTTGCACTAAATTTC
ATTGGTTCACGAGGAGCAAAGCCTGGTGTTACTAAAGAGAAAAGAATTAAATATGCAAAG
GAAGTTTTACAAAAAGAAATGCTCCCTCATGTTGGTGTCAGTGATTTTTGTGAGACCAAA
AAAGCCTATTTCTTGGGATACATGGTTCATAGGTTACTTCTGGCAGCTTTGGGTAGAAGA
GAACTAGATGACAGAGATCACTATGGAAACAAGAGATTGGATCTTGCTGGGCCGCTGCTT
GCATTCTTATTTAGAGGTATGTTTAAGAATTTGCTTAAAGAAGTGCGGATCTATGCACAG
AAATTTATTGATCGAGGAAAGGATTTTAACTTGGAGTTGGCAATTAAAACACGGATCATA
TCTGATGGCCTAAAATACTCTTTAGCTACTGGAAACTGGGGTGATCAAAAGAAAGCTCAT
CAAGCCAGAGCTGGAGTATCTCAGGTGTTAAACCGCCTGACTTTTGCGTCTACTCTTTCT
CACCTGCGTCGTTTAAATTCTCCTATTGGTAGAGACGGCAAGCTAGCAAAACCAAGACAG
TTGCATAATACGTTGTGGGGAATGGTGTGTCCTGCCGAGACCCCAGAGGGCCATGCTGTA
GGACTTGTGAAGAATTTAGCCTTGATGGCGTATATTTCAGTTGGATCTCAACCATCTCCA
ATTCTGGAATTTTTAGAAGAATGGAGTATGGAAAATTTAGAAGAAATTTCTCCTGCAGCT
ATTGCTGATGCAACCAAGATTTTTGTTAATGGCTGCTGGGTTGGAATACATAAAGATCCC
GAACAACTTATGAACACCCTAAGGAAATTGAGACGTCAGATGGACATCATTGTGTCTGAA
GTTTCTATGATCAGAGATATTCGAGAGAGGGAGATTCGGATCTATACGGATGCAGGCCGT
ATTTGTAGACCACTTCTGATTGTGGAAAAACAAAAGCTACTTTTGAAGAAGAGGCATATT
GACCAATTGAAAGAGAGAGAATATAACAACTATAGTTGGCAGGATCTTGTGGCCAGTGGG
GTAGTGGAGTATATTGATACCCTGGAAGAAGAAACAGTGATGCTTGCAATGACTCCAGAT
GATTTACAGGAGAAAGAAGTAGCTTATTGTTCCACATATACACACTGTGAGATTCATCCC
TCAATGATCCTTGGTGTCTGTGCATCTATTATTCCCTTTCCTGATCATAACCAGTCCCCT
AGAAACACATACCAGTCTGCTATGGGTAAGCAGGCTATGGGAGTTTACATCACCAACTTC
CATGTTCGCATGGACACATTGGCCCATGTTCTCTATTATCCTCAAAAGCCACTTGTGACT
ACACGGTCTATGGAATATCTACGATTTAGAGAGCTGCCAGCAGGCATCAACTCAATTGTG
GCCATTGCATCATACACTGGATATAATCAGGAAGACTCTGTTATCATGAATCGTTCAGCT
GTAGACCGCGGCTTCTTCAGGTCTGTTTTCTATCGCTCATACAAAGAACAGGAGTCTAAA
AAAGGATTTGATCAAGAAGAAGTTTTTGAGAAGCCTACACGTGAAACATGCCAGGGCATG
AGGCATGCCATTTACGACAAGCTGGATGATGATGGTTTGATAGCTCCAGGGGTTCGTGTA
TCAGGAGATGATGTTATTATAGGCAAAACAGTCACCTTGCCTGAAAATGAAGATGAATTG
GAGAGCACCAATAGACGCTATACCAAGAGAGACTGTAGCACTTTTCTCAGAACTAGTGAG
ACGGGCATTGTGGATCAGGTTATGGTAACTCTCAATCAGGAAGGATATAAATTTTGTAAA
ATAAGGGTACGCTCTGTTAGGATTCCACAGATTGGAGACAAATTTGCTAGTCGACATGGT
CAAAAGGGTACTTGTGGTATTCAGTATAGACAAGAGGATATGCCTTTCACCTGTGAAGGT
ATCACCCCTGATATCATCATCAATCCCCATGCCATCCCCTCTCGTATGACTATTGGTCAC
TTAATTGAATGCCTTCAAGGGAAGGTATCGGCTAACAAGGGTGAAATTGGTGATGCCACT
CCATTTAATGATGCTGTTAACGTGCAGAAGATTTCTAATCTTTTATCTGATTATGGCTAT
CATCTCAGAGGAAATGAGGTCCTGTACAATGGGTTCACTGGTCGAAAAATCACATCACAA
ATATTTATTGGCCCCACTTATTACCAGCGTTTGAAGCATATGGTGGATGATAAGATTCAC
TCTCGTGCTAGGGGACCTATTCAGATCCTCAATAGACAGCCCATGGAGGGTAGATCTCGT
GATGGTGGCCTGCGTTTTGGAGAAATGGAACGAGATTGTCAGATTGCCCATGGAGCAGCC
CAGTTTTTAAGGGAAAGATTGTTTGAGGCATCAGATCCATATCAGGTTCATGTTTGCAAT
CTTTGTGGAATAATGGCGATTGCCAACACCAGGACCCATACATATGAATGCAGGGGCTGC
CGCAATAAAACCCAGATTTCTTTGGTGCGAATGCCTTACGCATGCAAACTATTGTTTCAG
GAACTTATGTCTATGAGTATTGCACCGCGAATGATGAGTGTTTAG
|
| Enzyme 121 GenBank Gene ID |
X63563 |
| Enzyme 121 GeneCard ID |
POLR2B |
| Enzyme 121 GenAtlas ID |
POLR2B |
| Enzyme 121 HGNC ID |
HGNC:9188 |
| Enzyme 121 Chromosome Location |
4 |
| Enzyme 121 Locus |
4q12 |
| Enzyme 121 SNPs |
SNPJam Report |
| Enzyme 121 General References |
- Acker J, Wintzerith M, Vigneron M, Kedinger C: Primary structure of the second largest subunit of human RNA polymerase II (or B). J Mol Biol. 1992 Aug 20;226(4):1295-9. [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 ]
- 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 W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed ]
- Kershnar E, Wu SY, Chiang CM: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998 Dec 18;273(51):34444-53. [PubMed ]
|
| Enzyme 121 Metabolite References |
Not Available |
|
Enzyme 122
[top]
|
| Enzyme 122 ID |
6014 |
| Enzyme 122 Name |
DNA-directed RNA polymerase II subunit RPB1 |
| Enzyme 122 Synonyms |
- RNA polymerase II subunit B1
- DNA-directed RNA polymerase II subunit A
- DNA-directed RNA polymerase III largest subunit
- RNA-directed RNA polymerase II subunit RPB1
|
| Enzyme 122 Gene Name |
POLR2A |
| Enzyme 122 Protein Sequence |
>DNA-directed RNA polymerase II subunit RPB1
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDP
RQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVD
SNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKG
HGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEP
RYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAA
HVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVD
FSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYII
RDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWS
TFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQD
TLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHI
NCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEM
GHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKA
HNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKIN
ISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHA
MGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGES
VEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMR
EDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKL
VIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAI
AHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLT
VFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMP
DFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIR
IMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKI
IITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALER
ELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLM
EAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTG
MFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPG
YSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSP
SYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSP
TSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS
YSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPT
SPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKY
SPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTS
PKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN
|
| Enzyme 122 Number of Residues |
1970 |
| Enzyme 122 Molecular Weight |
217174.2 |
| Enzyme 122 Theoretical pI |
7.38 |
| Enzyme 122 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular macromolecule biosynthetic process
- macromolecule biosynthetic process
- metabolic process
- transcription
- transcription from RNA polymerase II promoter
- transcription, DNA-dependent
|
| Component |
- DNA-directed RNA polymerase II, core complex
- intracellular organelle part
- nuclear part
- nucleoplasm part
- organelle part
|
|
| Enzyme 122 General Function |
Involved in DNA binding |
| Enzyme 122 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA- dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome |
| Enzyme 122 Pathways |
|
| Enzyme 122 Reactions |
- nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
|
| Enzyme 122 Pfam Domain Function |
|
| Enzyme 122 Signals |
|
| Enzyme 122 Transmembrane Regions |
|
| Enzyme 122 Essentiality |
Not Available |
| Enzyme 122 GenBank ID Protein |
36124 |
| Enzyme 122 UniProtKB/Swiss-Prot ID |
P24928 |
| Enzyme 122 UniProtKB/Swiss-Prot Entry Name |
RPB1_HUMAN |
| Enzyme 122 PDB ID |
Not Available |
| Enzyme 122 Cellular Location |
Not Available |
| Enzyme 122 Gene Sequence |
>5913 bp
ATGCACGGGGGTGGCCCCCCCTCGGGGGACAGCGCATGCCCGCTGCGCACCATCAAGAGA
GTCCAGTTCGGAGTCCTGAGTCCGGATGAACTGAAGCGAATGTCTGTGACGGAGGGTGGC
ATCAAATACCCAGAGACGACTGAGGGAGGCCGCCCCAAGCTTGGGGGGCTGATGGACCCG
AGGCAGGGGGTGATTGAGCGGACTGGCCGCTGCCAAACATGTGCAGGAAACATGACAGAG
TGTCCTGGCCACTTTGGCCACATTGAACTGGCCAAGCCTGTGTTTCACGTGGGCTTCCTG
GTGAAGACAATGAAAGTTTTGCGCTGTGTCTGCTTCTTCTGCTCCAAACTGCTTGTGGAC
TCTAACAACCCAAAGATCAAGGATATCCTGGCTAAGTCCAAGGGACAGCCCAAGAAGCGG
CTCACACATGTCTACGACCTTTGCAAGGGCAAAAACATATGCGAGGGTGGGGAGGAGATG
GACAACAAGTTCGGTGTGGAACAACCTGAGGGTGACGAGGATCTGACCAAAGAAAAGGGC
CATGGTGGCTGTGGGCGGTACCAGCCCAGGATCCGGCGTTCTGGCCTAGAGCTGTATGCG
GAATGGAAGCACGTTAATGAGGACTCTCAGGAGAAGAAGATCCTGCTGAGTCCAGAGCGA
GTGCATGAGATCTTCAAACGCATCTCAGATGAGGAGTGTTTTGTGCTGGGCATGGAGCCC
CGCTATGCACGGCCAGAGTGGATGATTGTCACAGTGCTGCCTGTGCCCCCGCTCTCCGTG
CGGCCTGCTGTTGTGATGCAGGGCTCTGCCCGTAACCAGGATGACCTGACTCACAAACTG
GCTGACATCGTGAAGATCAACAATCAGCTGCGGCGCAATGAGCAGAACGGCGCAGCGGCC
CATGTCATTGCAGAGGATGTGAAGCTCCTCCAGTTCCATGTGGCCACCATGGTGGACAAT
GAGCTGCCTGGCTTGCCCCGTGCCATGCAGAAGTCTGGGCGTCCCCTCAAGTCCCTGAAG
CAGCGGTTGAAGGGCAAGGAAGGCCGGGTGCGAGGGAACCTGATGGGCAAAAGAGTGGAC
TTCTCGGCCCGTACTGTCATCACCCCCGACCCCAACCTCTCCATTGACCAGGTTGGCGTG
CCCCGCTCCATTGCTGCCAACATGACCTTTGCGGAGATTGTCACCCCCTTCAACATTGAC
AGACTTCAAGAACTAGTGCGCAGGGGGAACAGTCAGTACCCAGGCGCCAAGTACATCATC
CGAGACAATGGTGATCGCATTGACTTGCGTTTCCACCCCAAGCCCAGTGACCTTCACCTG
CAGACCGGCTATAAGGTGGAACGGCACATGTGTGATGGGGACATTGTTATCTTCAACCGG
CAGCCAACTCTGCACAAAATGTCCATGATGGGGCATCGGGTCCGCATTCTCCCATGGTCT
ACCTTTCGCTTGAATCTTAGCGTGACAACTCCGTACAATGCAGACTTTGACGGGGATGAG
ATGAACTTGCACCTGCCACAGTCTCTGGAGACGCGAGCAGAGATCCAGGAGCTGGCCATG
GTTCCTCGCATGATTGTCACCCCCCAGAGCAATCGGCCTGTCATGGGTATTGTGCAGGAC
ACACTCACAGCAGTGCGCAAATTCACCAAGAGAGACGTCTTCCTGGAGCGGGGTGAAGTG
ATGAACCTCCTGATGTTCCTGTCGACGTGGGATGGGAAGGTCCCACAGCCGGCCATCCTA
AAGCCCCGGCCCCTGTGGACAGGCAAGCAAATCTTCTCCCTCATCATACCTGGTCACATC
AATTGTATCCGTACCCACAGCACCCATCCCGATGATGAAGACAGTGGCCCTTACAAGCAC
ATCTCTCCTGGGGACACCAAGGTGGTGGTGGAGAATGGGGAGCTGATCATGGGCATCCTG
TGTAAGAAGTCTCTGGGCACGTCAGCTGGCTCCCTGGTCCACATCTCCTACCTAGAGATG
GGTCATGACATCACTCGCCTCTTCTACTCCAACATTCAGACTGTCATTAACAACTGGCTC
CTCATCGAGGGTCATACTATTGGCATTGGGGACTCCATTGCTGATTCTAAGACTTACCAG
GACATTCAGAACACTATTAAGAAGGCCAAGCAGGACGTAATAGAGGTCATCGAGAAGGCA
CACAACAATGAGCTGGAGCCCACCCCAGGGAACACTCTGCGGCAGACGTTTGAGAATCAG
GTGAACCGCATTCTTAACGATGCCCGAGACAAGACTGGCTCCTCTGCTCAGAAATCCCTG
TCTGAATACAACAACTTCAAGTCTATGGTCGTGTCCGGAGCTAAAGGTTCCAAGATTAAC
ATCTCCCAGGTCATTGCTGTCGTTGGACAGCAGAACGTCGAGGGCAAGCGGATTCCATTT
GGCTTCAAGCACCGGACTCTGCCTCACTTCATCAAGGATGACTACGGGCCTGAGAGCCGT
GGCTTTGTGGAGAACTCCTACCTAGCCGGCCTCACACCCACTGAGTTCTTTTTCCACGCC
ATGGGGGGTCGTGAGGGGCTCATTGACACGGCTGTCAAGACTGCTGAGACTGGATACATC
CAGCGGCGGCTGATCAAGTCCATGGAGTCAGTGATGGTGAAGTACGACGCGACTGTGCGG
AACTCCATCAACCAGGTGGTGCAGCTGCGCTACGGCGAAGACGGCCTGGCAGGCGAGAGC
GTTGAGTTCCAGAACCTGGCTACGCTTAAGCCTTCCAACAAGGCTTTTGAGAAGAAGTTC
CGCTTTGATTATACCAATGAGAGGGCCCTGCGGCGCACTCTGCAGGAGGACCTGGTGAAG
GACGTGCTGAGCAACGCACACATCCAGAACGAGTTGGAGCGGGAATTTGAGCGGATGCGG
GAGGATCGGGAGGTGCTCAGGGTCATCTTCCCAACTGGAGACAGCAAGGTCGTCCTCCCC
TGTAACCTGCTGCGGATGATCTGGAATGCTCAGAAAATCTTCCACATCAACCCACGCCTT
CCCTCCGACCTGCACCCCATCAAAGTGGTGGAGGGAGTCAAGGAATTGAGCAAGAAGCTG
GTGATTGTGAATGGGGATGACCCACTAAGTCGACAGGCCCAGGAAAATGCCACGCTGCTC
TTCAACATCCACCTGCGGTCCACGTTGTGTTCCCGCCGCATGGCAGAGGAGTTTCGGCTC
AGTGGGGAGGCCTTCGACTGGCTGCTTGGGGAGATTGAGTCCAAGTTCAACCAAGCCATT
GCGCATCCCGGGGAAATGGTGGGGGCTCTGGCTGCGCAGTCCCTTGGAGAACCTGCCACC
CAGATGACCTTGAATACCTTCCACTATGCTGGTGTGTCTGCCAAGAATGTGACGCTGGGT
GTGCCCCGACTTAAGGAGCTCATCAACATTTCCAAGAAGCCAAAGACTCCTTCGCTTACT
GTCTTCCTGTTGGGCCAGTCCGCTCGAGATGCTGAGAGAGCCAAGGATATTCTGTGCCGT
CTGGAGCATACAACGTTGAGGAAGGTGACTGCCAACACAGCCATCTACTATGACCCCAAC
CCCCAGAGCACGGTGGTGGCAGAGGATCAGGAATGGGTGAATGTCTACTATGAAATGCCT
GACTTTGATGTGGCCCGAATCTCCCCCTGGCTGTTGCGGGTGGAGCTGGATCGGAAGCAC
ATGACTGACCGGAAGCTCACCATGGAGCAGATTGCTGAAAAGATCAATGCTGGTTTTGGT
GACGACTTGAACTGCATCTTTAATGATGACAATGCAGAGAAGCTGGTGCTCCGTATTCGC
ATCATGAACAGCGATGAGAACAAGATGCAAGAGGAGGAAGAGGTGGTGGACAAGATGGAT
GATGATGTCTTCCTGCGCTGCATCGAGTCCAACATGCTGACAGATATGACCCTGCAGGGC
ATCGAGCAGATCAGCAAGGTGTACATGCACTTGCCACAGACAGACAACAAGAAGAAGATC
ATCATCACGGAGGATGGGGAATTCAAGGCCCTGCAGGAGTGGATCCTGGAGACGGACGGC
GTGAGCTTGATGCGGGTGCTGAGTGAGAAGGACGTGGACCCCGTACGCACCACGTCCAAT
GACATTGTGGAGATCTTCACGGTGCTGGGCATTGAAGCCGTGCGGAAGGCCCTGGAGCGG
GAGCTGTACCACGTCATCTCCTTTGATGGCTCCTATGTCAATTACCGACACTTGGCTCTC
TTGTGTGATACCATGACCTGTCGTGGCCACTTGATGGCCATCACCCGACACGGAGTCAAC
CGCCAGGACACAGGACCACTCATGAAGTGTTCCTTTGAGGAAACGGTGGACGTGCTTATG
GAAGCAGCCGCACACGGTGAGAGTGACCCCATGAAGGGGGTCTCTGAGAATATCATGCTG
GGCCAGCTGGCTCCGGCCGGCACTGGCTGCTTTGACCTCCTGCTTGATGCAGAGAAGTGC
AAGTATGGCATGGAGATCCCCACCAATATCCCCGGCCTGGGGGCTGCTGGACCCACCGGC
ATGTTCTTTGGTTCAGCACCCAGTCCCATGGGTGGAATCTCTCCTGCCATGACACCTTGG
AACCAGGGTGCAACCCCTGCCTATGGCGCCTGGTCCCCCAGTGTTGGGAGTGGAATGACC
CCAGGGGCAGCCGGTTTCTCTCCCAGTGCTGCGTCAGATGCCAGCGGCTTCAGCCCAGGT
TACTCCCCTGCCTGGTCTCCCACACCGGGCTCCCCGGGGTCCCCAGGTCCCTCAAGCCCC
TACATCCCTTCACCAGGTGGCGCCATGTCTCCCAGCTACTCGCCAACGTCACCTGCCTAC
GAGCCCCGCTCTCCTGGGGGCTACACACCCCAGAGTCCCTCTTATTCCCCCACTTCACCC
TCCTACTCCCCTACCTCTCCATCCTATTCTCCAACCAGTCCCAACTATAGTCCCACATCA
CCCAGCTATTCGCCAACGTCACCCAGCTACTCACCGACCTCTCCCAGCTACTCACCCACC
TCTCCCAGCTACTCGCCCACCTCTCCCAGCTATTCGCCCACCTCTCCCAGCTACTCACCC
ACTTCCCCTAGCTATTCGCCCACTTCCCCTAGCTACTCGCCAACGTCTCCCAGCTACTCG
CCGACATCTCCCAGCTACTCGCCAACTTCACCCAGCTATTCTCCCACTTCTCCCAGCTAC
TCACCTACCTCTCCAAGCTATTCACCCACCTCCCCCAGCTACTCACCCACTTCCCCAAGT
TACTCACCCACCAGCCCGAACTATTCTCCAACCAGTCCCAATTACACCCCAACATCACCC
AGCTACAGCCCGACATCACCCAGCTATTCCCCTACTAGTCCCAACTACACACCTACCAGC
CCTAACTACAGCCCAACCTCTCCAAGCTACTCTCCAACATCACCCAGCTATTCCCCGACC
TCACCAAGTTACTCCCCTTCCAGCCCACGATACACACCACAGTCTCCAACCTATACCCCA
AGCTCACCCAGCTACAGCCCCAGTTCGCCCAGCTACAGCCCAACCTCACCCAAGTACACC
CCAACCAGTCCTTCTTATAGTCCCAGCTCCCCAGAGTATACCCCAACCTCTCCCAAGTAC
TCACCTACCAGTCCCAAATATTCACCCACCTCTCCCAAGTACTCGCCTACCAGTCCCACC
TATTCACCCACCACCCCAAAATACTCCCCAACATCTCCTACTTATTCCCCAACCTCTCCA
GTCTACACCCCAACCTCTCCCAAGTACTCACCTACTAGCCCCACTTACTCGCCCACTTCC
CCCAAGTACTCGCCCACCAGCCCCACCTACTCGCCCACCTCCCCCAAAGGCTCAACCTAC
TCTCCCACTTCCCCTGGTTACTCGCCCACCAGCCCCACCTACAGTCTCACAAGCCCGGCT
ATCAGCCCGGATGACAGTGACGAGGAGAACTGA
|
| Enzyme 122 GenBank Gene ID |
X63564 |
| Enzyme 122 GeneCard ID |
POLR2A |
| Enzyme 122 GenAtlas ID |
POLR2A |
| Enzyme 122 HGNC ID |
HGNC:9187 |
| Enzyme 122 Chromosome Location |
1 |
| Enzyme 122 Locus |
17p13.1 |
| Enzyme 122 SNPs |
SNPJam Report |
| Enzyme 122 General References |
- Wintzerith M, Acker J, Vicaire S, Vigneron M, Kedinger C: Complete sequence of the human RNA polymerase II largest subunit. Nucleic Acids Res. 1992 Feb 25;20(4):910. [PubMed ]
- Mita K, Tsuji H, Morimyo M, Takahashi E, Nenoi M, Ichimura S, Yamauchi M, Hongo E, Hayashi A: The human gene encoding the largest subunit of RNA polymerase II. Gene. 1995 Jul 4;159(2):285-6. [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 ]
- Kershnar E, Wu SY, Chiang CM: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998 Dec 18;273(51):34444-53. [PubMed ]
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| Enzyme 122 Metabolite References |
Not Available |
|
Enzyme 123
[top]
|
| Enzyme 123 ID |
6017 |
| Enzyme 123 Name |
DNA-directed RNA polymerase, mitochondrial |
| Enzyme 123 Synonyms |
- MtRPOL
|
| Enzyme 123 Gene Name |
POLRMT |
| Enzyme 123 Protein Sequence |
>DNA-directed RNA polymerase, mitochondrial
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHV
ELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCG
RWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTR
QAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLP
LAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYA
AALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSL
PPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKP
TLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVV
RMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASD
AEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSS
RLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHS
GAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQL
FQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEAL
YRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDW
LKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCME
VANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVA
AQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDF
PQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQ
PYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCY
RKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILE
ASQLKETLQAVPKPGAFDLEQVKRSTYFFS
|
| Enzyme 123 Number of Residues |
1230 |
| Enzyme 123 Molecular Weight |
138619.3 |
| Enzyme 123 Theoretical pI |
9.25 |
| Enzyme 123 GO Classification |
| Function |
- DNA binding
- DNA-directed RNA polymerase activity
- RNA polymerase activity
- binding
- catalytic activity
- nucleic acid binding
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- cellular macromolecule biosynthetic process
- macromolecule biosynthetic process
- metabolic process
- transcription
|
| Component |
| — |
|
| Enzyme 123 General Function |
Involved in DNA binding |
| Enzyme 123 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
|
