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Human Metabolome Database Version 2.5

 

Showing metabocard for Butyric acid (HMDB00039)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:39
Accession Number HMDB00039
Secondary Accession Numbers Not Available
Common Name Butyric acid
Description Butyric acid, a four-carbon fatty acid, is formed in the human colon by bacterial fermentation of carbohydrates (including dietary fiber), and putatively suppresses colorectal cancer (CRC). Butyrate has diverse and apparently paradoxical effects on cellular proliferation, apoptosis and differentiation that may be either pro-neoplastic or anti-neoplastic, depending upon factors such as the level of exposure, availability of other metabolic substrate and the intracellular milieu. In humans, the relationship between luminal butyrate exposure and CRC has been examined only indirectly in case-control studies, by measuring fecal butyrate concentrations, although this may not accurately reflect effective butyrate exposure during carcinogenesis. Perhaps not surprisingly, results of these investigations have been mutually contradictory. The direct effect of butyrate on tumorigenesis has been assessed in a no. of in vivo animal models, which have also yielded conflicting results. In part, this may be explained by methodology: differences in the amount and route of butyrate administration, which are likely to significantly influence delivery of butyrate to the distal colon. (PMID: 16460475) Butyric acid is a carboxylic acid found in rancid butter, parmesan cheese, and vomit, and has an unpleasant odor and acrid taste, with a sweetish aftertaste (similar to ether). Butyric acid is a fatty acid occurring in the form of esters in animal fats and plant oils. Interestingly, low-molecular-weight esters of butyric acid, such as methyl butyrate, have mostly pleasant aromas or tastes. As a consequence, they find use as food and perfume additives. Butyrate is produced as end-product of a fermentation process solely performed by obligate anaerobic bacteria.
Synonyms
  1. 1-Butyrate
  2. 1-Butyric acid
  3. 1-Propanecarboxylate
  4. 1-Propanecarboxylic acid
  5. 1-butanoate
  6. 1-butanoic acid
  7. Butanate
  8. Butanic acid
  9. Butanoate
  10. Butanoic acid
  11. Buttersaeure
  12. Butyrate
  13. Ethylacetate
  14. Ethylacetic acid
  15. Honey robber
  16. Kyselina maselna
  17. Propanecarboxylate
  18. Propanecarboxylic acid
  19. Propylformate
  20. Propylformic acid
  21. butyric acid
  22. n-Butanoate
  23. n-Butanoic acid
  24. n-Butyrate
  25. n-Butyric acid
Chemical IUPAC Name Butanoic acid
Chemical Formula C4H8O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Short chain fatty acids
Family
  • Microbial Metabolite
Species
  • carboxylic acid
Biofunction
  • Energy source
  • DNA component
Application
Source
  • Endogenous
Average Molecular Weight 88.105
Monoisotopic Molecular Weight 88.052429
Isomeric SMILES CCCC(O)=O
Canonical SMILES CCCC(O)=O
KEGG Compound ID C00246 Link Image
BioCyc ID Not Available
BiGG ID 34376 Link Image
Wikipedia Link Butyric acid Link Image
NuGOwiki Link HMDB00039 Link Image
Metagene Link HMDB00039 Link Image
METLIN ID 107 Link Image
PubChem Compound 264 Link Image
PubChem Substance 3545 Link Image
ChEBI ID 30772 Link Image
CAS Registry Number 107-92-6
InChI Identifier InChI=1/C4H8O2/c1-2-3-4(5)6/h2-3H2,1H3,(H,5,6)
Synthesis Reference Shan, Zhiping. Preparation of butyric acid by hydrogenation of maleic anhydride. U.S. Pat. Appl. Publ. (2008), 6pp.
Melting Point (Experimental) -5.7 oC
Experimental Water Solubility 60.0 mg/mL [HEMPHILL,L & SWANSON,WS (1964)] Source: PhysProp
Predicted Water Solubility 239.00002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity 0.79 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 0.78 [Predicted by ALOGPS]; 0.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Fibroblasts
Intestine
Kidney
Large Intestine
Muscle
Neuron
Prostate
Concentrations (Normal)
Biofluid Blood
Value 1.0 (0.3- 1.5) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 1.4 (0-2.8) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Saliva
Value 1470 (0.00-2940) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 0.086 +/- 0.0085 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Stein TP, Koerner B, Schluter MD, Leskiw MJ, Gaprindachvilli T, Richards EW, Cope FO, Condolucci D: Weight loss, the gut and the inflammatory response in aids patients. Cytokine. 1997 Feb;9(2):143-7. [PubMed Link Image]
Biofluid Urine
Value 3.2 (0.0-6.4) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 42.0 (21.0-81.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal)
Biofluid Urine
Value 0.18 +/- 0.044 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition AIDS
Comments Not Available
References
  • Stein TP, Koerner B, Schluter MD, Leskiw MJ, Gaprindachvilli T, Richards EW, Cope FO, Condolucci D: Weight loss, the gut and the inflammatory response in aids patients. Cytokine. 1997 Feb;9(2):143-7. [PubMed Link Image]
Associated Disorders
Condition References
AIDS
  • Stein TP, Koerner B, Schluter MD, Leskiw MJ, Gaprindachvilli T, Richards EW, Cope FO, Condolucci D: Weight loss, the gut and the inflammatory response in aids patients. Cytokine. 1997 Feb;9(2):143-7. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Butyrate Metabolism SMP00073 Link Image map00650 Link Image
Fatty Acid Biosynthesis SMP00456 Link Image
General References
  1. McMillan L, Butcher SK, Pongracz J, Lord JM: Opposing effects of butyrate and bile acids on apoptosis of human colon adenoma cells: differential activation of PKC and MAP kinases. Br J Cancer. 2003 Mar 10;88(5):748-53. [PubMed Link Image]
  2. Bauer G: Induction of Epstein-Barr virus early antigens by corticosteroids: inhibition by TPA and retinoic acid. Int J Cancer. 1983 Mar 15;31(3):291-5. [PubMed Link Image]
  3. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  4. McIntosh GH, Noakes M, Royle PJ, Foster PR: Whole-grain rye and wheat foods and markers of bowel health in overweight middle-aged men. Am J Clin Nutr. 2003 Apr;77(4):967-74. [PubMed Link Image]
  5. Schwiertz A, Lehmann U, Jacobasch G, Blaut M: Influence of resistant starch on the SCFA production and cell counts of butyrate-producing Eubacterium spp. in the human intestine. J Appl Microbiol. 2002;93(1):157-62. [PubMed Link Image]
  6. Bauer G, Hofler P, Simon M: Epstein-Barr virus induction by a serum factor. Characterization of the purified factor and the mechanism of its activation. J Biol Chem. 1982 Oct 10;257(19):11411-5. [PubMed Link Image]
  7. Jin SE, Ban E, Kim YB, Kim CK: Development of HPLC method for the determination of levosulpiride in human plasma. J Pharm Biomed Anal. 2004 Jun 29;35(4):929-36. [PubMed Link Image]
  8. Welters CF, Heineman E, Thunnissen FB, van den Bogaard AE, Soeters PB, Baeten CG: Effect of dietary inulin supplementation on inflammation of pouch mucosa in patients with an ileal pouch-anal anastomosis. Dis Colon Rectum. 2002 May;45(5):621-7. [PubMed Link Image]
  9. Kurita-Ochiai T, Seto S, Ochiai K: Role of cell-cell communication in inhibiting butyric acid-induced T-cell apoptosis. Infect Immun. 2004 Oct;72(10):5947-54. [PubMed Link Image]
  10. Cruz HG, Ivanova T, Lunn ML, Stoffel M, Slesinger PA, Luscher C: Bi-directional effects of GABA(B) receptor agonists on the mesolimbic dopamine system. Nat Neurosci. 2004 Feb;7(2):153-9. Epub 2004 Jan 25. [PubMed Link Image]
  11. Yonemura K, Sairenji T, Hinuma Y: Inhibitory effect of 1-beta-D-arabinofuranosylthymine on synthesis of Epstein-Barr virus. Microbiol Immunol. 1981;25(6):557-63. [PubMed Link Image]
  12. Teichert J, Tuemmers T, Achenbach H, Preiss C, Hermann R, Ruus P, Preiss R: Pharmacokinetics of alpha-lipoic acid in subjects with severe kidney damage and end-stage renal disease. J Clin Pharmacol. 2005 Mar;45(3):313-28. [PubMed Link Image]
  13. Rephaeli A, Blank-Porat D, Tarasenko N, Entin-Meer M, Levovich I, Cutts SM, Phillips DR, Malik Z, Nudelman A: In vivo and in vitro antitumor activity of butyroyloxymethyl-diethyl phosphate (AN-7), a histone deacetylase inhibitor, in human prostate cancer. Int J Cancer. 2005 Aug 20;116(2):226-35. [PubMed Link Image]
  14. Kurita-Ochiai T, Ochiai K, Suzuki N, Otsuka K, Fukushima K: Human gingival fibroblasts rescue butyric acid-induced T-cell apoptosis. Infect Immun. 2002 May;70(5):2361-7. [PubMed Link Image]
  15. Jacobasch G, Jacobasch KH: [Molecular etiology of colorectal carcinogenesis, clinical manifestations and therapy] Z Arztl Fortbild Qualitatssich. 1997 Mar;91(2):125-33. [PubMed Link Image]
  16. Velazquez OC, Lederer HM, Rombeau JL: Butyrate and the colonocyte. Production, absorption, metabolism, and therapeutic implications. Adv Exp Med Biol. 1997;427:123-34. [PubMed Link Image]
  17. Kawanishi M, Ito Y: Effect of short-chain fatty acids on Epstein-Barr virus early and viral capsid antigen induction in P3HR-1 cells. Cancer Lett. 1980 Dec;11(2):129-32. [PubMed Link Image]
  18. Stein TP, Koerner B, Schluter MD, Leskiw MJ, Gaprindachvilli T, Richards EW, Cope FO, Condolucci D: Weight loss, the gut and the inflammatory response in aids patients. Cytokine. 1997 Feb;9(2):143-7. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Monocarboxylate transporter 1
  2. Caspase-3 precursor
  3. Tumor necrosis factor precursor
  4. Peroxisome proliferator-activated receptor gamma
  5. Histone deacetylase 4
  6. Histone deacetylase 9
  7. Histone deacetylase 1
  8. Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
  9. Uncharacterized protein C10orf129
  10. Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor
  11. Acyl-coenzyme A synthetase ACSM2B, mitochondrial precursor
  12. Acyl-coenzyme A synthetase ACSM3, mitochondrial precursor
  13. Acyl-coenzyme A synthetase ACSM5, mitochondrial precursor
  14. Coenzyme A transferase
  15. Histone deacetylase 2
  16. Histone deacetylase 3
  17. Histone deacetylase 5
  18. Not Available
Enzyme 1 [top]
Enzyme 1 ID 6404
Enzyme 1 Name Monocarboxylate transporter 1
Enzyme 1 Synonyms
  1. MCT 1
  2. 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 53959
Enzyme 1 Theoretical pI 8.82
Enzyme 1 GO Classification
Function
  • carboxylic acid transporter activity
  • monocarboxylate porter activity
  • monocarboxylic acid transporter activity
  • organic acid transporter activity
  • transporter activity
Process
  • anion transport
  • cellular physiological process
  • ion transport
  • organic anion transport
  • physiological process
  • transport
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 1 General Function Carbohydrate transport and metabolism
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
  • 1-35
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 561722 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P53985 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name MOT1_HUMAN Link Image
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 Link Image
Enzyme 1 GeneCard ID SLC16A1 Link Image
Enzyme 1 GenAtlas ID SLC16A1 Link Image
Enzyme 1 HGNC ID HGNC:10922 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 1 Metabolite References
  1. 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 Link Image]
Enzyme 2 [top]
Enzyme 2 ID 7434
Enzyme 2 Name Caspase-3 precursor
Enzyme 2 Synonyms
  1. CASP-3
  2. Apopain
  3. Cysteine protease CPP32
  4. Yama protein
  5. CPP-32
  6. SREBP cleavage activity 1
  7. SCA-1[Contains: Caspase-3 p17 subunit
  8. Caspase-3 p12 subunit]
Enzyme 2 Gene Name CASP3
Enzyme 2 Protein Sequence >Caspase-3 precursor
MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG
MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS
HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD
DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN
RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH
Enzyme 2 Number of Residues 277
Enzyme 2 Molecular Weight 31608
Enzyme 2 Theoretical pI 6.51
Enzyme 2 GO Classification
Function
  • caspase activity
  • catalytic activity
  • cysteine-type endopeptidase activity
  • endopeptidase activity
  • hydrolase activity
  • peptidase activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
Enzyme 2 General Function Not Available
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 Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 561666 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P42574 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CASP3_HUMAN Link Image
Enzyme 2 PDB ID 1CP3 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >834 bp
ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC
ATACATGGAAGCGAATCAATGGACTCTGGAATATCCCTGGACAACAGTTATAAAATGGAT
TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA
ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC
TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG
CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC
CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA
AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT
CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT
GACATGGCGTGTCATAAAATACCAGTGGATGCCGACTTCTTGTATGCATACTCCACAGCA
CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT
GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC
CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA
CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA
Enzyme 2 GenBank Gene ID U13737 Link Image
Enzyme 2 GeneCard ID CASP3 Link Image
Enzyme 2 GenAtlas ID CASP3 Link Image
Enzyme 2 HGNC ID HGNC:1504 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
Enzyme 2 Metabolite References
  1. 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 Link Image]
Enzyme 3 [top]
Enzyme 3 ID 7551
Enzyme 3 Name Tumor necrosis factor precursor
Enzyme 3 Synonyms
  1. TNF-alpha
  2. Tumor necrosis factor ligand superfamily member 2
  3. TNF-a
  4. Cachectin[Contains: Tumor necrosis factor, membrane form
  5. Tumor necrosis factor, soluble form]
Enzyme 3 Gene Name TNF
Enzyme 3 Protein Sequence >Tumor necrosis factor precursor
MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQR
EEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELR
DNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRE
TPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
Enzyme 3 Number of Residues 233
Enzyme 3 Molecular Weight 25645
Enzyme 3 Theoretical pI 6.92
Enzyme 3 GO Classification
Function
  • cytokine activity
  • receptor binding
  • signal transducer activity
  • tumor necrosis factor receptor binding
Process
  • defense response
  • immune response
  • response to biotic stimulus
  • response to stimulus
Component
  • cell
  • membrane
Enzyme 3 General Function Not Available
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
  • None
Enzyme 3 Transmembrane Regions
  • 36-56
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P01375 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name TNFA_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID M16441 Link Image
Enzyme 3 GeneCard ID TNF Link Image
Enzyme 3 GenAtlas ID TNF Link Image
Enzyme 3 HGNC ID HGNC:11892 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6p21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
  13. 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 Link Image]
  14. Jones EY, Stuart DI, Walker NP: Structure of tumour necrosis factor. Nature. 1989 Mar 16;338(6212):225-8. [PubMed Link Image]
  15. 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 Link Image]
  16. 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 Link Image]
  17. 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 Link Image]
  18. 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 Link Image]
Enzyme 3 Metabolite References
  1. 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 Link Image]
Enzyme 4 [top]
Enzyme 4 ID 7657
Enzyme 4 Name Peroxisome proliferator-activated receptor gamma
Enzyme 4 Synonyms
  1. PPAR-gamma
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 57621
Enzyme 4 Theoretical pI 5.77
Enzyme 4 GO Classification
Function
  • DNA binding
  • binding
  • ligand-dependent nuclear receptor activity
  • nucleic acid binding
  • receptor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transcription factor activity
Process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 4 General Function Not Available
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
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1711117 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P37231 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PPARG_HUMAN Link Image
Enzyme 4 PDB ID Not Available
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 Link Image
Enzyme 4 GeneCard ID PPARG Link Image
Enzyme 4 GenAtlas ID PPARG Link Image
Enzyme 4 HGNC ID HGNC:9236 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3p25
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. Shao W, Halachmi S, Brown M: ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol Cell Biol. 2002 May;22(10):3358-72. [PubMed Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
  13. 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 Link Image]
  14. 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 Link Image]
  15. 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 Link Image]
Enzyme 4 Metabolite References
  1. 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 Link Image]
Enzyme 5 [top]
Enzyme 5 ID 7680
Enzyme 5 Name Histone deacetylase 4
Enzyme 5 Synonyms
  1. HD4
Enzyme 5 Gene Name HDAC4
Enzyme 5 Protein Sequence >Histone deacetylase 4
MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLP
VAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLA
MKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVL
NKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFP
LRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGP
SSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPA
TGPSAGTAGQQDTERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLL
EQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHL
VIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPY
LDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQ
RIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDT
LMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHT
LLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVE
LVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWD
VHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDP
PMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQL
MGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKV
MEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEE
EPPL
Enzyme 5 Number of Residues 1084
Enzyme 5 Molecular Weight 119071
Enzyme 5 Theoretical pI 6.96
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
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 Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4754907 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P56524 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name HDAC4_HUMAN Link Image
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
ACCGGCCCCTCTGCGGGCACGGCGGGCCAGCAGGACACCGAGAGACTCACCCTTCCCGCC
CTCCAGCAGAGGCTCTCCCTTTTCCCCGGCACCCACCTCACTCCCTACCTGAGCACCTCG
CCCTTGGAGCGGGACGGAGGGGCAGCGCACAGCCCTCTTCTGCAGCACATGGTCTTACTG
GAGCAGCCACCGGCACAAGCACCCCTCGTCACAGGCCTGGGAGCACTGCCCCTCCACGCA
CAGTCCTTGGTTGGTGCAGACCGGGTGTCCCCCTCCATCCACAAGCTGCGGCAGCACCGC
CCACTGGGGCGGACCCAGTCGGCCCCGCTGCCCCAGAACGCCCAGGCTCTGCAGCACCTG
GTCATCCAGCAGCAGCATCAGCAGTTTCTGGAGAAACACAAGCAGCAGTTCCAGCAGCAG
CAACTGCAGATGAACAAGATCATCCCCAAGCCAAGCGAGCCAGCCCGGCAGCCGGAGAGC
CACCCGGAGGAGACGGAGGAGGAGCTCCGTGAGCACCAGGCTCTGCTGGACGAGCCCTAC
CTGGACCGGCTGCCGGGGCAGAAGGAGGCGCACGCACAGGCCGGCGTGCAGGTGAAGCAG
GAGCCCATTGAGAGCGATGAGGAAGAGGCAGAGCCCCCACGGGAGGTGGAGCCGGGCCAG
CGCCAGCCCAGTGAGCAGGAGCTGCTCTTCAGACAGCAAGCCCTCCTGCTGGAGCAGCAG
CGGATCCACCAGCTGAGGAACTACCAGGCGTCCATGGAGGCCGCCGGCATCCCCGTGTCC
TTCGGCGGCCACAGGCCTCTGTCCCGGGCGCAGTCCTCACCCGCGTCTGCCACCTTCCCC
GTGTCTGTGCAGGAGCCCCCCACCAAGCCGAGGTTCACGACAGGCCTCGTGTATGACACG
CTGATGCTGAAGCACCAGTGCACCTGCGGGAGTAGCAGCAGCCACCCCGAGCACGCCGGG
AGGATCCAGAGCATCTGGTCCCGCCTGCAGGAGACGGGCCTCCGGGGCAAATGCGAGTGC
ATCCGCGGACGCAAGGCCACCCTGGAGGAGCTACAGACGGTGCACTCGGAAGCCCACACC
CTCCTGTATGGCACGAACCCCCTCAACCGGCAGAAACTGGACAGTAAGAAACTTCTAGGC
TCGCTCGCCTCCGTGTTCGTCCGGCTCCCTTGCGGTGGTGTTGGGGTGGACAGTGACACC
ATATGGAACGAGGTGCACTCGGCGGGGGCAGCCCGCCTGGCTGTGGGCTGCGTGGTAGAG
CTGGTCTTCAAGGTGGCCACAGGGGAGCTGAAGAATGGCTTTGCTGTGGTCCGCCCCCCT
GGACACCATGCGGAGGAGAGCACGCCCATGGGCTTTTGCTACTTCAACTCCGTGGCCGTG
GCAGCCAAGCTTCTGCAGCAGAGGTTGAGCGTGAGCAAGATCCTCATCGTGGACTGGGAC
GTGCACCATGGAAACGGGACCCAGCAGGCTTTCTACAGCGACCCTAGCGTCCTGTACATG
TCCCTCCACCGCTACGACGATGGGAACTTCTTCCCAGGCAGCGGGGCTCCTGATGAGGTG
GGCACAGGGCCCGGCGTGGGTTTCAACGTCAACATGGCTTTCACCGGCGGCCTGGACCCC
CCCATGGGAGACGCTGAGTACTTGGCGGCCTTCAGAACGGTGGTCATGCCGATCGCCAGC
GAGTTTGCCCCGGATGTGGTGCTGGTGTCATCAGGCTTCGATGCCGTGGAGGGCCACCCC
ACCCCTCTTGGGGGCTACAACCTCTCCGCCAGATGCTTCGGGTACCTGACGAAGCAGCTG
ATGGGCCTGGCTGGCGGCCGGATTGTCCTGGCCCTCGAGGGAGGCCACGACCTGACCGCC
ATTTGCGACGCCTCGGAAGCATGTGTTTCTGCCTTGCTGGGAAACGAGCTTGATCCTCTC
CCAGAAAAGGTTTTACAGCAAAGACCCAATGCAAACGCTGTCCGTTCCATGGAGAAAGTC
ATGGAGATCCACAGCAAGTACTGGCGCTGCCTGCAGCGCACAACCTCCACAGCGGGGCGT
TCTCTGATCGAGGCTCAGACTTGCGAGAACGAAGAAGCCGAGACGGTCACCGCCATGGCC
TCGCTGTCCGTGGGCGTGAAGCCCGCCGAAAAGAGACCAGATGAGGAGCCCATGGAAGAG
GAGCCGCCCCTGTAG
Enzyme 5 GenBank Gene ID AF132607 Link Image
Enzyme 5 GeneCard ID HDAC4 Link Image
Enzyme 5 GenAtlas ID HDAC4 Link Image
Enzyme 5 HGNC ID HGNC:14063 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 2q37.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
Enzyme 5 Metabolite References
  1. 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 Link Image]
Enzyme 6 [top]
Enzyme 6 ID 7741
Enzyme 6 Name Histone deacetylase 9
Enzyme 6 Synonyms
  1. HD9
  2. HD7B
  3. HD7
  4. Histone deacetylase-related protein
  5. 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 111298
Enzyme 6 Theoretical pI 6.88
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Isoform 3, called MITR/HDRP, 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 c-Jun phosphorylation by MAPK10 and by repressing c-Jun transcription via HDAC1 recruitment to c-Jun promoter
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 15590680 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9UKV0 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HDAC9_HUMAN Link Image
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 Link Image
Enzyme 6 GeneCard ID HDAC9 Link Image
Enzyme 6 GenAtlas ID HDAC9 Link Image
Enzyme 6 HGNC ID HGNC:14065 Link Image
Enzyme 6 Chromosome Location 7
Enzyme 6 Locus 7p21.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
Enzyme 6 Metabolite References
  1. 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 Link Image]
Enzyme 7 [top]
Enzyme 7 ID 7816
Enzyme 7 Name Histone deacetylase 1
Enzyme 7 Synonyms
  1. 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 55104
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
  • biopolymer metabolism
  • biopolymer modification
  • histone deacetylation
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid deacetylation
  • protein modification
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 7 General Function Chromatin structure and dynamics
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
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1277084 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q13547 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name HDAC1_HUMAN Link Image
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 Link Image
Enzyme 7 GeneCard ID HDAC1 Link Image
Enzyme 7 GenAtlas ID HDAC1 Link Image
Enzyme 7 HGNC ID HGNC:4852 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p34
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
  13. 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 Link Image]
  14. 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 Link Image]
  15. Ahringer J: NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 2000 Aug;16(8):351-6. [PubMed Link Image]
Enzyme 7 Metabolite References
  1. 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 Link Image]
Enzyme 8 [top]
Enzyme 8 ID 9777
Enzyme 8 Name Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
Enzyme 8 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 1
  2. Middle-chain acyl- CoA synthetase 1
  3. Butyrate--CoA ligase 1
  4. Butyryl coenzyme A synthetase 1
  5. Lipoate-activating enzyme
Enzyme 8 Gene Name ACSM1
Enzyme 8 Protein Sequence >Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM
Enzyme 8 Number of Residues 577
Enzyme 8 Molecular Weight 65274
Enzyme 8 Theoretical pI Not Available
Enzyme 8 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Lipid transport and metabolism
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 + Butyrate (n-C4:0) + Coenzyme A --> AMP + Butanoyl-CoA + Diphosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 15487302 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q08AH1 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ACSM1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AB059429 Link Image
Enzyme 8 GeneCard ID Not Available
Enzyme 8 GenAtlas ID ACSM1 Link Image
Enzyme 8 HGNC ID HGNC:18049 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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 Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 14011
Enzyme 9 Name Uncharacterized protein C10orf129
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name C10orf129
Enzyme 9 Protein Sequence >Uncharacterized protein C10orf129
VANEAMAPVVNSAVSDCPTLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMA
IFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGT
WFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCV
AAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIV
DENSNLLPPGEEGNIAIRIKLNQPASLYCPHMVSWEEYASARGHMLYLTGDRGIMDEDGY
FWWSGRVDDVANALGQRL
Enzyme 9 Number of Residues 318
Enzyme 9 Molecular Weight 35252
Enzyme 9 Theoretical pI 7.30
Enzyme 9 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Lipid transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 39645901 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q6P461 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q6P461_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >957 bp
GTGGCTAATGAAGCTATGGCCCCAGTTGTAAACTCTGCCGTGTCCGACTGCCCCACCTTG
AAAACCAAGCTCCTGGTGTCAGATAAGAGCTATGATGGGTGGTTGGATTTCAAGAAGTTG
ATTCAAGTTGCCCCTCCAAAGCAGACCTACATGAGGACCAAAAGCCAAGATCCAATGGCC
ATATTCTTCACCAAGGGTACAACAGGAGCTCCCAAAATGGTCGAGTATTCCCAGTATGGT
TTGGGAATGGGATTCAGCCAGGCTTCCAGACGGTGGATGGATCTCCAGCCAACAGATGTC
TTGTGGAGTCTGGGTGATGCCTTTGGTGGATCTTTATCCCTGAGCGCTGTCTTGGGAACT
TGGTTCCAAGGAGCCTGTGTGTTTCTGTGTCACATGCCAACCTTCTGCCCTGAGACTGTT
CTAAATGTCCTGTCCAGATTTCCCATCACCACTCTATCTGCAAATCCAGAGATGTACCAG
GAACTGCTTCAGCACAAGTGTTTCACCAGCTACAGATTCAAGAGTCTGAAGCAGTGTGTG
GCTGCAGGAGGACCCATCAGCCCTGGGGTGATTGAGGACTGGAAACGCATCACTAAGTTG
GACATCTATGAAGGCTATGGGCAGACGGAAACTGGTCTACTCTGTGCCACTTCCAAAACA
ATAAAATTGAAGCCAAGCTCTCTGGGGAAGCCATTGCCACCTTATATTGTCCAGATTGTG
GATGAAAACTCAAATCTCCTGCCTCCAGGGGAAGAAGGAAATATTGCAATCCGCATAAAA
CTAAACCAACCTGCTTCTCTGTACTGTCCACACATGGTGAGCTGGGAGGAATATGCTTCA
GCAAGAGGCCACATGCTTTACCTCACAGGTGACAGAGGGATCATGGATGAAGACGGCTAC
TTCTGGTGGTCTGGTAGAGTTGATGATGTTGCCAATGCATTGGGTCAGAGATTGTGA
Enzyme 9 GenBank Gene ID BC063654 Link Image
Enzyme 9 GeneCard ID Q6P461 Link Image
Enzyme 9 GenAtlas ID ACSM6 Link Image
Enzyme 9 HGNC ID HGNC:31665 Link Image
Enzyme 9 Chromosome Location 10
Enzyme 9 Locus 10q23.33
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 14420
Enzyme 10 Name Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor
Enzyme 10 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 2A
  2. Middle-chain acyl-CoA synthetase 2A
  3. Butyrate--CoA ligase 2A
  4. Butyryl coenzyme A synthetase 2A
Enzyme 10 Gene Name ACSM2A
Enzyme 10 Protein Sequence >Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ
Enzyme 10 Number of Residues 577
Enzyme 10 Molecular Weight 64225
Enzyme 10 Theoretical pI 8.05
Enzyme 10 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Lipid transport and metabolism
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] ALL_REAC R00389 > R01176
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-19
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 115528937 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q08AH3 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name ACS2A_HUMAN Link Image
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 BC125176 Link Image
Enzyme 10 GeneCard ID Q08AH3 Link Image
Enzyme 10 GenAtlas ID ACSM2A Link Image
Enzyme 10 HGNC ID HGNC:32017 Link Image
Enzyme 10 Chromosome Location 16
Enzyme 10 Locus 16p12.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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 Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 14421
Enzyme 11 Name Acyl-coenzyme A synthetase ACSM2B, mitochondrial precursor
Enzyme 11 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 2B
  2. Middle-chain acyl-CoA synthetase 2B
  3. Butyrate--CoA ligase 2B
  4. Butyryl coenzyme A synthetase 2B
  5. Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A
Enzyme 11 Gene Name ACSM2B
Enzyme 11 Protein Sequence >Acyl-coenzyme A synthetase ACSM2B, mitochondrial precursor
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVMLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKARAQ
Enzyme 11 Number of Residues 577
Enzyme 11 Molecular Weight 64258
Enzyme 11 Theoretical pI 8.38
Enzyme 11 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 11 General Function Lipid transport and metabolism
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] ALL_REAC R00389 > R01176
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-19
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 27651993 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q68CK6 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ACS2B_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1734 bp
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTG
CCGGCCAAGTTTAACCTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGATGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCATTATGCCTGAAACCATCCAGATG
AAATCCGCTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGCGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGGGCTCACTTTTGGAATCTTGGACATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCTATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCCTCGCTGGAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATTC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGGTTATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGAAAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGAAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGATACTGGCCTCGCAGTTCCTATCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
ACCAAACTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
Enzyme 11 GenBank Gene ID AY160217 Link Image
Enzyme 11 GeneCard ID Q68CK6 Link Image
Enzyme 11 GenAtlas ID ACSM2B Link Image
Enzyme 11 HGNC ID HGNC:30931 Link Image
Enzyme 11 Chromosome Location 16
Enzyme 11 Locus 16p12.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 14422
Enzyme 12 Name Acyl-coenzyme A synthetase ACSM3, mitochondrial precursor
Enzyme 12 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 3
  2. Middle-chain acyl- CoA synthetase 3
  3. Butyrate--CoA ligase 3
  4. Butyryl coenzyme A synthetase 3
  5. Protein SA homolog
Enzyme 12 Gene Name ACSM3
Enzyme 12 Protein Sequence >Acyl-coenzyme A synthetase ACSM3, mitochondrial precursor
MLARVTRKMLRHAKCFQRLAIFGSVRALHKDNRTATPQNFSNYESMKQDFKLGIPEYFNF
AKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRG
DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPA
VDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG
YPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFT
HHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDV
TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPG
QEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDV
ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIK
EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKTI
Enzyme 12 Number of Residues 586
Enzyme 12 Molecular Weight 66153
Enzyme 12 Theoretical pI 9.45
Enzyme 12 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Lipid transport and metabolism
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] ALL_REAC R00389 > R01176
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 666014 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q53FZ2 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ACSM3_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1737 bp
ATGCTACGTCATGCCAAGTGTTTTCAGCGCCTAGCAATTTTTGGTTCTGTGAGGGCACTG
CATAAAGATAATAGAACAGCAACCCCTCAGAATTTCTCCAACTATGAATCCATGAAACAG
GACTTCAAACTGGGGATTCCAGAGTATTTCAACTTTGCTAAAGATGTCCTGGACCAATGG
ACTGATAAGGAAAAGGCTGGAAAGAAACCTTCAAATCCAGCCTTCTGGTGGATCAACAGA
AATGGAGAAGAGATGCGATGGAGTTTTGAGGAACTGGGATCTCTGTCCAGAAAATTTGCC
AATATACTTTCAGAAGCCTGTTCCCTACAAAGAGGAGATCGGGTAATTCTGATTCTGCCC
AGGGTCCCGAGATGGTGGCTTGCAAATGTGGCCTGTCTGCGAACAGGGACAGTTTTAATT
CCAGGAACCACTCAGCTGACCCAGAAAGACATTCTCTACAGACTACAATCTTCAAAAGCA
AACTGCATTATCACCAATGATGTTTTAGCCCCAGCAGTAGACGCTGTTGCATCCAAATGT
GAAAATCTGCACTCCAAGCTGATTGTATCAGAGAACTCCAGAGAGGGGTGGGGGAACCTC
AAGGAGTTGATGAAACATGCCAGTGACAGCCACACCTGTGTGAAGACAAAACACAATGAG
ATCATGGCCATATTCTTTACCAGTGCAACAAGTGGATATCCGAAAATGTCTGCACACACC
CACAGCAGTTTTGGTTTAGGTTTATCTGTAAATGGAAGGTTCTGGCTAGATTTGACACCC
TCAGATGTGATGTGGAATACCTCAGATACGGGCTGGGCAAAGTCTGCATGGAGTAGTGTT
TTTTCTCCGTGGATCCAGGGAGCATGTGTATTCACACACCATTTACCCCGTTTTGAGCCG
ACTTCTATCTTGCAAACACTCTCCAAGTACCCCATCACAGTCTTCTGTTCAGCACCAACT
GTATACCGAATGCTTGTACAGAATGATATAACCAGCTATAAGTTTAAAAGCTTAAAGCAC
TGTGTGAGTGCTGGGGAACCAATTACCCCTGACGTGACTGAAAAATGGAGAAACAAGACG
GGCCTGGATATCTACGAAGGATATGGACAGACTGAAACGGTGCTAATCTGTGGAAATTTT
AAGGGAATGAAAATTAAACCTGGCTCAATGGGAAAACCTTCTCCTGCTTTCGATGTTAAG
ATTGTAGATGTAAATGGCAATGTTCTACCTCCTGGACAAGAAGGAGATATTGGCATTCAA
GTTCTACCCAACCGACCATTTGGCCTTTTTACTCATTACGTAGATAATCCTTCAAAAACA
GCTTCAACTCTACGAGGCAATTTCTATATCACTGGGGACAGAGCATATATGGATAAAGAT
GGGTATTTCTGGTTTGTTGCAAGAGCAGATGATGTCATATTATCCTCTGGCTATCGAATT
GGACCATTTGAGGTAGAAAATGCCCTGAATGAACACCCTTCAGTTGCAGAGTCAGCTGTT
GTCAGCAGCCCAGACCCCATCAGAGGAGAGGTAGTAAAGGCTTTTGTCGTTCTAAATCCT
GATTACAAGTCACATGATCAAGAACAACTAATAAAGGAGATTCAGGAGCATGTTAAAAAA
ACTACAGCACCTTACAAATATCCCAGAAAGGTAGAATTTATTCAAGAGCTGCCAAAGACT
GTCAGTGGGAAGACAAAAAGAAATGAACTGAGGAAGAAAGAATGGAAGACAATTTAA
Enzyme 12 GenBank Gene ID D16350 Link Image
Enzyme 12 GeneCard ID Q53FZ2 Link Image
Enzyme 12 GenAtlas ID ACSM3 Link Image
Enzyme 12 HGNC ID HGNC:10522 Link Image
Enzyme 12 Chromosome Location 16
Enzyme 12 Locus 16p13.11
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 14424
Enzyme 13 Name Acyl-coenzyme A synthetase ACSM5, mitochondrial precursor
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name ACSM5
Enzyme 13 Protein Sequence >Acyl-coenzyme A synthetase ACSM5, mitochondrial precursor
MRPWLRHLVLQALRNSRAFCGSHGKPAPLPVPQKIVATWEAISLGRQLVPEYFNFAHDVL
DVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMML
VLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIS
AECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMV
EHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV
DAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH
QTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVA
VRIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSY
RIGPVEVESALAEHPAVLESAAVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHV
KRVTAPYKYPRKVAFVSELPKTVSGKIQRSKLRSQEWGK
Enzyme 13 Number of Residues 579
Enzyme 13 Molecular Weight 64733
Enzyme 13 Theoretical pI 8.52
Enzyme 13 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 13 General Function Lipid transport and metabolism
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] ALL_REAC R00389 > R01176
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 7020785 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q6NUN0 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ACSM5_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1716 bp
ATGAGACCATGGCTGAGACACCTAGTCCTCCAGGCACTGAGGAACTCCAGGGCATTCTGT
GGGTCTCATGGGAAGCCAGCACCTCTACCTGTTCCTCAGAAGATCGTGGCCACCTGGGAA
GCCATCAGCCTGGGAAGGCAGCTGGTGCCTGAGTACTTCAACTTCGCCCATGATGTGCTG
GATGTGTGGAGTCGGCTGGAAGAGGCTGGACACCGCCCCCCAAATCCTGCCTTCTGGTGG
GTCAATGGCACAGGAGCAGAGATCAAGTGGAGCTTTGAGGAGCTGGGGAAGCAGTCCAGG
AAGGCAGCCAATGTGCTGGGGGGTGCATGCGGCCTGCAGCCTGGGGACAGAATGATGCTG
GTACTCCCACGGCTCCCGGAGTGGTGGCTGGTCAGTGTGGCTTGCATGCGGACAGGGACT
GTGATGATTCCGGGTGTGACTCAGCTGACAGAGAAGGACCTCAAGTACCGGCTGCAGGCG
TCCAGGGCCAAGTCCATTATCACCAGTGACTCCCTAGCTCCAAGGGTGGATGCCATCAGT
GCCGAATGCCCCTCCCTCCAGACCAAGCTGCTGGTGTCAGACAGCAGTCGGCCAGGCTGG
TTGAACTTCAGGGAACTCCTCCGGGAGGCTTCTACAGAGCACAACTGCATGAGGACAAAG
AGTCGAGACCCGCTGGCCATCTACTTTACCAAGCGGGAACCACCGGGGGCCCCCAAGATG
GTCGAGCACTCCCAGAGCAGCTACGGACTGGGTTTTGTGGCCAGCGGAAGACGGTGGGTG
GCCTTGACCGAATCTGACATCTTCTGGAACACGACTGACACTGGCTGGGTGAAGGCAGCC
TGGACTCTCTTCTCTGCCTGGCCTAATGGATCTTGCATTTTTGTGCATGAGCTGCCCCGA
GTTGATGCCAAAGTTATCCTGAATACTCTCTCCAAATTCCCGATAACCACCCTCTGCTGT
GTCCCAACCATCTTTCGGCTGCTTGTGCAGGAGGATCTGACCAGGTACCAGTTTCAGAGC
TTGAGGCACTGTCTGACCGGAGGAGAGGCCCTCAACCCTGACGTGAGGGAGAAGTGGAAA
CACCAGACTGGTGTGGAGCTGTACGAAGGCTATGGCCAGTCTGAAACGGTTGTCATCTGT
GCCAATCCAAAAGGCATGAAAATCAAGTCTGGATCCATGGGGAAGGCGTCCCCACCCTAC
GATGTGCAGATTGTGGATGATGAGGGCAACGTCCTGCCTCCTGGAGAAGAGGGGAATGTT
GCTGTCCGTATCAGACCCACTCGGCCCTTCTGTTTCTTCAATTGCTATTTGGACAATCCT
GAGAAGACAGCTGCATCAGAACAAGGGGACTTTTACATCACAGGGGACCGAGCTCGCATG
GACAAGGATGGCTACTTTTGGTTCATGGGAAGAAACGACGATGTGATCAATTCTTCAAGC
TACCGGATCGGGCCTGTTGAAGTGGAAAGTGCCCTGGCAGAGCATCCTGCTGTCCTGGAG
TCGGCTGTGGTCAGCAGCCCAGACCCCATCAGGGGAGAGGTGGTAAAGGCATTTATAGTC
CTTACTCCAGCCTACTCCTCTCATGACCCAGAGGCACTAACGCGGGAACTCCAGGAGCAT
GTGAAAAGGGTGACTGCTCCATACAAATACCCCAGGAAGGTGGCCTTTGTTTCAGAACTT
GCCAAAGACGGTTTCTGGAAAGATCCAAAGGAGTAA
Enzyme 13 GenBank Gene ID AK000588 Link Image
Enzyme 13 GeneCard ID Q6NUN0 Link Image
Enzyme 13 GenAtlas ID ACSM5 Link Image
Enzyme 13 HGNC ID HGNC:26060 Link Image
Enzyme 13 Chromosome Location 16
Enzyme 13 Locus 16p12.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 14850
Enzyme 14 Name Coenzyme A transferase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 Protein Sequence >Coenzyme A transferase
MDQVAKNLLAARVARDIPNGSYVNLGIGLPTLVANHLPRHREIILHSENGVLGQWSAAEP
GQEDPDLINAGKEPVRLEKGAAFFHHADAFGMMRGGHLDICVLGAFQVSGHGDLANWHTG
DPDAIPAVGGAMDLAIGARRVFVMMDHMTRDGASKLRRQCSYPLTGLACVSRVYTELGTF
AIGPQGVAVIEIIGDMSPQALQSVTDVELDFTTLATAELA
Enzyme 14 Number of Residues 220
Enzyme 14 Molecular Weight 23416
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
  • metabolism
  • physiological process
Component
Enzyme 14 General Function Lipid transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
Enzyme 14 Reactions
  • succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA [RN:R02990] ALL_REAC R02990
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID Q471R1 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q471R1_RALEJ Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID CP000090 Link Image
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 Not Available
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
  1. 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 55365
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
  • biopolymer metabolism
  • biopolymer modification
  • histone deacetylation
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid deacetylation
  • protein modification
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 15 General Function Chromatin structure and dynamics
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
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 1667394 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q92769 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name HDAC2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1467 bp
ATGGCGTACAGTCAAGGAGGCGGCAAAAAAAAAGTCTGCTACTACTACGACGGTGATATT
GGAAATTATTATTATGGACAGGGTCATCCCATGAAGCCTCATAGAATCCGCATGACCCAT
AACTTGCTGTTAAATTATGGCTTATACAGAAAAATGGAAATATATAGGCCCCATAAAGCC
ACTGCCGAAGAAATGACAAAATATCACAGTGATGAGTATATCAAATTTCTACGGTCAATA
AGACCAGATAACATGTCTGAGTATAGTAAGCAGATGCATATATTTAATGTTGGAGAAGAT
TGTCCAGCGTTTGATGGACTCTTTGAGTTTTGTCAGCTCTCAACTGGCGGTTCAGTTGCT
GGAGCTGTGAAGTTAAACCGACAACAGACTGATATGGCTGTTAATTGGGCTGGAGGATTA
CATCATGCTAAGAAATACGAAGCATCAGGATTCTGTTACGTTAATGATATTGTGCTTGCC
ATCCTTGAATTACTAAAGTATCATCAGAGAGTCTTATATATTGATATAGATATTCATCAT
GGTGATGGTGTTGAAGAAGCTTTTTATACAACAGATCGTGTAATGACGGTATCATTCCAT
AAATATGGGGAATACTTTCCTGGCACAGGAGACTTGAGGGATATTGGTGCTGGAAAAGGC
AAATACTATGCTGTCAATTTTCCAATGTGTGATGGTATAGATGATGAGTCATATGGGCAG
ATATTTAAGCCTATTATCTCAAAGGTGATGGAGATGTATCAACCTAGTGCTGTGGTATTA
CAGTGTGGTGCAGACTCATTATCTGGTGATAGACTGGGTTGTTTCAATCTAACAGTCAAA
GGTCATGCTAAATGTGTAGAAGTTGTAAAAACTTTTAACTTACCATTACTGATGCTTGGA
GGAGGTGGCTACACAATCCGTAATGTTGCTCGATGTTGGACATATGAGACTGCAGTTGCC
CTTGATTGTGAGATTCCCAATGAGTTGCCATATAATGATTACTTTGAGTATTTTGGACCA
GACTTCAAACTGCATATTAGTCCTTCAAACATGACAAACCAGAACACTCCAGAATATATG
GAAAAGATAAAACAGCGTTTGTTTGAAAATTTGCGCATGTTACCTCATGCACCTGGTGTC
CAGATGCAAGCTATTCCAGAAGATGCTGTTCATGAAGACAGTGGAGATGAAGATGGAGAA
GATCCAGACAAGAGAATTTCTATTCGAGCATCAGACAAGCGGATAGCTTGTGATGAAGAA
TTCTCAGATTCTGAGGATGAAGGAGAAGGAGGTCGAAGAAATGTGGCTGATCATAAGAAA
GGAGCAAAGAAAGCTAGAATTGAAGAAGATAAGAAAGAAACAGAGGACAAAAAAACAGAC
GTTAAGGAAGAAGATAAATCCAAGGACAACAGTGGTGAAAAAACAGATACCAAAGGAACC
AAATCAGAACAGCTCAGCAACCCCTGA
Enzyme 15 GenBank Gene ID U31814 Link Image
Enzyme 15 GeneCard ID Q92769 Link Image
Enzyme 15 GenAtlas ID HDAC2 Link Image
Enzyme 15 HGNC ID HGNC:4853 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. Ahringer J: NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 2000 Aug;16(8):351-6. [PubMed Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
Enzyme 15 Metabolite References
  1. 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 Link Image]
Enzyme 16 [top]
Enzyme 16 ID 14852
Enzyme 16 Name Histone deacetylase 3
Enzyme 16 Synonyms
  1. HD3
  2. RPD3-2
  3. 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 48848
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
  • biopolymer metabolism
  • biopolymer modification
  • histone deacetylation
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid deacetylation
  • protein modification
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 16 General Function Chromatin structure and dynamics
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 Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 2326173 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O15379 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name HDAC3_HUMAN Link Image
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 Link Image
Enzyme 16 GeneCard ID O15379 Link Image
Enzyme 16 GenAtlas ID HDAC3 Link Image
Enzyme 16 HGNC ID HGNC:4854 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
  13. 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 Link Image]
  14. 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 Link Image]
Enzyme 16 Metabolite References
  1. 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 Link Image]
Enzyme 17 [top]
Enzyme 17 ID 14853
Enzyme 17 Name Histone deacetylase 5
Enzyme 17 Synonyms
  1. HD5
  2. 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
LPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEEDGEEEED
CIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQ
SSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQE
TGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLP
CGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAM
GFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNF
FPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVS
AGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVS
ALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGET
EEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL
Enzyme 17 Number of Residues 1122
Enzyme 17 Molecular Weight 121993
Enzyme 17 Theoretical pI 6.19
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
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 Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 4754909 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9UQL6 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name HDAC5_HUMAN Link Image
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
AGCACACAGGAAGACCTGGAGGAGGAGGACGAGGAAGAGGATGGGGAGGAGGAGGAGGAT
TGCATCCAGGTTAAGGACGAGGAGGGCGAGAGTGGTGCTGAGGAGGGGCCCGACTTGGAG
GAGCCTGGTGCTGGATACAAAAAACTGTTCTCAGATGCCCAGCCGCTGCAGCCTTTGCAG
GTGTACCAGGCGCCCCTCAGCCTGGCCACTGTGCCCCACCAGGCCCTGGGCCGTACCCAG
TCCTCCCCTGCTGCCCCTGGGGGCATGAAGAGCCCCCCAGACCAGCCCGTCAAGCACCTC
TTCACCACAGGTGTGGTCTACGACACGTTCATGCTAAAGCACCAGTGCATGTGCGGGAAC
ACACACGTGCACCCTGAGCATGCTGGCCGGATCCAGAGCATCTGGTCCCGGCTGCAGGAG
ACAGGCCTGCTTAGCAAGTGCGAGCGGATCCGAGGTCGCAAAGCCACGCTAGATGAGATC
CAGACAGTGCACTCTGAATACCACACCCTGCTCTATGGGACCAGTCCCCTCAACCGGCAG
AAGCTAGACAGCAAGAAGTTGCTCGGCCCCATCAGCCAGAAGATGTATGCTGTGCTGCCT
TGTGGGGGCATCGGGGTGGACAGTGACACCGTGTGGAATGAGATGCACTCCTCCAGTGCT
GTGCGCATGGCAGTGGGCTGCCTGCTGGAGCTGGCCTTCAAGGTGGCTGCAGGAGAGCTC
AAGAATGGATTTGCCATCATCCGGCCCCCAGGACACCACGCCGAGGAATCCACAGCCATG
GGATTCTGCTTCTTCAACTCTGTAGCCATCACCGCAAAACTCCTACAGCAGAAGTTGAAC
GTGGGCAAGGTCCTCATCGTGGACTGGGACATTCACCATGGCAATGGCACCCAGCAGGCG
TTCTATAATGACCCCTCTGTGCTCTACATCTCTCTGCATCGCTATGACAACGGGAACTTC
TTTCCAGGCTCTGGGGCTCCTGAAGAGGTTGGTGGAGGACCAGGCGTGGGGTACAATGTG
AACGTGGCATGGACAGGAGGTGTGGACCCCCCCATTGGAGACGTGGAGTACCTTACAGCC
TTCAGGACAGTGGTGATGCCCATTGCCCACGAGTTCTCACCTGATGTGGTCCTAGTCTCC
GCCGGGTTTGATGCTGTTGAAGGACATCTGTCTCCTCTGGGTGGCTACTCTGTCACCGCC
AGATGTTTTGGCCACTTGACCAGGCAGCTGATGACCCTGGCAGGGGGCCGGGTGGTGCTG
GCCCTGGAGGGAGGCCATGACTTGACCGCCATCTGTGATGCCTCTGAGGCTTGTGTCTCG
GCTCTGCTCAGTGTAGAGCTGCAGCCCTTGGATGAGGCAGTCTTGCAGCAAAAGCCCAAC
ATCAACGCAGTGGCCACGCTAGAGAAAGTCATCGAGATCCAGAGCAAACACTGGAGCTGT
GTGCAGAAGTTCGCCGCTGGTCTGGGCCGGTCCCTGCGAGAGGCCCAAGCAGGTGAGACC
GAGGAGGCCGAGACTGTGAGCGCCATGGCCTTGCTGTCGGTGGGGGCCGAGCAGGCCCAG
GCTGCGGCAGCCCGGGAACACAGCCCCAGGCCGGCAGAGGAGCCCATGGAGCAGGAGCCT
GCCCTGTGA
Enzyme 17 GenBank Gene ID AF132608 Link Image
Enzyme 17 GeneCard ID Q9UQL6 Link Image
Enzyme 17 GenAtlas ID HDAC5 Link Image
Enzyme 17 HGNC ID HGNC:14068 Link Image
Enzyme 17 Chromosome Location 17
Enzyme 17 Locus 17q21
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
Enzyme 17 Metabolite References
  1. 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 Link Image]
Enzyme 18 [top]
Enzyme 18 ID 14869
Enzyme 18 Name Not Available
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name ACSM4
Enzyme 18 Protein Sequence >MKIFFRYQTFRFIWLTKPPGRRLHKDHQLWTPLTLADFEAINRCNRPLPKNFNFAADVLDQWSQKEKTGE
RPANPALWWVNGKGDEVKWSFRELGSLSRKAANVLTKPCGLQRGDRLAVILPRIPEWWLV
NVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLL
VSPQSWNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGF
TLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLT
TYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRVQTGLELYEGY
GQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFC
FFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESA
LIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHVKKSTAPYKYP
RKVEFVQELPKTITGKIKRNVLRDQEWRGR
Enzyme 18 Number of Residues 580
Enzyme 18 Molecular Weight 65703
Enzyme 18 Theoretical pI 8.76
Enzyme 18 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Lipid transport and metabolism
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 Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID P0C7M7 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name ACSM4_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AC131205 Link Image
Enzyme 18 GeneCard ID P0C7M7 Link Image
Enzyme 18 GenAtlas ID ACSM4 Link Image
Enzyme 18 HGNC ID HGNC:32016 Link Image
Enzyme 18 Chromosome Location 12
Enzyme 18 Locus 12p13.31
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available