|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6404 |
| Enzyme 1 Name |
Monocarboxylate transporter 1 |
| Enzyme 1 Synonyms |
- MCT 1
- Solute carrier family 16 member 1
|
| Enzyme 1 Gene Name |
SLC16A1 |
| Enzyme 1 Protein Sequence |
>Monocarboxylate transporter 1
MPPAVGGPVGYTPPDGGWGWAVVIGAFISIGFSYAFPKSITVFFKEIEGIFHATTSEVSW
ISSIMLAVMYGGGPISSILVNKYGSRIVMIVGGCLSGCGLIAASFCNTVQQLYVCIGVIG
GLGLAFNLNPALTMIGKYFYKRRPLANGLAMAGSPVFLCTLAPLNQVFFGIFGWRGSFLI
LGGLLLNCCVAGALMRPIGPKPTKAGKDKSKASLEKAGKSGVKKDLHDANTDLIGRHPKQ
EKRSVFQTINQFLDLTLFTHRGFLLYLSGNVIMFFGLFAPLVFLSSYGKSQHYSSEKSAF
LLSILAFVDMVARPSMGLVANTKPIRPRIQYFFAASVVANGVCHMLAPLSTTYVGFCVYA
GFFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYK
YTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESKEEETSIDVAGKPNEVTKA
AESPDQKDTEGGPKEEESPV
|
| Enzyme 1 Number of Residues |
500 |
| Enzyme 1 Molecular Weight |
53957.7 |
| Enzyme 1 Theoretical pI |
8.82 |
| Enzyme 1 GO Classification |
| Function |
- carboxylic acid transmembrane transporter activity
- monocarboxylic acid transmembrane transporter activity
- organic acid transmembrane transporter activity
- secondary active monocarboxylate transmembrane transporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- anion transport
- establishment of localization
- ion transport
- organic anion transport
- transmembrane transport
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 1 General Function |
Involved in transmembrane transport |
| Enzyme 1 Specific Function |
Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate |
| Enzyme 1 Pathways |
Not Available |
| Enzyme 1 Reactions |
Not Available |
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
- 16-36
60-80
87-107
112-132
144-164
167-187
263-283
299-319
329-349
354-374
390-410
423-443
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
561722  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P53985  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
MOT1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1503 bp
ATGCCACCAGCAGTTGGAGGTCCAGTTGGATACACCCCCCCAGATGGAGGCTGGGGCTGG
GCAGTGGTAATTGGAGCTTTCATTTCCATCGGCTTCTCTTATGCATTTCCCAAATCAATT
ACTGTCTTCTTCAAAGAGATTGAAGGTATATTCCATGCCACCACCAGCGAAGTGTCATGG
ATATCCTCCATAATGTTGGCTGTCATGTATGGTGGAGGTCCTATCAGCAGTATCCTGGTG
AATAAATATGGAAGTCGTATAGTCATGATTGTTGGTGGCTGCTTGTCAGGCTGTGGCTTG
ATTGCAGCTTCTTTCTGTAACACCGTACAGCAACTATACGTCTGTATTGGAGTCATTGGA
GGTCTTGGGCTTGCCTTCAACTTGAATCCAGCTCTGACCATGATTGGCAAGTATTTCTAC
AAGAGGCGACCATTGGCCAACGGACTGGCCATGGCAGGCAGCCCTGTGTTCCTCTGTACT
CTGGCCCCCCTCAATCAGGTTTTCTTCGGTATCTTTGGATGGAGAGGAAGCTTTCTAATT
CTTGGGGGCTTGCTACTAAACTGCTGTGTTGCTGGAGCCCTCATGCGACCAATCGGGCCC
AAGCCAACCAAGGCAGGGAAAGATAAGTCTAAAGCATCCCTTGAGAAAGCTGGAAAATCT
GGTGTGAAAAAAGATCTGCATGATGCAAATACAGATCTTATTGGAAGACACCCTAAACAA
GAGAAACGATCAGTCTTCCAAACAATTAATCAGTTCCTGGACTTAACCCTATTCACCCAC
AGAGGCTTTTTGCTATACCTCTCTGGAAATGTGATCATGTTTTTTGGACTCTTTGCACCT
TTGGTGTTTCTTAGTAGTTATGGGAAGAGTCAGCATTATTCTAGTGAGAAGTCTGCCTTC
CTTCTTTCCATTCTGGCTTTTGTTGACATGGTAGCCCGACCATCTATGGGACTTGTAGCC
AACACAAAGCCAATAAGACCTCGAATTCAGTATTTCTTTGCGGCTTCCGTTGTTGCAAAT
GGAGTGTGTCATATGCTAGCACCTTTATCCACTACCTATGTTGGATTCTGTGTCTATGCG
GGATTCTTTGGATTTGCCTTCGGGTGGCTCAGCTCCGTATTGTTTGAAACATTGATGGAC
CTTGTTGGACCCCAGAGGTTCTCCAGCGCTGTGGGATTGGTGACCATTGTGGAATGCTGT
CCTGTCCTCCTGGGGCCACCACTTTTAGGTCGGCTCAATGACATGTATGGAGACTACAAA
TACACATACTGGGCATGTGGCGTCGTCCTAATTATTTCAGGTATCTATCTCTTCATTGGC
ATGGGCATCAATTATCGACTTTTGGCAAAAGAACAGAAAGCAAACGAGCAGAAAAAGGAA
AGTAAAGAGGAAGAGACCAGTATAGATGTTGCTGGGAAGCCAAATGAAGTTACCAAAACA
GCAGAATCTCCGGACCAGAAAGACACAGAAGGAGGGCCCAAGGAGGAGGAAAGTCCAGTC
TGA
|
| Enzyme 1 GenBank Gene ID |
L31801  |
| Enzyme 1 GeneCard ID |
SLC16A1  |
| Enzyme 1 GenAtlas ID |
SLC16A1  |
| Enzyme 1 HGNC ID |
HGNC:10922  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1p12 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Garcia CK, Li X, Luna J, Francke U: cDNA cloning of the human monocarboxylate transporter 1 and chromosomal localization of the SLC16A1 locus to 1p13.2-p12. Genomics. 1994 Sep 15;23(2):500-3. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- 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
]
- Merezhinskaya N, Fishbein WN, Davis JI, Foellmer JW: Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport. Muscle Nerve. 2000 Jan;23(1):90-7. [PubMed
]
- Otonkoski T, Jiao H, Kaminen-Ahola N, Tapia-Paez I, Ullah MS, Parton LE, Schuit F, Quintens R, Sipila I, Mayatepek E, Meissner T, Halestrap AP, Rutter GA, Kere J: Physical exercise-induced hypoglycemia caused by failed silencing of monocarboxylate transporter 1 in pancreatic beta cells. Am J Hum Genet. 2007 Sep;81(3):467-74. Epub 2007 Jul 26. [PubMed
]
|
| Enzyme 1 Metabolite References |
- Borthakur A, Saksena S, Gill RK, Alrefai WA, Ramaswamy K, Dudeja PK: Regulation of monocarboxylate transporter 1 (MCT1) promoter by butyrate in human intestinal epithelial cells: involvement of NF-kappaB pathway. J Cell Biochem. 2008 Apr 1;103(5):1452-63. [PubMed
]
|
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
7434 |
| Enzyme 2 Name |
Caspase-3 |
| Enzyme 2 Synonyms |
- CASP-3
- Apopain
- Cysteine protease CPP32
- CPP-32
- Protein Yama
- SREBP cleavage activity 1
- SCA-1
- Caspase-3 subunit p17
- Caspase-3 subunit p12
|
| Enzyme 2 Gene Name |
CASP3 |
| Enzyme 2 Protein Sequence |
>Caspase-3
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG
MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS
HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD
DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN
RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH
|
| Enzyme 2 Number of Residues |
277 |
| Enzyme 2 Molecular Weight |
31607.6 |
| Enzyme 2 Theoretical pI |
6.51 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- cysteine-type endopeptidase activity
- cysteine-type peptidase activity
- endopeptidase activity
- hydrolase activity
- peptidase activity
- peptidase activity, acting on L-amino acid peptides
|
| Process |
- apoptosis
- cell death
- cellular process
- macromolecule metabolic process
- metabolic process
- programmed cell death
- protein metabolic process
- proteolysis
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 2 General Function |
Involved in cysteine-type endopeptidase activity |
| Enzyme 2 Specific Function |
Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp! with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
16516817  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P42574  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CASP3_HUMAN  |
| Enzyme 2 PDB ID |
1CP3  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>834 bp
ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC
ATACATGGAAGCGAATCAATGGACTCTGGAATGTCCTGGGACACCGGTTATAAAATGGAT
TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA
ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC
TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG
CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC
CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA
AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT
CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT
GACATGGCGTGTCATAAAATACCAGTGGATGCCGACTTCTTGTATGCATACTCCACAGCA
CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT
GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC
CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA
CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA
|
| Enzyme 2 GenBank Gene ID |
AJ413269  |
| Enzyme 2 GeneCard ID |
CASP3  |
| Enzyme 2 GenAtlas ID |
CASP3  |
| Enzyme 2 HGNC ID |
HGNC:1504  |
| Enzyme 2 Chromosome Location |
4 |
| Enzyme 2 Locus |
4q34 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Fernandes-Alnemri T, Litwack G, Alnemri ES: CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J Biol Chem. 1994 Dec 9;269(49):30761-4. [PubMed
]
- Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM: Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 1995 Jun 2;81(5):801-9. [PubMed
]
- Pelletier M, Cartron PF, Delaval F, Meflah K, Vallette FM, Oliver L: Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit. Biochem Biophys Res Commun. 2004 Mar 26;316(1):93-9. [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
]
- Nicholson DW, Ali A, Thornberry NA, Vaillancourt JP, Ding CK, Gallant M, Gareau Y, Griffin PR, Labelle M, Lazebnik YA, et al.: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 1995 Jul 6;376(6535):37-43. [PubMed
]
- Fernandes-Alnemri T, Armstrong RC, Krebs J, Srinivasula SM, Wang L, Bullrich F, Fritz LC, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES: In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc Natl Acad Sci U S A. 1996 Jul 23;93(15):7464-9. [PubMed
]
- Goldberg YP, Nicholson DW, Rasper DM, Kalchman MA, Koide HB, Graham RK, Bromm M, Kazemi-Esfarjani P, Thornberry NA, Vaillancourt JP, Hayden MR: Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Genet. 1996 Aug;13(4):442-9. [PubMed
]
- Mannick JB, Hausladen A, Liu L, Hess DT, Zeng M, Miao QX, Kane LS, Gow AJ, Stamler JS: Fas-induced caspase denitrosylation. Science. 1999 Apr 23;284(5414):651-4. [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
]
- Rotonda J, Nicholson DW, Fazil KM, Gallant M, Gareau Y, Labelle M, Peterson EP, Rasper DM, Ruel R, Vaillancourt JP, Thornberry NA, Becker JW: The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat Struct Biol. 1996 Jul;3(7):619-25. [PubMed
]
- Mittl PR, Di Marco S, Krebs JF, Bai X, Karanewsky DS, Priestle JP, Tomaselli KJ, Grutter MG: Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone. J Biol Chem. 1997 Mar 7;272(10):6539-47. [PubMed
]
- Lee D, Long SA, Adams JL, Chan G, Vaidya KS, Francis TA, Kikly K, Winkler JD, Sung CM, Debouck C, Richardson S, Levy MA, DeWolf WE Jr, Keller PM, Tomaszek T, Head MS, Ryan MD, Haltiwanger RC, Liang PH, Janson CA, McDevitt PJ, Johanson K, Concha NO, Chan W, Abdel-Meguid SS, Badger AM, Lark MW, Nadeau DP, Suva LJ, Gowen M, Nuttall ME: Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality. J Biol Chem. 2000 May 26;275(21):16007-14. [PubMed
]
|
| Enzyme 2 Metabolite References |
- Schwab M, Reynders V, Ulrich S, Zahn N, Stein J, Schroder O: PPARgamma is a key target of butyrate-induced caspase-3 activation in the colorectal cancer cell line Caco-2. Apoptosis. 2006 Oct;11(10):1801-11. [PubMed
]
|
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
7551 |
| Enzyme 3 Name |
Tumor necrosis factor |
| Enzyme 3 Synonyms |
- Cachectin
- TNF-alpha
- Tumor necrosis factor ligand superfamily member 2
- TNF-a
- Tumor necrosis factor, membrane form
- Tumor necrosis factor, soluble form
|
| Enzyme 3 Gene Name |
TNF |
| Enzyme 3 Protein Sequence |
>Tumor necrosis factor
MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQR
EEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELR
DNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRE
TPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
|
| Enzyme 3 Number of Residues |
233 |
| Enzyme 3 Molecular Weight |
25644.1 |
| Enzyme 3 Theoretical pI |
6.92 |
| Enzyme 3 GO Classification |
| Function |
- binding
- cytokine receptor binding
- protein binding
- receptor binding
- tumor necrosis factor receptor binding
- tumor necrosis factor receptor superfamily binding
|
| Process |
- immune response
- immune system process
|
| Component |
|
|
| Enzyme 3 General Function |
Involved in tumor necrosis factor receptor binding |
| Enzyme 3 Specific Function |
Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
37220  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P01375  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
TNFA_HUMAN  |
| Enzyme 3 PDB ID |
1A8M  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>702 bp
ATGAGCACTGAAAGCATGATCCGGGACGTGGAGCTGGCCGAGGAGGCGCTCCCCAAGAAG
ACAGGGGGGCCCCAGGGCTCCAGGCGGTGCTTGTTCCTCAGCCTCTTCTCCTTCCTGATC
GTGGCAGGCGCCACCACGCTCTTCTGCCTGCTGCACTTTGGAGTGATCGGCCCCCAGAGG
GAAGAGTTCCCCAGGGACCTCTCTCTAATCAGCCCTCTGGCCCAGGCAGTCAGATCATCT
TCTCGAACCCCGAGTGACAAGCCTGTAGCCCATGTTGTAGCAAACCCTCAAGCTGAGGGG
CAGCTCCAGTGGCTGAACCGCCGGGCCAATGCCCTCCTGGCCAATGGCGTGGAGCTGAGA
GATAACCAGCTGGTGGTGCCATCAGAGGGCCTGTACCTCATCTACTCCCAGGTCCTCTTC
AAGGGCCAAGGCTGCCCCTCCACCCATGTGCTCCTCACCCACACCATCAGCCGCATCGCC
GTCTCCTACCAGACCAAGGTCAACCTCCTCTCTGCCATCAAGAGCCCCTGCCAGAGGGAG
ACCCCAGAGGGGGCTGAGGCCAAGCCCTGGTATGAGCCCATCTATCTGGGAGGGGTCTTC
CAGCTGGAGAAGGGTGACCGACTCAGCGCTGAGATCAATCGGCCCGACTATCTCGACTTT
GCCGAGTCTGGGCAGGTCTACTTTGGGATCATTGCCCTGTGA
|
| Enzyme 3 GenBank Gene ID |
X01394  |
| Enzyme 3 GeneCard ID |
TNF  |
| Enzyme 3 GenAtlas ID |
TNF  |
| Enzyme 3 HGNC ID |
HGNC:11892  |
| Enzyme 3 Chromosome Location |
6 |
| Enzyme 3 Locus |
6p21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Nedospasov SA, Shakhov AN, Turetskaya RL, Mett VA, Azizov MM, Georgiev GP, Korobko VG, Dobrynin VN, Filippov SA, Bystrov NS, et al.: Tandem arrangement of genes coding for tumor necrosis factor (TNF-alpha) and lymphotoxin (TNF-beta) in the human genome. Cold Spring Harb Symp Quant Biol. 1986;51 Pt 1:611-24. [PubMed
]
- Pennica D, Nedwin GE, Hayflick JS, Seeburg PH, Derynck R, Palladino MA, Kohr WJ, Aggarwal BB, Goeddel DV: Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin. Nature. 1984 Dec 20-1985 Jan 2;312(5996):724-9. [PubMed
]
- Shirai T, Yamaguchi H, Ito H, Todd CW, Wallace RB: Cloning and expression in Escherichia coli of the gene for human tumour necrosis factor. Nature. 1985 Feb 28-Mar 6;313(6005):803-6. [PubMed
]
- Nedwin GE, Naylor SL, Sakaguchi AY, Smith D, Jarrett-Nedwin J, Pennica D, Goeddel DV, Gray PW: Human lymphotoxin and tumor necrosis factor genes: structure, homology and chromosomal localization. Nucleic Acids Res. 1985 Sep 11;13(17):6361-73. [PubMed
]
- Wang AM, Creasey AA, Ladner MB, Lin LS, Strickler J, Van Arsdell JN, Yamamoto R, Mark DF: Molecular cloning of the complementary DNA for human tumor necrosis factor. Science. 1985 Apr 12;228(4696):149-54. [PubMed
]
- Marmenout A, Fransen L, Tavernier J, Van der Heyden J, Tizard R, Kawashima E, Shaw A, Johnson MJ, Semon D, Muller R, et al.: Molecular cloning and expression of human tumor necrosis factor and comparison with mouse tumor necrosis factor. Eur J Biochem. 1985 Nov 4;152(3):515-22. [PubMed
]
- Iris FJ, Bougueleret L, Prieur S, Caterina D, Primas G, Perrot V, Jurka J, Rodriguez-Tome P, Claverie JM, Dausset J, et al.: Dense Alu clustering and a potential new member of the NF kappa B family within a 90 kilobase HLA class III segment. Nat Genet. 1993 Feb;3(2):137-45. [PubMed
]
- Neville MJ, Campbell RD: A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC. J Immunol. 1999 Apr 15;162(8):4745-54. [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
]
- 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
]
- Takakura-Yamamoto R, Yamamoto S, Fukuda S, Kurimoto M: O-glycosylated species of natural human tumor-necrosis factor-alpha. Eur J Biochem. 1996 Jan 15;235(1-2):431-7. [PubMed
]
- Pocsik E, Duda E, Wallach D: Phosphorylation of the 26 kDa TNF precursor in monocytic cells and in transfected HeLa cells. J Inflamm. 1995;45(3):152-60. [PubMed
]
- Watts AD, Hunt NH, Wanigasekara Y, Bloomfield G, Wallach D, Roufogalis BD, Chaudhri G: A casein kinase I motif present in the cytoplasmic domain of members of the tumour necrosis factor ligand family is implicated in 'reverse signalling'. EMBO J. 1999 Apr 15;18(8):2119-26. [PubMed
]
- Van Ostade X, Tavernier J, Prange T, Fiers W: Localization of the active site of human tumour necrosis factor (hTNF) by mutational analysis. EMBO J. 1991 Apr;10(4):827-36. [PubMed
]
- Stevenson FT, Bursten SL, Locksley RM, Lovett DH: Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues. J Exp Med. 1992 Oct 1;176(4):1053-62. [PubMed
]
- Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, Carter HL, Chen WJ, Clay WC, Didsbury JR, Hassler D, Hoffman CR, Kost TA, Lambert MH, Leesnitzer MA, McCauley P, McGeehan G, Mitchell J, Moyer M, Pahel G, Rocque W, Overton LK, Schoenen F, Seaton T, Su JL, Becherer JD, et al.: Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature. 1997 Feb 20;385(6618):733-6. [PubMed
]
- Jones EY, Stuart DI, Walker NP: Structure of tumour necrosis factor. Nature. 1989 Mar 16;338(6212):225-8. [PubMed
]
- Jones EY, Stuart DI, Walker NP: The structure of tumour necrosis factor--implications for biological function. J Cell Sci Suppl. 1990;13:11-8. [PubMed
]
- Eck MJ, Sprang SR: The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding. J Biol Chem. 1989 Oct 15;264(29):17595-605. [PubMed
]
- Reed C, Fu ZQ, Wu J, Xue YN, Harrison RW, Chen MJ, Weber IT: Crystal structure of TNF-alpha mutant R31D with greater affinity for receptor R1 compared with R2. Protein Eng. 1997 Oct;10(10):1101-7. [PubMed
]
- Cha SS, Kim JS, Cho HS, Shin NK, Jeong W, Shin HC, Kim YJ, Hahn JH, Oh BH: High resolution crystal structure of a human tumor necrosis factor-alpha mutant with low systemic toxicity. J Biol Chem. 1998 Jan 23;273(4):2153-60. [PubMed
]
- Balding J, Kane D, Livingstone W, Mynett-Johnson L, Bresnihan B, Smith O, FitzGerald O: Cytokine gene polymorphisms: association with psoriatic arthritis susceptibility and severity. Arthritis Rheum. 2003 May;48(5):1408-13. [PubMed
]
- Kim YJ, Lee HS, Yoon JH, Kim CY, Park MH, Kim LH, Park BL, Shin HD: Association of TNF-alpha promoter polymorphisms with the clearance of hepatitis B virus infection. Hum Mol Genet. 2003 Oct 1;12(19):2541-6. Epub 2003 Aug 5. [PubMed
]
|
| Enzyme 3 Metabolite References |
- Fukae J, Amasaki Y, Yamashita Y, Bohgaki T, Yasuda S, Jodo S, Atsumi T, Koike T: Butyrate suppresses tumor necrosis factor alpha production by regulating specific messenger RNA degradation mediated through a cis-acting AU-rich element. Arthritis Rheum. 2005 Sep;52(9):2697-707. [PubMed
]
|
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
7657 |
| Enzyme 4 Name |
Peroxisome proliferator-activated receptor gamma |
| Enzyme 4 Synonyms |
- PPAR-gamma
- Nuclear receptor subfamily 1 group C member 3
|
| Enzyme 4 Gene Name |
PPARG |
| Enzyme 4 Protein Sequence |
>Peroxisome proliferator-activated receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC
RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR
ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE
QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS
LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII
LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL
LQVIKKTETDMSLHPLLQEIYKDLY
|
| Enzyme 4 Number of Residues |
505 |
| Enzyme 4 Molecular Weight |
57619.6 |
| Enzyme 4 Theoretical pI |
5.77 |
| Enzyme 4 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 4 General Function |
Involved in DNA binding |
| Enzyme 4 Specific Function |
Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P37231  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PPARG_HUMAN  |
| Enzyme 4 PDB ID |
1I7I  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1518 bp
ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA
CTGTCTGCAAACATATCACAAGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCC
ACCAACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTT
GATATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGAC
ATTCCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAA
GAGTACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACT
CAGCTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGT
GTCTGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAG
GGTTTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGT
CGGATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCA
GTGGGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAG
CTGTTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGG
GCCCTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAG
GCGAGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATG
AATTCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAG
CAGAGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCT
GTGCAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAAC
GACCAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCC
TTGATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTT
CTAAAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTG
AAGTTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATT
CTCAGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAAC
CTGCTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTT
GCCAAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTA
CTGCAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATC
TACAAGGACTTGTACTAG
|
| Enzyme 4 GenBank Gene ID |
U79012  |
| Enzyme 4 GeneCard ID |
PPARG  |
| Enzyme 4 GenAtlas ID |
PPARG  |
| Enzyme 4 HGNC ID |
HGNC:9236  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3p25 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Mukherjee R, Jow L, Croston GE, Paterniti JR Jr: Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2 versus PPARgamma1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem. 1997 Mar 21;272(12):8071-6. [PubMed
]
- Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz M, Moller DE, Berger J: Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2. Biochem Biophys Res Commun. 1996 Jul 16;224(2):431-7. [PubMed
]
- Yanase T, Yashiro T, Takitani K, Kato S, Taniguchi S, Takayanagi R, Nawata H: Differential expression of PPAR gamma1 and gamma2 isoforms in human adipose tissue. Biochem Biophys Res Commun. 1997 Apr 17;233(2):320-4. [PubMed
]
- Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD: Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping. Gene Expr. 1995;4(4-5):281-99. [PubMed
]
- Okazawa H, Mori H, Tamori Y, Araki S, Niki T, Masugi J, Kawanishi M, Kubota T, Shinoda H, Kasuga M: No coding mutations are detected in the peroxisome proliferator-activated receptor-gamma gene in Japanese patients with lipoatrophic diabetes. Diabetes. 1997 Nov;46(11):1904-6. [PubMed
]
- Lambe KG, Tugwood JD: A human peroxisome-proliferator-activated receptor-gamma is activated by inducers of adipogenesis, including thiazolidinedione drugs. Eur J Biochem. 1996 Jul 1;239(1):1-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Caira F, Antonson P, Pelto-Huikko M, Treuter E, Gustafsson JA: Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J Biol Chem. 2000 Feb 25;275(8):5308-17. [PubMed
]
- Zhou XP, Smith WM, Gimm O, Mueller E, Gao X, Sarraf P, Prior TW, Plass C, von Deimling A, Black PM, Yates AJ, Eng C: Over-representation of PPARgamma sequence variants in sporadic cases of glioblastoma multiforme: preliminary evidence for common low penetrance modifiers for brain tumour risk in the general population. J Med Genet. 2000 Jun;37(6):410-4. [PubMed
]
- Shao W, Halachmi S, Brown M: ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol Cell Biol. 2002 May;22(10):3358-72. [PubMed
]
- Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ: ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor. Biochem Biophys Res Commun. 2004 Apr 23;317(1):54-9. [PubMed
]
- Drori S, Girnun GD, Tou L, Szwaya JD, Mueller E, Xia K, Shivdasani RA, Spiegelman BM: Hic-5 regulates an epithelial program mediated by PPARgamma. Genes Dev. 2005 Feb 1;19(3):362-75. [PubMed
]
- Uppenberg J, Svensson C, Jaki M, Bertilsson G, Jendeberg L, Berkenstam A: Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma. J Biol Chem. 1998 Nov 20;273(47):31108-12. [PubMed
]
- Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998 Sep 10;395(6698):137-43. [PubMed
]
- Gampe RT Jr, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE: Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55. [PubMed
]
- Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed
]
- Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure. 2001 Aug;9(8):699-706. [PubMed
]
- Ebdrup S, Pettersson I, Rasmussen HB, Deussen HJ, Frost Jensen A, Mortensen SB, Fleckner J, Pridal L, Nygaard L, Sauerberg P: Synthesis and biological and structural characterization of the dual-acting peroxisome proliferator-activated receptor alpha/gamma agonist ragaglitazar. J Med Chem. 2003 Apr 10;46(8):1306-17. [PubMed
]
- Ostberg T, Svensson S, Selen G, Uppenberg J, Thor M, Sundbom M, Sydow-Backman M, Gustavsson AL, Jendeberg L: A new class of peroxisome proliferator-activated receptor agonists with a novel binding epitope shows antidiabetic effects. J Biol Chem. 2004 Sep 24;279(39):41124-30. Epub 2004 Jul 15. [PubMed
]
- Haffner CD, Lenhard JM, Miller AB, McDougald DL, Dwornik K, Ittoop OR, Gampe RT Jr, Xu HE, Blanchard S, Montana VG, Consler TG, Bledsoe RK, Ayscue A, Croom D: Structure-based design of potent retinoid X receptor alpha agonists. J Med Chem. 2004 Apr 8;47(8):2010-29. [PubMed
]
- Shi GQ, Dropinski JF, McKeever BM, Xu S, Becker JW, Berger JP, MacNaul KL, Elbrecht A, Zhou G, Doebber TW, Wang P, Chao YS, Forrest M, Heck JV, Moller DE, Jones AB: Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic and lipid modulating activity. J Med Chem. 2005 Jun 30;48(13):4457-68. [PubMed
]
- Li Y, Choi M, Suino K, Kovach A, Daugherty J, Kliewer SA, Xu HE: Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner. Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9505-10. Epub 2005 Jun 23. [PubMed
]
- Hopkins CR, O'neil SV, Laufersweiler MC, Wang Y, Pokross M, Mekel M, Evdokimov A, Walter R, Kontoyianni M, Petrey ME, Sabatakos G, Roesgen JT, Richardson E, Demuth TP Jr: Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent PPAR-gamma binding agents with potential application to the treatment of osteoporosis. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5659-63. Epub 2006 Aug 21. [PubMed
]
- Mahindroo N, Wang CC, Liao CC, Huang CF, Lu IL, Lien TW, Peng YH, Huang WJ, Lin YT, Hsu MC, Lin CH, Tsai CH, Hsu JT, Chen X, Lyu PC, Chao YS, Wu SY, Hsieh HP: Indol-1-yl acetic acids as peroxisome proliferator-activated receptor agonists: design, synthesis, structural biology, and molecular docking studies. J Med Chem. 2006 Feb 9;49(3):1212-6. [PubMed
]
- Lu IL, Huang CF, Peng YH, Lin YT, Hsieh HP, Chen CT, Lien TW, Lee HJ, Mahindroo N, Prakash E, Yueh A, Chen HY, Goparaju CM, Chen X, Liao CC, Chao YS, Hsu JT, Wu SY: Structure-based drug design of a novel family of PPARgamma partial agonists: virtual screening, X-ray crystallography, and in vitro/in vivo biological activities. J Med Chem. 2006 May 4;49(9):2703-12. [PubMed
]
- Yen CJ, Beamer BA, Negri C, Silver K, Brown KA, Yarnall DP, Burns DK, Roth J, Shuldiner AR: Molecular scanning of the human peroxisome proliferator activated receptor gamma (hPPAR gamma) gene in diabetic Caucasians: identification of a Pro12Ala PPAR gamma 2 missense mutation. Biochem Biophys Res Commun. 1997 Dec 18;241(2):270-4. [PubMed
]
- Ristow M, Muller-Wieland D, Pfeiffer A, Krone W, Kahn CR: Obesity associated with a mutation in a genetic regulator of adipocyte differentiation. N Engl J Med. 1998 Oct 1;339(14):953-9. [PubMed
]
- Deeb SS, Fajas L, Nemoto M, Pihlajamaki J, Mykkanen L, Kuusisto J, Laakso M, Fujimoto W, Auwerx J: A Pro12Ala substitution in PPARgamma2 associated with decreased receptor activity, lower body mass index and improved insulin sensitivity. Nat Genet. 1998 Nov;20(3):284-7. [PubMed
]
- Hamann A, Munzberg H, Buttron P, Busing B, Hinney A, Mayer H, Siegfried W, Hebebrand J, Greten H: Missense variants in the human peroxisome proliferator-activated receptor-gamma2 gene in lean and obese subjects. Eur J Endocrinol. 1999 Jul;141(1):90-2. [PubMed
]
- Valve R, Sivenius K, Miettinen R, Pihlajamaki J, Rissanen A, Deeb SS, Auwerx J, Uusitupa M, Laakso M: Two polymorphisms in the peroxisome proliferator-activated receptor-gamma gene are associated with severe overweight among obese women. J Clin Endocrinol Metab. 1999 Oct;84(10):3708-12. [PubMed
]
- Sarraf P, Mueller E, Smith WM, Wright HM, Kum JB, Aaltonen LA, de la Chapelle A, Spiegelman BM, Eng C: Loss-of-function mutations in PPAR gamma associated with human colon cancer. Mol Cell. 1999 Jun;3(6):799-804. [PubMed
]
- Barroso I, Gurnell M, Crowley VE, Agostini M, Schwabe JW, Soos MA, Maslen GL, Williams TD, Lewis H, Schafer AJ, Chatterjee VK, O'Rahilly S: Dominant negative mutations in human PPARgamma associated with severe insulin resistance, diabetes mellitus and hypertension. Nature. 1999 Dec 23-30;402(6764):880-3. [PubMed
]
- Hegele RA, Cao H, Frankowski C, Mathews ST, Leff T: PPARG F388L, a transactivation-deficient mutant, in familial partial lipodystrophy. Diabetes. 2002 Dec;51(12):3586-90. [PubMed
]
- Agarwal AK, Garg A: A novel heterozygous mutation in peroxisome proliferator-activated receptor-gamma gene in a patient with familial partial lipodystrophy. J Clin Endocrinol Metab. 2002 Jan;87(1):408-11. [PubMed
]
- Masud S, Ye S: Effect of the peroxisome proliferator activated receptor-gamma gene Pro12Ala variant on body mass index: a meta-analysis. J Med Genet. 2003 Oct;40(10):773-80. [PubMed
]
- Temelkova-Kurktschiev T, Hanefeld M, Chinetti G, Zawadzki C, Haulon S, Kubaszek A, Koehler C, Leonhardt W, Staels B, Laakso M: Ala12Ala genotype of the peroxisome proliferator-activated receptor gamma2 protects against atherosclerosis. J Clin Endocrinol Metab. 2004 Sep;89(9):4238-42. [PubMed
]
- Kim KS, Choi SM, Shin SU, Yang HS, Yoon Y: Effects of peroxisome proliferator-activated receptor-gamma 2 Pro12Ala polymorphism on body fat distribution in female Korean subjects. Metabolism. 2004 Dec;53(12):1538-43. [PubMed
]
|
| Enzyme 4 Metabolite References |
- Schwab M, Reynders V, Ulrich S, Zahn N, Stein J, Schroder O: PPARgamma is a key target of butyrate-induced caspase-3 activation in the colorectal cancer cell line Caco-2. Apoptosis. 2006 Oct;11(10):1801-11. [PubMed
]
|
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7680 |
| Enzyme 5 Name |
Histone deacetylase 4 |
| Enzyme 5 Synonyms |
- HD4
|
| Enzyme 5 Gene Name |
HDAC4 |
| Enzyme 5 Protein Sequence |
>Histone deacetylase 4
MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLP
VAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLA
MKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVL
NKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFP
LRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGP
SSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPA
TGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLL
EQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHL
VIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPY
LDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQ
RIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDT
LMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT
LLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVE
LVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWD
VHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDP
PMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQL
MGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKV
MEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEE
EPPL
|
| Enzyme 5 Number of Residues |
1084 |
| Enzyme 5 Molecular Weight |
119038.9 |
| Enzyme 5 Theoretical pI |
6.96 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- histone deacetylase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
|
| Component |
- chromatin remodeling complex
- histone deacetylase complex
- macromolecular complex
- protein complex
|
|
| Enzyme 5 General Function |
Involved in histone deacetylase activity |
| Enzyme 5 Specific Function |
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
153085395  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P56524  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
HDAC4_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3255 bp
ATGAGCTCCCAAAGCCATCCAGATGGACTTTCTGGCCGAGACCAGCCAGTGGAGCTGCTG
AATCCTGCCCGCGTGAACCACATGCCCAGCACGGTGGATGTGGCCACGGCGCTGCCTCTG
CAAGTGGCCCCCTCGGCAGTGCCCATGGACCTGCGCCTGGACCACCAGTTCTCACTGCCT
GTGGCAGAGCCGGCCCTGCGGGAGCAGCAGCTGCAGCAGGAGCTCCTGGCGCTCAAGCAG
AAGCAGCAGATCCAGAGGCAGATCCTCATCGCTGAGTTCCAGAGGCAGCACGAGCAGCTC
TCCCGGCAGCACGAGGCGCAGCTCCACGAGCACATCAAGCAACAACAGGAGATGCTGGCC
ATGAAGCACCAGCAGGAGCTGCTGGAACACCAGCGGAAGCTGGAGAGGCACCGCCAGGAG
CAGGAGCTGGAGAAGCAGCACCGGGAGCAGAAGCTGCAGCAGCTCAAGAACAAGGAGAAG
GGCAAAGAGAGTGCCGTGGCCAGCACAGAAGTGAAGATGAAGTTACAAGAATTTGTCCTC
AATAAAAAGAAGGCGCTGGCCCACCGGAATCTGAACCACTGCATTTCCAGCGACCCTCGC
TACTGGTACGGGAAAACGCAGCACAGTTCCCTTGACCAGAGTTCTCCACCCCAGAGCGGA
GTGTCGACCTCCTATAACCACCCGGTCCTGGGAATGTACGACGCCAAAGATGACTTCCCT
CTTAGGAAAACAGCTTCTGAACCGAATCTGAAATTACGGTCCAGGCTAAAGCAGAAAGTG
GCCGAAAGACGGAGCAGCCCCCTGTTACGCAGGAAAGACGGGCCAGTGGTCACTGCTCTA
AAAAAGCGTCCGTTGGATGTCACAGACTCCGCGTGCAGCAGCGCCCCAGGCTCCGGACCC
AGCTCACCCAACAACAGCTCCGGGAGCGTCAGCGCGGAGAACGGTATCGCGCCCGCCGTC
CCCAGCATCCCGGCGGAGACGAGTTTGGCGCACAGACTTGTGGCACGAGAAGGCTCGGCC
GCTCCACTTCCCCTCTACACATCGCCATCCTTGCCCAACATCACGCTGGGCCTGCCTGCC
ACCGGCCCCTCTGCGGGCACGGCGGGCCAGCAGGACGCCGAGAGACTCACCCTTCCCGCC
CTCCAGCAGAGGCTCTCCCTTTTCCCCGGCACCCACCTCACTCCCTACCTGAGCACCTCG
CCCTTGGAGCGGGACGGAGGGGCAGCGCACAGCCCTCTTCTGCAGCACATGGTCTTACTG
GAGCAGCCGCCGGCACAAGCACCCCTCGTCACAGGCCTGGGAGCACTGCCCCTCCACGCA
CAGTCCTTGGTTGGTGCAGACCGGGTGTCCCCCTCCATCCACAAGCTGCGGCAGCACCGC
CCACTGGGGCGGACCCAGTCGGCCCCGCTGCCCCAGAACGCCCAGGCTCTGCAGCACCTG
GTCATCCAGCAGCAGCATCAGCAGTTTCTGGAGAAACACAAGCAGCAGTTCCAGCAGCAG
CAACTGCAGATGAACAAGATCATCCCCAAGCCAAGCGAGCCAGCCCGGCAGCCGGAGAGC
CACCCGGAGGAGACGGAGGAGGAGCTCCGTGAGCACCAGGCTCTGCTGGACGAGCCCTAC
CTGGACCGGCTGCCGGGGCAGAAGGAGGCGCACGCACAGGCCGGCGTGCAGGTGAAGCAG
GAGCCCATTGAGAGCGATGAGGAAGAGGCAGAGCCCCCACGGGAGGTGGAGCCGGGCCAG
CGCCAGCCCAGTGAGCAGGAGCTGCTCTTCAGACAGCAAGCCCTCCTGCTGGAGCAGCAG
CGGATCCACCAGCTGAGGAACTACCAGGCGTCCATGGAGGCCGCCGGCATCCCCGTGTCC
TTCGGCGGCCACAGGCCTCTGTCCCGGGCGCAGTCCTCACCCGCGTCTGCCACCTTCCCC
GTGTCTGTGCAGGAGCCCCCCACCAAGCCGAGGTTCACGACAGGCCTCGTGTATGACACG
CTGATGCTGAAGCACCAGTGCACCTGCGGGAGTAGCAGCAGCCACCCCGAGCACGCCGGG
AGGATCCAGAGCATCTGGTCCCGCCTGCAGGAGACGGGCCTCCGGGGCAAATGCGAGTGC
ATCCGCGGACGCAAGGCCACCCTGGAGGAGCTACAGACGGTGCACTCGGAAGCCCACACC
CTCCTGTATGGCACGAACCCCCTCAACCGGCAGAAACTGGACAGTAAGAAACTTCTAGGC
TCGCTCGCCTCCGTGTTCGTCCGGCTCCCTTGCGGTGGTGTTGGGGTGGACAGTGACACC
ATATGGAACGAGGTGCACTCGGCGGGGGCAGCCCGCCTGGCTGTGGGCTGCGTGGTAGAG
CTGGTCTTCAAGGTGGCCACAGGGGAGCTGAAGAATGGCTTTGCTGTGGTCCGCCCCCCT
GGACACCATGCGGAGGAGAGCACGCCCATGGGCTTTTGCTACTTCAACTCCGTGGCCGTG
GCAGCCAAGCTTCTGCAGCAGAGGTTGAGCGTGAGCAAGATCCTCATCGTGGACTGGGAC
GTGCACCATGGAAACGGGACCCAGCAGGCTTTCTACAGCGACCCCAGCGTCCTGTACATG
TCCCTCCACCGCTACGACGATGGGAACTTCTTCCCAGGCAGCGGGGCTCCTGATGAGGTG
GGCACAGGGCCCGGCGTGGGTTTCAACGTCAACATGGCTTTCACCGGCGGCCTGGACCCC
CCCATGGGAGACGCTGAGTACTTGGCGGCCTTCAGAACGGTGGTCATGCCGATCGCCAGC
GAGTTTGCCCCGGATGTGGTGCTGGTGTCATCAGGCTTCGATGCCGTGGAGGGCCACCCC
ACCCCTCTTGGGGGCTACAACCTCTCCGCCAGATGCTTCGGGTACCTGACGAAGCAGCTG
ATGGGCCTGGCTGGCGGCCGGATTGTCCTGGCCCTCGAGGGAGGCCACGACCTGACCGCC
ATTTGCGACGCCTCGGAAGCATGTGTTTCTGCCTTGCTGGGAAACGAGCTTGATCCTCTC
CCAGAAAAGGTTTTACAGCAAAGACCCAATGCAAACGCTGTCCGTTCCATGGAGAAAGTC
ATGGAGATCCACAGCAAGTACTGGCGCTGCCTGCAGCGCACAACCTCCACAGCGGGGCGT
TCTCTGATCGAGGCTCAGACTTGCGAGAACGAAGAAGCCGAGACGGTCACCGCCATGGCC
TCGCTGTCCGTGGGCGTGAAGCCCGCCGAAAAGAGACCAGATGAGGAGCCCATGGAAGAG
GAGCCGCCCCTGTAG
|
| Enzyme 5 GenBank Gene ID |
NM_006037.3  |
| Enzyme 5 GeneCard ID |
HDAC4  |
| Enzyme 5 GenAtlas ID |
HDAC4  |
| Enzyme 5 HGNC ID |
HGNC:14063  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2q37.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Grozinger CM, Hassig CA, Schreiber SL: Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4868-73. [PubMed
]
- Ohara O, Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Nomura N: Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins. DNA Res. 1997 Feb 28;4(1):53-9. [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
]
- Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T: HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 1999 Sep 15;18(18):5099-107. [PubMed
]
- Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ: HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor. Mol Cell Biol. 1999 Nov;19(11):7816-27. [PubMed
]
- Wang AH, Kruhlak MJ, Wu J, Bertos NR, Vezmar M, Posner BI, Bazett-Jones DP, Yang XJ: Regulation of histone deacetylase 4 by binding of 14-3-3 proteins. Mol Cell Biol. 2000 Sep;20(18):6904-12. [PubMed
]
- Zhao X, Ito A, Kane CD, Liao TS, Bolger TA, Lemrow SM, Means AR, Yao TP: The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking. J Biol Chem. 2001 Sep 14;276(37):35042-8. Epub 2001 Jul 24. [PubMed
]
- McKinsey TA, Zhang CL, Olson EN: Identification of a signal-responsive nuclear export sequence in class II histone deacetylases. Mol Cell Biol. 2001 Sep;21(18):6312-21. [PubMed
]
- Franco PJ, Farooqui M, Seto E, Wei LN: The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases. Mol Endocrinol. 2001 Aug;15(8):1318-28. [PubMed
]
- Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 2002 Jun 3;21(11):2682-91. [PubMed
]
- Barrett A, Santangelo S, Tan K, Catchpole S, Roberts K, Spencer-Dene B, Hall D, Scibetta A, Burchell J, Verdin E, Freemont P, Taylor-Papadimitriou J: Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases. Int J Cancer. 2007 Jul 15;121(2):265-75. [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
]
- 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 5 Metabolite References |
- Ishihara K, Takahashi A, Kaneko M, Sugeno H, Hirasawa N, Hong J, Zee O, Ohuchi K: Differentiation of eosinophilic leukemia EoL-1 cells into eosinophils induced by histone deacetylase inhibitors. Life Sci. 2007 Mar 6;80(13):1213-20. Epub 2007 Jan 11. [PubMed
]
|
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
7741 |
| Enzyme 6 Name |
Histone deacetylase 9 |
| Enzyme 6 Synonyms |
- HD9
- Histone deacetylase 7B
- HD7
- HD7b
- Histone deacetylase-related protein
- MEF2-interacting transcription repressor MITR
|
| Enzyme 6 Gene Name |
HDAC9 |
| Enzyme 6 Protein Sequence |
>Histone deacetylase 9
MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQ
KQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRR
EQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAA
HHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSS
PLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHA
EQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQ
GVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHP
QSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQ
QIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLG
QVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGL
EKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGR
IQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGD
DSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPP
GHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYI
SLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAK
EFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTA
ICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS
|
| Enzyme 6 Number of Residues |
1011 |
| Enzyme 6 Molecular Weight |
111296.3 |
| Enzyme 6 Theoretical pI |
6.88 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- histone deacetylase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
|
| Component |
- chromatin remodeling complex
- histone deacetylase complex
- macromolecular complex
- protein complex
|
|
| Enzyme 6 General Function |
Involved in histone deacetylase activity |
| Enzyme 6 Specific Function |
Isoform 3 lacks active site residues and therefore is catalytically inactive. Represses MEF2-dependent transcription by recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and to be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
15590680  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9UKV0  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
HDAC9_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>3036 bp
ATGCACAGTATGATCAGCTCAGTGGATGTGAAGTCAGAAGTTCCTGTGGGCCTGGAGCCC
ATCTCACCTTTAGACCTAAGGACAGACCTCAGGATGATGATGCCCGTGGTGGACCCTGTT
GTCCGTGAGAAGCAATTGCAGCAGGAATTACTTCTTATCCAGCAGCAGCAACAAATCCAG
AAGCAGCTTCTGATAGCAGAGTTTCAGAAACAGCATGAGAACTTGACACGGCAGCACCAG
GCTCAGCTTCAGGAGCATATCAAGGAACTTCTAGCCATAAAACAGCAACAAGAACTCCTA
GAAAAGGAGCAGAAACTGGAGCAGCAGAGGCAAGAACAGGAAGTAGAGAGGCATCGCAGA
GAACAGCAGCTTCCTCCTCTCAGAGGCAAAGATAGAGGACGAGAAAGGGCAGTGGCAAGT
ACAGAAGTAAAGCAGAAGCTTCAAGAGTTCCTACTGAGTAAATCAGCAACGAAAGACACT
CCAACTAATGGAAAAAATCATTCCGTGAGCCGCCATCCCAAGCTCTGGTACACGGCTGCC
CACCACACATCATTGGATCAAAGCTCTCCACCCCTTAGTGGAACATCTCCATCCTACAAG
TACACATTACCAGGAGCACAAGATGCAAAGGATGATTTCCCCCTTCGAAAAACTGCCTCT
GAGCCCAACTTGAAGGTGCGGTCCAGGTTAAAACAGAAAGTGGCAGAGAGGAGAAGCAGC
CCCTTACTCAGGCGGAAGGATGGAAATGTTGTCACTTCATTCAAGAAGCGAATGTTTGAG
GTGACAGAATCCTCAGTCAGTAGCAGTTCTCCAGGCTCTGGTCCCAGTTCACCAAACAAT
GGGCCAACTGGAAGTGTTACTGAAAATGAGACTTCGGTTTTGCCCCCTACCCCTCATGCC
GAGCAAATGGTTTCACAGCAACGCATTCTAATTCATGAAGATTCCATGAACCTGCTAAGT
CTTTATACCTCTCCTTCTTTGCCCAACATTACCTTGGGGCTTCCCGCAGTGCCATCCCAG
CTCAATGCTTCGAATTCACTCAAAGAAAAGCAGAAGTGTGAGACGCAGACGCTTAGGCAA
GGTGTTCCTCTGCCTGGGCAGTATGGAGGCAGCATCCCGGCATCTTCCAGCCACCCTCAT
GTTACTTTAGAGGGAAAGCCACCCAACAGCAGCCACCAGGCTCTCCTGCAGCATTTATTA
TTGAAAGAACAAATGCGACAGCAAAAGCTTCTTGTAGCTGGTGGAGTTCCCTTACATCCT
CAGTCTCCCTTGGCAACAAAAGAGAGAATTTCACCTGGCATTAGAGGTACCCACAAATTG
CCCCGTCACAGACCCCTGAACCGAACCCAGTCTGCACCTTTGCCTCAGAGCACGTTGGCT
CAGCTGGTCATTCAACAGCAACACCAGCAATTCTTGGAGAAGCAGAAGCAATACCAGCAG
CAGATCCACATGAACAAACTGCTTTCGAAATCTATTGAACAACTGAAGCAACCAGGCAGT
CACCTTGAGGAAGCAGAGGAAGAGCTTCAGGGGGACCAGGCGATGCAGGAAGACAGAGCG
CCCTCTAGTGGCAACAGCACTAGGAGCGACAGCAGTGCTTGTGTGGATGACACACTGGGA
CAAGTTGGGGCTGTGAAGGTCAAGGAGGAACCAGTGGACAGTGATGAAGATGCTCAGATC
CAGGAAATGGAATCTGGGGAGCAGGCTGCTTTTATGCAACAGCCTTTCCTGGAACCCACG
CACACACGTGCGCTCTCTGTGCGCCAAGCTCCGCTGGCTGCGGTTGGCATGGATGGATTA
GAGAAACACCGTCTCGTCTCCAGGACTCACTCTTCCCCTGCTGCCTCTGTTTTACCTCAC
CCAGCAATGGACCGCCCCCTCCAGCCTGGCTCTGCAACTGGAATTGCCTATGACCCCTTG
ATGCTGAAACACCAGTGCGTTTGTGGCAATTCCACCACCCACCCTGAGCATGCTGGACGA
ATACAGAGTATCTGGTCACGACTGCAAGAAACTGGGCTGCTAAATAAATGTGAGCGAATT
CAAGGTCGAAAAGCCAGCCTGGAGGAAATACAGCTTGTTCATTCTGAACATCACTCACTG
TTGTATGGCACCAACCCCCTGGACGGACAGAAGCTGGACCCCAGGATACTCCTAGGTGAT
GACTCTCAAAAGTTTTTTTCCTCATTACCTTGTGGTGGACTTGGGGTGGACAGTGACACC
ATTTGGAATGAGCTACACTCGTCCGGTGCTGCACGCATGGCTGTTGGCTGTGTCATCGAG
CTGGCTTCCAAAGTGGCCTCAGGAGAGCTGAAGAATGGGTTTGCTGTTGTGAGGCCCCCT
GGCCATCACGCTGAAGAATCCACAGCCATGGGGTTCTGCTTTTTTAATTCAGTTGCAATT
ACCGCCAAATACTTGAGAGACCAACTAAATATAAGCAAGATATTGATTGTAGATCTGGAT
GTTCACCATGGAAACGGTACCCAGCAGGCCTTTTATGCTGACCCCAGCATCCTGTACATT
TCACTCCATCGCTATGATGAAGGGAACTTTTTCCCTGGCAGTGGAGCCCCAAATGAGGTT
GGAACAGGCCTTGGAGAAGGGTACAATATAAATATTGCCTGGACAGGTGGCCTTGATCCT
CCCATGGGAGATGTTGAGTACCTTGAAGCATTCAGGACCATCGTGAAGCCTGTGGCCAAA
GAGTTTGATCCAGACATGGTCTTAGTATCTGCTGGATTTGATGCATTGGAAGGCCACACC
CCTCCTCTAGGAGGGTACAAAGTGACGGCAAAATGTTTTGGTCATTTGACGAAGCAATTG
ATGACATTGGCTGATGGACGTGTGGTGTTGGCTCTAGAAGGAGGACATGATCTCACAGCC
ATCTGTGATGCATCAGAAGCCTGTGTAAATGCCCTTCTAGGAAATGAGCTGGAGCCACTT
GCAGAAGATATTCTCCACCAAAGCCCGAATATGAATGCTGTTATTTCTTTACAGAAGATC
ATTGAAATTCAAAGTATGTCTTTAAAGTTCTCTTAA
|
| Enzyme 6 GenBank Gene ID |
AY032737  |
| Enzyme 6 GeneCard ID |
HDAC9  |
| Enzyme 6 GenAtlas ID |
HDAC9  |
| Enzyme 6 HGNC ID |
HGNC:14065  |
| Enzyme 6 Chromosome Location |
7 |
| Enzyme 6 Locus |
7p21.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Zhou X, Marks PA, Rifkind RA, Richon VM: Cloning and characterization of a histone deacetylase, HDAC9. Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10572-7. Epub 2001 Sep 4. [PubMed
]
- David D, Cardoso J, Marques B, Marques R, Silva ED, Santos H, Boavida MG: Molecular characterization of a familial translocation implicates disruption of HDAC9 and possible position effect on TGFbeta2 in the pathogenesis of Peters' anomaly. Genomics. 2003 May;81(5):489-503. [PubMed
]
- Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A: The histone deacetylase 9 gene encodes multiple protein isoforms. J Biol Chem. 2003 May 2;278(18):16059-72. Epub 2003 Feb 17. [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
]
- 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
]
- Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ: HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor. Mol Cell Biol. 1999 Nov;19(11):7816-27. [PubMed
]
- Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ: MEF-2 function is modified by a novel co-repressor, MITR. EMBO J. 1999 Sep 15;18(18):5085-98. [PubMed
]
- Zhou X, Richon VM, Rifkind RA, Marks PA: Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5. Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1056-61. [PubMed
]
- Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T: HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J. 1999 Sep 15;18(18):5099-107. [PubMed
]
- Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 2002 Jun 3;21(11):2682-91. [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
]
- Morrison BE, Majdzadeh N, Zhang X, Lyles A, Bassel-Duby R, Olson EN, D'Mello SR: Neuroprotection by histone deacetylase-related protein. Mol Cell Biol. 2006 May;26(9):3550-64. [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
]
- Harrison BC, Huynh K, Lundgaard GL, Helmke SM, Perryman MB, McKinsey TA: Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases. FEBS Lett. 2010 Mar 19;584(6):1103-10. Epub 2010 Feb 24. [PubMed
]
|
| Enzyme 6 Metabolite References |
- Ishihara K, Takahashi A, Kaneko M, Sugeno H, Hirasawa N, Hong J, Zee O, Ohuchi K: Differentiation of eosinophilic leukemia EoL-1 cells into eosinophils induced by histone deacetylase inhibitors. Life Sci. 2007 Mar 6;80(13):1213-20. Epub 2007 Jan 11. [PubMed
]
|
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
7816 |
| Enzyme 7 Name |
Histone deacetylase 1 |
| Enzyme 7 Synonyms |
- HD1
|
| Enzyme 7 Gene Name |
HDAC1 |
| Enzyme 7 Protein Sequence |
>Histone deacetylase 1
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKAN
AEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAS
AVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHG
DGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAI
FKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGG
GGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLE
KIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEF
SDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVK
LA
|
| Enzyme 7 Number of Residues |
482 |
| Enzyme 7 Molecular Weight |
55102.6 |
| Enzyme 7 Theoretical pI |
5.16 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- histone deacetylase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- histone deacetylation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein amino acid deacetylation
- protein modification process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in histone deacetylase activity |
| Enzyme 7 Specific Function |
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q13547  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
HDAC1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1449 bp
ATGGCGCAGACGCAGGGCACCCGGAGGAAAGTCTGTTACTACTACGACGGGGATGTTGGA
AATTACTATTATGGACAAGGCCACCCAATGAAGCCTCACCGAATCCGCATGACTCATAAT
TTGCTGCTCAACTATGGTCTCTACCGAAAAATGGAAATCTATCGCCCTCACAAAGCCAAT
GCTGAGGAGATGACCAAGTACCACAGCGATGACTACATTAAATTCTTGCGCTCCATCCGT
CCAGATAACATGTCGGAGTACAGCAAGCAGATGCAGAGATTCAACGTTGGTGAGGACTGT
CCAGTATTCGATGGCCTGTTTGAGTTCTGTCAGTTGTCTACTGGTGGTTCTGTGGCAAGT
GCTGTGAAACTTAATAAGCAGCAGACGGACATCGCTGTGAATTGGGCTGGGGGCCTGCAC
CATGCAAAGAAGTCCGAGGCATCTGGCTTCTGTTACGTCAATGATATCGTCTTGGCCATC
CTGGAACTGCTAAAGTATCACCAGAGGGTGCTGTACATTGACATTGATATTCACCATGGT
GACGGCGTGGAAGAGGCCTTCTACACCACGGACCGGGTCATGACTGTGTCCTTTCATAAG
TATGGAGAGTACTTCCCAGGAACTGGGGACCTACGGGATATCGGGGCTGGCAAAGGCAAG
TATTATGCTGTTAACTACCCGCTCCGAGACGGGATTGATGACGAGTCCTATGAGGCCATT
TTCAAGCCGGTCATGTCCAAAGTAATGGAGATGTTCCAGCCTAGTGCGGTGGTCTTACAG
TGTGGCTCAGACTCCCTATCTGGGGATCGGTTAGGTTGCTTCAATCTAACTATCAAAGGA
CACGCCAAGTGTGTGGAATTTGTCAAGAGCTTTAACCTGCCTATGCTGATGCTGGGAGGC
GGTGGTTACACCATTCGTAACGTTGCCCGGTGCTGGACATATGAGACAGCTGTGGCCCTG
GATACGGAGATCCCTAATGAGCTTCCATACAATGACTACTTTGAATACTTTGGACCAGAT
TTCAAGCTCCACATCAGTCCTTCCAATATGACTAACCAGAACACGAATGAGTACCTGGAG
AAGATCAAACAGCGACTGTTTGAGAACCTTAGAATGCTGCCGCACGCACCTGGGGTCCAA
ATGCAGGCGATTCCTGAGGACGCCATCCCTGAGGAGAGTGGCGATGAGGACGAAGACGAC
CCTGACAAGCGCATCTCGATCTGCTCCTCTGACAAACGAATTGCCTGTGAGGAAGAGTTC
TCCGATTCTGAAGAGGAGGGAGAGGGGGGCCGCAAGAACTCTTCCAACTTCAAAAAAGCC
AAGAGAGTCAAAACAGAGGATGAAAAAGAGAAAGACCCAGAGGAGAAGAAAGAAGTCACC
GAAGAGGAGAAAACCAAGGAGGAGAAGCCAGAAGCCAAAGGGGTCAAGGAGGAGGTCAAG
TTGGCCTGA
|
| Enzyme 7 GenBank Gene ID |
U50079  |
| Enzyme 7 GeneCard ID |
HDAC1  |
| Enzyme 7 GenAtlas ID |
HDAC1  |
| Enzyme 7 HGNC ID |
HGNC:4852  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p34 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Taunton J, Hassig CA, Schreiber SL: A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science. 1996 Apr 19;272(5260):408-11. [PubMed
]
- Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y: Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae. Cytogenet Cell Genet. 1996;73(1-2):130-3. [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
]
- Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ: MEF-2 function is modified by a novel co-repressor, MITR. EMBO J. 1999 Sep 15;18(18):5085-98. [PubMed
]
- Huynh KD, Fischle W, Verdin E, Bardwell VJ: BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev. 2000 Jul 15;14(14):1810-23. [PubMed
]
- Cai RL, Yan-Neale Y, Cueto MA, Xu H, Cohen D: HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins. J Biol Chem. 2000 Sep 8;275(36):27909-16. [PubMed
]
- Wei LN, Hu X, Chandra D, Seto E, Farooqui M: Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J Biol Chem. 2000 Dec 29;275(52):40782-7. [PubMed
]
- Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol. 2000 Mar;20(5):1784-96. [PubMed
]
- Zhou X, Richon VM, Rifkind RA, Marks PA: Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5. Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1056-61. [PubMed
]
- Pflum MK, Tong JK, Lane WS, Schreiber SL: Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J Biol Chem. 2001 Dec 14;276(50):47733-41. Epub 2001 Oct 15. [PubMed
]
- Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM: Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. Genes Dev. 2001 May 1;15(9):1140-51. [PubMed
]
- Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH: Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. J Biol Chem. 2001 Mar 2;276(9):6817-24. Epub 2000 Dec 1. [PubMed
]
- Melhuish TA, Gallo CM, Wotton D: TGIF2 interacts with histone deacetylase 1 and represses transcription. J Biol Chem. 2001 Aug 24;276(34):32109-14. Epub 2001 Jun 26. [PubMed
]
- Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW: ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol Cell Biol. 2001 Oct;21(19):6470-83. [PubMed
]
- Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 2002 Jun 3;21(11):2682-91. [PubMed
]
- David G, Neptune MA, DePinho RA: SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J Biol Chem. 2002 Jun 28;277(26):23658-63. Epub 2002 Apr 17. [PubMed
]
- Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W: Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 2003 Apr 1;17(7):896-911. [PubMed
]
- Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R: A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes. J Biol Chem. 2003 Feb 28;278(9):7234-9. Epub 2002 Dec 18. [PubMed
]
- Ammanamanchi S, Freeman JW, Brattain MG: Acetylated sp3 is a transcriptional activator. J Biol Chem. 2003 Sep 12;278(37):35775-80. Epub 2003 Jun 30. [PubMed
]
- Ding Z, Gillespie LL, Paterno GD: Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain. Mol Cell Biol. 2003 Jan;23(1):250-8. [PubMed
]
- Fleischer TC, Yun UJ, Ayer DE: Identification and characterization of three new components of the mSin3A corepressor complex. Mol Cell Biol. 2003 May;23(10):3456-67. [PubMed
]
- Colombo R, Draetta GF, Chiocca S: Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein. Oncogene. 2003 May 1;22(17):2541-7. [PubMed
]
- Nikolaev AY, Papanikolaou NA, Li M, Qin J, Gu W: Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex. Biochem Biophys Res Commun. 2004 Oct 29;323(4):1216-22. [PubMed
]
- Zhao Q, Cumming H, Cerruti L, Cunningham JM, Jane SM: Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1. J Biol Chem. 2004 Oct 1;279(40):41477-86. Epub 2004 Jul 24. [PubMed
]
- Cheng J, Wang D, Wang Z, Yeh ET: SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol Cell Biol. 2004 Jul;24(13):6021-8. [PubMed
]
- Unoki M, Nishidate T, Nakamura Y: ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. Oncogene. 2004 Oct 7;23(46):7601-10. [PubMed
]
- Ahringer J: NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 2000 Aug;16(8):351-6. [PubMed
]
- Gray SG, Iglesias AH, Lizcano F, Villanueva R, Camelo S, Jingu H, Teh BT, Koibuchi N, Chin WW, Kokkotou E, Dangond F: Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem. 2005 Aug 5;280(31):28507-18. Epub 2005 May 31. [PubMed
]
- Rampalli S, Pavithra L, Bhatt A, Kundu TK, Chattopadhyay S: Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex. Mol Cell Biol. 2005 Oct;25(19):8415-29. [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
]
- Hung JJ, Wang YT, Chang WC: Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol Cell Biol. 2006 Mar;26(5):1770-85. [PubMed
]
- Viiri KM, Korkeamaki H, Kukkonen MK, Nieminen LK, Lindfors K, Peterson P, Maki M, Kainulainen H, Lohi O: SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus. Nucleic Acids Res. 2006 Jul 4;34(11):3288-98. Print 2006. [PubMed
]
- Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed
]
- Barrett A, Santangelo S, Tan K, Catchpole S, Roberts K, Spencer-Dene B, Hall D, Scibetta A, Burchell J, Verdin E, Freemont P, Taylor-Papadimitriou J: Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases. Int J Cancer. 2007 Jul 15;121(2):265-75. [PubMed
]
- Valls E, Blanco-Garcia N, Aquizu N, Piedra D, Estaras C, de la Cruz X, Martinez-Balbas MA: Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation. Nucleic Acids Res. 2007;35(6):1958-68. Epub 2007 Mar 6. [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
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Pham LV, Zhou HJ, Lin-Lee YC, Tamayo AT, Yoshimura LC, Fu L, Darnay BG, Ford RJ: Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification. J Biol Chem. 2008 Feb 22;283(8):5081-9. 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
]
- Qiu Z, Ghosh A: A calcium-dependent switch in a CREST-BRG1 complex regulates activity-dependent gene expression. Neuron. 2008 Dec 10;60(5):775-87. [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
]
- Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed
]
- 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
]
- Takahata M, Inoue Y, Tsuda H, Imoto I, Koinuma D, Hayashi M, Ichikura T, Yamori T, Nagasaki K, Yoshida M, Matsuoka M, Morishita K, Yuki K, Hanyu A, Miyazawa K, Inazawa J, Miyazono K, Imamura T: SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells. J Biol Chem. 2009 Jan 30;284(5):3334-44. Epub 2008 Dec 1. [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
]
- Kajiwara Y, Akram A, Katsel P, Haroutunian V, Schmeidler J, Beecham G, Haines JL, Pericak-Vance MA, Buxbaum JD: FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4. PLoS One. 2009;4(4):e5071. Epub 2009 Apr 3. [PubMed
]
- Oh YM, Kwon YE, Kim JM, Bae SJ, Lee BK, Yoo SJ, Chung CH, Deshaies RJ, Seol JH: Chfr is linked to tumour metastasis through the downregulation of HDAC1. Nat Cell Biol. 2009 Mar;11(3):295-302. Epub 2009 Feb 1. [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 7 Metabolite References |
- Ishihara K, Takahashi A, Kaneko M, Sugeno H, Hirasawa N, Hong J, Zee O, Ohuchi K: Differentiation of eosinophilic leukemia EoL-1 cells into eosinophils induced by histone deacetylase inhibitors. Life Sci. 2007 Mar 6;80(13):1213-20. Epub 2007 Jan 11. [PubMed
]
|
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
9777 |
| Enzyme 8 Name |
Acyl-coenzyme A synthetase ACSM1, mitochondrial |
| Enzyme 8 Synonyms |
- Acyl-CoA synthetase medium-chain family member 1
- Butyrate--CoA ligase 1
- Butyryl-coenzyme A synthetase 1
- Lipoate-activating enzyme
- Middle-chain acyl-CoA synthetase 1
|
| Enzyme 8 Gene Name |
ACSM1 |
| Enzyme 8 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM1, mitochondrial
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM
|
| Enzyme 8 Number of Residues |
577 |
| Enzyme 8 Molecular Weight |
65272.7 |
| Enzyme 8 Theoretical pI |
8.40 |
| Enzyme 8 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in catalytic activity |
| Enzyme 8 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). Functions as GTP-dependent lipoate- activating enzyme that generates the substrate for lipoyltransferase |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
15487302  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q08AH1  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ACSM1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1734 bp
ATGCAGTGGCTAATGAGGTTCCGGACCCTCTGGGGCATCCACAAATCCTTCCACAACATC
CACCCTGCCCCTTCACAGCTGCGCTGCCGGTCTTTATCAGAATTTGGAGCCCCAAGATGG
AATGACTATGAAGTACCGGAGGAATTTAACTTTGCAAGTTATGTACTGGACTACTGGGCT
CAAAAGGAGAAGGAGGGCAAGAGAGGTCCAAATCCAGCTTTTTGGTGGGTGAATGGCCAA
GGGGATGAAGTAAAGTGGAGCTTCAGAGAGATGGGAGACCTAACCCGCCGTGTAGCCAAC
GTCTTCACACAGACCTGTGGCCTACAACAGGGAGACCATCTGGCCTTGATGCTGCCTCGA
GTTCCTGAGTGGTGGCTGGTGGCTGTGGGCTGCATGCGAACAGGGATCATCTTCATTCCT
GCGACCATCCTGTTGAAGGCCAAAGACATTCTCTATCGACTACAGTTGTCTAAAGCCAAG
GGCATTGTGACCATAGATGCCCTTGCCTCAGAGGTGGACTCCATAGCTTCTCAGTGCCCC
TCTCTGAAAACCAAGCTCCTGGTGTCTGATCACAGCCGTGAAGGGTGGCTGGACTTCCGA
TCGCTGGTTAAATCAGCATCCCCAGAACACACCTGTGTTAAGTCAAAGACCTTGGACCCA
ATGGTCATCTTCTTCACCAGTGGGACCACAGGCTTCCCCAAGATGGCAAAACACTCCCAT
GGGTTGGCCTTACAACCCTCCTTCCCAGGAAGTAGGAAATTACGGAGCCTGAAGACATCT
GATGTCTCCTGGTGCCTGTCGGACTCAGGATGGATTGTGGCTACCATTTGGACCCTGGTA
GAACCATGGACAGCGGGTTGTACAGTCTTTATCCACCATCTGCCACAGTTTGACACCAAG
GTCATCATACAGACATTGTTGAAATACCCCATTAACCACTTTTGGGGGGTATCATCTATA
TATCGAATGATTCTGCAGCAGGATTTCACCAGCATCAGGTTCCCTGCCCTGGAGCACTGC
TATACTGGCGGGGAGGTCGTGTTGCCCAAGGATCAGGAGGAGTGGAAAAGACGGACGGGC
CTTCTGCTCTACGAGAACTATGGGCAGTCGGAAACGGGACTAATTTGTGCCACCTACTGG
GGAATGAAGATCAAGCCGGGTTTCATGGGGAAGGCCACTCCACCCTATGACGTCCAGGTC
ATTGATGACAAGGGCAGCATCCTGCCACCTAACACAGAAGGAAACATTGGCATCAGAATC
AAACCTGTCAGGCCTGTGAGCCTCTTCATGTGCTATGAGGGTGACCCAGAGAAGACAGCT
AAAGTGGAATGTGGGGACTTCTACAACACTGGGGACAGAGGAAAGATGGATGAAGAGGGC
TACATTTGTTTCCTGGGGAGGAGTGATGACATCATTAATGCCTCTGGGTATCGCATCGGG
CCTGCAGAGGTTGAAAGCGCTTTGGTGGAGCACCCAGCGGTGGCGGAGTCAGCCGTGGTG
GGCAGCCCAGACCCGATTCGAGGGGAGGTGGTGAAGGCCTTTATTGTCCTGACCCCACAG
TTCCTGTCCCATGACAAGGATCAGCTGACCAAGGAACTGCAGCAGCATGTCAAGTCAGTG
ACAGCCCCATACAAGTACCCAAGGAACGTGGAGTTTGTCTCAGAGCTGCCAAAAACCATC
ACTGGCAAGATTGAACGGAAGGAACTTCGGAAAAAGGAGACTGGTCAGATGTAA
|
| Enzyme 8 GenBank Gene ID |
AB059429  |
| Enzyme 8 GeneCard ID |
ACSM1  |
| Enzyme 8 GenAtlas ID |
ACSM1  |
| Enzyme 8 HGNC ID |
HGNC:18049  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
16p12.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Fujino T, Takei YA, Sone H, Ioka RX, Kamataki A, Magoori K, Takahashi S, Sakai J, Yamamoto TT: Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol Chem. 2001 Sep 21;276(38):35961-6. Epub 2001 Jul 24. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
14011 |
| Enzyme 9 Name |
Acyl-coenzyme A synthetase ACSM6, mitochondrial |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
ACSM6 |
| Enzyme 9 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM6, mitochondrial
MLGRFQPFSLVRSFRLGFEACCYPNQKCATQTIRPPDSRCLVQAVSQNFNFAKDVLDQWS
QLEKDGLRGPYPALWKVSAKGEEDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPP
TPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCP
TLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQ
YGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPE
TVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRIT
KLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR
IKLNQPASLYCPHMVSWEEYASARGHMLYLTGDRGIMDEDGYFWWSGRVDDVANALGQRL
|
| Enzyme 9 Number of Residues |
480 |
| Enzyme 9 Molecular Weight |
53584.5 |
| Enzyme 9 Theoretical pI |
8.50 |
| Enzyme 9 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in catalytic activity |
| Enzyme 9 Specific Function |
ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
195947378  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q6P461  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
ACSM6_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1443 bp
ATGCTAGGCCGATTTCAACCCTTCTCCTTGGTCCGGAGTTTCAGACTGGGATTTGAAGCC
TGCTGCTATCCAAACCAAAAATGTGCTACTCAGACCATCAGACCCCCTGACTCCAGGTGC
CTAGTCCAAGCAGTTTCTCAGAACTTTAATTTTGCAAAGGATGTGTTGGATCAGTGGTCC
CAGCTGGAAAAGGACGGACTCAGAGGGCCTTACCCCGCCCTCTGGAAGGTTAGTGCCAAA
GGAGAAGAGGACAAATGGAGCTTTGAAAGGATGACTCAACTCTCCAAGAAGGCCGCCAGC
ATCCTCTCAGACACCTGTGCCCTTAGCCATGGAGACCGGCTGATGATAATCTTGCCCCCA
ACACCTGAAGCCTACTGGATCTGCCTGGCCTGTGTGCGCTTGGGAATCACCTTTGTGCCT
GGGAGCCCCCAGCTGACTGCCAAGAAAATTCGCTATCAATTACGCATGTCTAAGGCCCAG
TGCATTGTGGCTAATGAAGCTATGGCCCCAGTTGTAAACTCTGCCGTGTCCGACTGCCCC
ACCTTGAAAACCAAGCTCCTGGTGTCAGATAAGAGCTATGATGGGTGGTTGGATTTCAAG
AAGTTGATTCAAGTTGCCCCTCCAAAGCAGACCTACATGAGGACCAAAAGCCAAGATCCA
ATGGCCATATTCTTCACCAAGGGTACAACAGGAGCTCCCAAAATGGTCGAGTATTCCCAG
TATGGTTTGGGAATGGGATTCAGCCAGGCTTCCAGACGGTGGATGGATCTCCAGCCAACA
GATGTCTTGTGGAGTCTGGGTGATGCCTTTGGTGGATCTTTATCCCTGAGCGCTGTCTTG
GGAACTTGGTTCCAAGGAGCCTGTGTGTTTCTGTGTCACATGCCAACCTTCTGCCCTGAG
ACTGTTCTAAATGTCCTGTCCAGATTTCCCATCACCACTCTATCTGCAAATCCAGAGATG
TACCAGGAACTGCTTCAGCACAAGTGTTTCACCAGCTACAGATTCAAGAGTCTGAAGCAG
TGTGTGGCTGCAGGAGGACCCATCAGCCCTGGGGTGATTGAGGACTGGAAACGCATCACT
AAGTTGGACATCTATGAAGGCTATGGGCAGACGGAAACTGGTCTACTCTGTGCCACTTCC
AAAACAATAAAATTGAAGCCAAGCTCTCTGGGGAAGCCATTGCCACCTTATATTGTCCAG
ATTGTGGATGAAAACTCAAATCTCCTGCCTCCAGGGGAAGAAGGAAATATTGCAATCCGC
ATAAAACTAAACCAACCTGCTTCTCTGTACTGTCCACACATGGTGAGCTGGGAGGAATAT
GCTTCAGCAAGAGGCCACATGCTTTACCTCACAGGTGACAGAGGGATCATGGATGAAGAC
GGCTACTTCTGGTGGTCTGGTAGAGTTGATGATGTTGCCAATGCATTGGGTCAGAGATTG
TGA
|
| Enzyme 9 GenBank Gene ID |
NM_207321.2  |
| Enzyme 9 GeneCard ID |
ACSM6  |
| Enzyme 9 GenAtlas ID |
ACSM6  |
| Enzyme 9 HGNC ID |
HGNC:31665  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
14420 |
| Enzyme 10 Name |
Acyl-coenzyme A synthetase ACSM2A, mitochondrial |
| Enzyme 10 Synonyms |
- Acyl-CoA synthetase medium-chain family member 2A
- Butyrate--CoA ligase 2A
- Butyryl-coenzyme A synthetase 2A
- Middle-chain acyl-CoA synthetase 2A
|
| Enzyme 10 Gene Name |
ACSM2A |
| Enzyme 10 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM2A, mitochondrial
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN
ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ
|
| Enzyme 10 Number of Residues |
577 |
| Enzyme 10 Molecular Weight |
64222.7 |
| Enzyme 10 Theoretical pI |
8.20 |
| Enzyme 10 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in catalytic activity |
| Enzyme 10 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
58082049  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q08AH3  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ACS2A_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1734 bp
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTG
CCGGCCAAGTTTAACTTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGGTGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCTTTATGCCTGGAACCATCCAGATG
AAATCCACTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGTGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGTGCTCACTTATGGAACCTTGGGCATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCCATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCGTCACTGTAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATCC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGATCATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGACAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGGAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGGTCCTGGCCTCGCAGTTCCTGTCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
GCCAAGCTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
|
| Enzyme 10 GenBank Gene ID |
NM_001010845.2  |
| Enzyme 10 GeneCard ID |
ACSM2A  |
| Enzyme 10 GenAtlas ID |
ACSM2A  |
| Enzyme 10 HGNC ID |
HGNC:32017  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
16p12.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed
]
- Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW: Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A. J Mol Biol. 2009 May 22;388(5):997-1008. Epub 2009 Apr 1. [PubMed
]
- Iwai N, Mannami T, Tomoike H, Ono K, Iwanaga Y: An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors. Hypertension. 2003 May;41(5):1041-6. Epub 2003 Mar 24. [PubMed
]
- Lindner I, Rubin D, Helwig U, Nitz I, Hampe J, Schreiber S, Schrezenmeir J, Doring F: The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population. Mol Nutr Food Res. 2006 Mar;50(3):270-4. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
14421 |
| Enzyme 11 Name |
Acyl-coenzyme A synthetase ACSM2B, mitochondrial |
| Enzyme 11 Synonyms |
- Acyl-CoA synthetase medium-chain family member 2B
- Butyrate--CoA ligase 2B
- Butyryl-coenzyme A synthetase 2B
- Middle-chain acyl-CoA synthetase 2B
- Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A
|
| Enzyme 11 Gene Name |
ACSM2B |
| Enzyme 11 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM2B, mitochondrial
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKARAQ
|
| Enzyme 11 Number of Residues |
577 |
| Enzyme 11 Molecular Weight |
64270.8 |
| Enzyme 11 Theoretical pI |
8.38 |
| Enzyme 11 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in catalytic activity |
| Enzyme 11 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
51555772  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q68CK6  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
ACS2B_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1734 bp
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTT
CCGGCCAAGTTTAACTTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGATGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCTTTATGCCTGGAACCATCCAGATG
AAATCCACTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGCGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGGGCTCACTTTTGGAATCTTGGACATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCTATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCCTCGCTGGAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATTC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGGTTATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGAAAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGAAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGATCCTGGCCTCGCAGTTCCTATCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
ACCAAACTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
|
| Enzyme 11 GenBank Gene ID |
AB073604  |
| Enzyme 11 GeneCard ID |
ACSM2B  |
| Enzyme 11 GenAtlas ID |
ACSM2B  |
| Enzyme 11 HGNC ID |
HGNC:30931  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
16p12.3 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Vessey DA, Lau E, Kelley M, Warren RS: Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria. J Biochem Mol Toxicol. 2003;17(1):1-6. [PubMed
]
- Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Vessey DA, Kelley M, Warren RS: Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids. Biochim Biophys Acta. 1999 Aug 5;1428(2-3):455-62. [PubMed
]
- Boomgaarden I, Vock C, Klapper M, Doring F: Comparative analyses of disease risk genes belonging to the acyl-CoA synthetase medium-chain (ACSM) family in human liver and cell lines. Biochem Genet. 2009 Oct;47(9-10):739-48. Epub 2009 Jul 26. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
14422 |
| Enzyme 12 Name |
Acyl-coenzyme A synthetase ACSM3, mitochondrial |
| Enzyme 12 Synonyms |
- Acyl-CoA synthetase medium-chain family member 3
- Butyrate--CoA ligase 3
- Butyryl-coenzyme A synthetase 3
- Middle-chain acyl-CoA synthetase 3
- Protein SA homolog
|
| Enzyme 12 Gene Name |
ACSM3 |
| Enzyme 12 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM3, mitochondrial
MLARVTRKMLRHAKCFQRLAIFGSVRALHKDNRTATPQNFSNYESMKQDFKLGIPEYFNF
AKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRG
DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPA
VDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG
YPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFT
HHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDV
TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPG
QEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDV
ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIK
EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKTI
|
| Enzyme 12 Number of Residues |
586 |
| Enzyme 12 Molecular Weight |
66152.2 |
| Enzyme 12 Theoretical pI |
9.45 |
| Enzyme 12 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in catalytic activity |
| Enzyme 12 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
42544132  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q53FZ2  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
ACSM3_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1761 bp
ATGCTAGCTCGTGTCACCAGGAAGATGCTACGTCATGCCAAGTGTTTTCAGCGCCTAGCA
ATTTTTGGTTCTGTGAGGGCACTGCATAAAGATAATAGAACAGCAACCCCTCAGAATTTC
TCCAACTATGAATCCATGAAACAGGACTTCAAACTGGGGATTCCAGAGTATTTCAACTTT
GCTAAAGATGTCCTGGACCAATGGACTGATAAGGAAAAGGCTGGAAAGAAACCTTCAAAT
CCAGCCTTCTGGTGGATCAACAGAAATGGAGAAGAGATGCGATGGAGTTTTGAGGAACTG
GGATCTCTGTCCAGAAAATTTGCCAATATACTTTCAGAAGCCTGTTCCCTACAAAGAGGA
GATCGGGTAATTCTGATTCTGCCCAGGGTCCCAGAGTGGTGGCTTGCAAATGTGGCCTGT
CTGCGAACAGGGACAGTTTTAATTCCAGGAACCACTCAGCTGACCCAGAAAGACATTCTC
TACAGACTACAATCTTCAAAAGCAAACTGCATTATCACCAATGATGTTTTAGCCCCAGCA
GTAGACGCTGTTGCATCCAAATGTGAAAATCTGCACTCCAAGCTGATTGTATCAGAGAAC
TCCAGAGAGGGGTGGGGGAACCTCAAGGAGTTGATGAAACATGCCAGTGACAGCCACACC
TGTGTGAAGACAAAACACAATGAGATCATGGCCATATTCTTTACCAGTGGAACAAGTGGA
TATCCGAAAATGACTGCACACACCCACAGCAGTTTTGGTTTAGGATTATCTGTAAATGGA
AGGTTCTGGCTAGATTTGACACCCTCAGATGTGATGTGGAATACCTCAGATACGGGCTGG
GCAAAGTCTGCATGGAGTAGTGTTTTTTCTCCGTGGATCCAGGGAGCATGTGTATTCACA
CACCATTTACCCCGTTTTGAGCCGACTTCTATCTTGCAAACACTCTCCAAGTACCCCATC
ACAGTCTTCTGTTCAGCACCAACTGTATACCGAATGCTTGTACAGAATGATATAACCAGC
TATAAGTTTAAAAGCTTAAAGCACTGTGTGAGTGCTGGGGAACCAATTACCCCTGACGTG
ACTGAAAAATGGAGAAACAAGACGGGCCTGGATATCTACGAAGGATATGGACAGACTGAA
ACGGTGCTAATCTGTGGAAATTTTAAGGGAATGAAAATTAAACCTGGCTCAATGGGAAAA
CCTTCTCCTGCTTTCGATGTTAAGATTGTAGATGTAAATGGCAATGTTCTACCTCCTGGA
CAAGAAGGAGATATTGGCATTCAAGTTCTACCCAACCGACCATTTGGCCTTTTTACTCAT
TACGTAGATAATCCTTCAAAAACAGCTTCAACTCTACGAGGCAATTTCTATATCACTGGG
GACAGAGGATATATGGATAAAGATGGGTATTTCTGGTTTGTTGCAAGAGCAGATGATGTC
ATATTATCCTCTGGCTATCGAATTGGACCATTTGAGGTAGAAAATGCCCTGAATGAACAC
CCTTCAGTTGCAGAGTCAGCTGTTGTCAGCAGCCCAGACCCCATCAGAGGAGAGGTAGTA
AAGGCTTTTGTCGTTCTAAATCCTGATTACAAGTCACATGATCAAGAACAACTAATAAAG
GAGATTCAGGAGCATGTTAAAAAAACTACAGCACCTTACAAATATCCCAGAAAGGTAGAA
TTTATTCAAGAGCTGCCAAAGACTATCAGTGGGAAGACAAAAAGAAATGAACTGAGGAAG
AAAGAATGGAAGACAATTTAA
|
| Enzyme 12 GenBank Gene ID |
NM_005622.3  |
| Enzyme 12 GeneCard ID |
ACSM3  |
| Enzyme 12 GenAtlas ID |
ACSM3  |
| Enzyme 12 HGNC ID |
HGNC:10522  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
16p13.11 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Iwai N, Ohmichi N, Hanai K, Nakamura Y, Kinoshita M: Human SA gene locus as a candidate locus for essential hypertension. Hypertension. 1994 Mar;23(3):375-80. [PubMed
]
- Nabika T, Bonnardeaux A, James M, Julier C, Jeunemaitre X, Corvol P, Lathrop M, Soubrier F: Evaluation of the SA locus in human hypertension. Hypertension. 1995 Jan;25(1):6-13. [PubMed
]
- Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed
]
- Telgmann R, Brand E, Nicaud V, Hagedorn C, Beining K, Schonfelder J, Brink-Spalink V, Schmidt-Petersen K, Matanis T, Vischer P, Nofer JR, Hasenkamp S, Plouin PF, Drouet L, Cambien F, Paul M, Tiret L, Brand-Herrmann SM: SAH gene variants are associated with obesity-related hypertension in Caucasians: the PEGASE Study. J Hypertens. 2007 Mar;25(3):557-64. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
14424 |
| Enzyme 13 Name |
Acyl-coenzyme A synthetase ACSM5, mitochondrial |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
ACSM5 |
| Enzyme 13 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM5, mitochondrial
MRPWLRHLVLQALRNSRAFCGSHGKPAPLPVPQKIVATWEAISLGRQLVPEYFNFAHDVL
DVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMML
VLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIS
AECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMV
EHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV
DAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH
QTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVA
VRIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSY
RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHV
KRVTAPYKYPRKVAFVSELPKTVSGKIQRSKLRSQEWGK
|
| Enzyme 13 Number of Residues |
579 |
| Enzyme 13 Molecular Weight |
64759.6 |
| Enzyme 13 Theoretical pI |
8.52 |
| Enzyme 13 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 13 General Function |
Involved in catalytic activity |
| Enzyme 13 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
38505220  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q6NUN0  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
ACSM5_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1740 bp
ATGAGACCATGGCTGAGACACCTAGTCCTCCAGGCACTGAGGAACTCCAGGGCATTCTGT
GGGTCTCATGGGAAGCCAGCACCTCTACCTGTTCCTCAGAAGATCGTGGCCACCTGGGAA
GCCATCAGCCTGGGAAGGCAGCTGGTGCCTGAGTACTTCAACTTCGCCCATGATGTGCTG
GATGTGTGGAGTCGGCTGGAAGAGGCTGGACACCGCCCCCCAAATCCTGCCTTCTGGTGG
GTCAATGGCACAGGAGCAGAGATCAAGTGGAGCTTTGAGGAGCTGGGGAAGCAGTCCAGG
AAGGCAGCCAATGTGCTGGGGGGTGCATGCGGCCTGCAGCCTGGGGACAGAATGATGCTG
GTACTCCCACGGCTCCCGGAGTGGTGGCTGGTCAGTGTGGCTTGCATGCGGACAGGGACT
GTGATGATTCCGGGTGTGACTCAGCTGACAGAGAAGGACCTCAAGTACCGGCTGCAGGCG
TCCAGGGCCAAGTCCATTATCACCAGTGACTCCCTAGCTCCAAGGGTGGATGCCATCAGT
GCCGAATGCCCCTCCCTCCAGACCAAGCTGCTGGTGTCAGACAGCAGTCGGCCAGGCTGG
TTGAACTTCAGGGAACTCCTCCGGGAGGCTTCTACAGAGCACAACTGCATGAGGACAAAG
AGTCGAGACCCGCTGGCCATCTACTTTACCAGCGGAACCACCGGGGCCCCCAAGATGGTC
GAGCACTCCCAGAGCAGCTACGGACTGGGTTTTGTGGCCAGCGGAAGACGGTGGGTGGCC
TTGACCGAATCTGACATCTTCTGGAACACGACTGACACTGGCTGGGTGAAGGCAGCCTGG
ACTCTCTTCTCTGCCTGGCCTAATGGATCTTGCATTTTTGTGCATGAGCTGCCCCGAGTT
GATGCCAAAGTTATCCTGAATACTCTCTCCAAATTCCCGATAACCACCCTCTGCTGTGTC
CCAACCATCTTTCGGCTGCTTGTGCAGGAGGATCTGACCAGGTACCAGTTTCAGAGCCTG
AGGCACTGTCTGACCGGAGGAGAGGCCCTCAACCCTGACGTGAGGGAGAAGTGGAAACAC
CAGACTGGTGTGGAGCTGTACGAAGGCTATGGCCAGTCTGAAACGGTTGTCATCTGTGCC
AATCCAAAAGGCATGAAAATCAAGTCTGGATCCATGGGGAAGGCGTCCCCACCCTACGAT
GTGCAGATTGTGGATGATGAGGGCAACGTCCTGCCTCCTGGAGAAGAGGGGAATGTTGCC
GTCCGTATCAGACCCACTCGGCCCTTCTGTTTCTTCAATTGCTATTTGGACAATCCTGAG
AAGACAGCTGCATCAGAACAAGGGGACTTTTACATCACAGGGGACCGAGCTCGCATGGAC
AAGGATGGCTACTTTTGGTTCATGGGAAGAAACGACGATGTGATCAATTCTTCAAGCTAC
CGGATCGGGCCTGTTGAAGTGGAAAGTGCCCTGGCAGAGCATCCTGCTGTCCTGGAGTCG
GCTGTGGTCAGCAGCCCAGACCCCATCAGGGGAGAGGTGGTAAAGGCATTTATAGTCCTT
ACTCCAGCCTACTCCTCTCATGACCCAGAGGCACTAACGCGGGAACTCCAGGAGCATGTG
AAAAGGGTGACTGCTCCATACAAATACCCCAGGAAGGTGGCCTTTGTTTCAGAACTGCCA
AAGACGGTTTCTGGAAAGATCCAAAGGAGTAAATTGCGAAGTCAGGAGTGGGGGAAATGA
|
| Enzyme 13 GenBank Gene ID |
NM_017888.2  |
| Enzyme 13 GeneCard ID |
ACSM5  |
| Enzyme 13 GenAtlas ID |
ACSM5  |
| Enzyme 13 HGNC ID |
HGNC:26060  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
16p12.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Iwai N, Mannami T, Tomoike H, Ono K, Iwanaga Y: An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors. Hypertension. 2003 May;41(5):1041-6. Epub 2003 Mar 24. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
14850 |
| Enzyme 14 Name |
Butyryl-CoA:acetate CoA transferase |
| Enzyme 14 Synonyms |
Not Available |
| Enzyme 14 Gene Name |
Not Available |
| Enzyme 14 Protein Sequence |
>Butyryl-CoA:acetate CoA transferase
MDQVAKNLLAARVARDIPNGSYVNLGIGLPTLVANHLPRHREIILHSENGVLGQWSAAEP
GQEDPDLINAGKEPVRLEKGAAFFHHADAFGMMRGGHLDICVLGAFQVSGHGDLANWHTG
DPDAIPAVGGAMDLAIGARRVFVMMDHMTRDGASKLRRQCSYPLTGLACVSRVYTELGTF
AIGPQGVAVIEIIGDMSPQALQSVTDVELDFTTLATAELA
|
| Enzyme 14 Number of Residues |
220 |
| Enzyme 14 Molecular Weight |
23415.5 |
| Enzyme 14 Theoretical pI |
5.48 |
| Enzyme 14 GO Classification |
| Function |
- CoA-transferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in CoA-transferase activity |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
|
| Enzyme 14 Reactions |
- acyl-CoA + acetate = a fatty acid anion + acetyl-CoA [RN:R00393]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
72117301  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q471R1  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
Q471R1_RALEJ  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>663 bp
ATGGAAAGCAACGGAAACCCGCCGGAAGCGGTCCTGCCGGGCGGGCAGGATGCCGCGCCG
GCTACTGAAACCGCGCCGCCTGCGCGCAAGCGGCCGCGGCCGGGCGAGCGCCGCGTGCAG
ATCCTGCAGACGCTGGCAGCGATGCTCGAGCACCCGCGCGGGGAAAAGATCACCACCGCC
GCGCTGGCAGCACGCCTGAGCGTGTCGGAGGCCGCGCTGTACCGCCATTTCGCGAGCAAG
GCGCAGATGTACGAAGGCCTGATCGCCTTCATCGAGCAGACCGTGTTCGGCCTGATCAAC
CAGATCACGACGACCGAGGAGCATGGCCTGCGCCAGGTGCAGGCCATCGTGCGCATGCTG
CTGTCGTTCGCGGAGAAGAACCCCGGCATGACGCGCGTGTTGACCGGCGAGGCGCTCGTC
GGCGAGCACGAGCGCCTGCAGGACCGCATCAACCAGATGGTCGACCGCATCGAGGCCTCG
CTGCGCCAGTGCCTGAAGATCGCCGTGACGCAGGGCGCGTTCCCGGCCGATGCCGATGTC
GCGCTGCGCGCCGCGCTGGTCATGGCGTACGTGCAGGGCCAGTGGCATCGTTATGCCAAG
AGCGGTTTCCGCAAGTCGCCGGGCGAGCGCGTGGACGCGCAGTTGCGCGTGCTGCTCGGC
TAG
|
| Enzyme 14 GenBank Gene ID |
CP000090  |
| Enzyme 14 GeneCard ID |
Not Available |
| Enzyme 14 GenAtlas ID |
Not Available |
| Enzyme 14 HGNC ID |
Not Available |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Reut_A1505 |
| Enzyme 14 SNPs |
Not Available |
| Enzyme 14 General References |
Not Available |
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
14851 |
| Enzyme 15 Name |
Histone deacetylase 2 |
| Enzyme 15 Synonyms |
- HD2
|
| Enzyme 15 Gene Name |
HDAC2 |
| Enzyme 15 Protein Sequence |
>Histone deacetylase 2
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKA
TAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVA
GAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHH
GDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ
IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLG
GGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYM
EKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEE
FSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT
KSEQLSNP
|
| Enzyme 15 Number of Residues |
488 |
| Enzyme 15 Molecular Weight |
55363.9 |
| Enzyme 15 Theoretical pI |
5.75 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- histone deacetylase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- histone deacetylation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein amino acid deacetylation
- protein modification process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in histone deacetylase activity |
| Enzyme 15 Specific Function |
Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
- Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
293336691  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q92769  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
HDAC2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1467 bp
ATGGCGTACAGTCAAGGAGGCGGCAAAAAAAAAGTCTGCTACTACTACGACGGTGATATT
GGAAATTATTATTATGGACAGGGTCATCCCATGAAGCCTCATAGAATCCGCATGACCCAT
AACTTGCTGTTAAATTATGGCTTATACAGAAAAATGGAAATATATAGGCCCCATAAAGCC
ACTGCCGAAGAAATGACAAAATATCACAGTGATGAGTATATCAAATTTCTACGGTCAATA
AGACCAGATAACATGTCTGAGTATAGTAAGCAGATGCAGAGATTTAATGTTGGAGAAGAT
TGTCCAGTGTTTGATGGACTCTTTGAGTTTTGTCAGCTCTCAACTGGCGGTTCAGTTGCT
GGAGCTGTGAAGTTAAACCGACAACAGACTGATATGGCTGTTAATTGGGCTGGAGGATTA
CATCATGCTAAGAAATCAGAAGCATCAGGATTCTGTTACGTTAATGATATTGTGCTTGCC
ATCCTTGAATTACTAAAGTATCATCAGAGAGTCTTATATATTGATATAGATATTCATCAT
GGTGATGGTGTTGAAGAAGCTTTTTATACAACAGATCGTGTAATGACGGTATCATTCCAT
AAATATGGGGAATACTTTCCTGGCACAGGAGACTTGAGGGATATTGGTGCTGGAAAAGGC
AAATACTATGCTGTCAATTTTCCAATGAGAGATGGTATAGATGATGAGTCATATGGGCAG
ATATTTAAGCCTATTATCTCAAAGGTGATGGAGATGTATCAACCTAGTGCTGTGGTATTA
CAGTGTGGTGCAGACTCATTATCTGGTGATAGACTGGGTTGTTTCAATCTAACAGTCAAA
GGTCATGCTAAATGTGTAGAAGTTGTAAAAACTTTTAACTTACCATTACTGATGCTTGGA
GGAGGTGGCTACACAATCCGTAATGTTGCTCGATGTTGGACATATGAGACTGCAGTTGCC
CTTGATTGTGAGATTCCCAATGAGTTGCCATATAATGATTACTTTGAGTATTTTGGACCA
GACTTCAAACTGCATATTAGTCCTTCAAACATGACAAACCAGAACACTCCAGAATATATG
GAAAAGATAAAACAGCGTTTGTTTGAAAATTTGCGCATGTTACCTCATGCACCTGGTGTC
CAGATGCAAGCTATTCCAGAAGATGCTGTTCATGAAGACAGTGGAGATGAAGATGGAGAA
GATCCAGACAAGAGAATTTCTATTCGAGCATCAGACAAGCGGATAGCTTGTGATGAAGAA
TTCTCAGATTCTGAGGATGAAGGAGAAGGAGGTCGAAGAAATGTGGCTGATCATAAGAAA
GGAGCAAAGAAAGCTAGAATTGAAGAAGATAAGAAAGAAACAGAGGACAAAAAAACAGAC
GTTAAGGAAGAAGATAAATCCAAGGACAACAGTGGTGAAAAAACAGATACCAAAGGAACC
AAATCAGAACAGCTCAGCAACCCCTGA
|
| Enzyme 15 GenBank Gene ID |
NM_001527.3  |
| Enzyme 15 GeneCard ID |
HDAC2  |
| Enzyme 15 GenAtlas ID |
HDAC2  |
| Enzyme 15 HGNC ID |
HGNC:4853  |
| Enzyme 15 Chromosome Location |
6 |
| Enzyme 15 Locus |
6q21 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Yang WM, Inouye C, Zeng Y, Bearss D, Seto E: Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12845-50. [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
]
- 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
]
- Schmidt DR, Schreiber SL: Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4. Biochemistry. 1999 Nov 2;38(44):14711-7. [PubMed
]
- Rountree MR, Bachman KE, Baylin SB: DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. Nat Genet. 2000 Jul;25(3):269-77. [PubMed
]
- Ahringer J: NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 2000 Aug;16(8):351-6. [PubMed
]
- Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM: Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. Genes Dev. 2001 May 1;15(9):1140-51. [PubMed
]
- Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW: ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol Cell Biol. 2001 Oct;21(19):6470-83. [PubMed
]
- Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D: Isolation and characterization of a novel class II histone deacetylase, HDAC10. J Biol Chem. 2002 Feb 22;277(8):6656-66. Epub 2001 Dec 5. [PubMed
]
- Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR: The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2. J Biol Chem. 2002 Sep 27;277(39):35783-6. Epub 2002 Aug 9. [PubMed
]
- Hollenbach AD, McPherson CJ, Mientjes EJ, Iyengar R, Grosveld G: Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J Cell Sci. 2002 Aug 15;115(Pt 16):3319-30. [PubMed
]
- Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W: Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 2003 Apr 1;17(7):896-911. [PubMed
]
- Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R: A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes. J Biol Chem. 2003 Feb 28;278(9):7234-9. Epub 2002 Dec 18. [PubMed
]
- Fleischer TC, Yun UJ, Ayer DE: Identification and characterization of three new components of the mSin3A corepressor complex. Mol Cell Biol. 2003 May;23(10):3456-67. [PubMed
]
- Choi YB, Ko JK, Shin J: The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains. J Biol Chem. 2004 Dec 3;279(49):50930-41. Epub 2004 Sep 27. [PubMed
]
- Castet A, Boulahtouf A, Versini G, Bonnet S, Augereau P, Vignon F, Khochbin S, Jalaguier S, Cavailles V: Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition. Nucleic Acids Res. 2004 Apr 1;32(6):1957-66. Print 2004. [PubMed
]
- Gray SG, Iglesias AH, Lizcano F, Villanueva R, Camelo S, Jingu H, Teh BT, Koibuchi N, Chin WW, Kokkotou E, Dangond F: Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem. 2005 Aug 5;280(31):28507-18. Epub 2005 May 31. [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
]
- Viiri KM, Korkeamaki H, Kukkonen MK, Nieminen LK, Lindfors K, Peterson P, Maki M, Kainulainen H, Lohi O: SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus. Nucleic Acids Res. 2006 Jul 4;34(11):3288-98. Print 2006. [PubMed
]
- Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [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
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- 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
]
- Kajiwara Y, Akram A, Katsel P, Haroutunian V, Schmeidler J, Beecham G, Haines JL, Pericak-Vance MA, Buxbaum JD: FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4. PLoS One. 2009;4(4):e5071. Epub 2009 Apr 3. [PubMed
]
- Oh YM, Kwon YE, Kim JM, Bae SJ, Lee BK, Yoo SJ, Chung CH, Deshaies RJ, Seol JH: Chfr is linked to tumour metastasis through the downregulation of HDAC1. Nat Cell Biol. 2009 Mar;11(3):295-302. Epub 2009 Feb 1. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 15 Metabolite References |
- Ishihara K, Takahashi A, Kaneko M, Sugeno H, Hirasawa N, Hong J, Zee O, Ohuchi K: Differentiation of eosinophilic leukemia EoL-1 cells into eosinophils induced by histone deacetylase inhibitors. Life Sci. 2007 Mar 6;80(13):1213-20. Epub 2007 Jan 11. [PubMed
]
|
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
14852 |
| Enzyme 16 Name |
Histone deacetylase 3 |
| Enzyme 16 Synonyms |
- HD3
- RPD3-2
- SMAP45
|
| Enzyme 16 Gene Name |
HDAC3 |
| Enzyme 16 Protein Sequence |
>Histone deacetylase 3
MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCR
FHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNN
KICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEA
FYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVI
NQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTV
RNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQ
TIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDN
DKESDVEI
|
| Enzyme 16 Number of Residues |
428 |
| Enzyme 16 Molecular Weight |
48847.4 |
| Enzyme 16 Theoretical pI |
4.79 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- histone deacetylase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- histone deacetylation
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- post-translational protein modification
- protein amino acid deacetylation
- protein modification process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in histone deacetylase activity |
| Enzyme 16 Specific Function |
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
- Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
2326173  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
O15379  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
HDAC3_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1287 bp
ATGGCCAAGACCGTGGCCTATTTCTACGACCCCGACGTGGGCAACTTCCACTACGGAGCT
GGACACCCTATGAAGCCCCATCGCCTGGCATTGACCCATAGCCTGGTCCTGCATTACGGT
CTCTATAAGAAGATGATCGTCTTCAAGCCATACCAGGCCTCCCAACATGACATGTGCCGC
TTCCACTCCGAGGACTACATTGACTTCCTGCAGAGAGTCAGCCCCACCAATATGCAAGGC
TTCACCAAGAGTCTTAATGCCTTCAACGTAGGCGATGACTGCCCAGTGTTTCCCGGGCTC
TTTGAGTTCTGCTCGCGTTACACAGGCGCATCTCTGCAAGGAGCAACCCAGCTGAACAAC
AAGATCTGTGATATTGCCATTAACTGGGCTGGTGGTCTGCACCATGCCAAGAAGTTTGAG
GCCTCTGGCTTCTGCTATGTCAACGACATTGTGATTGGCATCCTGGAGCTGCTCAAGTAC
CACCCTCGGGTGCTCTACATTGACATTGACATCCACCATGGTGACGGGGTTCAAGAAGCT
TTCTACCTCACTGACCGGGTCATGACGGTGTCCTTCCACAAATACGGAAATTACTTCTTC
CCTGGCACAGGTGACATGTATGAAGTCGGGGCAGAGAGTGGCCGCTACTACTGTCTGAAC
GTGCCCCTGCGGGATGGCATTGATGACCAGAGTTACAAGCACCTTTTCCAGCCGGTTATC
AACCAGGTAGTGGACTTCTACCAACCCACGTGCATTGTGCTCCAGTGTGGAGCTGACTCT
CTGGGCTGTGATCGATTGGGCTGCTTTAACCTCAGCATCCGAGGGCATGGGGAATGCGTT
GAATATGTCAAGAGCTTCAATATCCCTCTACTCGTGCTGGGTGGTGGTGGTTATACTGTC
CGAAATGTTGCCCGCTGCTGGACATATGAGACATCGCTGCTGGTAGAAGAGGCCATTAGT
GAGGAGCTTCCCTATAGTGAATACTTCGAGTACTTTGCCCCAGACTTCACACTTCATCCA
GATGTCAGCACCCGCATCGAGAATCAGAACTCACGCCAGTATCTGGACCAGATCCTCCAG
ACAATCTTTGAAAACCTGAAGATGCTGAACCATGCACCTAGTGTCCAGATTCATGACGTG
CCTGCAGACCTCCTGACCTATGACAGGACTGATGAGGCTGATGCAGAGGAGAGGGGTCCT
GAGGAGAACTATAGCAGGCCAGAGGCACCCAATGAGTTCTATGATGGAGACCATGACAAT
GACAAGGAAAGCGATGTGGAGATTTAA
|
| Enzyme 16 GenBank Gene ID |
U66914  |
| Enzyme 16 GeneCard ID |
HDAC3  |
| Enzyme 16 GenAtlas ID |
HDAC3  |
| Enzyme 16 HGNC ID |
HGNC:4854  |
| Enzyme 16 Chromosome Location |
5 |
| Enzyme 16 Locus |
5q31 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Dangond F, Hafler DA, Tong JK, Randall J, Kojima R, Utku N, Gullans SR: Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells. Biochem Biophys Res Commun. 1998 Jan 26;242(3):648-52. [PubMed
]
- Yang WM, Yao YL, Sun JM, Davie JR, Seto E: Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J Biol Chem. 1997 Oct 31;272(44):28001-7. [PubMed
]
- Emiliani S, Fischle W, Van Lint C, Al-Abed Y, Verdin E: Characterization of a human RPD3 ortholog, HDAC3. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):2795-800. [PubMed
]
- Mahlknecht U, Emiliani S, Najfeld V, Young S, Verdin E: Genomic organization and chromosomal localization of the human histone deacetylase 3 gene. Genomics. 1999 Mar 1;56(2):197-202. [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
]
- Wei LN, Hu X, Chandra D, Seto E, Farooqui M: Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J Biol Chem. 2000 Dec 29;275(52):40782-7. [PubMed
]
- Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol. 2000 Mar;20(5):1784-96. [PubMed
]
- Zhou X, Richon VM, Rifkind RA, Marks PA: Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5. Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1056-61. [PubMed
]
- Wen YD, Perissi V, Staszewski LM, Yang WM, Krones A, Glass CK, Rosenfeld MG, Seto E: The histone deacetylase-3 complex contains nuclear receptor corepressors. Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7202-7. [PubMed
]
- Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E: Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo. J Biol Chem. 2001 Sep 21;276(38):35826-35. Epub 2001 Jul 20. [PubMed
]
- Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW: ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol Cell Biol. 2001 Oct;21(19):6470-83. [PubMed
]
- Tong JJ, Liu J, Bertos NR, Yang XJ: Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain. Nucleic Acids Res. 2002 Mar 1;30(5):1114-23. [PubMed
]
- Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 2002 Jun 3;21(11):2682-91. [PubMed
]
- Guenther MG, Lane WS, Fischle W, Verdin E, Lazar MA, Shiekhattar R: A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes Dev. 2000 May 1;14(9):1048-57. [PubMed
]
- Li J, Wang J, Wang J, Nawaz Z, Liu JM, Qin J, Wong J: Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. EMBO J. 2000 Aug 15;19(16):4342-50. [PubMed
]
- Huynh KD, Fischle W, Verdin E, Bardwell VJ: BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev. 2000 Jul 15;14(14):1810-23. [PubMed
]
- Zhang J, Kalkum M, Chait BT, Roeder RG: The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol Cell. 2002 Mar;9(3):611-23. [PubMed
]
- Yoon HG, Chan DW, Huang ZQ, Li J, Fondell JD, Qin J, Wong J: Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. EMBO J. 2003 Mar 17;22(6):1336-46. [PubMed
]
- Wu K, Yang Y, Wang C, Davoli MA, D'Amico M, Li A, Cveklova K, Kozmik Z, Lisanti MP, Russell RG, Cvekl A, Pestell RG: DACH1 inhibits transforming growth factor-beta signaling through binding Smad4. J Biol Chem. 2003 Dec 19;278(51):51673-84. Epub 2003 Oct 2. [PubMed
]
- Thevenet L, Mejean C, Moniot B, Bonneaud N, Galeotti N, Aldrian-Herrada G, Poulat F, Berta P, Benkirane M, Boizet-Bonhoure B: Regulation of human SRY subcellular distribution by its acetylation/deacetylation. EMBO J. 2004 Aug 18;23(16):3336-45. Epub 2004 Aug 5. [PubMed
]
- Gray SG, Iglesias AH, Lizcano F, Villanueva R, Camelo S, Jingu H, Teh BT, Koibuchi N, Chin WW, Kokkotou E, Dangond F: Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem. 2005 Aug 5;280(31):28507-18. Epub 2005 May 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
]
- Pajerowski AG, Nguyen C, Aghajanian H, Shapiro MJ, Shapiro VS: NKAP is a transcriptional repressor of notch signaling and is required for T cell development. Immunity. 2009 May;30(5):696-707. Epub 2009 Apr 30. [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 16 Metabolite References |
- Ishihara K, Takahashi A, Kaneko M, Sugeno H, Hirasawa N, Hong J, Zee O, Ohuchi K: Differentiation of eosinophilic leukemia EoL-1 cells into eosinophils induced by histone deacetylase inhibitors. Life Sci. 2007 Mar 6;80(13):1213-20. Epub 2007 Jan 11. [PubMed
]
|
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
14853 |
| Enzyme 17 Name |
Histone deacetylase 5 |
| Enzyme 17 Synonyms |
- HD5
- Antigen NY-CO-9
|
| Enzyme 17 Gene Name |
HDAC5 |
| Enzyme 17 Protein Sequence |
>Histone deacetylase 5
MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELR
GALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQ
QEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIAS
TEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKL
PLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEI
TGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQ
FSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMST
SSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATS
MRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGE
LPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEED
CIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQ
SSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQE
TGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLP
CGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM
GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNF
FPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVS
AGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVS
ALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGET
EEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL
|
| Enzyme 17 Number of Residues |
1122 |
| Enzyme 17 Molecular Weight |
121976.9 |
| Enzyme 17 Theoretical pI |
6.19 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- histone deacetylase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
|
| Component |
- chromatin remodeling complex
- histone deacetylase complex
- macromolecular complex
- protein complex
|
|
| Enzyme 17 General Function |
Involved in histone deacetylase activity |
| Enzyme 17 Specific Function |
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
- Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
62750347  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q9UQL6  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
HDAC5_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>3369 bp
ATGAACTCTCCCAACGAGTCGGATGGGATGTCAGGTCGGGAACCATCCTTGGAAATCCTG
CCGCGGACTTCTCTGCACAGCATCCCTGTGACAGTGGAGGTGAAGCCGGTGCTGCCAAGA
GCCATGCCCAGTTCCATGGGGGGTGGGGGTGGAGGCAGCCCCAGCCCTGTGGAGCTACGG
GGGGCTCTGGTGGGCTCTGTGGACCCCACACTGCGGGAGCAGCAACTGCAGCAGGAGCTC
CTGGCGCTCAAGCAGCAGCAGCAGCTGCAGAAGCAGCTCCTGTTCGCTGAGTTCCAGAAA
CAGCATGACCACCTGACAAGGCAGCATGAGGTCCAGCTGCAGAAGCACCTCAAGCAGCAG
CAGGAGATGCTGGCAGCCAAGCAGCAGCAGGAGATGCTGGCAGCCAAGCGGCAGCAGGAG
CTGGAGCAGCAGCGGCAGCGGGAGCAGCAGCGGCAGGAAGAGCTGGAGAAGCAGCGGCTG
GAGCAGCAGCTGCTCATCCTGCGGAACAAGGAGAAGAGCAAAGAGAGTGCCATTGCCAGC
ACTGAGGTAAAGCTGAGGCTCCAGGAATTCCTCTTGTCGAAGTCAAAGGAGCCCACACCA
GGCGGCCTCAACCATTCCCTCCCACAGCACCCCAAATGCTGGGGAGCCCACCATGCTTCT
TTGGACCAGAGTTCCCCTCCCCAGAGCGGCCCCCCTGGGACGCCTCCCTCCTACAAACTG
CCTTTGCCTGGGCCCTACGACAGTCGAGACGACTTCCCCCTCCGCAAAACAGCCTCTGAA
CCCAACTTGAAAGTGCGTTCAAGGCTAAAACAGAAGGTGGCTGAGCGGAGAAGCAGTCCC
CTCCTGCGTCGCAAGGATGGGACTGTTATTAGCACCTTTAAGAAGAGAGCTGTTGAGATC
ACAGGTGCCGGGCCTGGGGCGTCGTCCGTGTGTAACAGCGCACCCGGCTCCGGCCCCAGC
TCTCCCAACAGCTCCCACAGCACCATCGCTGAGAATGGCTTTACTGGCTCAGTCCCCAAC
ATCCCCACTGAGATGCTCCCTCAGCACCGAGCCCTCCCTCTGGACAGCTCCCCCAACCAG
TTCAGCCTCTACACGTCTCCTTCTCTGCCCAACATCTCCCTAGGGCTGCAGGCCACGGTC
ACTGTCACCAACTCACACCTCACTGCCTCCCCGAAGCTGTCGACACAGCAGGAGGCCGAG
AGGCAGGCCCTCCAGTCCCTGCGGCAGGGTGGCACGCTGACCGGCAAGTTCATGAGCACA
TCCTCTATTCCTGGCTGCCTGCTGGGCGTGGCACTGGAGGGCGACGGGAGCCCCCACGGG
CATGCCTCCCTGCTGCAGCATGTGCTGTTGCTGGAGCAGGCCCGGCAGCAGAGCACCCTC
ATTGCTGTGCCACTCCACGGGCAGTCCCCACTAGTGACGGGTGAACGTGTGGCCACCAGC
ATGCGGACGGTAGGCAAGCTCCCGCGGCATCGGCCCCTGAGCCGCACTCAGTCCTCACCG
CTGCCGCAGAGTCCCCAGGCCCTGCAGCAGCTGGTCATGCAACAACAGCACCAGCAGTTC
CTGGAGAAGCAGAAGCAGCAGCAGCTACAGCTGGGCAAGATCCTCACCAAGACAGGGGAG
CTGCCCAGGCAGCCCACCACCCACCCTGAGGAGACAGAGGAGGAGCTGACGGAGCAGCAG
GAGGTCTTGCTGGGGGAGGGAGCCCTGACCATGCCCCGGGAGGGCTCCACAGAGAGTGAG
AGCACACAGGAAGACCTGGAGGAGGAGGACGAGGAAGACGATGGGGAGGAGGAGGAGGAT
TGCATCCAGGTTAAGGACGAGGAGGGCGAGAGTGGTGCTGAGGAGGGGCCCGACTTGGAG
GAGCCTGGTGCTGGATACAAAAAACTGTTCTCAGATGCCCAGCCGCTGCAGCCTTTGCAG
GTGTACCAGGCGCCCCTCAGCCTGGCCACTGTGCCCCACCAGGCCCTGGGCCGTACCCAG
TCCTCCCCTGCTGCCCCTGGGGGCATGAAGAGCCCCCCAGACCAGCCCGTCAAGCACCTC
TTCACCACAGGTGTGGTCTACGACACGTTCATGCTAAAGCACCAGTGCATGTGCGGGAAC
ACACACGTGCACCCTGAGCATGCTGGCCGGATCCAGAGCATCTGGTCCCGGCTGCAGGAG
ACAGGCCTGCTTAGCAAGTGCGAGCGGATCCGAGGTCGCAAAGCCACGCTAGATGAGATC
CAGACAGTGCACTCTGAATACCACACCCTGCTCTATGGGACCAGTCCCCTCAACCGGCAG
AAGCTAGACAGCAAGAAGTTGCTCGGCCCCATCAGCCAGAAGATGTATGCTGTGCTGCCT
TGTGGGGGCATCGGGGTGGACAGTGACACCGTGTGGAATGAGATGCACTCCTCCAGTGCT
GTGCGCATGGCAGTGGGCTGCCTGCTGGAGCTGGCCTTCAAGGTGGCTGCAGGAGAGCTC
AAGAATGGATTTGCCATCATCCGGCCCCCAGGACACCACGCCGAGGAATCCACAGCCATG
GGATTCTGCTTCTTCAACTCTGTAGCCATCACCGCAAAACTCCTACAGCAGAAGTTGAAC
GTGGGCAAGGTCCTCATCGTGGACTGGGACATTCACCATGGCAATGGCACCCAGCAGGCG
TTCTACAATGACCCCTCTGTGCTCTACATCTCTCTGCATCGCTATGACAACGGGAACTTC
TTTCCAGGCTCTGGGGCTCCTGAAGAGGTTGGTGGAGGACCAGGCGTGGGGTACAATGTG
AACGTGGCATGGACAGGAGGTGTGGACCCCCCCATTGGAGACGTGGAGTACCTTACAGCC
TTCAGGACAGTGGTGATGCCCATTGCCCACGAGTTCTCACCTGATGTGGTCCTAGTCTCC
GCCGGGTTTGATGCTGTTGAAGGACATCTGTCTCCTCTGGGTGGCTACTCTGTCACCGCC
AGATGTTTTGGCCACTTGACCAGGCAGCTGATGACCCTGGCAGGGGGCCGGGTGGTGCTG
GCCCTGGAGGGAGGCCATGACTTGACCGCCATCTGTGATGCCTCTGAGGCTTGTGTCTCG
GCTCTGCTCAGTGTAGAGCTGCAGCCCTTGGATGAGGCAGTCTTGCAGCAAAAGCCCAAC
ATCAACGCAGTGGCCACGCTAGAGAAAGTCATCGAGATCCAGAGCAAACACTGGAGCTGT
GTGCAGAAGTTCGCCGCTGGTCTGGGCCGGTCCCTGCGAGAGGCCCAAGCAGGTGAGACC
GAGGAGGCCGAGACTGTGAGCGCCATGGCCTTGCTGTCGGTGGGGGCCGAGCAGGCCCAG
GCTGCGGCAGCCCGGGAACACAGCCCCAGGCCGGCAGAGGAGCCCATGGAGCAGGAGCCT
GCCCTGTGA
|
| Enzyme 17 GenBank Gene ID |
NM_005474.4  |
| Enzyme 17 GeneCard ID |
HDAC5  |
| Enzyme 17 GenAtlas ID |
HDAC5  |
| Enzyme 17 HGNC ID |
HGNC:14068  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
17q21 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Grozinger CM, Hassig CA, Schreiber SL: Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4868-73. [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
]
- 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
]
- 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
]
- Scanlan MJ, Chen YT, Williamson B, Gure AO, Stockert E, Gordan JD, Tureci O, Sahin U, Pfreundschuh M, Old LJ: Characterization of human colon cancer antigens recognized by autologous antibodies. Int J Cancer. 1998 May 29;76(5):652-8. [PubMed
]
- Mahlknecht U, Schnittger S, Ottmann OG, Schoch C, Mosebach M, Hiddemann W, Hoelzer D: Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5). Biochim Biophys Acta. 2000 Oct 2;1493(3):342-8. [PubMed
]
- Huynh KD, Fischle W, Verdin E, Bardwell VJ: BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev. 2000 Jul 15;14(14):1810-23. [PubMed
]
- McKinsey TA, Zhang CL, Lu J, Olson EN: Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature. 2000 Nov 2;408(6808):106-11. [PubMed
]
- McKinsey TA, Zhang CL, Olson EN: Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14400-5. [PubMed
]
- McKinsey TA, Zhang CL, Olson EN: Identification of a signal-responsive nuclear export sequence in class II histone deacetylases. Mol Cell Biol. 2001 Sep;21(18):6312-21. [PubMed
]
- Hook SS, Orian A, Cowley SM, Eisenman RN: Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13425-30. Epub 2002 Sep 27. [PubMed
]
- Barrett A, Santangelo S, Tan K, Catchpole S, Roberts K, Spencer-Dene B, Hall D, Scibetta A, Burchell J, Verdin E, Freemont P, Taylor-Papadimitriou J: Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases. Int J Cancer. 2007 Jul 15;121(2):265-75. [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
]
- Bierne H, Tham TN, Batsche E, Dumay A, Leguillou M, Kerneis-Golsteyn S, Regnault B, Seeler JS, Muchardt C, Feunteun J, Cossart P: Human BAHD1 promotes heterochromatic gene silencing. Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13826-31. Epub 2009 Aug 3. [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
]
- Harrison BC, Huynh K, Lundgaard GL, Helmke SM, Perryman MB, McKinsey TA: Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases. FEBS Lett. 2010 Mar 19;584(6):1103-10. Epub 2010 Feb 24. [PubMed
]
|
| Enzyme 17 Metabolite References |
- Ishihara K, Takahashi A, Kaneko M, Sugeno H, Hirasawa N, Hong J, Zee O, Ohuchi K: Differentiation of eosinophilic leukemia EoL-1 cells into eosinophils induced by histone deacetylase inhibitors. Life Sci. 2007 Mar 6;80(13):1213-20. Epub 2007 Jan 11. [PubMed
]
|
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
14869 |
| Enzyme 18 Name |
Acyl-coenzyme A synthetase ACSM4, mitochondrial |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
ACSM4 |
| Enzyme 18 Protein Sequence |
>Acyl-coenzyme A synthetase ACSM4, mitochondrial
MKIFFRYQTFRFIWLTKPPGRRLHKDHQLWTPLTLADFEAINRCNRPLPKNFNFAADVLD
QWSQKEKTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANVLTKPCGLQRGDRLAVI
LPRIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVL
ECPDLKTKLLVSPQSWNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQ
HSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQF
DTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRV
QTGLELYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIA
LRLKPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGY
RIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHV
KKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR
|
| Enzyme 18 Number of Residues |
580 |
| Enzyme 18 Molecular Weight |
65702.2 |
| Enzyme 18 Theoretical pI |
8.76 |
| Enzyme 18 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in catalytic activity |
| Enzyme 18 Specific Function |
Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro) |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
- ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
122937307  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P0C7M7  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
ACSM4_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1743 bp
ATGAAGATTTTTTTCCGCTACCAGACATTTAGATTCATCTGGCTCACCAAGCCACCTGGC
CGGCGCTTACACAAAGATCACCAGCTTTGGACGCCTCTGACTCTTGCTGACTTTGAAGCC
ATAAATCGCTGTAACAGGCCATTGCCTAAAAACTTTAACTTTGCTGCAGATGTGCTGGAC
CAGTGGTCCCAAAAGGAGAAGACAGGGGAGAGACCAGCTAACCCAGCCCTGTGGTGGGTG
AATGGCAAAGGGGATGAGGTAAAATGGAGCTTCAGAGAACTGGGCTCCTTGTCCCGAAAA
GCTGCCAACGTGCTCACCAAGCCCTGTGGCCTGCAGAGAGGAGACCGTTTGGCCGTGATT
CTGCCCAGAATCCCTGAGTGGTGGCTGGTCAATGTAGCTTGCATACGAACAGGGATCATC
TTCATGCCGGGAACAATCCAGCTGACAGCAAAAGACATCCTCTACCGGCTGCGAGCATCC
AAGGCCAAGTGCATTGTGGCCAGTGAGGAGGTGGCCCCAGCGGTGGAGTCCATTGTATTG
GAGTGTCCTGACCTTAAGACAAAACTCCTGGTGTCTCCACAAAGCTGGAATGGGTGGCTC
AGCTTCCAGGAGTTATTTCAATTCGCCTCTGAAGAGCACAGCTGTGTGGAAACAGGAAGT
CAAGAACCAATGACCATTTATTTCACCAGTGGGACCACAGGCTTTCCTAAAATGGCCCAG
CACTCTCAGAGCAGCCTCGGCATTGGGTTCACCCTCTGCGGAAGGTATTGGCTGGACTTG
AAGTCCTCAGATATCATATGGAATATGTCTGACACGGGCTGGGTCAAGGCCGCCATTGGC
AGTGTGTTTTCTTCCTGGCTGTGTGGAGCCTGTGTTTTTGTGCATCGAATGGCACAGTTT
GACACTGACACCTTCCTAGACACACTTACTACTTATCCCATCACGACCCTGTGCAGTCCT
CCCACTGTGTACCGGATGCTCGTGCAAAAAGACCTTAAGAGATATAAATTCAAGAGTCTG
CGGCACTGCTTGACCGGAGGGGAGCCACTCAACCCAGAAGTGCTGGAGCAGTGGAGGGTG
CAAACTGGGCTGGAGCTATATGAGGGCTATGGACAGACGGAAGTGGGAATGATTTGTGCC
AATCAGAAAGGCCAAGAAATTAAACCAGGTTCAATGGGGAAAGGAATGCTGCCCTATGAT
GTCCAGATTATAGATGAAAATGGCAATGTTCTACCACCTGGCAAAGAAGGGGAAATTGCC
CTCAGACTCAAACCTACACGGCCCTTCTGTTTCTTCTCTAAATATGTGGACAATCCACAG
AAAACTGCTGCCACGATAAGAGGAGATTTTTATGTCACTGGAGACAGAGGAGTGATGGAC
AGTGATGGGTATTTCTGGTTTGTCGGCAGAGCTGATGATGTCATTATATCCTCTGGGTAC
CGTATTGGGCCATTTGAAGTGGAGAGTGCACTCATTGAGCATCCAGCAGTTGTTGAATCG
GCTGTTGTCAGTAGTCCAGATCAAATCCGCGGAGAGGTGGTGAAAGCTTTTGTTGTCTTA
GCTGCACCCTTTAAGTCCTACAACCCAGAGAAATTAACTCTTGAACTTCAGGATCATGTG
AAAAAATCAACTGCACCTTACAAATATCCAAGAAAGGTGGAATTTGTTCAAGAACTCCCA
AAGACAATCACTGGGAAAATCAAACGCAACGTTTTAAGAGACCAAGAATGGAGAGGAAGA
TAG
|
| Enzyme 18 GenBank Gene ID |
NM_001080454.1  |
| Enzyme 18 GeneCard ID |
ACSM4  |
| Enzyme 18 GenAtlas ID |
ACSM4  |
| Enzyme 18 HGNC ID |
HGNC:32016  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
12p13.31 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Watkins PA, Maiguel D, Jia Z, Pevsner J: Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J Lipid Res. 2007 Dec;48(12):2736-50. Epub 2007 Aug 30. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |