We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Acrylyl-CoA (HMDB02307)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:47
Update Date 2009-05-05 20:59:22
Accession Number HMDB02307
Secondary Accession Numbers HMDB06507
Common Name Acrylyl-CoA
Description Acrylyl-CoA is involved in alternative pathways of propionate metabolism.
Synonyms
  1. Acryloyl coenzyme A
  2. Acryloyl-CoA
  3. Acrylyl coenzyme A
  4. Acrylyl-CoA
  5. Coenzyme A S-2-propenoate
  6. Coenzyme A S-acrylate
  7. Thioacrylic acid S-ester with coenzyme A
  8. Propenoyl-coa
  9. Acryloyl-Coenzyme A
  10. Acrylyl-Coenzyme A
  11. CoA S-2-propenoate
  12. CoA S-acrylate
  13. Coenzyme A S-2-propenoic acid
  14. CoA S-2-propenoic acid
Chemical IUPAC Name S-[2-[3-[[4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethyl] prop-2-enethioate
Chemical Formula C24H38N7O17P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Short chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • alkene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Lipid biosynthesis, Fatty acid transport
Application
Source
  • Endogenous
Average Molecular Weight 821.581
Monoisotopic Molecular Weight 821.125793
Isomeric SMILES CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12)C(O)C(=O)NCCC(=O)NCCSC(=O)C=C
Canonical SMILES CC(C)(COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12)C(O)C(=O)NCCC(=O)NCCSC(=O)C=C
KEGG Compound ID C00894 Link Image
BioCyc ID ACRYLYL-COA Link Image
BiGG ID 36320 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB02307 Link Image
Metagene Link HMDB02307 Link Image
METLIN ID 446 Link Image
PubChem Compound 439340 Link Image
PubChem Substance 4150 Link Image
ChEBI ID 15513 Link Image
CAS Registry Number 5776-58-9
InChI Identifier InChI=1/C24H38N7O17P3S/c1-4-15(33)52-8-7-26-14(32)5-6-27-22(36)19(35)24(2,3)10-45-51(42,43)48-50(40,41)44-9-13-18(47-49(37,38)39)17(34)23(46-13)31-12-30-16-20(25)28-11-29-21(16)31/h4,11-13,17-19,23,34-35H,1,5-10H2,2-3H3,(H,26,32)(H,27,36)(H,40,41)(H,42,43)(H2,25,28,29)(H2,37,38,39)/t13-,17-,18-,19?,23-/m1/s1
Synthesis Reference Symes, Kenneth Charles; Collier, Simon Andrew; Armitage, Yvonne Christine; Mistry, Rajesh; Baranyai, Robert. Biocatalytic manufacturing of (meth)acrylic esters. PCT Int. Appl. (2007), 40pp. CODEN: PIXXD2 WO 2007039415 A1 20070412 CAN 146:400675 AN 2007:409912
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.22 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -5.8 [Predicted by PubChem via XLOGP]; -0.49 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
General References
  1. OMMBID: http://genetics.accessmedicine.com/server-java/Arknoid/amed/mmbid/co_chapters/ch094/ch094_p03.html
Metabolic Enzymes
  1. 3-ketoacyl-CoA thiolase, mitochondrial
  2. 3-ketoacyl-CoA thiolase, peroxisomal
  3. Trifunctional enzyme subunit beta, mitochondrial
  4. Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
  5. Long-chain specific acyl-CoA dehydrogenase, mitochondrial
  6. Short-chain specific acyl-CoA dehydrogenase, mitochondrial
  7. Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
  8. Peroxisomal acyl-coenzyme A oxidase 1
  9. Peroxisomal acyl-coenzyme A oxidase 2
  10. Isovaleryl-CoA dehydrogenase, mitochondrial
  11. Peroxisomal acyl-coenzyme A oxidase 3
  12. Glutaryl-CoA dehydrogenase, mitochondrial
  13. Hepatic triacylglycerol lipase
  14. Diacylglycerol O-acyltransferase 1
  15. 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
  16. 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
  17. Acyl-CoA desaturase
  18. Peroxisomal bifunctional enzyme
  19. Enoyl-CoA hydratase, mitochondrial
  20. Trifunctional enzyme subunit alpha, mitochondrial
  21. Sterol O-acyltransferase 2
  22. Sterol O-acyltransferase 1
  23. Bile acid-CoA:amino acid N-acyltransferase
  24. Long-chain-fatty-acid--CoA ligase 4
  25. Long-chain-fatty-acid--CoA ligase 1
  26. Long-chain-fatty-acid--CoA ligase 6
  27. Long-chain-fatty-acid--CoA ligase 5
  28. Long-chain-fatty-acid--CoA ligase 3
  29. Glycerol-3-phosphate acyltransferase 1, mitochondrial
  30. Trans-2-enoyl-CoA reductase, mitochondrial
  31. Peroxisomal trans-2-enoyl-CoA reductase
  32. Cytosolic acyl coenzyme A thioester hydrolase
  33. Acyl-coenzyme A thioesterase 2, mitochondrial
  34. Acyl-coenzyme A thioesterase 4
  35. Acyl-coenzyme A thioesterase 8
  36. Dihydroxyacetone phosphate acyltransferase
  37. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
  38. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
  39. 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
  40. Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
  41. Very long-chain acyl-CoA synthetase
  42. Peroxisome proliferator-activated receptor gamma
  43. Peroxisome proliferator-activated receptor alpha
  44. Peroxisome proliferator-activated receptor delta
  45. Acyl-CoA-binding protein
  46. Fatty acid-binding protein, heart
  47. 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
  48. Bile acyl-CoA synthetase
  49. Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
  50. 2-acylglycerol O-acyltransferase 2
  51. Long-chain fatty acid transport protein 3
  52. Long-chain fatty acid transport protein 1
  53. Acyl-CoA dehydrogenase family member 10
  54. Acyl-CoA dehydrogenase family member 11
  55. Glycerol-3-phosphate acyltransferase 4
  56. Acyl-coenzyme A synthetase ACSM1, mitochondrial
  57. Diacylglycerol O-acyltransferase 2
  58. 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
  59. 2-acylglycerol O-acyltransferase 1
  60. Isobutyryl-CoA dehydrogenase, mitochondrial
  61. Acyl-CoA dehydrogenase family member 9, mitochondrial
  62. Long-chain fatty acid transport protein 4
  63. Fatty acyl-CoA reductase 1
  64. Fatty acyl-CoA reductase 2
  65. Acyl-CoA wax alcohol acyltransferase 1
  66. Acyl-CoA wax alcohol acyltransferase 2
  67. Diacylglycerol O-acyltransferase 2-like protein 6
  68. Putative diacylglycerol O-acyltransferase 2-like protein 7
  69. 2-acylglycerol O-acyltransferase 3
  70. Lysophospholipid acyltransferase 5
  71. Lysophosphatidylcholine acyltransferase 1
  72. Lysocardiolipin acyltransferase 1
  73. Lysophospholipid acyltransferase LPCAT4
  74. Glycerol-3-phosphate acyltransferase 3
  75. Glycine N-acyltransferase
  76. Glycine N-acyltransferase-like protein 1
  77. Glycine N-acyltransferase-like protein 2
  78. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
  79. Putative uncharacterized protein
  80. Peroxisomal 3,2-trans-enoyl-CoA isomerase
  81. Acyl-CoA synthetase family member 4
  82. Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
  83. Acyl-coenzyme A oxidase-like protein
  84. Acyl-coenzyme A synthetase ACSM6, mitochondrial
  85. Acyl-coenzyme A synthetase ACSM2A, mitochondrial
  86. Acyl-coenzyme A synthetase ACSM2B, mitochondrial
  87. Acyl-coenzyme A synthetase ACSM3, mitochondrial
  88. Acyl-coenzyme A synthetase ACSM5, mitochondrial
  89. Peroxisomal coenzyme A diphosphatase NUDT7
  90. Acyl-coenzyme A synthetase ACSM4, mitochondrial
  91. Glycerol-3-phosphate acyltransferase 2, mitochondrial
  92. Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
  93. cDNA FLJ56683, highly similar to Peroxisomal 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8)
  94. Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
  95. Nef-associated protein 1
  96. Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
  97. Acyl-coenzyme A thioesterase 9, mitochondrial
  98. Acyl-CoA synthetase family member 3, mitochondrial
  99. Acyl-coenzyme A thioesterase 1
  100. Cytosolic acyl coenzyme A thioester hydrolase-like
  101. Acyl-CoA synthetase family member 2, mitochondrial
  102. Acyl-coenzyme A thioesterase 11
  103. Long-chain-fatty-acid--CoA ligase ACSBG2
  104. Long-chain-fatty-acid--CoA ligase ACSBG1
  105. Golgi resident protein GCP60
  106. Acyl-CoA-binding domain-containing protein 4
  107. Not Available
  108. cDNA, FLJ94802
  109. Acyl-CoA-binding domain-containing protein 5
  110. Not Available
  111. ACAD11 protein
  112. Putative uncharacterized protein HADHA
  113. KIAA1996 protein
  114. Benzodiazepine receptor ligand
  115. Not Available
  116. Putative uncharacterized protein HADHA
  117. Acyl-CoA-binding domain-containing protein 6
  118. Not Available
  119. PECI protein
  120. cDNA FLJ53969, highly similar to Trifunctional enzyme subunit alpha, mitochondrial
  121. Acyl-Coenzyme A binding domain containing 5
  122. Acyl-Coenzyme A binding domain containing 5, isoform CRA_a
  123. cDNA FLJ50016, highly similar to Acyl-CoA-binding domain-containing protein 4
  124. Acyl-CoA-binding domain-containing protein 7
  125. Fatty acid-binding protein, intestinal
Enzyme 1 [top]
Enzyme 1 ID 5260
Enzyme 1 Name 3-ketoacyl-CoA thiolase, mitochondrial
Enzyme 1 Synonyms
  1. Acetyl-CoA acyltransferase
  2. Beta-ketothiolase
  3. Mitochondrial 3-oxoacyl-CoA thiolase
  4. T1
Enzyme 1 Gene Name ACAA2
Enzyme 1 Protein Sequence >3-ketoacyl-CoA thiolase, mitochondrial
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Enzyme 1 Number of Residues 397
Enzyme 1 Molecular Weight 41923.8
Enzyme 1 Theoretical pI 8.21
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 1 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 1 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 12804931 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P42765 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name THIM_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1194 bp
ATGGCTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTGCTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
Enzyme 1 GenBank Gene ID BC001918 Link Image
Enzyme 1 GeneCard ID ACAA2 Link Image
Enzyme 1 GenAtlas ID ACAA2 Link Image
Enzyme 1 HGNC ID HGNC:83 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 18q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5274
Enzyme 2 Name 3-ketoacyl-CoA thiolase, peroxisomal
Enzyme 2 Synonyms
  1. Acetyl-CoA acyltransferase
  2. Beta-ketothiolase
  3. Peroxisomal 3-oxoacyl-CoA thiolase
Enzyme 2 Gene Name ACAA1
Enzyme 2 Protein Sequence >3-ketoacyl-CoA thiolase, peroxisomal
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIP
MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSI
TVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPI
LGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLR
LPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFE
YPGN
Enzyme 2 Number of Residues 424
Enzyme 2 Molecular Weight 44291.6
Enzyme 2 Theoretical pI 8.55
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 2 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 2 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 2 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 23874 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09110 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name THIK_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1275 bp
ATGCAGAGGCTGCAGGTAGTGCTGGGCCACCTGAGGGGTCCGGCCGATTCCGGCTGGATG
CCGCAGGCCGCGCCTTGCCTGAGCGGTGCCCCGCAGGCCTCGGCCGCGGACGTGGTGGTG
GTGCACGGGCGGCGCACGGCCATCTGCCGGGCGGGCCGCGGCGGCTTCAAGGACACCACC
CCCGACGAGCTTCTCTCGGCAGTCATGACCGCGGTTCTCAAGGACGTGAATCTGAGGCCG
GAACAGCTGGGGGACATCTGTGTCGGAAATGTGCTGCAGCCTGGGGCCGGGGCAATCATG
GCCCGAATCGCCCAGTTTCTGAGTGACATCCCGGAGACTGTGCCTTTGTCCACTGTCAAT
AGACAGTGCTCGTCGGGGCTACAGGCAGTGGCCAGCATAGCAGGTGGCATCAGAAATGGG
TCTTATGACATTGGCATGGCCTGTGGGGTGGAGTCCATGTCCCTGGCTGACAGAGGGAAC
CCTGGAAATATTACTTCGCGCTTGATGGAGAAGGAGAAGGCCAGAGATTGCCTGATTCCT
ATGGGGATAACCTCTGAGAATGTGGCTGAGCGGTTTGGCATTTCACGGGAGAAGCAGGAT
ACCTTTGCCCTGGCTTCCCAGCAGAAGGCAGCAAGAGCCCAGAGCAAGGGCTGTTTCCAA
GCTGAGATTGTGCCTGTGACCACCACGGTCCATGATGACAAGGGCACCAAGAGGAGCATC
ACTGTGACCCAGGATGAGGGTATCCGCCCCAGCACCACCATGGAGGGCCTGGCCAAACTG
AAGCCTGCCTTCAAGAAAGATGGTTCTACCACAGCTGGAAACTCTAGCCAGGTGAGTGAT
GGGGCAGCTGCCATCCTGCTGGCCCGGAGGTCCAAGGCAGAAGAGTTGGGCCTTCCCATC
CTTGGGGTCCTGAGGTCTTATGCAGTGGTTGGGGTCCCACCTGACATCATGGGCATTGGA
CCTGCCTATGCCATCCCAGTAGCTTTGCAAAAAGCAGGGCTGACAGTGAGTGACGTGGAC
ATCTTCGAGATCAATGAGGCCTTTGCAAGCCAGGCTGCCTACTGTGTGGAGAAGCTACGA
CTCCCCCCTGAGAAGGTGAACCCCCTGGGGGGTGCAGTGGCCTTAGGGCACCCACTGGGC
TGCACTGGGGCACGACAGGTCATCACGCTGCTCAATGAGCTGAAGCGCCGTGGGAAGAGG
GCATACGGAGTGGTGTCCATGTGCATCGGGACTGGAATGGGAGCCGCTGCCGTCTTTGAA
TACCCTGGGAACTGA
Enzyme 2 GenBank Gene ID X12966 Link Image
Enzyme 2 GeneCard ID ACAA1 Link Image
Enzyme 2 GenAtlas ID ACAA1 Link Image
Enzyme 2 HGNC ID HGNC:82 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3p23-p22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Bout A, Teunissen Y, Hashimoto T, Benne R, Tager JM: Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase. Nucleic Acids Res. 1988 Nov 11;16(21):10369. [PubMed Link Image]
  2. Fairbairn LJ, Tanner MJ: Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase. Nucleic Acids Res. 1989 May 11;17(9):3588. [PubMed Link Image]
  3. Bout A, Franse MM, Collins J, Blonden L, Tager JM, Benne R: Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient. Biochim Biophys Acta. 1991 Aug 27;1090(1):43-51. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5277
Enzyme 3 Name Trifunctional enzyme subunit beta, mitochondrial
Enzyme 3 Synonyms
  1. TP-beta
  2. 3-ketoacyl-CoA thiolase
  3. Acetyl-CoA acyltransferase
  4. Beta-ketothiolase
Enzyme 3 Gene Name HADHB
Enzyme 3 Protein Sequence >Trifunctional enzyme subunit beta, mitochondrial
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Enzyme 3 Number of Residues 474
Enzyme 3 Molecular Weight 51294.0
Enzyme 3 Theoretical pI 9.94
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 3 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 3 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 3 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 3 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P55084 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ECHB_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1425 bp
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
Enzyme 3 GenBank Gene ID D16481 Link Image
Enzyme 3 GeneCard ID HADHB Link Image
Enzyme 3 GenAtlas ID HADHB Link Image
Enzyme 3 HGNC ID HGNC:4803 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed Link Image]
  2. Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Middleton B: The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase. Biochem Soc Trans. 1994 May;22(2):427-31. [PubMed Link Image]
  8. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  9. Kamijo T, Wanders RJ, Saudubray JM, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest. 1994 Apr;93(4):1740-7. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  11. Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed Link Image]
  12. Spiekerkoetter U, Sun B, Khuchua Z, Bennett MJ, Strauss AW: Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations. Hum Mutat. 2003 Jun;21(6):598-607. [PubMed Link Image]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5280
Enzyme 4 Name Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
Enzyme 4 Synonyms
  1. MMSDH
  2. Malonate-semialdehyde dehydrogenase [acylating]
  3. Aldehyde dehydrogenase family 6 member A1
Enzyme 4 Gene Name ALDH6A1
Enzyme 4 Protein Sequence >Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIH
NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA
KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCA
GIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG
QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKEN
TLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLIT
PQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFG
PVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLP
MFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR
Enzyme 4 Number of Residues 535
Enzyme 4 Molecular Weight 57839.3
Enzyme 4 Theoretical pI 8.69
Enzyme 4 GO Classification
Function
  • catalytic activity
  • methylmalonate-semialdehyde dehydrogenase (acylating) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • branched chain family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
  • valine metabolic process
Component
Enzyme 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH [RN:R00922]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 6164678 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q02252 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name MMSA_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1608 bp
ATGGCGGCGCTATTGGCGGCGGCGGCAGTGCGAGCCCGGATCCTGCAGGTTTCTTCCAAG
GTGAAATCCAGTCCCACCTGGTATTCAGCATCTTCCTTCTCTTCTTCAGTGCCAACTGTA
AAGCTCTTCATTGGTGGGAAATTCGTTGAATCCAAAAGTGACAAATGGATCGATATCCAC
AACCCAGCCACCAATGAGGTCATTGGTCGGGTCCCTCAGGCCACCAAGGCAGAAATGGAT
GCAGCCATTGCTTCCTGCAAACGTGCTTTTCCTGCATGGGCAGACACTTCAGTATTAAGC
CGCCAGCAGGTCTTGCTCCGCTATCAACAACTTATTAAAGAAAACTTGAAAGAAATTGCC
AAGTTAATCACATTGGAACAAGGGAAGACCCTAGCTGATGCTGAAGGAGATGTATTTCGA
GGCCTTCAGGTGGTTGAGCATGCCTGTAGTGTGACATCCCTCATGATGGGAGAGACCATG
CCATCCATCACCAAAGACATGGACCTTTATTCCTACCGTCTGCCTCTGGGAGTGTGTGCA
GGCATTGCTCCATTCAATTTTCCTGCCATGATCCCCCTTTGGATGTTTCCCATGGCCATG
GTGTGTGGAAATACCTTCCTAATGAAACCATCTGAGCGAGTCCCTGGAGCAACTATGCTT
CTTGCTAAGTTGCTCCAGGATTCTGGTGCCCCTGATGGAACATTAAACATCATCCATGGA
CAGCATGAAGCTGTAAATTTTATTTGCGATCATCCGGACATCAAAGCAATCAGCTTTGTG
GGATCCAACAAGGCAGGAGAGTATATCTTCGAGAGAGGATCAAGACATGGCAAGAGGGTT
CAAGCCAATATGGGAGCCAAGAACCATGGGGTAGTCATGCCAGATGCCAATAAGGAAAAT
ACCCTGAACCAGCTGGTTGGGGCAGCATTTGGAGCTGCTGGTCAGCGCTGCATGGCTCTT
TCAACAGCAGTCCTTGTGGGAGAAGCCAAGAAGTGGCTGCCAGAGCTGGTGGAGCATGCC
AAAAACCTGAGAGTCAATGCAGGAGATCAGCCTGGAGCTGATCTTGGCCCTCTGATCACT
CCCCAGGCCAAAGAGCGAGTCTGTAATCTGATTGATAGTGGAACAAAGGAGGGAGCTTCC
ATCCTTCTTGATGGACGAAAAATTAAAGTGAAAGGCTATGAAAATGGCAACTTTGTTGGA
CCAACCATCATCTCGAATGTCAAGCCAAATATGACCTGTTACAAAGAGGAGATTTTTGGT
CCAGTTCTTGTGGTTCTGGAGACAGAAACATTGGATGAAGCCATCCAGATTGTAAATAAC
AACCCATATGGAAATGGAACTGCCATCTTCACCACCAATGGAGCCACTGCTCGGAAATAT
GCCCACTTGGTGGATGTTGGACAGGTGGGAGTGAATGTCCCCATTCCAGTGCCTTTGCCA
ATGTTCTCATTCACCGGCTCTCGATCCTCCTTCAGGGGAGACACCAATTTCTATGGCAAA
CAGGGCATCCAATTCTACACTCAGTTAAAGACCATTACTTCTCAGTGGAAAGAAGAAGAT
GCTACTCTTTCCTCACCTGCTGTTGTCATGCCTACCATGGGCCGTTAG
Enzyme 4 GenBank Gene ID AF148505 Link Image
Enzyme 4 GeneCard ID ALDH6A1 Link Image
Enzyme 4 GenAtlas ID ALDH6A1 Link Image
Enzyme 4 HGNC ID HGNC:7179 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 14q24.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Chambliss KL, Gray RG, Rylance G, Pollitt RJ, Gibson KM: Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency. J Inherit Metab Dis. 2000 Jul;23(5):497-504. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Kedishvili NY, Popov KM, Rougraff PM, Zhao Y, Crabb DW, Harris RA: CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. J Biol Chem. 1992 Sep 25;267(27):19724-9. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5334
Enzyme 5 Name Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 5 Synonyms
  1. LCAD
Enzyme 5 Gene Name ACADL
Enzyme 5 Protein Sequence >Long-chain specific acyl-CoA dehydrogenase, mitochondrial
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
Enzyme 5 Number of Residues 430
Enzyme 5 Molecular Weight 47655.3
Enzyme 5 Theoretical pI 7.89
Enzyme 5 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 5 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 5 Specific Function Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor
Enzyme 5 Pathways
Enzyme 5 Reactions
  • acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 177962 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P28330 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ACADL_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1293 bp
ATGGCCGCACGCCTTCTCCGAGGGTCCCTACGCGTCCTGGGCGGCCACCGTGCGCCGCGC
CAGCTGCCCGCCGCGCGATGTTCTCATTCCGGAGGGGAAGAACGTCTAGAAACTCCTTCT
GCTAAAAAATTAACAGATATAGGAATTCGAAGAATCTTTTCTCCAGAGCATGACATTTTC
CGGAAAAGTGTAAGGAAGTTTTTCCAAGAAGAAGTGATTCCTCATCACTCAGAATGGGAG
AAAGCTGGAGAAGTAAGTAGGGAGGTTTGGGAAAAAGCTGGAAAACAAGGACTGCTTGGT
GTCAATATTGCAGAGCATCTTGGTGGAATTGGAGGGGATCTGTACTCCGCAGCTATTGTC
TGGGAGGAGCAAGCTTATTCAAATTGTTCAGGCCCAGGTTTTAGTATTCATTCAGGTATT
GTCATGTCCTATATTACAAACCATGGCTCAGAAGAACAGATTAAGCACTTTATTCCCCAG
ATGACTGCAGGCAAATGTATTGGTGCAATAGCAATGACAGAGCCTGGAGCTGGAAGTGAC
TTACAGGGAATAAAAACAAATGCTAAAAAGGATGGAAGTGACTGGATTCTCAATGGAAGC
AAGGTGTTCATCAGTAATGGGTCATTAAGTGATGTTGTGATTGTAGTTGCGGTCACAAAT
CATGAAGCTCCCTCCCCTGCCCATGGTATTAGCCTTTTTCTGGTGGAAAATGGAATGAAA
GGATTTATCAAGGGACGAAAGCTACATAAAATGGGATTAAAAGCCCAGGATACCGCAGAA
CTATTCTTTGAAGATATACGGTTGCCAGCTAGTGCCCTACTTGGAGAAGAGAATAAAGGC
TTCTATTACATCATGAAAGAGCTTCCACAGGAAAGGCTGTTAATTGCTGATGTGGCAATT
TCAGCTAGTGAATTCATGTTTGAAGAAACCAGGAACTATGTTAAACAAAGAAAAGCTTTT
GGCAAAACAGTTGCTCACCTACAGACAGTGCAACATAAATTAGCAGAATTAAAAACACAT
ATATGTGTAACCCGAGCATTTGTGGACAACTGTCTCCAGCTGCATGAAGCGAAACGTTTG
GACTCCGCCACTGCTTGCATGGCGAAATATTGGGCATCTGAGTTACAAAATAGTGTAGCT
TACGACTGTGTACAGCTCCATGGAGGTTGGGGATACATGTGGGAGTACCCAATTGCAAAA
GCTTATGTGGATGCCAGAGTTCAGCCAATCTATGGTGGTACAAATGAAATAATGAAGGAG
CTGATTGCAAGAGAGATTGTCTTTGACAAGTAG
Enzyme 5 GenBank Gene ID M74096 Link Image
Enzyme 5 GeneCard ID ACADL Link Image
Enzyme 5 GenAtlas ID ACADL Link Image
Enzyme 5 HGNC ID HGNC:88 Link Image
Enzyme 5 Chromosome Location 2
Enzyme 5 Locus 2q34-q35
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1991 Nov;11(3):609-20. [PubMed Link Image]
  2. Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1992 Mar;12(3):626. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5335
Enzyme 6 Name Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 6 Synonyms
  1. SCAD
  2. Butyryl-CoA dehydrogenase
Enzyme 6 Gene Name ACADS
Enzyme 6 Protein Sequence >Short-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQV
DKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN
SLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLN
GTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTAN
LIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF
GAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
Enzyme 6 Number of Residues 412
Enzyme 6 Molecular Weight 44296.7
Enzyme 6 Theoretical pI 8.12
Enzyme 6 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 6 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 6 Specific Function Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor
Enzyme 6 Pathways
Enzyme 6 Reactions
  • butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor [RN:R01178]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 337928 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P16219 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ACADS_HUMAN Link Image
Enzyme 6 PDB ID 1JQI Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1239 bp
ATGGCCGCCGCGCTGCTCGCCCGGGCCTCGGGCCCTGCCCGCAGAGCTCTCTGTCCTAGG
GCCTGGCGGCAGTTACACACCATCTACCAGTCTGTGGAACTGCCCGAGACACACCAGATG
TTGCTCCAGACATGCCGGGACTTTGCCGAGAAGGAGTTGTTTCCCATTGCAGCCCAGGTG
GATAAGGAACATCTCTTCCCAGCGGCTCAGGTGAAGAAGATGGGCGGGCTTGGGCTTCTG
GCCATGGACGTGCCCGAGGAGCTTGGCGGTGCTGGCCTCGATTACCTGGCCTACGCCATC
GCCATGGAGGAGATCAGCCGTGGCTGCGCCTCCACCGGAGTCATCATGAGTGTCAACAAC
TCTCTCTACCTGGGGCCCATCTTGAAGTTTGGCTCCAAGGAGCAGAAGCAGGCGTGGGTC
ACGCCTTTCACCAGTGGTGACAAAATTGGCTGCTTTGCCCTCAGCGAACCAGGGAACGGC
AGTGATGCAGGAGCTGCGTCCACCACCGCCCGGGCCGAGGGCGACTCATGGGTTCTGAAT
GGAACCAAAGCCTGGATCACCAATGCCTGGGAGGCTTCGGCTGCCGTGGTCTTTGCCAGC
ACGGACAGAGCCCTGCAAAACAAGGGCATCAGTGCCTTCCTGGTCCCCATGCCAACGCCT
GGGCTCACGTTGGGGAAGAAAGAAGACAAGCTGGGCATCCGGGGCTCATCCACGGCCAAC
CTCATCTTTGAGGACTGTCGCATCCCCAAGGACAGCATCCTGGGGGAGCCAGGGATGGGC
TTCAAGATAGCCATGCAAACCCTGGACATGGGCCGCATCGGCATCGCCTCCCAGGCCCTG
GGCATTGCCCAGACCGCCCTCGATTGTGCTGTGAACTACGCTGAGAATCGCATGGCCTTC
GGGGCGCCCCTCACCAAGCTCCAGGTCATCCAGTTCAAGTTGGCAGACATGGCCCTGGCC
CTGGAGAGTGCCCGGCTGCTGACCTGGCGCGCTGCCATGCTGAAGGATAACAAGAAGCCT
TTCATCAAGGAGGCAGCCATGGCCAAGCTGGCCGCCTCGGAGGCCGCGACCGCCATCAGC
CACCAGGCCATCCAGATCCTGGGCGGCATGGGCTACGTGACAGAGATGCCGGCAGAGCGG
CACTACCGCGACGCCCGCATCACTGAGATCTACGAGGGCACCAGCGAAATCCAGCGGCTG
GTGATCGCCGGGCATCTGCTCAGGAGCTACCGGAGCTGA
Enzyme 6 GenBank Gene ID M26393 Link Image
Enzyme 6 GeneCard ID ACADS Link Image
Enzyme 6 GenAtlas ID ACADS Link Image
Enzyme 6 HGNC ID HGNC:90 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 12q22-qter
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Naito E, Ozasa H, Ikeda Y, Tanaka K: Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1989 May;83(5):1605-13. [PubMed Link Image]
  2. Corydon MJ, Andresen BS, Bross P, Kjeldsen M, Andreasen PH, Eiberg H, Kolvraa S, Gregersen N: Structural organization of the human short-chain acyl-CoA dehydrogenase gene. Mamm Genome. 1997 Dec;8(12):922-6. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  5. Naito E, Indo Y, Tanaka K: Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1990 May;85(5):1575-82. [PubMed Link Image]
  6. Gregersen N, Winter VS, Corydon MJ, Corydon TJ, Rinaldo P, Ribes A, Martinez G, Bennett MJ, Vianey-Saban C, Bhala A, Hale DE, Lehnert W, Kmoch S, Roig M, Riudor E, Eiberg H, Andresen BS, Bross P, Bolund LA, Kolvraa S: Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet. 1998 Apr;7(4):619-27. [PubMed Link Image]
  7. Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N: Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5336
Enzyme 7 Name Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 7 Synonyms
  1. MCAD
Enzyme 7 Gene Name ACADM
Enzyme 7 Protein Sequence >Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEI
IPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ
TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNM
GQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEAT
KYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF
AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK
N
Enzyme 7 Number of Residues 421
Enzyme 7 Molecular Weight 46588.0
Enzyme 7 Theoretical pI 8.51
Enzyme 7 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 7 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 7 Specific Function This enzyme is specific for acyl chain lengths of 4 to 16
Enzyme 7 Pathways
Enzyme 7 Reactions
  • acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 177964 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P11310 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ACADM_HUMAN Link Image
Enzyme 7 PDB ID 1T9G Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1266 bp
ATGGCAGCGGGGTTCGGGCGATGCTGCAGGGTCCTGAGAAGTATTTCTCGTTTTCATTGG
AGATCACAGCATACAAAAGCCAATCGACAACGTGAACCAGGATTAGGATTTAGTTTTGAG
TTCACCGAACAGCAGAAAGAATTTCAAGCTACTGCTCGTAAATTTGCCAGAGAGGAAATC
ATCCCAGTGGCTGCAGAATATGATAAAACTGGTGAATATCCAGTCCCCCTAATTAGAAGA
GCCTGGGAACTTGGTTTAATGAACACACACATTCCAGAGAACTGTGGAGGTCTTGGACTT
GGAACTTTTGATGCTTGTTTAATTAGTGAAGAATTGGCTTATGGATGTACAGGGGTTCAG
ACTGCTATTGAAGGAAATTCTTTGGGGCAAATGCCTATTATTATTGCTGGAAATGATCAA
CAAAAGAAGAAGTATTTGGGGAGAATGACTGAGGAGCCATTGATGTGTGCTTATTGTGTA
ACAGAACCTGGAGCAGGCTCTGATGTAGCTGGTATAAAGACCAAAGCAGAAAAGAAAGGA
GATGAGTATATTATTAATGGTCAGAAGATGTGGATAACCAACGGAGGAAAAGCTAATTGG
TATTTTTTATTGGCACGTTCTGATCCAGATCCTAAAGCTCCTGCTAATAAAGCCTTTACT
GGATTCATTGTGGAAGCAGATACCCCAGGAATTCAGATTGGGAGAAAGGAATTAAACATG
GGCCAGCGATGTTCAGATACTAGAGGAATTGTCTTCGAAGATGTGAAAGTGCCTAAAGAA
AATGTTTTAATTGGTGACGGAGCTGGTTTCAAAGTTGCAATGGGAGCTTTTGATAAAACC
AGACCTGTAGTAGCTGCTGGTGCTGTTGGATTAGCACAAAGAGCTTTGGATGAAGCTACC
AAGTATGCCCTGGAAAGGAAAACTTTCGGAAAGCTACTTGTAGAGCACCAAGCAATATCA
TTTATGCTGGCTGAAATGGCAATGAAAGTTGAACTAGCTAGAATGAGTTACCAGAGAGCA
GCTTGGGAGGTTGATTCTGGTCGTCGAAATACCTATTATGCTTCTATTGCAAAGGCATTT
GCTGGAGATATTGCAAATCAGTTAGCTACTGATGCTGTGCAGATACTTGGAGGCAATGGA
TTTAATACAGAATATCCTGTAGAAAAACTAATGAGGGATGCCAAAATCTATCAGATTTAT
GAAGGTACTTCACAAATTCAAAGACTTATTGTAGCCCGTGAACACATTGACAAGTACAAA
AATTAA
Enzyme 7 GenBank Gene ID M16827 Link Image
Enzyme 7 GeneCard ID ACADM Link Image
Enzyme 7 GenAtlas ID ACADM Link Image
Enzyme 7 HGNC ID HGNC:89 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p31
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Kelly DP, Kim JJ, Billadello JJ, Hainline BE, Chu TW, Strauss AW: Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4068-72. [PubMed Link Image]
  2. Zhang ZF, Kelly DP, Kim JJ, Zhou YQ, Ogden ML, Whelan AJ, Strauss AW: Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene. Biochemistry. 1992 Jan 14;31(1):81-9. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR: Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. [PubMed Link Image]
  9. Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D: Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J Biol Chem. 2004 Jul 30;279(31):32904-12. Epub 2004 May 24. [PubMed Link Image]
  10. Toogood HS, van Thiel A, Scrutton NS, Leys D: Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. [PubMed Link Image]
  11. Tanaka K, Yokota I, Coates PM, Strauss AW, Kelly DP, Zhang Z, Gregersen N, Andresen BS, Matsubara Y, Curtis D, et al.: Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. Hum Mutat. 1992;1(4):271-9. [PubMed Link Image]
  12. Yokota I, Indo Y, Coates PM, Tanaka K: Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. [PubMed Link Image]
  13. Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW: Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. [PubMed Link Image]
  14. Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K: Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. [PubMed Link Image]
  15. Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.: Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. [PubMed Link Image]
  16. Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D: Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. [PubMed Link Image]
  17. Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.: Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. [PubMed Link Image]
  18. Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW: Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. [PubMed Link Image]
  19. Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW: A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. [PubMed Link Image]
  20. Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N: The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. [PubMed Link Image]
  21. Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S: Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. [PubMed Link Image]
  22. Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR: Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. [PubMed Link Image]
  23. Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N: Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. [PubMed Link Image]
  24. Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E: Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. [PubMed Link Image]
  25. Albers S, Levy HL, Irons M, Strauss AW, Marsden D: Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. [PubMed Link Image]
  26. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5378
Enzyme 8 Name Peroxisomal acyl-coenzyme A oxidase 1
Enzyme 8 Synonyms
  1. AOX
  2. Palmitoyl-CoA oxidase
  3. Straight-chain acyl-CoA oxidase
  4. SCOX
Enzyme 8 Gene Name ACOX1
Enzyme 8 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 1
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
Enzyme 8 Number of Residues 660
Enzyme 8 Molecular Weight 74423.0
Enzyme 8 Theoretical pI 8.29
Enzyme 8 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 8 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 8 Specific Function Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs
Enzyme 8 Pathways
Enzyme 8 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 14250616 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q15067 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ACOX1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1983 bp
ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACCCGGCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAATTTTGTGCACCGAGGGCGGCCTGAGCCTCTG
GATCTTCACTTGGGCATGTTCCTGCCCACCTTGCTTCACCAGGCAACTGCGGAGCAGCAG
GAGCGCTTCTTCATGCCCGCCTGGAACTTGGAGATCATTGGCACTTATGCCCAGACAGAG
ATGGGTCATGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGGAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAATCGGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGCACATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATGAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTGCCACTATGTGGTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA
Enzyme 8 GenBank Gene ID BC008767 Link Image
Enzyme 8 GeneCard ID ACOX1 Link Image
Enzyme 8 GenAtlas ID ACOX1 Link Image
Enzyme 8 HGNC ID HGNC:119 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 17q24-q25|17q25.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed Link Image]
  2. Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed Link Image]
  3. Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed Link Image]
  4. Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Suzuki Y, Iai M, Kamei A, Tanabe Y, Chida S, Yamaguchi S, Zhang Z, Takemoto Y, Shimozawa N, Kondo N: Peroxisomal acyl CoA oxidase deficiency. J Pediatr. 2002 Jan;140(1):128-30. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5396
Enzyme 9 Name Peroxisomal acyl-coenzyme A oxidase 2
Enzyme 9 Synonyms
  1. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase
  2. 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase
  3. Trihydroxycoprostanoyl-CoA oxidase
  4. THCA-CoA oxidase
  5. THCCox
Enzyme 9 Gene Name ACOX2
Enzyme 9 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 2
MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSY
PEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHR
VFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVI
HSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGD
IGPKMDFDQTDNGFLQLNHVRVPRENMLSRFAQVLPDGTYVKLGTAQSNYLPMVVVRVEL
LSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFL
AVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKL
SGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAP
DLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHL
QAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGA
QVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNT
QENPAYEEYIRPLLQSWRSKL
Enzyme 9 Number of Residues 681
Enzyme 9 Molecular Weight 76826.1
Enzyme 9 Theoretical pI 7.59
Enzyme 9 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 9 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 9 Specific Function Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor [RN:R07374]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1780991 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q99424 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ACOX2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2046 bp
ATGGGCAGCCCAGTGCACCGAGTGTCATTGGGGGATACCTGGAGCAGGCAAATGCACCCC
GACATAGAGAGCGAGAGGTATATGCAGTCCTTTGACGTGGAACGGCTCACCAACATCCTT
GATGGAGGTGCCCAGAACACTGCACTCCGCAGGAAAGTTGAGAGCATCATCCACAGTTAC
CCGGAGTTTAGCTGTAAGGACAATTATTTCATGACCCAGAATGAGCGTTATAAGGCTGCC
ATGCGGAGGGCATTCCACATCCGGTTGATAGCTCGGCGCCTGGGTTGGTTAGAAGATGGT
CGTGAATTAGGCTACGCTTACAGAGCCCTTTCTGGAGACGTGGCCTTAAATATACACAGA
GTCTTCGTGAGAGCCCTCAGGAGCCTGGGCTCAGAGGAGCAGATTGCCAAATGGGACCCA
CTCTGCAAAAACATCCAGATCATCGCAACGTATGCACAGACAGAGTTGGGACATGGGACA
TATCTTCAGGGCCTGGAGACTGAAGCCACCTATGACGCAGCCACCCAGGAGTTTGTGATA
CACAGCCCCACGCTGACTGCCACCAAATGGTGGCCTGGAGACTTGGGACGGTCAGCCACC
CATGCCCTGGTCCAGGCCCAGCTGATCTGCTCAGGAGCCAGGCGGGGCATGCACGCTTTT
ATTGTGCCAATCCGGAGTCTTCAGGACCACACCCCACTGCCAGGAATCATCATTGGGGAC
ATCGGACCCAAGATGGACTTTGATCAAACAGACAATGGCTTCCTGCAGCTGAACCATGTG
CGGGTCCCCAGGGAGAACATGCTGAGTCGCTTTGCACAGGTCTTGCCAGATGGCACCTAC
GTCAAACTCGGTACAGCACAGAGCAACTACCTTCCCATGGTGGTGGTGCGGGTGGAGCTG
CTGTCAGGGGAGATCCTCCCTATACTGCAGAAGGCCTGTGTCATCGCCATGCGCTACTCG
GTCATCCGCCGCCAATCCCGGCTCCGGCCCAGTGACCCAGAGGCAAAGGTCCTGGACTAC
CAGACACAACAGCAGAAACTCTTTCCTCAGCTGGCCATCAGTTATGCCTTCCATTTCCTG
GCAGTCAGCCTCTTGGAGTTCTTCCAGCACTCCTACACTGCCATTCTGAACCAAGACTTC
AGCTTCCTGCCTGAGCTCCACGCGCTGAGCACGGGCATGAAGGCCATGATGTCAGAATTC
TGCACCCAGGGAGCTGAGATGTGCCGCAGGGCCTGTGGCGGACATGGCTACTCAAAGCTG
AGTGGCCTGCCATCACTGGTCACCAAATTGTCGGCCTCCTGCACCTACGAGGGTGAGAAC
ACAGTGCTCTACCTGCAGGTGGCCAGGTTCCTGGTGAAGAGCTACCTGCAGACTCAGATG
TCCCCTGGCTCCACGCCACAGAGATCTCTCTCTCCATCTGTCGCATATCTCACCGCACCT
GACCTGGCCAGGTGTCCAGCCCAGAGGGCAGCCGACTTCCTCTGCCCGGAGCTCTACACC
ACGGCCTGGGCACATGTGGCAGTAAGGCTCATAAAGGACTCAGTGCAGCATTTACAGACC
CTGACGCAATCCGGAGCTGACCAGCACGAGGCTTGGAACCAGACCACTGTCATACACCTC
CAGGCTGCTAAGGTGCACTGCTACTATGTCACTGTGAAGGGTTTTACAGAAGCTCTGGAG
AAACTAGAAAATGAACCAGCGATTCAGCAGGTGCTCAAGCGCCTCTGTGACCTCCATGCC
ATACATGGAATCTTGACTAACTCGGGTGACTTTCTCCATGACGCCTTCCTGTCTGGTGCC
CAAGTGGACATGGCAAGAACAGCCTACCTGGACCTGCTCCGCCTGATCCGGAAGGATGCC
ATCCTGTTAACTGATGCTTTTGACTTCACCGATCAGTGTTTAAATTCAGCCCTTGGCTGT
TATGATGGAAACGTCTACGAACGCCTGTTCCAGTGGGCTCAGAAGTCACCAACCAATACT
CAGGAGAACCCTGCCTATGAGGAATATATAAGACCACTTTTACAAAGTTGGAGATCCAAG
CTATGA
Enzyme 9 GenBank Gene ID X95190 Link Image
Enzyme 9 GeneCard ID ACOX2 Link Image
Enzyme 9 GenAtlas ID ACOX2 Link Image
Enzyme 9 HGNC ID HGNC:120 Link Image
Enzyme 9 Chromosome Location 3
Enzyme 9 Locus 3p14.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Baumgart E, Vanhooren JC, Fransen M, Marynen P, Puype M, Vandekerckhove J, Leunissen JA, Fahimi HD, Mannaerts GP, van Veldhoven PP: Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13748-53. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5398
Enzyme 10 Name Isovaleryl-CoA dehydrogenase, mitochondrial
Enzyme 10 Synonyms
  1. IVD
Enzyme 10 Gene Name IVD
Enzyme 10 Protein Sequence >Isovaleryl-CoA dehydrogenase, mitochondrial
MATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEH
LAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG
AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA
EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKL
DKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLD
HTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGV
ILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA
DFH
Enzyme 10 Number of Residues 423
Enzyme 10 Molecular Weight 46319.0
Enzyme 10 Theoretical pI 8.31
Enzyme 10 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 10 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 10 Specific Function 3-methylbutanoyl-CoA + acceptor = 3-methylbut- 2-enoyl-CoA + reduced acceptor
Enzyme 10 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 10 Reactions
  • 3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor [RN:R04096]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 306897 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P26440 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name IVD_HUMAN Link Image
Enzyme 10 PDB ID 1IVH Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1272 bp
ATGGCGACTGCGACTCGGCTGCTGGGGTGGCGTGTGGCGAGCTGGAGGCTGCGGCCGCCG
CTTGCCGGCTTCGTTTCCCAGCGGGCCCACTCGCTTTTGCCCGTGGACGATGCAATCAAT
GGGCTAAGCGAGGAGCAGAGGCAGCTTCGTCAGACCATGGCTAAGTTCCTTCAGGAGCAC
CTGGCCCCCAAGGCCCAGGAGATCGATCGCAGCAATGAGTTCAAGAACCTGCGAGAATTT
TGGAAGCAGCTGGGGAACCTGGGCGTATTGGGCATCACAGCCCCTGTTCAGTATGGCGGC
TCCGGCCTGGGCTACCTGGAGCATGTGCTGGTGATGGAGGAGATATCCCGAGCTTCCGGA
GCAGTGGGGCTCAGTTACGGTGCCCACTCCAACCTCTGCATCAACCAGCTTGTACGCAAT
GGGAATGAGGCCCAGAAAGAGAAGTATCTCCCGAAGCTGATCAGTGGTGAGTACATCGGA
GCCCTGGCCATGAGTGAGCCCAATGCAGGCTCTGATGTTGTCTCTATGAAGCTCAAAGCG
GAAAAGAAAGGAAATCACTACATCCTGAATGGCAACAAGTTCTGGATCACTAATGGCCCT
GATGCTGACGTCCTGATTGTCTATGCCAAGACAGATCTGGCTGCTGTGCCAGCTTCTCGG
GGCATCACAGCCTTCATTGTGGAGAAGGGTATGCCTGGCTTTAGCACCTCTAAGAAGCTG
GACAAGCTGGGGATGAGGGGCTCTAACACCTGTGAGCTAATCTTTGAAGACTGCAAGATT
CCTGCTGCCAACATCCTGGGCCATGAGAATAAGGGTGTCTACGTGCTGATGAGTGGGCTG
GACCTGGAGCGGCTGGTGCTGGCCGGGGGGCCTCTTGGGCTCATGCAAGCGGTCCTGGAC
CACACCATTCCCTACCTGCACGTGAGGGAAGCCTTTGGCCAGAAGATCGGCCACTTCCAG
TTGATGCAGGGGAAGATGGCTGACATGTACACCCGCCTCATGGCGTGTCGGCAGTATGTC
TACAATGTCGCCAAGGCCTGCGATGAGGGCCATTGCACTGCTAAGGACTGTGCAGGTGTG
ATTCTTTACTCAGCTGAGTGTGCTACACAGGTAGCCCTGGACGGCATTCAGTGTTTTGGT
GGCAATGGCTACATCAATGACTTTCCCATGGGCCGCTTTCTTCGAGATGCCAAGCTGTAT
GAGATAGGGGCTGGGACCAGCGAGGTGAGGCGGCTGGTCATCGGCAGAGCCTTCAATGCA
GACTTTCACTAG
Enzyme 10 GenBank Gene ID M34192 Link Image
Enzyme 10 GeneCard ID IVD Link Image
Enzyme 10 GenAtlas ID IVD Link Image
Enzyme 10 HGNC ID HGNC:6186 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 15q14-q15
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Matsubara Y, Ito M, Glassberg R, Satyabhama S, Ikeda Y, Tanaka K: Nucleotide sequence of messenger RNA encoding human isovaleryl-coenzyme A dehydrogenase and its expression in isovaleric acidemia fibroblasts. J Clin Invest. 1990 Apr;85(4):1058-64. [PubMed Link Image]
  2. Vockley J, Rogan PK, Anderson BD, Willard J, Seelan RS, Smith DI, Liu W: Exon skipping in IVD RNA processing in isovaleric acidemia caused by point mutations in the coding region of the IVD gene. Am J Hum Genet. 2000 Feb;66(2):356-67. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Parimoo B, Tanaka K: Structural organization of the human isovaleryl-CoA dehydrogenase gene. Genomics. 1993 Mar;15(3):582-90. [PubMed Link Image]
  6. Vockley J, Nagao M, Parimoo B, Tanaka K: The variant human isovaleryl-CoA dehydrogenase gene responsible for type II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire second coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors. J Biol Chem. 1992 Feb 5;267(4):2494-501. [PubMed Link Image]
  7. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  8. Mohsen AW, Vockley J: Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase. Biochemistry. 1995 Aug 15;34(32):10146-52. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Tiffany KA, Roberts DL, Wang M, Paschke R, Mohsen AW, Vockley J, Kim JJ: Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,. Biochemistry. 1997 Jul 15;36(28):8455-64. [PubMed Link Image]
  11. Vockley J, Parimoo B, Tanaka K: Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia. Am J Hum Genet. 1991 Jul;49(1):147-57. [PubMed Link Image]
  12. Mohsen AW, Anderson BD, Volchenboum SL, Battaile KP, Tiffany K, Roberts D, Kim JJ, Vockley J: Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia. Biochemistry. 1998 Jul 14;37(28):10325-35. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5424
Enzyme 11 Name Peroxisomal acyl-coenzyme A oxidase 3
Enzyme 11 Synonyms
  1. Branched-chain acyl-CoA oxidase
  2. BRCACox
  3. Pristanoyl-CoA oxidase
Enzyme 11 Gene Name ACOX3
Enzyme 11 Protein Sequence >Peroxisomal acyl-coenzyme A oxidase 3
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
Enzyme 11 Number of Residues 700
Enzyme 11 Molecular Weight 77628.3
Enzyme 11 Theoretical pI 7.27
Enzyme 11 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 11 General Function Involved in oxidoreductase activity, acting on the CH-CH group of donors
Enzyme 11 Specific Function Oxidizes the CoA-esters of 2-methyl-branched fatty acids
Enzyme 11 Pathways
Enzyme 11 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 2326549 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O15254 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ACOX3_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2103 bp
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG
Enzyme 11 GenBank Gene ID Y11411 Link Image
Enzyme 11 GeneCard ID ACOX3 Link Image
Enzyme 11 GenAtlas ID ACOX3 Link Image
Enzyme 11 HGNC ID HGNC:121 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4p15.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5434
Enzyme 12 Name Glutaryl-CoA dehydrogenase, mitochondrial
Enzyme 12 Synonyms
  1. GCD
Enzyme 12 Gene Name GCDH
Enzyme 12 Protein Sequence >Glutaryl-CoA dehydrogenase, mitochondrial
MALRGVSVRLLSRGPGLHVLRTWVSSAAQTEKGGRTQSQLAKSSRPEFDWQDPLVLEEQL
TTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSS
VAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLT
EPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEK
GMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWG
VLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQD
KAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIH
ALILGRAITGIQAFTASK
Enzyme 12 Number of Residues 438
Enzyme 12 Molecular Weight 48126.7
Enzyme 12 Theoretical pI 8.15
Enzyme 12 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 12 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 12 Specific Function Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive
Enzyme 12 Pathways
Enzyme 12 Reactions
  • glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor [RN:R02488]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q92947 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GCDH_HUMAN Link Image
Enzyme 12 PDB ID 1SIR Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1317 bp
ATGGCCCTGAGAGGCGTCTCCGTGCGGCTGCTGAGCCGCGGACCCGGCCTGCACGTCCTT
CGCACGTGGGTCTCGTCGGCGGCGCAGACCGAGAAAGGCGGGAGAACACAGAGCCAACTG
GCTAAGTCCTCGCGTCCCGAGTTTGACTGGCAGGACCCGCTGGTGCTGGAGGAGCAGCTG
ACCACAGATGAGATCCTCATCAGGGACACCTTCCGCACCTACTGCCAGGAGAGACTCATG
CCTCGCATCCTGTTGGCCAATCGCAACGAAGTTTTTCATCGGGAGATCATTTCGGAGATG
GGGGAGTTGGGTGTGCTGGGCCCCACCATCAAAGGATATGGCTGTGCTGGGGTTTCGTCT
GTGGCCTATGGGCTCCTGGCCCGAGAGCTGGAGCGGGTGGACAGTGGCTACAGGTCGGCG
ATGAGTGTCCAGTCCTCCCTCGTCATGCACCCTATCTATGCCTATGGCAGCGAGGAACAG
CGGCAGAAGTACCTGCCCCAGCTGGCCAAGGGGGAGCTCCTGGGCTGCTTCGGGCTCACA
GAGCCCAACAGCGGAAGTGACCCCAGCAGCATGGAGACCAGAGCCCACTACAACTCATCC
AACAAGAGCTACACCCTCAATGGGACCAAGACCTGGATCACGAACTCGCCTATGGCCGAT
CTGTTTGTAGTGTGGGCTCGGTGTGAAGATGGCTGCATTCGGGGCTTCCTGCTGGAGAAG
GGGATGCGGGGTCTCTCGGCCCCCAGGATCCAGGGCAAGTTCTCGCTGCGGGCCTCAGCC
ACAGGCATGATCATCATGGACGGTGTGGAGGTGCCAGAGGAGAATGTGCTCCCTGGTGCA
TCCAGCCTGGGGGGTCCCTTCGGCTGCCTGAACAACGCCCGGTACGGCATCGCGTGGGGC
GTGCTTGGAGCTTCGGAGTTCTGCTTGCACACAGCCCGGCAGTACGCCCTCGACAGGATG
CAGTTTGGTGTCCCACTGGCCAGGAACCAGCTGATTCAGAAGAAGCTGGCAGACATGCTC
ACTGAGATTACCCTGGGCCTTCACGCCTGCCTGCAGCTCGGCCGCTTGAAGGACCAGGAC
AAGGCTGCCCCCGAGATGGTTTCTCTGCTGAAGAGGAATAACTGTGGGAAAGCCCTGGAC
ATCGCCCGCCAGGCCCGAGACATGCTGGGGGGGAATGGGATTTCTGACGAGTATCACGTG
ATCCGGCACGCCATGAACCTGGAGGCCGTGAACACCTACGAAGGTACACATGACATTCAC
GCCCTGATCCTTGGGAGAGCTATCACGGGAATCCAGGCGTTCACGGCCAGCAAGTGA
Enzyme 12 GenBank Gene ID U69141 Link Image
Enzyme 12 GeneCard ID GCDH Link Image
Enzyme 12 GenAtlas ID GCDH Link Image
Enzyme 12 HGNC ID HGNC:4189 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 19p13.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Goodman SI, Kratz LE, Frerman FE: Pork and human cDNAs encoding glutaryl-CoA dehydrogenase. Prog Clin Biol Res. 1992;375:169-73. [PubMed Link Image]
  2. Goodman SI, Kratz LE, DiGiulio KA, Biery BJ, Goodman KE, Isaya G, Frerman FE: Cloning of glutaryl-CoA dehydrogenase cDNA, and expression of wild type and mutant enzymes in Escherichia coli. Hum Mol Genet. 1995 Sep;4(9):1493-8. [PubMed Link Image]
  3. Schwartz M, Christensen E, Superti-Furga A, Brandt NJ: The human glutaryl-CoA dehydrogenase gene: report of intronic sequences and of 13 novel mutations causing glutaric aciduria type I. Hum Genet. 1998 Apr;102(4):452-8. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Goodman SI, Stein DE, Schlesinger S, Christensen E, Schwartz M, Greenberg CR, Elpeleg ON: Glutaryl-CoA dehydrogenase mutations in glutaric acidemia (type I): review and report of thirty novel mutations. Hum Mutat. 1998;12(3):141-4. [PubMed Link Image]
  8. Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ: Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry. 2004 Aug 3;43(30):9674-84. [PubMed Link Image]
  9. Rao KS, Fu Z, Albro M, Narayanan B, Baddam S, Lee HJ, Kim JJ, Frerman FE: The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate. Biochemistry. 2007 Dec 18;46(50):14468-77. Epub 2007 Nov 17. [PubMed Link Image]
  10. Biery BJ, Stein DE, Morton DH, Goodman SI: Gene structure and mutations of glutaryl-coenzyme A dehydrogenase: impaired association of enzyme subunits that is due to an A421V substitution causes glutaric acidemia type I in the Amish. Am J Hum Genet. 1996 Nov;59(5):1006-11. [PubMed Link Image]
  11. Anikster Y, Shaag A, Joseph A, Mandel H, Ben-Zeev B, Christensen E, Elpeleg ON: Glutaric aciduria type I in the Arab and Jewish communities in Israel. Am J Hum Genet. 1996 Nov;59(5):1012-8. [PubMed Link Image]
  12. Muhlhausen C, Christensen E, Schwartz M, Muschol N, Ullrich K, Lukacs Z: Severe phenotype despite high residual glutaryl-CoA dehydrogenase activity: a novel mutation in a Turkish patient with glutaric aciduria type I. J Inherit Metab Dis. 2003;26(7):713-4. [PubMed Link Image]
  13. Keyser B, Muhlhausen C, Dickmanns A, Christensen E, Muschol N, Ullrich K, Braulke T: Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH). Hum Mol Genet. 2008 Dec 15;17(24):3854-63. Epub 2008 Sep 5. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5458
Enzyme 13 Name Hepatic triacylglycerol lipase
Enzyme 13 Synonyms
  1. HL
  2. Hepatic lipase
  3. Lipase member C
Enzyme 13 Gene Name LIPC
Enzyme 13 Protein Sequence >Hepatic triacylglycerol lipase
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
Enzyme 13 Number of Residues 499
Enzyme 13 Molecular Weight 55880.1
Enzyme 13 Theoretical pI 9.37
Enzyme 13 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • triglyceride lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 13 General Function Involved in catalytic activity
Enzyme 13 Specific Function Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin
Enzyme 13 Pathways
Enzyme 13 Reactions
  • triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-22
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 194097335 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P11150 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name LIPC_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACCCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTTCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTCAAGATCCAGTTC
ATCAACCAAACTGAGACACCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
Enzyme 13 GenBank Gene ID NM_000236.2 Link Image
Enzyme 13 GeneCard ID LIPC Link Image
Enzyme 13 GenAtlas ID LIPC Link Image
Enzyme 13 HGNC ID HGNC:6619 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 15q21-q23
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed Link Image]
  2. Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed Link Image]
  3. Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed Link Image]
  4. Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed Link Image]
  5. Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Tiebel O, Gehrisch S, Pietzsch J, Gromeier S, Jaross W: 18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. Hum Mutat. 1998;12(3):216. [PubMed Link Image]
  9. Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed Link Image]
  10. Todorova B, Kubaszek A, Pihlajamaki J, Lindstrom J, Eriksson J, Valle TT, Hamalainen H, Ilanne-Parikka P, Keinanen-Kiukaanniemi S, Tuomilehto J, Uusitupa M, Laakso M: The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish Diabetes Prevention Study. J Clin Endocrinol Metab. 2004 May;89(5):2019-23. [PubMed Link Image]
  11. Grarup N, Andreasen CH, Andersen MK, Albrechtsen A, Sandbaek A, Lauritzen T, Borch-Johnsen K, Jorgensen T, Schmitz O, Hansen T, Pedersen O: The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects. J Clin Endocrinol Metab. 2008 Jun;93(6):2294-9. Epub 2008 Mar 25. [PubMed Link Image]
  12. Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed Link Image]
  13. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  14. Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5475
Enzyme 14 Name Diacylglycerol O-acyltransferase 1
Enzyme 14 Synonyms
  1. ACAT-related gene product 1
  2. Diglyceride acyltransferase
Enzyme 14 Gene Name DGAT1
Enzyme 14 Protein Sequence >Diacylglycerol O-acyltransferase 1
MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVG
SGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQV
VSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPA
AVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHT
VSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWM
VPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREF
YRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVS
VPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLN
YEAPAAEA
Enzyme 14 Number of Residues 488
Enzyme 14 Molecular Weight 55277.7
Enzyme 14 Theoretical pI 9.60
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Involved in diacylglycerol O-acyltransferase activity
Enzyme 14 Specific Function Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly
Enzyme 14 Pathways
Enzyme 14 Reactions
  • acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 104-124 130-150 166-186 189-209 282-302 332-352 406-426 428-448 453-473
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 29170487 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O75907 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name DGAT1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1467 bp
ATGGGCGACCGCGGCAGCTCCCGGCGCCGGAGGACAGGGTCGCGGCCCTCGAGCCACGGC
GGCGGCGGGCCTGCGGCGGCGGAAGAGGAGGTGCGGGACGCCGCTGCGGGCCCCGACGTG
GGAGCCGCGGGGGACGCGCCAGCCCCGGCCCCCAACAAGGACGGAGACGCCGGCGTGGGC
AGCGGCCACTGGGAGCTGAGGTGCCATCGCCTGCAGGATTCTTTATTCAGCTCTGACAGT
GGCTTCAGCAACTACCGTGGCATCCTGAACTGGTGTGTGGTGATGCTGATCTTGAGCAAT
GCCCGGTTATTTCTGGAGAACCTCATCAAGTATGGCATCCTGGTGGACCCCATCCAGGTG
GTTTCTCTGTTCCTGAAGGATCCCTATAGCTGGCCCGCCCCATGCCTGGTTATTGCGGCC
AATGTCTTTGCTGTGGCTGCATTCCAGGTTGAGAAGCGCCTGGCGGTGGGTGCCCTGACG
GAGCAGGCGGGACTGCTGCTGCACGTGGCCAACCTGGCCACCATTCTGTGTTTCCCAGCG
GCTGTGGTCTTACTGGTTGAGTCTATCACTCCAGTGGGCTCCCTGCTGGCGCTGATGGCG
CACACCATCCTCTTCCTCAAGCTCTTCTCCTACCGCGACGTCAACTCATGGTGCCGCAGG
GCCAGGGCCAAGGCTGCCTCTGCAGGGAAGAAGGCCAGCAGTGCTGCTGCCCCGCACACC
GTGAGCTACCCGGACAATCTGACCTACCGCGATCTCTACTACTTCCTCTTCGCCCCCACC
TTGTGCTACGAGCTCAACTTTCCCCGCTCTCCCCGCATCCGGAAGCGCTTTCTGCTGCGA
CGGATCCTTGAGATGCTGTTCTTCACCCAGCTCCAGGTGGGGCTGATCCAGCAGTGGATG
GTCCCCACCATCCAGAACTCCATGAAGCCCTTCAAGGACATGGACTACTCACGCATCATC
GAGCGCCTCCTGAAGCTGGCGGTCCCCAATCACCTCATCTGGCTCATCTTCTTCTACTGG
CTCTTCCACTCCTGCCTGAATGCCGTGGCTGAGCTCATGCAGTTTGGAGACCGGGAGTTC
TACCGGGACTGGTGGAACTCCGAGTCTGTCACCTACTTCTGGCAGAACTGGAACATCCCT
GTGCACAAGTGGTGCATCAGACACTTCTACAAGCCCATGCTTCGACGGGGCAGCAGCAAG
TGGATGGCCAGGACAGGGGTGTTCCTGGCCTCGGCCTTCTTCCACGAGTACCTGGTGAGC
GTCCCTCTGCGAATGTTCCGCCTCTGGGCGTTCACGGGCATGATGGCTCAGATCCCACTG
GCCTGGTTCGTGGGCCGCTTTTTCCAGGGCAACTATGGCAACGCAGCTGTGTGGCTGTCG
CTCATCATCGGACAGCCAATAGCCGTCCTCATGTACGTCCACGACTACTACGTGCTCAAC
TATGAGGCCCCAGCGGCAGAGGCCTGA
Enzyme 14 GenBank Gene ID AB057815 Link Image
Enzyme 14 GeneCard ID DGAT1 Link Image
Enzyme 14 GenAtlas ID DGAT1 Link Image
Enzyme 14 HGNC ID HGNC:2843 Link Image
Enzyme 14 Chromosome Location 8
Enzyme 14 Locus 8q24.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5534
Enzyme 15 Name 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
Enzyme 15 Synonyms
  1. Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
  2. BCKDE1B
  3. BCKDH E1-beta
Enzyme 15 Gene Name BCKDHB
Enzyme 15 Protein Sequence >2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
MAVVAAAAGWLLRLRAAGAEGHWRRLPGAGLARGFLHPAATVEDAAQRRQVAHFTFQPDP
EPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVF
NTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSL
TIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEP
KILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCE
VIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRV
CGYDTPFPHIFEPFYIPDKWKCYDALRKMINY
Enzyme 15 Number of Residues 392
Enzyme 15 Molecular Weight 43122.1
Enzyme 15 Theoretical pI 6.24
Enzyme 15 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 15 General Function Involved in catalytic activity
Enzyme 15 Specific Function The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 15 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 15 Reactions
  • 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 [RN:R01701]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 179362 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P21953 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name ODBB_HUMAN Link Image
Enzyme 15 PDB ID 1X80 Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1179 bp
ATGGCGGTTGTAGCGGCGGCTGCCGGCTGGCTACTCAGGCTCAGGGCGGCAGGGGCTGAG
GGGCACTGGCGTCGGCTTCCTGGCGCGGGGCTGGCGCGGGGCTTTTTGCACCCCGCCGCG
ACTGTCGAGGATGCGGCCCAGAGGCGGCAGGTGGCTCATTTTACTTTCCAGCCAGATCCG
GAGCCCCGGGAGTACGGGCAAACTCAGAAAATGAATCTTTTCCAGTCTGTAACAAGTGCC
TTGGATAACTCATTGGCCAAAGATCCTACTGCAGTAATATTTGGTGAAGATGTTGCCTTT
GGTGGAGTCTTTAGATGCACTGTTGGCTTGCGAGACAAATATGGAAAAGATAGAGTTTTT
AATACCCCATTGTGTGAACAAGGAATTGTTGGATTTGGAATCGGAATTGCGGTCACTGGA
GCTACTGCCATTGCGGAAATTCAGTTTGCAGATTATATTTTCCCTGCATTTGATCAGATT
GTTAATGAAGCTGCCAAGTATCGCTATCGCTCTGGGGATCTTTTTAACTGTGGAAGCCTC
ACTATCCGGTCCCCTTGGGGCTGTGTTGGTCATGGGGCTCTCTATCATTCTCAGAGTCCT
GAAGCATTTTTTGCCCATTGCCCAGGAATCAAGGTGGTTATACCCAGAAGCCCTTTCCAG
GCCAAAGGACTTCTTTTGTCATGCATAGAGGATAAAAATCCTTGTATATTTTTTGAACCT
AAAATACTTTACAGGGCAGCAGCGGAAGAAGTCCCTATAGAACCATACAACATCCCACTG
TCCCAGGCCGAAGTCATACAGGAAGGGAGTGATGTTACTCTAGTTGCCTGGGGCACTCAG
GTTCATGTGATCCGAGAGGTAGCTTCCATGGCAAAAGAAAAGCTTGGAGTGTCTTGTGAA
GTCATTGATCTGAGGACTATAATACCTTGGGATGTGGACACAATTTGTAAGTCTGTGATC
AAAACAGGGCGACTGCTAATCAGTCACGAGGCTCCCTTGACAGGCGGCTTTGCATCGGAA
ATCAGCTCTACAGTTCAGGAGGAATGTTTCTTGAACCTAGAGGCTCCTATATCAAGAGTA
TGTGGTTATGACACACCATTTCCTCACATTTTTGAACCATTCTACATCCCAGACAAATGG
AAGTGTTATGATGCCCTTCGAAAAATGATCAACTATTGA
Enzyme 15 GenBank Gene ID M55575 Link Image
Enzyme 15 GeneCard ID BCKDHB Link Image
Enzyme 15 GenAtlas ID BCKDHB Link Image
Enzyme 15 HGNC ID HGNC:987 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6q14.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Nobukuni Y, Mitsubuchi H, Endo F, Akaboshi I, Asaka J, Matsuda I: Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease. J Clin Invest. 1990 Jul;86(1):242-7. [PubMed Link Image]
  2. Chuang JL, Cox RP, Chuang DT: Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences. Am J Hum Genet. 1996 Jun;58(6):1373-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Chuang JL, Cox RP, Chuang DT: Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1990 Mar 26;262(2):305-9. [PubMed Link Image]
  5. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed Link Image]
  8. Edelmann L, Wasserstein MP, Kornreich R, Sansaricq C, Snyderman SE, Diaz GA: Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population. Am J Hum Genet. 2001 Oct;69(4):863-8. Epub 2001 Aug 16. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5535
Enzyme 16 Name 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Enzyme 16 Synonyms
  1. Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
  2. BCKDE1A
  3. BCKDH E1-alpha
Enzyme 16 Gene Name BCKDHA
Enzyme 16 Protein Sequence >2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAE
FIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILY
ESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYG
NISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGA
ASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDG
NDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHP
ISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQL
RKQQESLARHLQTYGEHYPLDHFDK
Enzyme 16 Number of Residues 445
Enzyme 16 Molecular Weight 50470.6
Enzyme 16 Theoretical pI 8.41
Enzyme 16 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
  • metabolic process
Component
Enzyme 16 General Function Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Enzyme 16 Specific Function The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 16 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 16 Reactions
  • 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 [RN:R01701]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 29391 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P12694 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name ODBA_HUMAN Link Image
Enzyme 16 PDB ID 1U5B Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1338 bp
ATGGCGGTAGCGATCGCTGCAGCGAGGGTCTGGCGGCTAAACCGTGGTTTGAGCCAGGCT
GCCCTCCTGCTGCTGCGGCAGCCTGGGGCTCGGGGACTGGCTAGATCTCACCCCCCCAGG
CAGCAGCAGCAGTTTTCATCTCTGGATGACAAGCCCCAGTTCCCAGGGGCCTCGGCGGAG
TTTATAGATAAGTTGGAATTCATCCAGCCCAACGTCATCTCTGGAATCCCCATCTACCGC
GTCATGGACCGGCAAGGCCAGATCATCAACCCCAGCGAGGACCCCCACCTGCCGAAGGAG
AAGGTGCTGAAGCTCTACAAGAGCATGACACTGCTTAACACCATGGACCGCATCCTCTAT
GAGTCTCAGCGGCAGGGCCGGATCTCCTTCTACATGACCAACTATGGTGAGGAGGGCACG
CACGTGGGGAGTGCCGCCGCCCTGGACAACACGGACCTGGTGTTTGGCCAGTACCGGGAG
GCAGGTGTGCTGATGTATCGGGACTACCCCCTGGAACTATTCATGGCCCAGTGCTATGGC
AACATCAGTGACTTGGGCAAGGGGCGCCAGATGCCTGTCCACTACGGCTGCAAGGAACGC
CACTTCGTCACTATCTCCTCTCCACTGGCCACGCAGATCCCTCAGGCGGTGGGGGCGGCG
TACGCAGCCAAGCGGGCCAATGCCAACAGGGTCGTCATCTGTTACTTCGGCGAGGGGGCA
GCCAGTGAGGGGGACGCCCATGCCGGCTTCAACTTCGCTGCCACACTTGAGTGCCCCATC
ATCTTCTTCTGCCGGAACAATGGCTACGCCATCTCCACGCCCACCTCTGAGCAGTATCGC
GGCGATGGCATTGCAGCACGAGGCCCCGGGTATGGCATCATGTCAATCCGCGTGGATGGT
AATGATGTGTTTGCCGTATACAACGCCACAAAGGAGGCCCGACGGCGGGCTGTGGCAGAG
AACCAGCCCTTTCTCATCGAGGCCATGACCTACAGGATCGGGCACCACAGCACCAGTGAC
GACAGTTCAGCGTACCGCTCGGTGGATGAGGTCAATTACTGGGATAAACAGGACCACCCC
ATCTCCCGGCTGCGGCACTATCTGCTGAGCCAAGGCTGGTGGGATGAGGAGCAGGAGAAG
GCCTGGAGGAAGCAGTCCCGCAGGAAGGTGATGGAGGCCTTTGAGCAGGCCGAGCGGAAG
CCCAAACCCAACCCCAACCTGCTCTTCTCAGACGTGTATCAGGAGATGCCCGCCCAGCTC
CGCAAGCAGCAGGAGTCTCTGGCCCGCCACCTGCAGACCTACGGGGAGCACTACCCACTG
GATCACTTCGATAAGTGA
Enzyme 16 GenBank Gene ID Z14093 Link Image
Enzyme 16 GeneCard ID BCKDHA Link Image
Enzyme 16 GenAtlas ID BCKDHA Link Image
Enzyme 16 HGNC ID HGNC:986 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 19q13.1-q13.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. McKean MC, Winkeler KA, Danner DJ: Nucleotide sequence of the 5' end including the initiation codon of cDNA for the E1 alpha subunit of the human branched chain alpha-ketoacid dehydrogenase complex. Biochim Biophys Acta. 1992 Nov 15;1171(1):109-12. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Fisher CW, Chuang JL, Griffin TA, Lau KS, Cox RP, Chuang DT: Molecular phenotypes in cultured maple syrup urine disease cells. Complete E1 alpha cDNA sequence and mRNA and subunit contents of the human branched chain alpha-keto acid dehydrogenase complex. J Biol Chem. 1989 Feb 25;264(6):3448-53. [PubMed Link Image]
  4. Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1991 Jun 17;284(1):34-8. [PubMed Link Image]
  5. Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex (1991) FEBS Letters 284, 34-38. FEBS Lett. 1991 Oct 21;291(2):376-7. [PubMed Link Image]
  6. Zhang B, Crabb DW, Harris RA: Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase. Gene. 1988 Sep 15;69(1):159-64. [PubMed Link Image]
  7. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  10. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  11. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  12. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. AEvarsson A, Chuang JL, Wynn RM, Turley S, Chuang DT, Hol WG: Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure. 2000 Mar 15;8(3):277-91. [PubMed Link Image]
  15. Chuang JL, Fisher CR, Cox RP, Chuang DT: Molecular basis of maple syrup urine disease: novel mutations at the E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid dehydrogenase complex. Am J Hum Genet. 1994 Aug;55(2):297-304. [PubMed Link Image]
  16. Zhang B, Edenberg HJ, Crabb DW, Harris RA: Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease. J Clin Invest. 1989 Apr;83(4):1425-9. [PubMed Link Image]
  17. Matsuda I, Nobukuni Y, Mitsubuchi H, Indo Y, Endo F, Asaka J, Harada A: A T-to-A substitution in the E1 alpha subunit gene of the branched-chain alpha-ketoacid dehydrogenase complex in two cell lines derived from Menonite maple syrup urine disease patients. Biochem Biophys Res Commun. 1990 Oct 30;172(2):646-51. [PubMed Link Image]
  18. Fisher CR, Fisher CW, Chuang DT, Cox RP: Occurrence of a Tyr393----Asn (Y393N) mutation in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population. Am J Hum Genet. 1991 Aug;49(2):429-34. [PubMed Link Image]
  19. Fisher CR, Chuang JL, Cox RP, Fisher CW, Star RA, Chuang DT: Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1 alpha impedes assembly of the E1 component of branched-chain alpha-keto acid dehydrogenase complex. J Clin Invest. 1991 Sep;88(3):1034-7. [PubMed Link Image]
  20. Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed Link Image]
  21. Chuang JL, Davie JR, Chinsky JM, Wynn RM, Cox RP, Chuang DT: Molecular and biochemical basis of intermediate maple syrup urine disease. Occurrence of homozygous G245R and F364C mutations at the E1 alpha locus of Hispanic-Mexican patients. J Clin Invest. 1995 Mar;95(3):954-63. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5548
Enzyme 17 Name Acyl-CoA desaturase
Enzyme 17 Synonyms
  1. Delta(9)-desaturase
  2. Fatty acid desaturase
  3. Stearoyl-CoA desaturase
Enzyme 17 Gene Name SCD
Enzyme 17 Protein Sequence >Acyl-CoA desaturase
MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYK
DKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAH
RLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFS
HVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGE
TFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNY
HHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG
Enzyme 17 Number of Residues 359
Enzyme 17 Molecular Weight 41522.3
Enzyme 17 Theoretical pI 9.28
Enzyme 17 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
  • stearoyl-CoA 9-desaturase activity
  • transition metal ion binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid biosynthetic process
  • fatty acid metabolic process
  • lipid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
  • primary metabolic process
Component
  • cell part
  • endoplasmic reticulum
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 17 General Function Involved in oxidoreductase activity
Enzyme 17 Specific Function Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O [RN:R02222]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 76-96 98-118 223-243 315-335
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 7415721 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O00767 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name ACOD_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1080 bp
ATGCCGGCCCACTTGCTGCAGGACGATATCTCTAGCTCCTATACCACCACCACCACCATT
ACAGCGCCTCCCTCCAGGGTCCTGCAGAATGGAGGAGATAAGTTGGAGACGATGCCCCTC
TACTTGGAAGACGACATTCGCCCTGATATAAAAGATGATATATATGACCCCACCTACAAG
GATAAGGAAGGCCCAAGCCCCAAGGTTGAATATGTCTGGAGAAACATCATCCTTATGTCT
CTGCTACACTTGGGAGCCCTGTATGGGATCACTTTGATTCCTACCTGCAAGTTCTACACC
TGGCTTTGGGGGGTATTCTACTATTTTGTCAGTGCCCTGGGCATAACAGCAGGAGCTCAT
CGTCTGTGGAGCCACCGCTCTTACAAAGCTCGGCTGCCCCTACGGCTCTTTCTGATCATT
GCCAACACAATGGCATTCCAGAATGATGTCTATGAATGGGCTCGTGACCACCGTGCCCAC
CACAAGTTTTCAGAAACACATGCTGATCCTCATAATTCCCGACGTGGCTTTTTCTTCTCT
CACGTGGGTTGGCTGCTTGTGCGCAAACACCCAGCTGTCAAAGAGAAGGGGAGTACGCTA
GACTTGTCTGACCTAGAAGCTGAGAAACTGGTGATGTTCCAGAGGAGGTACTACAAACCT
GGCTTGCTGCTGATGTGCTTCATCCTGCCCACGCTTGTGCCCTGGTATTTCTGGGGTGAA
ACTTTTCAAAACAGTGTGTTCGTTGCCACTTTCTTGCGATATGCTGTGGTGCTTAATGCC
ACCTGGCTGGTGAACAGTGCTGCCCACCTCTTCGGATATCGTCCTTATGACAAGAACATT
AGCCCCCGGGAGAATATCCTGGTTTCACTTGGAGCTGTGGGTGAGGGCTTCCACAACTAC
CACCACTCCTTTCCCTATGACTACTCTGCCAGTGAGTACCGCTGGCACATCAACTTCACC
ACATTCTTCATTGATTGCATGGCCGCCCTCGGTCTGGCCTATGACCGGAAGAAAGTCTCC
AAGGCCGCCATCTTGGCCAGGATTAAAAGAACCGGAGATGGAAACTACAAGAGTGGCTGA
Enzyme 17 GenBank Gene ID AB032261 Link Image
Enzyme 17 GeneCard ID SCD Link Image
Enzyme 17 GenAtlas ID SCD Link Image
Enzyme 17 HGNC ID HGNC:10571 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 10q24.31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Zhang L, Ge L, Parimoo S, Stenn K, Prouty SM: Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites. Biochem J. 1999 May 15;340 ( Pt 1):255-64. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Zhang L, Ge L, Tran T, Stenn K, Prouty SM: Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element. Biochem J. 2001 Jul 1;357(Pt 1):183-93. [PubMed Link Image]
  6. Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [PubMed Link Image]
  7. Li J, Ding SF, Habib NA, Fermor BF, Wood CB, Gilmour RS: Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues. Int J Cancer. 1994 May 1;57(3):348-52. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5617
Enzyme 18 Name Peroxisomal bifunctional enzyme
Enzyme 18 Synonyms
  1. PBE
  2. PBFE
  3. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
  4. 3-hydroxyacyl-CoA dehydrogenase
Enzyme 18 Gene Name EHHADH
Enzyme 18 Protein Sequence >Peroxisomal bifunctional enzyme
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAG
ADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQV
GLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEE
AIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAA
VQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSV
GVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSG
PKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIAS
STDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFV
GNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLT
GPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFL
SRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHK
GGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPS
SKL
Enzyme 18 Number of Residues 723
Enzyme 18 Molecular Weight 79494.2
Enzyme 18 Theoretical pI 9.54
Enzyme 18 GO Classification
Function
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • oxidoreductase activity
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
Component
Enzyme 18 General Function Involved in oxidoreductase activity
Enzyme 18 Specific Function (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CoA + H(2)O
Enzyme 18 Pathways
Enzyme 18 Reactions
  • (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA [RN:R04100]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 452045 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q08426 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name ECHP_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >2172 bp
ATGGCCGAGTATACGCGGCTGCACAACGCCTTGGCGCTAATCCGCCTCCGAAACCCGCCG
GTCAACGCGATCAGTACGACTTTACTCCGTGATATAAAAGAAGGACTACAGAAAGCTGGA
AGAGACCATACAATAAAAGCCATTGTGATTTGTGGAGCAGAGGGCAAATTTTCTGCAGGT
GCTGATATTCGTGGCTTCAGTGCTCCTAGGACATTTGGCCTTATACTGGGACATGTAGTA
GATGAAATACAGAGAAATGAGAAGCCCGTGGTGGCAGCAATCCAAGGCATGGCTTTCGGA
GGGGGACTAGAGCTGGCCCTGGGCTGTCACTATAGGATTGCCCACGCAGACGCTCAAGTT
GGCTTACCAGAAGTTACACTTGGACTTCTCCCTGGTGCAAGAGGAACCCAGCTTCTCCCC
AGACTCACTGGAGTTCCTGCTGCACTTGACTTAATTACCTCAGGAAGACGTATTTTAGCA
GATGAAGCACTCAAGCTGGGCATTCTAGATAAAGTTGTAAACTCAGACCCGGTTGAAGAA
GCAATCAGATTTGCTCAGAGAGTTTCAGATCAACCTCTAGAATCCCGTAGACTCTGCAAC
AAGCCAATTCAGAGCTTGCCCAACATGGACAGCATTTTTAGTGAGGCCCTCTTGAAGATG
CGGAGGCAGCACCCTGGGTGTCTTGCACAGGAGGCTTGTGTCCGTGCAGTCCAGGCTGCT
GTGCAGTATCCCTATGAAGTGGGCATCAAGAAGGAGGAGGAGCTGTTTCTATATCTTTTG
CAATCAGGGCAGGCTAGAGCCCTGCAATATGCTTTCTTCGCTGAAAGGAAAGCAAATAAG
TGGTCAACTCCCTCCGGAGCATCGTGGAAAACAGCATCAGCGCGGCCTGTCTCCTCAGTT
GGTGTTGTTGGCTTGGGAACAATGGGCCGAGGCATTGTCATTTCTTTTGCAAGGGCCAGG
ATTCCTGTGATTGGTGTAGACTCGGACAAAAACCAGCTAGCAACTGCAAACAAGATGATA
ACCTCTGTCTTGGAAAAAGAAGCCTCCAAAATGCAACAGAGCGGCCACCCTTGGTCAGGA
CCAAAACCCAGGTTAACTTCATCTGTGAAGGAGCTTGGTGGTGTAGATTTAGTCATTGAA
GCAGTATTTGAGGAAATGAGCCTGAAGAAGCAGGTCTTTGCTGAACTCTCAGCTGTGTGC
AAACCAGAAGCATTTTTGTGCACTAATACTTCAGCCCTGGATGTTGATGAGATTGCTTCT
TCCACTGATCGTCCTCACTTGGTCATTGGCACCCACTTCTTTTCGCCAGCTCATGTCATG
AAGTTGTTAGAGGTTATTCCCAGCCAATACTCTTCCCCCACTACCATTGCCACTGTTATG
AACTTATCAAAAAAGATTAAAAAGATTGGAGTCGTTGTAGGCAACTGTTTTGGATTTGTG
GGGAATCGAATGTTGAATCCTTACTACAATCAGGCATATTTCTTGTTAGAAGAAGGCAGC
AAACCAGAGGAGGTAGATCAGGTGCTGGAAGAGTTTGGTTTTAAAATGGGACCTTTTAGA
GTGTCTGATCTTGCTGGGTTGGATGTGGGCTGGAAATCTAGAAAGGGGCAAGGTCTTACT
GGACCTACATTGCTTCCAGGAACTCCTGCCCGAAAAAGGGGTAATAGGAGGTACTGCCCA
ATTCCTGATGTGCTCTGTGAATTAGGACGATTTGGCCAGAAGACAGGTAAGGGTTGGTAT
CAATATGACAAGCCATTGGGTAGGATTCACAAACCTGATCCCTGGCTTTCCACATTCCTA
TCACGGTATAGAAAACCCCATCACATTGAACCACGTACCATTAGCCAGGATGAGATCCTT
GAACGCTGCTTATATTCACTTATCAATGAAGCATTCCGTATCTTGGGAGAAGGGATAGCT
GCTAGCCCAGAGCACATTGATGTTGTCTATTTACATGGATATGGATGCGCAAGGCACAAG
GGCGGGCCCATGTTCTATGCTTCCACAGTTGGGTTGCCCACAGTTCTAGAGAAATTGCAG
AAATATTACAGGCAGAACCCTGATATTCCCCAACTGGAGCCAAGTGACTATCTAAAAAAA
CTGGCTTCTCAGGGAAACCCTCCCCTGAAAGAATGGCAAAGCTTGGCAGGCTCCCCTAGC
AGTAAATTGTGA
Enzyme 18 GenBank Gene ID L07077 Link Image
Enzyme 18 GeneCard ID EHHADH Link Image
Enzyme 18 GenAtlas ID EHHADH Link Image
Enzyme 18 HGNC ID HGNC:3247 Link Image
Enzyme 18 Chromosome Location 3
Enzyme 18 Locus 3q26.3-q28
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hoefler G, Forstner M, McGuinness MC, Hulla W, Hiden M, Krisper P, Kenner L, Ried T, Lengauer C, Zechner R, et al.: cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region. Genomics. 1994 Jan 1;19(1):60-7. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Chen GL, Balfe A, Erwa W, Hoefler G, Gaertner J, Aikawa J, Chen WW: Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1084-91. [PubMed Link Image]
  5. Chen WW, Watkins PA, Osumi T, Hashimoto T, Moser HW: Peroxisomal beta-oxidation enzyme proteins in adrenoleukodystrophy: distinction between X-linked adrenoleukodystrophy and neonatal adrenoleukodystrophy. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1425-8. [PubMed Link Image]
  6. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL: Regulation of cellular metabolism by protein lysine acetylation. Science. 2010 Feb 19;327(5968):1000-4. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5625
Enzyme 19 Name Enoyl-CoA hydratase, mitochondrial
Enzyme 19 Synonyms
  1. Enoyl-CoA hydratase 1
  2. Short-chain enoyl-CoA hydratase
  3. SCEH
Enzyme 19 Gene Name ECHS1
Enzyme 19 Protein Sequence >Enoyl-CoA hydratase, mitochondrial
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNA
LCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHW
DHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLT
RAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMA
KESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
Enzyme 19 Number of Residues 290
Enzyme 19 Molecular Weight 31387.1
Enzyme 19 Theoretical pI 8.19
Enzyme 19 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 19 General Function Involved in catalytic activity
Enzyme 19 Specific Function Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O [RN:R02685 R07314]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 55664849 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P30084 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name ECHM_HUMAN Link Image
Enzyme 19 PDB ID 2DUB Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >873 bp
ATGGCCGCCCTGCGTGTCCTGCTGTCCTGCGTCCGCGGCCCGCTGAGGCCCCCGGTTCGC
TGTCCCGCCTGGCGTCCCTTCGCCTCGGGTGCTAACTTTGAGTACATCATCGCAGAAAAA
AGAGGGAAGAATAACACCGTGGGGTTGATCCAACTGAACCGCCCCAAGGCCCTCAATGCA
CTTTGCGATGGCCTGATTGACGAGCTCAACCAGGCCCTGAAGACCTTCGAGGAGGACCCG
GCCGTGGGGGCCATTGTCCTCACCGGCGGGGATAAGGCCTTTGCAGCTGGAGCTGATATC
AAGGAAATGCAGAACCTGAGTTTCCAGGACTGTTACTCCAGCAAGTTCTTGAAGCACTGG
GACCACCTCACCCAGGTCAAGAAGCCAGTCATCGCTGCTGTCAATGGCTATGCCTTTGGC
GGGGGCTGTGAGCTTGCCATGATGTGTGATATCATCTATGCCGGTGAGAAGGCCCAGTTT
GCACAGCCGGAGATCTTAATAGGAACCATCCCAGGTGCGGGCGGCACCCAGAGACTCACC
CGTGCTGTTGGGAAGTCGCTGGCGATGGAGATGGTCCTCACTGGTGACCGGATCTCAGCC
CAGGACGCCAAGCAAGCAGGTCTTGTCAGCAAGATTTGTCCTGTTGAGACACTGGTGGAA
GAAGCCATCCAGTGTGCAGAAAAAATTGCCAGCAATTCTAAAATTGTAGTAGCGATGGCC
AAAGAATCAGTGAATGCAGCTTTTGAAATGACATTAACAGAAGGAAGTAAGTTGGAGAAG
AAACTCTTTTATTCAACCTTTGCCACTGATGACCGGAAAGAAGGGATGACCGCGTTTGTG
GAAAAGAGAAAGGCCAACTTCAAAGACCAGTGA
Enzyme 19 GenBank Gene ID AL360181 Link Image
Enzyme 19 GeneCard ID ECHS1 Link Image
Enzyme 19 GenAtlas ID ECHS1 Link Image
Enzyme 19 HGNC ID HGNC:3151 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 10q26.2-q26.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Kanazawa M, Ohtake A, Abe H, Yamamoto S, Satoh Y, Takayanagi M, Niimi H, Mori M, Hashimoto T: Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase. Enzyme Protein. 1993;47(1):9-13. [PubMed Link Image]
  2. Janssen U, Davis EM, Le Beau MM, Stoffel W: Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3. Genomics. 1997 Mar 15;40(3):470-5. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  6. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5626
Enzyme 20 Name Trifunctional enzyme subunit alpha, mitochondrial
Enzyme 20 Synonyms
  1. 78 kDa gastrin-binding protein
  2. TP-alpha
  3. Long-chain enoyl-CoA hydratase
  4. Long chain 3-hydroxyacyl-CoA dehydrogenase
Enzyme 20 Gene Name HADHA
Enzyme 20 Protein Sequence >Trifunctional enzyme subunit alpha, mitochondrial
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 20 Number of Residues 763
Enzyme 20 Molecular Weight 82999.0
Enzyme 20 Theoretical pI 9.52
Enzyme 20 GO Classification
Function
  • 3-hydroxyacyl-CoA dehydrogenase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • enoyl-CoA hydratase activity
  • hydro-lyase activity
  • lyase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • fatty acid beta-oxidation multienzyme complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • mitochondrion
  • organelle
  • protein complex
Enzyme 20 General Function Involved in oxidoreductase activity
Enzyme 20 Specific Function Bifunctional subunit
Enzyme 20 Pathways
Enzyme 20 Reactions
  • (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O [RN:R02685 R07314]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 189053609 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P40939 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name ECHA_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2292 bp
ATGGTGGCCTGCCGGGCGATTGGCATCCTCAGCCGCTTTTCTGCCTTCAGGATCCTCCGC
TCCCGAGGTTATATATGCCGCAATTTTACAGGGTCTTCTGCTTTGCTGACCAGAACCCAT
ATTAACTATGGAGTCAAAGGGGATGTGGCAGTTGTTCGAATTAACTCTCCCAATTCAAAG
GTAAATACACTGAGTAAAGAGCTACATTCAGAGTTCTCAGAAGTTATGAATGAAATCTGG
GCTAGTGATCAAATCAGAAGTGCCGTCCTTATCTCATCAAAGCCAGGCTGCTTTATTGCA
GGTGCTGATATCAACATGTTAGCCGCTTGCAAGACCCTTCAAGAAGTAACACAGCTATCA
CAAGAAGCACAGAGAATAGTTGAGAAACTTGAAAAGTCCACAAAGCCTATTGTGGCTGCC
ATCAATGGATCCTGCCTGGGAGGAGGACTTGAGGTTGCCATTTCATGCCAATATAGAATA
GCAACAAAAGACAGAAAAACAGTATTAGGTACCCCTGAAGTTTTGCTGGGGGCCTTACCA
GGAGCAGGAGGCACACAAAGGCTGCCCAAAATGGTGGGTGTGCCTGCTGCTTTGGACATG
ATGCTGACTGGTAGAAGCATTCGTGCAGACAGGGCAAAGAAAATGGGACTGGTTGACCAA
CTGGTGGAACCCCTGGGACCAGGACTAAAACCTCCAGAGGAACGGACAATAGAATACCTA
GAAGAAGTTGCAATTACTTTTGCCAAAGGACTAGCTGATAAGAAGATCTCTCCAAAGAGA
GACAAGGGATTGGTGGAAAAATTGACAGCGTATGCCATGACTATTCCATTTGTCAGGCAA
CAGGTTTACAAAAAAGTGGAAGAAAAAGTGCGAAAGCAGACTAAAGGCCTTTATCCTGCA
CCTCTGAAAATAATTGATGTGGTAAAGACTGGAATTGAGCAAGGGAGTGATGCCGGTTAT
CTCTGTGAATCTCAGAAATTTGGAGAGCTTGTAATGACCAAAGAATCAAAGGCCTTGATG
GGACTCTACCATGGTCAGGTCCTGTGCAAGAAGAATAAATTTGGAGCTCCACAGAAGGAT
GTTAAGCATCTGGCTATTCTTGGTGCAGGGCTGATGGGAGCAGGCATCGCCCAAGTCTCC
GTGGATAAGGGGCTAAAGACTATACTTAAAGATGCCACCCTCACTGCGCTAGACCGAGGA
CAGCAACAAGTGTTCAAAGGATTGAATGACAAAGTGAAGAAGAAAGCTCTAACATCATTT
GAAAGGGATTCCATCTTCAGCAACTTGACTGGGCAGCTTGATTACCAAGGTTTTGAAAAG
GCCGACATGGTGATTGAAGCTGTGTTTGAGGACCTTAGTCTTAAGCACAGAGTGCTAAAG
GAAGTAGAAGCGGTGATTCCAGATCACTGTATCTTTGCCAGTAACACATCTGCTCTCCCA
ATCAGTGAAATCGCTGCTGTCAGCAAAAGACCTGAGAAGGTGATTGGCATGCACTACTTC
TCTCCCGTGGACAAGATGCAGCTGCTGGAGATTATCACGACCGAGAAAACTTCCAAAGAC
ACCAGTGCTTCAGCTGTAGCAGTTGGTCTCAAGCAGGGGAAGGTCATCATTGTGGTTAAG
GATGGACCTGGCTTCTATACTACCAGGTGTCTTGCGCCCATGATGTCTGAAGTCATCCGA
ATCCTCCAGGAAGGAGTTGACCCGAAGAAGCTGGATTCCCTGACCACAAGCTTTGGCTTT
CCTGTGGGTGCCGCCACACTGGTGGATGAAGTTGGTGTGGATGTAGCGAAACATGTGGCG
GAAGATCTGGGCAAAGTCTTTGGGGAGCGGTTTGGAGGTGGAAACCCAGAACTGCTGACA
CAGATGGTGTCCAAGGGCTTCCTAGGTCGTAAATCTGGGAAGGGCTTTTACATCTATCAG
GAGGGTGTGAAGAGGAAGGATTTGAATTCTGACATGGATAGTATTTTAGCGAGTCTGAAG
CTGCCTCCTAAGTCTGAAGTCTCATCAGACGAAGACATCCAGTTCCGCCTGGTGACAAGA
TTTGTGAATGAGGCAGTCATGTGCCTGCAAGAGGGGATCTTGGCCACACCTGCAGAGGGA
GACATCGGAGCCGTCTTTGGGCTTGGCTTCCCGCCTTGTCTGGGAGGGCCTTTCCGCTTT
GTGGATCTGTATGGCGCCCAGAAGATAGTGGACCGGCTCAAGAAATATGAAGCTGCCTAT
GGAAAACAGTTCACCCCATGCCAGCTGCTAGCTGACCATGCTAACAGCCCTAACAAGAAG
TTCTACCAGTGA
Enzyme 20 GenBank Gene ID AK313027 Link Image
Enzyme 20 GeneCard ID HADHA Link Image
Enzyme 20 GenAtlas ID HADHA Link Image
Enzyme 20 HGNC ID HGNC:4801 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 2p23
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed Link Image]
  2. Zhang QX, Baldwin GS: Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene. Biochim Biophys Acta. 1994 Oct 18;1219(2):567-75. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kamijo T, Wanders RJ, Saudubray JM, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest. 1994 Apr;93(4):1740-7. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. IJlst L, Wanders RJ, Ushikubo S, Kamijo T, Hashimoto T: Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein. Biochim Biophys Acta. 1994 Dec 8;1215(3):347-50. [PubMed Link Image]
  9. Sims HF, Brackett JC, Powell CK, Treem WR, Hale DE, Bennett MJ, Gibson B, Shapiro S, Strauss AW: The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):841-5. [PubMed Link Image]
  10. IJlst L, Ruiter JP, Hoovers JM, Jakobs ME, Wanders RJ: Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene. J Clin Invest. 1996 Aug 15;98(4):1028-33. [PubMed Link Image]
  11. IJlst L, Oostheim W, Ruiter JP, Wanders RJ: Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of two new mutations. J Inherit Metab Dis. 1997 Jul;20(3):420-2. [PubMed Link Image]
  12. Ibdah JA, Tein I, Dionisi-Vici C, Bennett MJ, IJlst L, Gibson B, Wanders RJ, Strauss AW: Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation. J Clin Invest. 1998 Sep 15;102(6):1193-9. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5746
Enzyme 21 Name Sterol O-acyltransferase 2
Enzyme 21 Synonyms
  1. Acyl-coenzyme A:cholesterol acyltransferase 2
  2. ACAT-2
  3. Cholesterol acyltransferase 2
Enzyme 21 Gene Name SOAT2
Enzyme 21 Protein Sequence >Sterol O-acyltransferase 2
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQL
RELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHF
RTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLA
PYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFL
MKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKN
FAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLH
CWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARG
VAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTM
LFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT
Enzyme 21 Number of Residues 522
Enzyme 21 Molecular Weight 59895.7
Enzyme 21 Theoretical pI 8.71
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Involved in acyl-CoA binding
Enzyme 21 Specific Function Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa
Enzyme 21 Pathways
Enzyme 21 Reactions
  • acyl-CoA + cholesterol = CoA + cholesterol ester [RN:R01461]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 124-144 155-175 200-220 262-282 304-324 344-366 437-457 472-492
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID O75908 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name SOAT2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1569 bp
ATGGAGCCAGGCGGGGCCCGTCTGCGTCTGCAGAGGACAGAAGGGCTGGGAGGGGAGCGG
GAGCGCCAACCCTGTGGAGATGGAAACACTGAGACGCACAGAGCCCCGGACTTGGTACAA
TGGACCCGACACATGGAGGCTGTGAAGGCACAATTGCTGGAGCAAGCGCAGGGACAACTG
AGGGAGCTGCTGGATCGGGCCATGCGGGAGGCTATACAATCCTACCCATCACAAGACAAA
CCTCTGCCCCCACCTCCCCCAGGTTCCTTGAGCAGGACCCAGGAGCCATCCCTGGGGAAA
CAGAAAGTTTTCATCATCCGCAAGTCCCTGCTTGATGAGCTGATGGAGGTGCAGCATTTC
CGCACCATCTACCACATGTTCATCGCTGGCCTGTGTGTCTTCATCATCAGCACCCTGGCC
ATCGACTTCATTGATGAGGGCAGGCTGCTGCTGGAGTTTGACCTACTGATCTTCAGCTTC
GGACAGCTGCCATTGGCGCTGGTGACCTGGGTGCCCATGTTTCTGTCCACCCTGTTGGCG
CCGTACCAGGCCCTACGGCTGTGGGCCAGGGGCACCTGGACGCAGGCGACGGGCCTGGGC
TGTGCGCTGCTAGCCGCCCACGCCGTGGTGCTCTGCGCGCTGCCGGTCCACGTGGCCGTG
GAGCATCAGCTCCCGCCGGCCTCCCGTTGTGTCCTGGTCTTCGAGCAGGTTAGGTTCCTG
ATGAAAAGCTACTCCTTCCTGAGAGAGGCTGTGCCTGGGACCCTTCGTGCCAGACGAGGT
GAGGGGATCCAGGCCCCCAGTTTCTCCAGCTACCTCTACTTCCTCTTCTGCCCAACACTC
ATCTACAGGGAGACTTACCCTAGGACGCCCTATGTCAGGTGGAATTATGTGGCCAAGAAC
TTTGCCCAGGCCCTGGGATGTGTGCTCTATGCCTGCTTCATCCTGGGCCGCCTCTGTGTT
CCTGTCTTTGCCAACATGAGCCGAGAGCCCTTCAGCACCCGTGCCCTGGTGCTCTCTATC
CTGCATGCCACGTTGCCAGGCATCTTCATGCTGCTGCTCATCTTCTTTGCCTTCCTCCAT
TGCTGGCTCAACGCCTTTGCCGAGATGCTACGATTTGGAGACAGGATGTTCTACCGGGAC
TGGTGGAACTCAACGTCCTTCTCCAACTACTACCGCACTTGGAACGTGGTGGTCCATGAC
TGGCTGTACAGCTACGTGTATCAGGATGGGCTGCGGCTCCTTGGTGCCCGGGCCCGAGGG
GTAGCCATGCTGGGTGTGTTCCTGGTCTCCGCAGTGGCCCATGAGTATATCTTCTGCTTC
GTCCTGGGGTTCTTCTATCCCGTCATGCTGATACTCTTCCTTGTCATTGGAGGAATGTTG
AACTTCATGATGCATGACCAGCGCACCGGCCCGGCATGGAACGTGCTGATGTGGACCATG
CTGTTTCTAGGCCAGGGAATCCAGGTCAGCCTGTACTGCCAGGAGTGGTACGCACGGCGG
CACTGCCCCTTACCCCAGGCAACTTTCTGGGGGCTGGTGACACCTCGATCTTGGTCCTGC
CATACCTAG
Enzyme 21 GenBank Gene ID AF059203 Link Image
Enzyme 21 GeneCard ID SOAT2 Link Image
Enzyme 21 GenAtlas ID SOAT2 Link Image
Enzyme 21 HGNC ID HGNC:11178 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 12q13.13
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Oelkers P, Behari A, Cromley D, Billheimer JT, Sturley SL: Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes. J Biol Chem. 1998 Oct 9;273(41):26765-71. [PubMed Link Image]
  2. Chang CC, Sakashita N, Ornvold K, Lee O, Chang ET, Dong R, Lin S, Lee CY, Strom SC, Kashyap R, Fung JJ, Farese RV Jr, Patoiseau JF, Delhon A, Chang TY: Immunological quantitation and localization of ACAT-1 and ACAT-2 in human liver and small intestine. J Biol Chem. 2000 Sep 8;275(36):28083-92. [PubMed Link Image]
  3. Katsuren K, Tamura T, Arashiro R, Takata K, Matsuura T, Niikawa N, Ohta T: Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2) gene and its relation to dyslipidemia. Biochim Biophys Acta. 2001 Apr 30;1531(3):230-40. [PubMed Link Image]
  4. Song BL, Qi W, Yang XY, Chang CC, Zhu JQ, Chang TY, Li BL: Organization of human ACAT-2 gene and its cell-type-specific promoter activity. Biochem Biophys Res Commun. 2001 Mar 30;282(2):580-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5751
Enzyme 22 Name Sterol O-acyltransferase 1
Enzyme 22 Synonyms
  1. Acyl-coenzyme A:cholesterol acyltransferase 1
  2. ACAT-1
  3. Cholesterol acyltransferase 1
Enzyme 22 Gene Name SOAT1
Enzyme 22 Protein Sequence >Sterol O-acyltransferase 1
MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEE
LKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGK
IFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGK
FPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPT
YVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYF
LFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSAR
VLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTW
NVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFM
FFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVR
PRSWTCRYVF
Enzyme 22 Number of Residues 550
Enzyme 22 Molecular Weight 64734.0
Enzyme 22 Theoretical pI 9.18
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Involved in acyl-CoA binding
Enzyme 22 Specific Function Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase
Enzyme 22 Pathways
Enzyme 22 Reactions
  • acyl-CoA + cholesterol = CoA + cholesterol ester [RN:R01461]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 141-159 320-341 361-382 470-490 498-518
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 55959989 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P35610 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name SOAT1_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1653 bp
ATGGTGGGTGAAGAGAAGATGTCTCTAAGAAACCGGCTGTCAAAGTCCAGGGAAAATCCT
GAGGAAGATGAAGACCAGAGAAACCCTGCAAAGGAGTCCCTAGAGACACCTAGTAATGGT
CGAATTGACATAAAACAGTTGATAGCAAAGAAGATAAAGTTGACAGCAGAGGCAGAGGAA
TTGAAGCCATTTTTTATGAAGGAAGTTGGCAGTCACTTTGATGATTTTGTGACCAATCTC
ATTGAAAAGTCAGCATCATTAGATAATGGTGGGTGCGCTCTCACAACCTTTTCTGTTCTT
GAAGGAGAGAAAAACAACCATAGAGCGAAGGATTTGAGAGCACCTCCAGAACAAGGAAAG
ATTTTTATTGCAAGGCGCTCTCTCTTAGATGAACTGCTTGAAGTGGACCACATCAGAACA
ATATATCACATGTTTATTGCCCTCCTCATTCTCTTTATCCTCAGCACACTTGTAGTAGAT
TACATTGATGAAGGAAGGCTGGTGCTTGAGTTCAGCCTCCTGTCTTATGCTTTTGGCAAA
TTTCCTACCGTTGTTTGGACCTGGTGGATCATGTTCCTGTCTACATTTTCAGTTCCCTAT
TTTCTGTTTCAACATTGGGCCACTGGCTATAGCAAGAGTTCTCATCCGCTGATCCGTTCT
CTCTTCCATGGCTTTCTTTTCATGATCTTCCAGATTGGAGTTCTAGGTTTTGGACCAACA
TATGTTGTGTTAGCATATACACTGCCACCAGCTTCCCGGTTCATCATTATATTCGAGCAG
ATTCGTTTTGTAATGAAGGCCCACTCATTTGTCAGAGAGAACGTGCCTCGGGTACTAAAT
TCAGCTAAGGAGAAATCAAGCACTGTTCCAATACCTACAGTCAACCAGTATTTGTACTTC
TTATTTGCTCCTACCCTTATCTACCGTGACAGCTATCCCAGGAATCCCACTGTAAGATGG
GGTTATGTCGCTATGAAGTTTGCACAGGTCTTTGGTTGCTTTTTCTATGTGTACTACATC
TTTGAAAGGCTTTGTGCCCCCTTGTTTCGGAATATCAAACAGGAGCCCTTCAGCGCTCGT
GTTCTGGTCCTATGTGTATTTAACTCCATCTTGCCAGGTGTGCTGATTCTCTTCCTTACT
TTTTTTGCCTTTTTGCACTGCTGGCTCAATGCCTTTGCTGAGATGTTACGCTTTGGTGAC
AGGATGTTCTATAAGGATTGGTGGAACTCCACGTCATACTCCAACTATTATAGAACCTGG
AATGTGGTGGTCCATGACTGGCTATATTACTATGCTTACAAGGACTTTCTCTGGTTTTTC
TCCAAGAGATTCAAATCTGCTGCCATGTTAGCTGTCTTTGCTGTATCTGCTGTAGTACAC
GAATATGCCTTGGCTGTTTGCTTGAGCTTTTTCTATCCCGTGCTCTTCGTGCTCTTCATG
TTCTTTGGAATGGCTTTCAACTTCATTGTCAATGATAGTCGGAAAAAGCCGATTTGGAAT
GTTCTGATGTGGACTTCTCTTTTCTTGGGCAATGGAGTCTTACTCTGCTTTTATTCTCAA
GAATGGTATGCACGTCAGCACTGTCCTCTGAAAAATCCCACATTTTTGGATTATGTCCGG
CCACGTTCCTGGACTTGTCGTTACGTGTTTTAG
Enzyme 22 GenBank Gene ID AL451075 Link Image
Enzyme 22 GeneCard ID SOAT1 Link Image
Enzyme 22 GenAtlas ID SOAT1 Link Image
Enzyme 22 HGNC ID HGNC:11177 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 1q25
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Chang CC, Huh HY, Cadigan KM, Chang TY: Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells. J Biol Chem. 1993 Oct 5;268(28):20747-55. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Lin S, Cheng D, Liu MS, Chen J, Chang TY: Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains. J Biol Chem. 1999 Aug 13;274(33):23276-85. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5821
Enzyme 23 Name Bile acid-CoA:amino acid N-acyltransferase
Enzyme 23 Synonyms
  1. BACAT
  2. BAT
  3. Glycine N-choloyltransferase
  4. Long-chain fatty-acyl-CoA hydrolase
Enzyme 23 Gene Name BAAT
Enzyme 23 Protein Sequence >Bile acid-CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Enzyme 23 Number of Residues 418
Enzyme 23 Molecular Weight 46298.9
Enzyme 23 Theoretical pI 7.00
Enzyme 23 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 23 General Function Involved in thiolester hydrolase activity
Enzyme 23 Specific Function Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs
Enzyme 23 Pathways
Enzyme 23 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID Q14032 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name BAAT_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
Enzyme 23 GenBank Gene ID L34081 Link Image
Enzyme 23 GeneCard ID BAAT Link Image
Enzyme 23 GenAtlas ID BAAT Link Image
Enzyme 23 HGNC ID HGNC:932 Link Image
Enzyme 23 Chromosome Location 9
Enzyme 23 Locus 9q22.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Johnson MR, Barnes S, Kwakye JB, Diasio RB: Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J Biol Chem. 1991 Jun 5;266(16):10227-33. [PubMed Link Image]
  5. Sfakianos MK, Wilson L, Sakalian M, Falany CN, Barnes S: Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. J Biol Chem. 2002 Dec 6;277(49):47270-5. Epub 2002 Sep 17. [PubMed Link Image]
  6. O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE: The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J Biol Chem. 2003 Sep 5;278(36):34237-44. Epub 2003 Jun 16. [PubMed Link Image]
  7. Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5842
Enzyme 24 Name Long-chain-fatty-acid--CoA ligase 4
Enzyme 24 Synonyms
  1. Long-chain acyl-CoA synthetase 4
  2. LACS 4
Enzyme 24 Gene Name ACSL4
Enzyme 24 Protein Sequence >Long-chain-fatty-acid--CoA ligase 4
MKLKLNVLTIILLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYR
SVTHFDSLAVIDIPGADTLDKLFDHAVSKFGKKDSLGTREILSEENEMQPNGKVFKKLIL
GNYKWMNYLEVNRRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTL
YATLGKEAVVHGLNESEASYLITSVELLESKLKTALLDISCVKHIIYVDNKAINKAEYPE
GFEIHSMQSVEELGSNPENLGIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT
GQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSK
GDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLC
NLLLFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEV
TDYTTGRVGAPLICCEIKLKDWQEGGYTINDKPNPRGEIVIGGQNISMGYFKNEEKTAED
YSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDN
ICAFAKSDQSYVISFVVPNQKRLTLLAQQKGVEGTWVDICNNPAMEAEILKEIREAANAM
KLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELRNHYLKDIERMYGGK
Enzyme 24 Number of Residues 711
Enzyme 24 Molecular Weight 79187.4
Enzyme 24 Theoretical pI 8.51
Enzyme 24 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 24 General Function Involved in catalytic activity
Enzyme 24 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 8-28
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 12669909 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID O60488 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name ACSL4_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2136 bp
ATGAAACTTAAGCTAAATGTGCTCACCATTATTTTGCTGCCTGTCCACTTGTTAATAACA
ATATACAGTGCCCTTATATTTATTCCATGGTATTTTCTTACCAATGCCAAGAAGAAAAAC
GCTATGGCAAAGAGAATAAAAGCTAAGCCCACTTCAGACAAACCTGGAAGTCCATATCGC
TCTGTCACACACTTCGACTCACTAGCTGTAATAGACATCCCTGGAGCAGATACTCTGGAT
AAATTATTTGACCATGCTGTATCCAAGTTTGGGAAGAAGGACAGCCTTGGGACCAGGGAA
ATCCTAAGTGAAGAAAATGAAATGCAGCCAAATGGAAAAGTTTTTAAGAAGTTAATTCTT
GGGAATTATAAATGGATGAACTATCTTGAAGTGAATCGCAGAGTGAATAACTTTGGTAGT
GGACTCACTGCACTGGGACTAAAACCAAAGAACACCATTGCCATCTTCTGTGAGACCAGG
GCCGAATGGATGATTGCAGCACAGACCTGCTTTAAGTACAACTTTCCTCTTGTGACTTTA
TATGCCACACTTGGCAAAGAAGCAGTAGTTCATGGGCTAAATGAATCTGAGGCTTCCTAT
CTGATTACCAGTGTTGAACTTCTGGAAAGTAAACTTAAGACTGCATTGTTAGATATCAGT
TGTGTTAAACATATCATTTATGTGGACAATAAGGCTATCAATAAAGCAGAGTACCCTGAA
GGATTTGAGATTCACAGCATGCAATCAGTAGAAGAGTTGGGATCTAACCCAGAAAACTTG
GGCATTCCTCCAAGTAGACCAACGCCTTCAGACATGGCCATTGTTATGTATACTAGTGGT
TCTACTGGCCGACCTAAGGGAGTGATGATGCATCATAGCAATTTGATAGCTGGAATGACA
GGCCAGTGTGAAAGAATACCTGGACTGGGACCGAAGGACACATATATTGGCTACTTGCCT
TTGGCTCATGTGCTAGAACTGACAGCAGAGATATCTTGCTTTACCTATGGCTGCAGGATT
GGATATTCTTCTCCGCTTACACTCTCTGACCAGTCCAGCAAAATTAAAAAAGGAAGCAAA
GGAGACTGTACTGTACTGAAGCCCACACTTATGGCTGCTGTTCCGGAAATCATGGATAGA
ATTTATAAGAATGTTATGAGCAAAGTCCAAGAGATGAATTATATTCAGAAAACTCTGTTC
AAGATAGGGTATGATTACAAATTGGAACAGATCAAAAAGGGATATGATGCACCTCTTTGC
AATCTGTTACTGTTTAAAAAGGTCAAGGCCCTGCTGGGAGGGAATGTCCGCATGATGCTG
TCTGGAGGGGCCCCGCTATCTCCTCAGACACACCGATTCATGAATGTCTGCTTCTGCTGC
CCAATTGGCCAGGGTTATGGACTGACAGAATCATGTGGTGCTGGGACAGTTACTGAAGTA
ACTGACTATACTACTGGCAGAGTTGGAGCACCTCTTATTTGCTGTGAAATTAAGCTAAAA
GACTGGCAAGAAGGCGGTTATACAATTAATGACAAGCCAAACCCCAGAGGTGAAATCGTA
ATTGGTGGACAGAACATCTCCATGGGATATTTTAAAAATGAAGAGAAAACAGCAGAAGAT
TATTCTGTGGATGAAAATGGACAAAGGTGGTTTTGCACTGGTGATATTGGAGAATTCCAT
CCCGATGGATGTTTACAGATTATAGATCGTAAGAAAGATCTAGTGAAGTTACAAGCAGGA
GAGTATGTATCTCTTGGGAAAGTAGAAGCTGCACTGAAGAATTGTCCACTTATTGACAAC
ATCTGTGCTTTTGCCAAAAGTGATCAGTCCTATGTGATCAGTTTTGTGGTTCCTAACCAG
AAAAGGTTGACACTTTTGGCACAACAGAAAGGGGTAGAAGGAACTTGGGTTGATATCTGC
AATAATCCTGCTATGGAAGCTGAAATACTGAAAGAAATTCGAGAAGCTGCAAATGCCATG
AAATTGGAGCGATTTGAAATTCCAATCAAGGTTCGATTAAGCCCAGAGCCATGGACCCCT
GAAACTGGTTTGGTAACTGATGCTTTCAAACTGAAAAGGAAGGAGCTGAGGAACCATTAC
CTCAAAGACATTGAACGAATGTATGGGGGCAAATAA
Enzyme 24 GenBank Gene ID NM_022977.2 Link Image
Enzyme 24 GeneCard ID ACSL4 Link Image
Enzyme 24 GenAtlas ID ACSL4 Link Image
Enzyme 24 HGNC ID HGNC:3571 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Cao Y, Traer E, Zimmerman GA, McIntyre TM, Prescott SM: Cloning, expression, and chromosomal localization of human long-chain fatty acid-CoA ligase 4 (FACL4). Genomics. 1998 Apr 15;49(2):327-30. [PubMed Link Image]
  2. Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ, Villanova M, Zollo M, Borsani G, Ballabio A, Renieri A: FACL4, a new gene encoding long-chain acyl-CoA synthetase 4, is deleted in a family with Alport syndrome, elliptocytosis, and mental retardation. Genomics. 1998 Feb 1;47(3):350-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  5. Meloni I, Muscettola M, Raynaud M, Longo I, Bruttini M, Moizard MP, Gomot M, Chelly J, des Portes V, Fryns JP, Ropers HH, Magi B, Bellan C, Volpi N, Yntema HG, Lewis SE, Schaffer JE, Renieri A: FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat Genet. 2002 Apr;30(4):436-40. Epub 2002 Mar 11. [PubMed Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5849
Enzyme 25 Name Long-chain-fatty-acid--CoA ligase 1
Enzyme 25 Synonyms
  1. Acyl-CoA synthetase 1
  2. ACS1
  3. Long-chain acyl-CoA synthetase 1
  4. LACS 1
  5. Long-chain acyl-CoA synthetase 2
  6. LACS 2
  7. Long-chain fatty acid-CoA ligase 2
  8. Palmitoyl-CoA ligase 1
  9. Palmitoyl-CoA ligase 2
Enzyme 25 Gene Name ACSL1
Enzyme 25 Protein Sequence >Long-chain-fatty-acid--CoA ligase 1
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
Enzyme 25 Number of Residues 698
Enzyme 25 Molecular Weight 77942.7
Enzyme 25 Theoretical pI 7.16
Enzyme 25 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 25 General Function Involved in catalytic activity
Enzyme 25 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 25-45
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID P33121 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name ACSL1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2097 bp
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
Enzyme 25 GenBank Gene ID D10040 Link Image
Enzyme 25 GeneCard ID ACSL1 Link Image
Enzyme 25 GenAtlas ID ACSL1 Link Image
Enzyme 25 HGNC ID HGNC:3569 Link Image
Enzyme 25 Chromosome Location 4
Enzyme 25 Locus 4q35
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed Link Image]
  2. Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5894
Enzyme 26 Name Long-chain-fatty-acid--CoA ligase 6
Enzyme 26 Synonyms
  1. Long-chain acyl-CoA synthetase 6
  2. LACS 6
Enzyme 26 Gene Name ACSL6
Enzyme 26 Protein Sequence >Long-chain-fatty-acid--CoA ligase 6
MQTQEILRILRLPELGDLGQFFRSLSATTLVSMGALAAILAYWFTHRPKALQPPCNLLMQ
SEEVEDSGGARRSVIGSGPQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPKQPYQW
LSYQEVADRAEFLGSGLLQHNCKACTDQFIGVFAQNRPEWIIVELACYTYSMVVVPLYDT
LGPGAIRYIINTADISTVIVDKPQKAVLLLEHVERKETPGLKLIILMDPFEEALKERGQK
CGVVIKSMQAVEDCGQENHQAPVPPQPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGF
LKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALCP
TIFPVVPRLLNRMYDKIFSQANTPLKRWLLEFAAKRKQAEVRSGIIRNDSIWDELFFNKI
QASLGGCVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV
GAPLPCNHIKLVDVEELNYWACKGEGEICVRGPNVFKGYLKDPDRTKEALDSDGWLHTGD
IGKWLPAGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSQPVAQIYVHGDSLKAFLVGI
VVPDPEVMPSWAQKRGIEGTYADLCTNKDLKKAILEDMVRLGKESGLHSFEQVKAIHIHS
DMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM
Enzyme 26 Number of Residues 697
Enzyme 26 Molecular Weight 77751.3
Enzyme 26 Theoretical pI 7.46
Enzyme 26 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 26 General Function Involved in catalytic activity
Enzyme 26 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 25-45
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 5702202 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9UKU0 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name ACSL6_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >2094 bp
ATGCAGACACAGGAGATCCTGAGGATACTGCGACTGCCTGAGCTAGGTGACTTGGAACAG
TTTTTCCGCAGCCTCTCGGCCACCACCCTCGTGAGTATGGGTGCCCTGGCTGCCATCCTT
GCCTACTGGTTCACTCAGCGGCCAAAGGCCTTGCAGCCGCCATGCAACCTCCTGATGCAG
TCAGAAGAAGTAGAGGACAGTGGCGGGGCACGGCGATCTGTGATTGGGTCTGGCCCTCAG
CTACTTACCCACTACTATGATGATGCCCGGACCATGTACCAGGTGTTCCGCCGTGGGCTT
AGCATCTCAGGGAATGGGCCCTGTCTTGGTTTCAGGAAGCCTAAGCAGCCTTACCAGTGG
CTGTCCTACCAGGAGGTGGCCGACAGGGCTGAATTTCTGGGGTCCGGACTTCTCCAGCAC
AATTGTAAAGCATGCACTGATCAGTTTATTGGTGTTTTTGCACAAAATCGGCCAGAGTGG
ATCATTGTGGAGCTGGCCTGCTACACATATTCCATGGTGGTGGTCCCGCTCTATGACACC
CTGGGCCCTGGGGCTATCCGCTACATCATCAATACAGCGGACATCAGCACCGTGATTGTG
GACAAACCTCAGAAGGCTGTGCTTCTGCTAGAGCATGTGGAGAGGAAGGAGACTCCAGGC
CTCAAGCTGATCATCCTCATGGACCCATTCGAAGAAGCCCTGAAAGAGAGAGGGCAGAAG
TGCGGGGTGGTCATTAAGTCCATGCAGGCCGTGGAGGACTGTGGCCAAGAGAATCACCAG
GCTCCTGTGCCCCCGCAGCCTGATGACCTCTCCATTGTGTGTTTCACAAGCGGCACGACA
GGGAACCCAAAAGGTGCGATGCTCACCCATGGGAACGTGGTGGCTGATTTCTCAGGCTTT
CTGAAAGTGACAGAGAGTCAGTGGGCTCCCACTTGTGCGGATGTGCACATTTCCTATTTG
CCTTTAGCACACATGTTTGAGCGAATGGTGCAGTCTGTCGTCTATTGCCACGGAGGGCGT
GTTGGCTTCTTCCAGGGAGATATCCGCCTTCTCTCAGATGACATGAAGGCTCTATGCCCC
ACCATCTTCCCTGTGGTCCCACGACTGCTGAACCGGATGTACGACAAGATCTTCAGCCAG
GCAAACACACCATTAAAGCGCTGGCTCCTGGAGTTTGCAGCAAAGCGTAAGCAAGCCGAG
GTCCGGAGTGGAATCATCAGGAATGATAGTATCTGGGATGAACTCTTCTTTAATAAGATT
CAGGCCAGTCTTGGTGGGTGTGTGCGGATGATTGTTACTGGAGCAGCCCCAGCATCACCA
ACAGTTCTGGGATTTCTCCGGGCAGCTCTAGGGTGCCAGGTTTATGAAGGTTATGGCCAA
ACTGAGTGCACAGCTGGATGTACCTTCACCACTCCTGGCGACTGGACCTCAGGGCACGTA
GGGGCGCCACTTCCCTGCAATCATATCAAGCTCGTTGATGTTGAGGAACTGAACTACTGG
GCCTGCAAAGGAGAGGGAGAGATATGTGTGAGAGGACCAAATGTGTTCAAAGGCTACTTG
AAAGATCCAGACAGGACGAAGGAGGCCCTGGACAGCGATGGCTGGCTTCACACTGGAGAC
ATCGGAAAATGGCTGCCGGCAGGAACTCTTAAAATTATTGATCGGAAAAAGCATATATTT
AAACTTGCTCAGGGAGAATATGTTGCACCCGAGAAGATTGAGAACATCTACATCCGGAGC
CAACCTGTGGCGCAAATCTATGTCCATGGGGACAGCTTAAAGGCCTTTTTGGTAGGCATT
GTTGTGCCTGACCCTGAAGTTATGCCCTCCTGGGCCCAGAAGAGAGGAATTGAAGGAACA
TATGCAGATCTCTGCACAAATAAGGATCTGAAGAAAGCCATTTTGGAAGATATGGTGAGG
TTAGGAAAAGAAAGTGGACTCCATTCTTTTGAGCAGGTTAAAGCCATTCACATCCATTCT
GACATGTTCTCAGTTCAAAATGGCTTGCTGACCCCAACACTAAAAGCTAAGAGACCTGAG
CTGAGAGAGTACTTCAAAAAACAAATAGAAGAGCTTTACTCAATCCCCATGTGA
Enzyme 26 GenBank Gene ID AF129166 Link Image
Enzyme 26 GeneCard ID ACSL6 Link Image
Enzyme 26 GenAtlas ID ACSL6 Link Image
Enzyme 26 HGNC ID HGNC:16496 Link Image
Enzyme 26 Chromosome Location 5
Enzyme 26 Locus 5q31
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
  2. Yagasaki F, Jinnai I, Yoshida S, Yokoyama Y, Matsuda A, Kusumoto S, Kobayashi H, Terasaki H, Ohyashiki K, Asou N, Murohashi I, Bessho M, Hirashima K: Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). Genes Chromosomes Cancer. 1999 Nov;26(3):192-202. [PubMed Link Image]
  3. Soupene E, Kuypers FA: Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains. BMC Mol Biol. 2006 Jul 11;7:21. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
  5. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5916
Enzyme 27 Name Long-chain-fatty-acid--CoA ligase 5
Enzyme 27 Synonyms
  1. Long-chain acyl-CoA synthetase 5
  2. LACS 5
Enzyme 27 Gene Name ACSL5
Enzyme 27 Protein Sequence >Long-chain-fatty-acid--CoA ligase 5
MLFIFNFLFSPLPTPALICILTFGAAIFLWLITRPQPVLPLLDLNNQSVGIEGGARKGVS
QKNNDLTSCCFSDAKTMYEVFQRGLAVSDNGPCLGYRKPNQPYRWLSYKQVSDRAEYLGS
CLLHKGYKSSPDQFVGIFAQNRPEWIISELACYTYSMVAVPLYDTLGPEAIVHIVNKADI
AMVICDTPQKALVLIGNVEKGFTPSLKVIILMDPFDDDLKQRGEKSGIEILSLYDAENLG
KEHFRKPVPPSPEDLSVICFTSGTTGDPKGAMITHQNIVSNAAAFLKCVEHAYEPTPDDV
AISYLPLAHMFERIVQAVVYSCGARVGFFQGDIRLLADDMKTLKPTLFPAVPRLLNRIYD
KVQNEAKTPLKKFLLKLAVSSKFKELQKGIIRHDSFWDKLIFAKIQDSLGGRVRVIVTGA
APMSTSVMTFFRAAMGCQVYEAYGQTECTGGCTFTLPGDWTSGHVGVPLACNYVKLEDVA
DMNYFTVNNEGEVCIKGTNVFKGYLKDPEKTQEALDSDGWLHTGDIGRWLPNGTLKIIDR
KKNIFKLAQGEYIAPEKIENIYNRSQPVLQIFVHGESLRSSLVGVVVPDTDVLPSFAAKL
GVKGSFEELCQNQVVREAILEDLQKIGKESGLKTFEQVKAIFLHPEPFSIENGLLTPTLK
AKRGELSKYFRTQIDSLYEHIQD
Enzyme 27 Number of Residues 683
Enzyme 27 Molecular Weight 75990.1
Enzyme 27 Theoretical pI 6.91
Enzyme 27 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 27 General Function Involved in catalytic activity
Enzyme 27 Specific Function Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids. It was suggested that it may also stimulate fatty acid oxidation. At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 12-32
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 6174680 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q9ULC5 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name ACSL5_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2052 bp
ATGCTTTTTATCTTTAACTTTTTGTTTTCCCCACTTCCGACCCCGGCGTTGATCTGCATC
CTGACATTTGGAGCTGCCATCTTCTTGTGGCTGATCACCAGACCTCAACCCGTCTTACCT
CTTCTTGACCTGAACAATCAGTCTGTGGGAATTGAGGGAGGAGCACGGAAGGGGGTTTCC
CAGAAGAACAATGACCTAACAAGTTGCTGCTTCTCAGATGCCAAGACTATGTATGAGGTT
TTCCAAAGAGGACTCGCTGTGTCTGACAATGGGCCCTGCTTGGGATATAGAAAACCAAAC
CAGCCCTACAGATGGCTATCTTACAAACAGGTGTCTGATAGAGCAGAGTACCTGGGTTCC
TGTCTCTTGCATAAAGGTTATAAATCATCACCAGACCAGTTTGTCGGCATCTTTGCTCAG
AATAGGCCAGAGTGGATCATCTCCGAATTGGCTTGTTACACGTACTCTATGGTAGCTGTA
CCTCTGTATGACACCTTGGGACCAGAAGCCATCGTACATATTGTCAACAAGGCTGATATC
GCCATGGTGATCTGTGACACACCCCAAAAGGCATTGGTGCTGATAGGGAATGTAGAGAAA
GGCTTCACCCCGAGCCTGAAGGTGATCATCCTTATGGACCCCTTTGATGATGACCTGAAG
CAAAGAGGGGAGAAGAGTGGAATTGAGATCTTATCCCTATATGATGCTGAGAACCTAGGC
AAAGAGCACTTCAGAAAACCTGTGCCTCCTAGCCCAGAAGACCTGAGCGTCATCTGCTTC
ACCAGTGGGACCACAGGTGACCCCAAAGGAGCCATGATAACCCATCAAAATATTGTTTCA
AATGCTGCTGCCTTTCTCAAATGTGTGGAGCATGCTTATGAGCCCACTCCTGATGATGTG
GCCATATCCTACCTCCCTCTGGCTCATATGTTTGAGAGGATTGTACAGGCTGTTGTGTAC
AGCTGTGGAGCCAGAGTTGGATTCTTCCAAGGGGATATTCGGTTGCTGGCTGACGACATG
AAGACTTTGAAGCCCACATTGTTTCCCGCGGTGCCTCGACTCCTTAACAGGATCTACGAT
AAGGTACAAAATGAGGCCAAGACACCCTTGAAGAAGTTCTTGTTGAAGCTGGCTGTTTCC
AGTAAATTCAAAGAGCTTCAAAAGGGTATCATCAGGCATGATAGTTTCTGGGACAAGCTC
ATCTTTGCAAAGATCCAGGACAGCCTGGGCGGAAGGGTTCGTGTAATTGTCACTGGAGCT
GCCCCCATGTCCACTTCAGTCATGACATTCTTCCGGGCAGCAATGGGATGTCAGGTGTAT
GAAGCTTATGGTCAAACAGAATGCACAGGTGGCTGTACATTTACATTACCTGGGGACTGG
ACATCAGGTCACGTTGGGGTGCCCCTGGCTTGCAATTACGTGAAGCTGGAAGATGTGGCT
GACATGAACTACTTTACAGTGAATAATGAAGGAGAGGTCTGCATCAAGGGTACAAACGTG
TTCAAAGGATACCTGAAGGACCCTGAGAAGACACAGGAAGCCCTGGACAGTGATGGCTGG
CTTCACACAGGAGACATTGGTCGCTGGCTCCCGAATGGAACTCTGAAGATCATCGACCGT
AAAAAGAACATTTTCAAGCTGGCCCAAGGAGAATACATTGCACCAGAGAAGATAGAAAAT
ATCTACAACAGGAGTCAACCAGTGTTACAAATTTTTGTACACGGGGAGAGCTTACGGTCA
TCCTTAGTAGGAGTGGTGGTTCCTGACACAGATGTACTTCCCTCATTTGCAGCCAAGCTT
GGGGTGAAGGGCTCCTTTGAGGAACTGTGCCAAAACCAAGTTGTAAGGGAAGCCATTTTA
GAAGACTTGCAGAAAATTGGGAAAGAAAGTGGCCTTAAAACTTTTGAACAGGTCAAAGCC
ATTTTTCTTCATCCAGAGCCATTTTCCATTGAAAATGGGCTCTTGACACCAACATTGAAA
GCAAAGCGAGGAGAGCTTTCCAAATACTTTCGGACCCAAATTGACAGCCTGTATGAGCAC
ATCCAGGATTAG
Enzyme 27 GenBank Gene ID AB033899 Link Image
Enzyme 27 GeneCard ID ACSL5 Link Image
Enzyme 27 GenAtlas ID ACSL5 Link Image
Enzyme 27 HGNC ID HGNC:16526 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 10q25.1-q25.2
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gassler N, Roth W, Funke B, Schneider A, Herzog F, Tischendorf JJ, Grund K, Penzel R, Bravo IG, Mariadason J, Ehemann V, Sykora J, Haas TL, Walczak H, Ganten T, Zentgraf H, Erb P, Alonso A, Autschbach F, Schirmacher P, Knuchel R, Kopitz J: Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing. Gastroenterology. 2007 Aug;133(2):587-98. Epub 2007 Jun 8. [PubMed Link Image]
  6. Mashima T, Sato S, Okabe S, Miyata S, Matsuura M, Sugimoto Y, Tsuruo T, Seimiya H: Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide. Cancer Sci. 2009 Aug;100(8):1556-62. Epub 2009 May 13. [PubMed Link Image]
  7. Mashima T, Sato S, Sugimoto Y, Tsuruo T, Seimiya H: Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions. Oncogene. 2009 Jan 8;28(1):9-19. Epub 2008 Sep 22. [PubMed Link Image]
  8. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5919
Enzyme 28 Name Long-chain-fatty-acid--CoA ligase 3
Enzyme 28 Synonyms
  1. Long-chain acyl-CoA synthetase 3
  2. LACS 3
Enzyme 28 Gene Name ACSL3
Enzyme 28 Protein Sequence >Long-chain-fatty-acid--CoA ligase 3
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV
NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN
GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF
MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK
PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS
HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ
SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI
SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES
AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY
KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA
LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK
VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
Enzyme 28 Number of Residues 720
Enzyme 28 Molecular Weight 80419.4
Enzyme 28 Theoretical pI 8.51
Enzyme 28 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 28 General Function Involved in catalytic activity
Enzyme 28 Specific Function Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins)
Enzyme 28 Pathways
Enzyme 28 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 21-41
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 17026088 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID O95573 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name ACSL3_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >2163 bp
ATGAATAACCACGTGTCTTCAAAACCATCTACCATGAAGCTAAAACATACCATCAACCCT
ATTCTTTTATATTTTATACATTTTCTAATATCACTTTATACTATTTTAACATACATTCCG
TTTTATTTTTTCTCCGAGTCAAGACAAGAAAAATCAAACCGAATTAAAGCAAAGCCTGTA
AATTCAAAACCTGATTCTGCATACAGATCTGTTAATAGTTTGGATGGTTTGGCTTCAGTA
TTATACCCTGGATGTGATACTTTAGATAAAGTTTTTACATATGCAAAAAACAAATTTAAG
AACAAAAGACTCTTGGGAACACGTGAAGTTTTAAATGAGGAAGATGAAGTACAACCAAAT
GGAAAAATTTTTAAAAAGGTTATTCTTGGACAGTATAATTGGCTTTCCTATGAAGATGTC
TTTGTTCGAGCCTTTAATTTTGGAAATGGATTACAGATGTTGGGTCAGAAACCAAAGACC
AACATCGCCATCTTCTGTGAGACCAGGGCCGAGTGGATGATAGCTGCACAGGCGTGTTTT
ATGTATAATTTTCAGCTTGTTACATTATATGCCACTCTAGGAGGTCCAGCCATTGTTCAT
GCATTAAATGAAACAGAGGTGACCAACATCATTACTAGTAAAGAACTCTTACAAACAAAG
TTGAAGGATATAGTTTCTTTGGTCCCACGCCTGCGGCACATCATCACTGTTGATGGAAAG
CCACCGACCTGGTCCGACTTCCCCAAGGGCATCATTGTGCATACCATGGCTGCAGTGGAG
GCCCTGGGAGCCAAGGCCAGCATGGAAAACCAACCTCATAGCAAACCATTGCCCTCAGAT
ATTGCAGTAATCATGTACACAAGTGGATCCACAGGACTTCCAAAGGGAGTCATGATCTCA
CATAGTAACATTATTGCTGGTATAACTGGGATGGCAGAAAGGATTCCAGAACTAGGAGAG
GAAGATGTCTACATTGGATATTTGCCTCTGGCCCATGTTCTAGAATTAAGTGCTGAGCTT
GTCTGTCTTTCTCACGGATGCCGCATTGGTTACTCTTCACCACAGACTTTAGCAGATCAG
TCTTCAAAAATTAAAAAAGGAAGCAAAGGGGATACATCCATGTTGAAACCAACACTGATG
GCAGCAGTTCCGGAAATCATGGATCGGATCTACAAAAATGTCATGAATAAAGTCAGTGAA
ATGAGTAGTTTTCAACGTAATCTGTTTATTCTGGCCTATAATTACAAAATGGAACAGATT
TCAAAAGGACGTAATACTCCACTGTGCGACAGCTTTGTTTTCCGGAAAGTTCGAAGCTTG
CTAGGGGGAAATATTCGTCTCCTGTTGTGTGGTGGCGCTCCACTTTCTGCAACCACGCAG
CGATTCATGAACATCTGTTTCTGCTGTCCTGTTGGTCAGGGATACGGGCTCACTGAATCT
GCTGGGGCTGGAACAATTTCCGAAGTGTGGGACTACAATACTGGCAGAGTGGGAGCACCA
TTAGTTTGCTGTGAAATCAAATTAAAAAACTGGGAGGAAGGTGGATACTTTAATACTGAT
AAGCCACACCCCAGGGGTGAAATTCTTATTGGGGGCCAAAGTGTGACAATGGGGTACTAC
AAAAATGAAGCAAAAACAAAAGCTGATTTCTCTGAAGATGAAAATGGACAAAGGTGGCTC
TGTACTGGGGATATTGGAGAGTTTGAACCCGATGGATGCTTAAAGATTATTGATCGTAAA
AAGGACCTTGTAAAACTACAGGCAGGGGAATATGTTTCTCTTGGGAAAGTAGAGGCAGCT
TTGAAGAATCTTCCACTAGTAGATAACATTTGTGCATATGCAAACAGTTATCATTCTTAT
GTCATTGGATTTGTTGTGCCAAATCAAAAGGAACTAACTGAACTAGCTCGAAAGAAAGGA
CTTAAAGGGACTTGGGAGGAGCTGTGTAACAGTTGTGAAATGGAAAATGAGGTACTTAAA
GTGCTTTCCGAAGCTGCTATTTCAGCAAGTCTGGAAAAGTTTGAAATTCCAGTAAAAATT
CGTTTGAGTCCTGAACCGTGGACCCCTGAAACTGGTCTGGTGACAGATGCCTTCAAGCTG
AAACGCAAAGAGCTTAAAACACATTACCAGGCGGACATTGAGCGAATGTATGGAAGAAAA
TAA
Enzyme 28 GenBank Gene ID AB061436 Link Image
Enzyme 28 GeneCard ID ACSL3 Link Image
Enzyme 28 GenAtlas ID ACSL3 Link Image
Enzyme 28 HGNC ID HGNC:3570 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 2q34-q35
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT: Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. Genomics. 1997 May 15;42(1):180-1. [PubMed Link Image]
  2. Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT: Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 2001 Oct 31;278(1-2):185-92. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  5. Yao H, Ye J: Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells. J Biol Chem. 2008 Jan 11;283(2):849-54. Epub 2007 Nov 14. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6119
Enzyme 29 Name Glycerol-3-phosphate acyltransferase 1, mitochondrial
Enzyme 29 Synonyms
  1. GPAT-1
Enzyme 29 Gene Name GPAM
Enzyme 29 Protein Sequence >Glycerol-3-phosphate acyltransferase 1, mitochondrial
MDESALTLGTIDVSYLPHSSEYSVGRCKHTSEEWGECGFRPTIFRSATLKWKESLMSRKR
PFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDV
HKGMFATNVTENVLNSSRVQEAIAEVAAELNPDGSAQQQSKAVNKVKKKAKRILQEMVAT
VSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLT
FILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDVLYRALLHGHI
VELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSTNVIPDILIIPVGISYDRII
EGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGCVRVDFAQPFSLKEYLESQSQKPVSA
LLSLEQALLPAILPSRPSDAADEGRDTSINESRNATDESLRRRLIANLAEHILFTASKSC
AIMSTHIVACLLLYRHRQGIDLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLL
GNCVTITHTSRNDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSLYAVLNKRGLG
GPTSTPPNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAE
HDDQEDISPSLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITF
LQRLLGPLLEAYSSAAIFVHNFSGPVPEPEYLQKLHKYLITRTERNVAVYAESATYCLVK
NAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL
Enzyme 29 Number of Residues 828
Enzyme 29 Molecular Weight 93793.9
Enzyme 29 Theoretical pI 7.78
Enzyme 29 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 29 General Function Involved in acyltransferase activity
Enzyme 29 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis
Enzyme 29 Pathways
Enzyme 29 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 472-494 575-593
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 190358539 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9HCL2 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name GPAT1_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2487 bp
ATGGATGAATCTGCACTGACCCTTGGTACAATAGATGTTTCTTATCTGCCACATTCATCA
GAATACAGTGTTGGTCGATGTAAGCACACAAGTGAGGAATGGGGTGAGTGTGGCTTTAGA
CCCACCATCTTCAGATCTGCAACTTTAAAATGGAAAGAAAGCCTAATGAGTCGGAAAAGG
CCATTTGTTGGAAGATGTTGTTACTCCTGCACTCCCCAGAGCTGGGACAAATTTTTCAAC
CCCAGTATCCCGTCTTTGGGTTTGCGGAATGTTATTTATATCAATGAAACTCACACAAGA
CACCGCGGATGGCTTGCAAGACGCCTTTCTTACGTTCTTTTTATTCAAGAGCGAGATGTG
CATAAGGGCATGTTTGCCACCAATGTGACTGAAAATGTGCTGAACAGCAGTAGAGTACAA
GAGGCAATTGCAGAAGTGGCTGCTGAATTAAACCCTGATGGTTCTGCCCAGCAGCAATCA
AAAGCCGTTAACAAAGTGAAAAAGAAAGCTAAAAGGATTCTTCAAGAAATGGTTGCCACT
GTCTCACCGGCAATGATCAGACTGACTGGGTGGGTGCTGCTAAAACTGTTCAACAGCTTC
TTTTGGAACATTCAAATTCACAAAGGTCAACTTGAGATGGTTAAAGCTGCAACTGAGACG
AATTTGCCGCTTCTGTTTCTACCAGTTCATAGATCCCATATTGACTATCTGCTGCTCACT
TTCATTCTCTTCTGCCATAACATCAAAGCACCATACATTGCTTCAGGCAATAATCTCAAC
ATCCCAATCTTCAGTACCTTGATCCATAAGCTTGGGGGCTTCTTCATACGACGAAGGCTC
GATGAAACACCAGATGGACGGAAAGATGTTCTCTATAGAGCTTTGCTCCATGGGCATATA
GTTGAATTACTTCGACAGCAGCAATTCTTGGAGATCTTCCTGGAAGGCACACGTTCTAGG
AGTGGAAAAACCTCTTGTGCTCGGGCAGGACTTTTGTCAGTTGTGGTAGATACTCTGTCT
ACCAATGTCATCCCAGACATCTTGATAATACCTGTTGGAATCTCCTATGATCGCATTATC
GAAGGTCACTACAATGGTGAACAACTGGGCAAACCTAAGAAGAATGAGAGCCTGTGGAGT
GTAGCAAGAGGTGTTATTAGAATGTTACGAAAAAACTATGGTTGTGTCCGAGTGGATTTT
GCACAGCCATTTTCCTTAAAGGAATATTTAGAAAGCCAAAGTCAGAAACCGGTGTCTGCT
CTACTTTCCCTGGAGCAAGCGTTGTTACCAGCTATACTTCCTTCAAGACCCAGTGATGCT
GCTGATGAAGGTAGAGACACGTCCATTAATGAGTCCAGAAATGCAACAGATGAATCCCTA
CGAAGGAGGTTGATTGCAAATCTGGCTGAGCATATTCTATTCACTGCTAGCAAGTCCTGT
GCCATTATGTCCACACACATTGTGGCTTGCCTGCTCCTCTACAGACACAGGCAGGGAATT
GATCTCTCCACATTGGTCGAAGACTTCTTTGTGATGAAAGAGGAAGTCCTGGCTCGTGAT
TTTGACCTGGGGTTCTCAGGAAATTCAGAAGATGTAGTAATGCATGCCATACAGCTGCTG
GGAAATTGTGTCACAATCACCCACACTAGCAGGAACGATGAGTTTTTTATCACCCCCAGC
ACAACTGTCCCATCAGTCTTCGAACTCAACTTCTACAGCAATGGGGTACTTCATGTCTTT
ATCATGGAGGCCATCATAGCTTGCAGCCTTTATGCAGTTCTGAACAAGAGGGGACTGGGG
GGTCCCACTAGCACCCCACCTAACCTGATCAGCCAGGAGCAGCTGGTGCGGAAGGCGGCC
AGCCTGTGCTACCTTCTCTCCAATGAAGGCACCATCTCACTGCCTTGCCAGACATTTTAC
CAAGTCTGCCATGAAACAGTAGGAAAGTTTATCCAGTATGGCATTCTTACAGTGGCAGAG
CACGATGACCAGGAAGATATCAGTCCTAGTCTTGCTGAGCAGCAGTGGGACAAGAAGCTT
CCAGAACCTTTGTCTTGGAGAAGTGATGAAGAAGATGAAGACAGTGACTTTGGGGAGGAA
CAGCGAGATTGCTACCTGAAGGTGAGCCAATCCAAGGAGCACCAGCAGTTTATCACCTTC
TTACAGAGACTCCTTGGGCCTTTGCTGGAGGCCTACAGCTCTGCTGCCATCTTTGTTCAC
AACTTCAGTGGTCCTGTTCCAGAACCTGAGTATCTGCAAAAGTTGCACAAATACCTAATA
ACCAGAACAGAAAGAAATGTTGCAGTATATGCTGAGAGTGCCACATATTGTCTTGTGAAG
AATGCTGTGAAAATGTTTAAGGATATTGGGGTTTTCAAGGAGACCAAACAAAAGAGAGTG
TCTGTTTTAGAACTGAGCAGCACTTTTCTACCTCAATGCAACCGACAAAAACTTCTAGAA
TATATTCTGAGTTTTGTGGTGCTGTAG
Enzyme 29 GenBank Gene ID NM_020918.4 Link Image
Enzyme 29 GeneCard ID GPAM Link Image
Enzyme 29 GenAtlas ID GPAM Link Image
Enzyme 29 HGNC ID HGNC:24865 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 10q25.2
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed Link Image]
  4. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  5. Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G: AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase. J Biol Chem. 2008 Apr 11;283(15):10048-57. Epub 2008 Jan 31. [PubMed Link Image]
  6. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6298
Enzyme 30 Name Trans-2-enoyl-CoA reductase, mitochondrial
Enzyme 30 Synonyms
  1. Nuclear receptor-binding factor 1
  2. HsNrbf-1
  3. NRBF-1
Enzyme 30 Gene Name MECR
Enzyme 30 Protein Sequence >Trans-2-enoyl-CoA reductase, mitochondrial
MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVEL
KNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGLLPELPAVGGNEGVAQVVAVGSNVT
GLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ
LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEE
ELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLL
IFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS
MKPFISSKQILTM
Enzyme 30 Number of Residues 373
Enzyme 30 Molecular Weight 40427.4
Enzyme 30 Theoretical pI 9.01
Enzyme 30 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 30 General Function Involved in zinc ion binding
Enzyme 30 Specific Function Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 4929595 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9BV79 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name MECR_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1122 bp
ATGTGGGTCTGCAGTACCCTGTGGCGGGTGCGAACCCCGCCCGGCAGTGGCGGGGGCCTG
CTCCCAGCTTCTGGCTGTCACGGACCTGCCGCCTCCTCCTACTCCGCATCCGCCGAGCCT
GCCCGGGTCCGCGGCGTTGTCTATGGGCACCACGGGGATCCAGCCAAGGTCGTCGAACTC
AAGAACCTGGAGCTAGCTGCTGTGAGAGGATCAGATGTCCGTGTGAAGATGCTGGCGGCC
CCTATCAATCCATCTGACATAAATATGATCCAAGGAAACTACGGACTCCTTCCTGAACTG
CCTGCTGTTGGAGGGAACGAAGGTGTTGCACAGGTGGTAGCGGTGGGCAGCAATGTGACC
GGGCTGAAGCCAGGAGACTGGGTGATTCCAGCAAATGCTGGTTTAGGAACCTGGCGGACC
GAGGCTGTGTTCAGCGAGGAAGCACTGATCCAAGTTCCGAGTGACATCCCTCTTCAGAGC
GCTGCCACCCTGGGTGTCAATCCCTGCACAGCCTACAGGATGTTGATGGACTTCGAGCAA
CTGCAGCCAGGGGATTCTGTCATCCAGAATGCATCCAACAGCGGAGTGGGGCAAGCGGTC
ATCCAGATCGCCGCAGCCCTGGGCCTAAGAACCATCAATGTGGTCCGAGACAGACCTGAT
ATCCAGAAGCTGAGTGACAGACTGAAGAGTCTGGGGGCTGAGCATGTCATCACAGAAGAG
GAGCTAAGAAGGCCCGAAATGAAAAACTTCTTTAAGGACATGCCCCAGCCACGGCTTGCT
CTCAACTGTGTTGGTGGGAAAAGCTCCACAGAGCTGCTGCGCCAGTTAGCGCGTGGAGGA
ACCATGGTAACCTATGGGGGGATGGCCAAGCAGCCCGTCGTAGCCTCTGTGAGCCTGCTC
ATTTTTAAGGATCTCAAACTTCGAGGCTTTTGGTTGTCCCAGTGGAAGAAGGATCACAGT
CCAGACCAGTTCAAGGAGCTGATCCTCACACTGTGCGATCTCATCCGCCGAGGCCAGCTC
ACAGCCCCTGCCTGCTCCCAGGTCCCGCTGCAGGACTACCAGTCTGCCTTGGAAGCCTCC
ATGAAGCCCTTCATATCTTCAAAGCAGATTCTCACCATGTGA
Enzyme 30 GenBank Gene ID AF151821 Link Image
Enzyme 30 GeneCard ID MECR Link Image
Enzyme 30 GenAtlas ID MECR Link Image
Enzyme 30 HGNC ID HGNC:19691 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 1p36.1-p35.1
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Miinalainen IJ, Chen ZJ, Torkko JM, Pirila PL, Sormunen RT, Bergmann U, Qin YM, Hiltunen JK: Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J Biol Chem. 2003 May 30;278(22):20154-61. Epub 2003 Mar 24. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6299
Enzyme 31 Name Peroxisomal trans-2-enoyl-CoA reductase
Enzyme 31 Synonyms
  1. TERP
  2. 2,4-dienoyl-CoA reductase-related protein
  3. DCR-RP
  4. HPDHase
  5. pVI-ARL
Enzyme 31 Gene Name PECR
Enzyme 31 Protein Sequence >Peroxisomal trans-2-enoyl-CoA reductase
MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAD
ELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHIS
SKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYN
LTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVS
SVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEK
AKL
Enzyme 31 Number of Residues 303
Enzyme 31 Molecular Weight 32544.1
Enzyme 31 Theoretical pI 9.12
Enzyme 31 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • biological regulation
  • metabolic process
  • oxidation reduction
  • regulation of apoptosis
  • regulation of biological process
  • regulation of cell death
  • regulation of cellular process
  • regulation of programmed cell death
Component
Enzyme 31 General Function Involved in regulation of apoptosis
Enzyme 31 Specific Function Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+ [RN:R07162]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID Q9BY49 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PECR_HUMAN Link Image
Enzyme 31 PDB ID 1YXM Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >912 bp
ATGGCCTCCTGGGCTAAGGGCAGGAGCTACCTGGCGCCTGGTTTGCTGCAGGGCCAAGTG
GCCATCGTCACCGGCGGGGCCACGGGCATCGGAAAAGCCATCGTGAAGGAGCTCCTGGAG
CTGGGGAGTAATGTGGTCATTGCATCCCGTAAGTTGGAGAGATTGAAGTCTGCGGCAGAT
GAACTGCAGGCCAACCTACCTCCCACAAAGCAGGCACGAGTCATTCCCATACAATGCAAC
ATCCGGAATGAGGAGGAGGTGAATAATTTGGTCAAATCTACCTTAGATACTTTTGGTAAG
ATCAATTTCTTGGTGAACAATGGAGGAGGCCAGTTTCTTTCCCCTGCTGAACACATCAGT
TCTAAGGGATGGCACGCTGTGCTTGAGACCAACCTGACGGGTACCTTCTACATGTGCAAA
GCAGTTTACAGCTCCTGGATGAAAGAGCATGGAGGATCTATCGTCAATATCATTGTCCCT
ACTAAAGCTGGATTTCCATTAGCTGTGCATTCTGGAGCTGCAAGAGCAGGTGTTTACAAC
CTCACCAAATCTTTAGCTTTGGAATGGGCCTGCAGTGGAATACGGATCAATTGTGTTGCC
CCTGGAGTTATTTATTCCCAGACTGCTGTGGAGAACTATGGTTCCTGGGGACAAAGCTTC
TTTGAAGGGTCTTTTCAGAAAATCCCCGCTAAACGAATTGGTGTTCCTGAGGAGGTCTCC
TCTGTGGTCTGCTTCCTACTGTCTCCTGCAGCTTCCTTCATCACTGGACAGTCAGTGGAT
GTGGATGGGGGCCGGAGTCTCTATACTCACTCGTATGAGGTACCAGATCATGACAACTGG
CCCAAGGGAGCAGGGGACCTTTCTGTTGTCAAAAAGATGAAGGAGACCTTTAAGGAGAAA
GCTAAGCTCTGA
Enzyme 31 GenBank Gene ID AF232009 Link Image
Enzyme 31 GeneCard ID PECR Link Image
Enzyme 31 GenAtlas ID PECR Link Image
Enzyme 31 HGNC ID HGNC:18281 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 2q35
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Das AK, Uhler MD, Hajra AK: Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J Biol Chem. 2000 Aug 11;275(32):24333-40. [PubMed Link Image]
  2. Amery L, Mannaerts GP, Subramani S, Van Veldhoven PP, Fransen M: Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology. Comb Chem High Throughput Screen. 2001 Nov;4(7):545-52. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Braastad CD, Leguia M, Hendrickson EA: Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element. Nucleic Acids Res. 2002 Apr 15;30(8):1713-24. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6335
Enzyme 32 Name Cytosolic acyl coenzyme A thioester hydrolase
Enzyme 32 Synonyms
  1. Acyl-CoA thioesterase 7
  2. Brain acyl-CoA hydrolase
  3. CTE-IIa
  4. CTE-II
  5. Long chain acyl-CoA thioester hydrolase
Enzyme 32 Gene Name ACOT7
Enzyme 32 Protein Sequence >Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
Enzyme 32 Number of Residues 380
Enzyme 32 Molecular Weight 41795.8
Enzyme 32 Theoretical pI 8.66
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Lipid transport and metabolism
Enzyme 32 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 32528282 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID O00154 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name BACH_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1143 bp
ATGAAGCTGCTTGCCAGGGCTCTCCGGCTCTGTGAGTTTGGGAGGCAGGCATCTTCCAGG
AGGCTGGTGGCTGGCCAGGGATGTGTGGGGCCCCGGCGAGGGTGCTGCGCTCCCGTCCAG
GTGGTTGGGCCCAGGGCTGATCTCCCACCCTGTGGAGCCTGCATTACTGGAAGGATCATG
CGGCCAGATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATC
GAGGAGGCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGT
GTGGCCGCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAG
GTGGCGCATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTC
AACGTGATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTG
TGGTATGTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTG
TATTCCCGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAG
CGCATGGAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCG
AACACTGTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACC
CTGCACGGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATC
GTGGCTGCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTT
CATGACAAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGC
AATAAGTCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAG
AAGCGCTACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGG
TCGCTGCCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAA
GGCAAAGGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCC
TAG
Enzyme 32 GenBank Gene ID NM_181864.2 Link Image
Enzyme 32 GeneCard ID ACOT7 Link Image
Enzyme 32 GenAtlas ID ACOT7 Link Image
Enzyme 32 HGNC ID HGNC:24157 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 1p36
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed Link Image]
  2. Yamada J, Kuramochi Y, Takagi M, Watanabe T, Suga T: Human brain acyl-CoA hydrolase isoforms encoded by a single gene. Biochem Biophys Res Commun. 2002 Nov 22;299(1):49-56. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6336
Enzyme 33 Name Acyl-coenzyme A thioesterase 2, mitochondrial
Enzyme 33 Synonyms
  1. Acyl-CoA thioesterase 2
  2. Acyl-coenzyme A thioester hydrolase 2a
  3. CTE-Ia
  4. Long-chain acyl-CoA thioesterase 2
  5. ZAP128
Enzyme 33 Gene Name ACOT2
Enzyme 33 Protein Sequence >Acyl-coenzyme A thioesterase 2, mitochondrial
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIP
SKV
Enzyme 33 Number of Residues 483
Enzyme 33 Molecular Weight 53218.0
Enzyme 33 Theoretical pI 8.62
Enzyme 33 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 33 General Function Involved in thiolester hydrolase activity
Enzyme 33 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 7023514 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P49753 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name ACOT2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1452 bp
ATGTCTAACAAGCTTCTTTCTCCCCACCCCCATTCAGTTGTTCTCAGGTCTGAATTCAAA
ATGGCCTCATCTCCTGCTGTCCTTCGAGCGTCCCGGCTGTACCAATGGAGCCTGAAGAGT
TCGGCGCAGTTCCTGGGGTCTCCACAGCTGAGGCAGGTTGGTCAGATCATTAGGGTTCCT
GCTCGGATGGCGGCGACGCTGATCCTGGAGCCTGCGGGCCGCTGCTGCTGGGACGAACCG
GTGCGAATCGCCGTGCGCGGCCTAGCCCCGGAGCAGCCGGTCACGCTGCGCGCGTCCCTG
CGCGACGAGAAGGGCGCGCTTTTCCAGGCCCACGCGCGCTACCGCGCCGACACTCTTGGC
GAGCTGGACCTGGAGCGCGCGCCCGCGCTGGGCGGCAGCTTCGCGGGGCTTGAGCCCATG
GGGCTGCTCTGGGCCTTGGAGCCCGAGAAACCTTTGGTGCGGCTGGTGAAGCGCGACGTG
CGAACGCCCTTGGCCGTGGTGCTGGAGGTGCTGGATGGCCACGACCCCGACCCCGGGCGG
CTGCTGTGCCAGACGCGGCACGAGCGCTACTTCCTCCCGCCCGGGGTGCGGCGCGAGCCG
GTGCGCGTGGGCCGGGTGCGAGGCACGCTCTTCCTGCCGCCAGAACCTGGGCCCTTTCCT
GGGATTGTGGACATGTTCGGAACTGGAGGTGGCCTGCTGGAGTATCGGGCTAGTCTGCTG
GCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTATTATAACTATGAAGACCTCCCCAAG
ACCATGGAGACGCTCCATCTGGAGTACTTTGAAGAAGCCATGAACTACTTGCTCAGTCAT
CCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGGAATTTCCAAAGGGGGTGAGCTCTGC
CTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGCTGCTGTCGTCATCAACGGCTCTGTG
GCCAATGTTGGGGGAACCTTACGCTACAAGGGCGAGACCCTGCCCCCTGTGGGCGTCAAC
AGAAATCGCATCAAGGTGACCAAAGATGGCTATGCAGACATTGTGGATGTCCTGAACAGC
CCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCCTGTGGAAAGGGCAGAGAGCACCTTC
CTGTTCCTGGTAGGTCAGGATGACCACAACTGGAAGAGTGAGTTCTATGCTAATGAGGCC
TGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCCCCAGATCATCTGTTACCCAGAGACA
GGGCACTATATTGAGCCTCCTTACTTCCCCCTGTGTCGGGCTTCCCTGCATGCCTTGGTG
GGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGCTCATGCCATGGCTCAGGTGGATGCT
TGGAAACAACTCCAGACTTTCTTCCACAAACACTTGGGTGGCCGCGAGGGGACAATCCCA
TCAAAAGTGTAA
Enzyme 33 GenBank Gene ID AK001939 Link Image
Enzyme 33 GeneCard ID ACOT2 Link Image
Enzyme 33 GenAtlas ID ACOT2 Link Image
Enzyme 33 HGNC ID HGNC:18431 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 14q24.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed Link Image]
  2. Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6337
Enzyme 34 Name Acyl-coenzyme A thioesterase 4
Enzyme 34 Synonyms
  1. Acyl-CoA thioesterase 4
  2. PTE-2b
  3. Peroxisomal acyl coenzyme A thioester hydrolase Ib
  4. Peroxisomal long-chain acyl-CoA thioesterase Ib
  5. PTE-Ib
Enzyme 34 Gene Name ACOT4
Enzyme 34 Protein Sequence >Acyl-coenzyme A thioesterase 4
MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADARGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLL
CQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAG
HGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLS
MASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALV
GGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGH
YIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPK
L
Enzyme 34 Number of Residues 421
Enzyme 34 Molecular Weight 46326.1
Enzyme 34 Theoretical pI 8.16
Enzyme 34 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 34 General Function Involved in thiolester hydrolase activity
Enzyme 34 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 187761341 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q8N9L9 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name ACOT4_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1266 bp
ATGTCAGCAACGCTGATCCTGGAGCCCCCAGGCCGCTGCTGCTGGAACGAGCCGGTGCGC
ATTGCCGTGCGCGGCCTGGCCCCGGAGCAGCGGGTTACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTCTTCCGGGCCCACGCGCGCTACTGCGCCGACGCCCGCGGCGAGCTG
GACCTGGAGCGCGCACCCGCGCTGGGCGGCAGCTTCGCGGGACTCGAGCCCATGGGGCTG
CTCTGGGCCCTGGAACCCGAGAAGCCTTTTTGGCGCTTCCTGAAGCGGGACGTACAGATT
CCTTTTGTCGTGGAGTTGGAGGTGCTGGACGGCCACGACCCCGAGCCTGGACGGCTGCTG
TGCCAGGCGCAGCACGAGCGCCACTTCCTCCCGCCAGGGGTGCGGCGCCAGTCGGTGCGA
GCGGGCCGGGTGCGCGCCACGCTCTTCCTGCCGCCAGGACCTGGACCCTTCCCAGGGATC
ATTGACATCTTTGGTATTGGAGGGGGCCTCTTGGAATATCGAGCCAGCCTCCTTGCTGGC
CATGGCTTTGCCACGTTGGCTCTAGCTTATTATAACTTTGAAGATCTCCCCAATAACATG
GACAACATATCCCTGGAGTACTTCGAAGAAGCCGTATGCTACATGCTTCAACATCCCCAG
GTAAAAGGCCCAGGCATTGGGCTTTTGGGCATTTCTCTAGGAGCTGATATTTGTCTCTCA
ATGGCCTCATTCTTGAAGAATGTCTCAGCCACAGTTTCCATCAATGGATCTGGGATCAGT
GGGAACACAGCCATCAACTATAAGCACAGTAGCATTCCACCATTGGGCTATGACCTGAGG
AGAATCAAGGTAGCTTTCTCAGGCCTCGTGGACATTGTGGATATAAGGAATGCTCTCGTA
GGAGGGTACAAGAACCCCAGCATGATTCCAATAGAGAAGGCCCAGGGGCCCATCCTGCTC
ATTGTTGGTCAGGATGACCATAACTGGAGAAGTGAGTTGTATGCCCAAACAGTCTCTGAA
CGGTTACAGGCCCATGGAAAGGAAAAACCCCAGATCATCTGTTACCCTGGGACTGGGCAT
TACATCGAGCCTCCTTACTTCCCCCTGTGCCCAGCTTCCCTTCACAGATTACTGAACAAA
CATGTTATATGGGGTGGGGAGCCCAGGGCTCATTCTAAGGCCCAGGAAGATGCCTGGAAG
CAAATTCTAGCCTTCTTCTGCAAACACCTGGGAGGTACCCAGAAAACAGCTGTCCCTAAA
TTGTAA
Enzyme 34 GenBank Gene ID NM_152331.3 Link Image
Enzyme 34 GeneCard ID ACOT4 Link Image
Enzyme 34 GenAtlas ID ACOT4 Link Image
Enzyme 34 HGNC ID HGNC:19748 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 14q24.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6338
Enzyme 35 Name Acyl-coenzyme A thioesterase 8
Enzyme 35 Synonyms
  1. Acyl-CoA thioesterase 8
  2. Choloyl-coenzyme A thioesterase
  3. HIV-Nef-associated acyl-CoA thioesterase
  4. PTE-2
  5. Peroxisomal acyl-coenzyme A thioester hydrolase 1
  6. PTE-1
  7. Peroxisomal long-chain acyl-CoA thioesterase 1
  8. Thioesterase II
  9. hACTE-III
  10. hACTEIII
  11. hTE
Enzyme 35 Gene Name ACOT8
Enzyme 35 Protein Sequence >Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
Enzyme 35 Number of Residues 319
Enzyme 35 Molecular Weight 35914.0
Enzyme 35 Theoretical pI 7.60
Enzyme 35 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
Component
Enzyme 35 General Function Involved in acyl-CoA thioesterase activity
Enzyme 35 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions
  • choloyl-CoA + H2O = cholate + CoA [RN:R07296]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein Not Available
Enzyme 35 UniProtKB/Swiss-Prot ID O14734 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name ACOT8_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
Enzyme 35 GenBank Gene ID AF014404 Link Image
Enzyme 35 GeneCard ID ACOT8 Link Image
Enzyme 35 GenAtlas ID ACOT8 Link Image
Enzyme 35 HGNC ID HGNC:15919 Link Image
Enzyme 35 Chromosome Location 2
Enzyme 35 Locus 20q13.12
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed Link Image]
  2. Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed Link Image]
  3. Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Ishizuka M, Toyama Y, Watanabe H, Fujiki Y, Takeuchi A, Yamasaki S, Yuasa S, Miyazaki M, Nakajima N, Taki S, Saito T: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp Cell Res. 2004 Jul 1;297(1):127-41. [PubMed Link Image]
  7. Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6839
Enzyme 36 Name Dihydroxyacetone phosphate acyltransferase
Enzyme 36 Synonyms
  1. DAP-AT
  2. DHAP-AT
  3. Acyl-CoA:dihydroxyacetonephosphateacyltransferase
  4. Glycerone-phosphate O-acyltransferase
Enzyme 36 Gene Name GNPAT
Enzyme 36 Protein Sequence >Dihydroxyacetone phosphate acyltransferase
MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVY
KGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIR
FCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDL
PVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEF
FLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGV
PKPKESTTGLLKARKILSENFGSIHVYFGDPVSLRSLAAGRMSRSSYNLVPRYIPQKQSE
DMHAFVTEVAYKMELLQIENMVLSPWTLIVAVLLQNRPSMDFDALVEKTLWLKGLTQAFG
GFLIWPDNKPAEEVVPASILLHSNIASLVKDQVILKVDSGDSEVVDGLMLQHITLLMCSA
YRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSCFRFLRDVFADEFIFLPGNTLKDFEEGC
YLLCKSEAIQVTTKDILVTEKGNTVLEFLVGLFKPFVESYQIICKYLLSEEEDHFSEEQY
LAAVRKFTSQLLDQGTSQCYDVLSSDVQKNALAACVRLGVVEKKKINNNCIFNVNEPATT
KLEEMLGCKTPIGKPATAKL
Enzyme 36 Number of Residues 680
Enzyme 36 Molecular Weight 77187.2
Enzyme 36 Theoretical pI 6.52
Enzyme 36 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 36 General Function Lipid transport and metabolism
Enzyme 36 Specific Function Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Enzyme 36 Pathways
Enzyme 36 Reactions
  • acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate [RN:R01013]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 3258645 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID O15228 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name GNPAT_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2043 bp
ATGGAGTCTTCCAGTTCATCTAACTCTTATTTCTCCGTTGGCCCAACCAGTCCCAGCGCT
GTCGTGCTCCTCTACTCGAAGGAGCTCAAAAAGTGGGATGAGTTTGAAGATATTTTAGAA
GAGAGGAGGCATGTCAGTGACTTGAAATTTGCAATGAAATGCTACACACCTCTTGTCTAT
AAGGGAATTACTCCATGTAAACCAATTGATATTAAATGTAGTGTTCTCAATTCTGAGGAG
ATTCATTATGTCATTAAACAGCTTTCCAAGGAATCCCTTCAATCTGTGGATGTCCTCCGA
GAGGAAGTGAGTGAGATCTTAGATGAAATGAGTCACAAACTGCGTCTTGGAGCCATTCGG
TTTTGTGCCTTCACCCTGAGCAAAGTATTTAAACAAATTTTCTCGAAGGTGTGTGTAAAT
GAAGAAGGTATTCAGAAACTACAAAGAGCCATCCAGGAGCATCCTGTTGTTCTGCTGCCT
AGTCATCGAAGTTACATTGACTTCCTCATGTTGTCTTTTCTTCTATACAATTATGATTTG
CCTGTGCCAGTTATAGCAGCAGGAATGGACTTCCTGGGAATGAAAATGGTTGGTGAGCTG
CTACGAATGTCGGGTGCCTTTTTCATGCGGCGTACCTTTGGTGGCAATAAACTCTACTGG
GCTGTATTCTCTGAATATGTAAAAACTATGTTACGGAATGGTTATGCTCCTGTTGAATTT
TTCCTCGAAGGGACAAGAAGCCGCTCTGCCAAGACATTGACTCCTAAATTTGGTCTTCTG
AATATTGTGATGGAGCCATTTTTTAAAAGAGAAGTTTTTGATACCTACCTTGTCCCAATT
AGTATCAGTTATGATAAGATCTTGGAAGAAACTCTTTATGTGTATGAGCTTCTAGGGGTT
CCTAAACCAAAAGAATCTACAACTGGGTTGCTGAAAGCCAGAAAGATTCTCTCTGAAAAT
TTTGGAAGCATCCATGTGTACTTTGGAGATCCTGTGTCACTTCGATCTTTGGCAGCTGGG
AGGATGAGTCGGAGCTCATATAACTTGGTTCCAAGATACATTCCTCAGAAACAGTCTGAG
GACATGCATGCCTTTGTCACTGAAGTTGCCTACAAAATGGAGCTTCTGCAAATTGAAAAC
ATGGTTTTGAGCCCCTGGACCCTAATAGTTGCTGTTCTGCTTCAGAACCGGCCATCCATG
GACTTTGATGCTCTGGTGGAAAAGACTTTATGGCTAAAAGGCTTAACCCAGGCATTTGGA
GGGTTTCTCATTTGGCCTGATAATAAACCTGCTGAAGAAGTTGTCCCGGCCAGCATTCTT
CTGCATTCCAACATTGCCAGCCTTGTCAAAGACCAGGTGATTCTGAAAGTGGACTCCGGA
GACTCGGAAGTGGTCGATGGGCTTATGCTCCAGCACATCACTCTCCTCATGTGCTCAGCT
TATAGGAACCAGCTGCTCAACATTTTTGTGCGCCCATCCTTAGTAGCAGTAGCATTGCAG
ATGACACCAGGGTTCAGGAAAGAGGATGTCTACAGTTGCTTTCGCTTCCTACGTGATGTT
TTTGCAGATGAGTTCATCTTCCTTCCAGGAAACACACTAAAGGACTTTGAAGAAGGCTGT
TACCTGCTTTGTAAAAGTGAAGCCATACAAGTGACTACGAAAGACATCCTAGTTACAGAG
AAAGGAAATACTGTGTTAGAATTTTTAGTAGGACTCTTTAAACCTTTTGTGGAAAGCTAT
CAGATAATTTGCAAGTACCTTTTGAGTGAAGAAGAGGACCACTTCAGTGAGGAACAGTAC
TTGGCTGCAGTCAGAAAATTCACAAGTCAGCTTCTCGATCAAGGTACCTCTCAATGTTAT
GATGTATTATCTTCTGATGTGCAGAAAAACGCCTTAGCAGCCTGTGTGAGGCTCGGAGTA
GTGGAGAAGAAGAAGATAAATAATAACTGTATATTTAATGTGAATGAACCTGCCACAACC
AAATTAGAAGAAATGCTTGGTTGTAAGACACCAATAGGAAAACCAGCCACTGCAAAACTT
TAA
Enzyme 36 GenBank Gene ID AF043937 Link Image
Enzyme 36 GeneCard ID GNPAT Link Image
Enzyme 36 GenAtlas ID Not Available
Enzyme 36 HGNC ID Not Available
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1q42
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Thai TP, Heid H, Rackwitz HR, Hunziker A, Gorgas K, Just WW: Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase. FEBS Lett. 1997 Dec 29;420(2-3):205-11. [PubMed Link Image]
  2. Ofman R, Hettema EH, Hogenhout EM, Caruso U, Muijsers AO, Wanders RJ: Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2. Hum Mol Genet. 1998 May;7(5):847-53. [PubMed Link Image]
  3. Ofman R, Lajmir S, Wanders RJ: Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human gnpat gene and its use in the identification of novel mutations. Biochem Biophys Res Commun. 2001 Mar 2;281(3):754-60. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Thai TP, Rodemer C, Jauch A, Hunziker A, Moser A, Gorgas K, Just WW: Impaired membrane traffic in defective ether lipid biosynthesis. Hum Mol Genet. 2001 Jan 15;10(2):127-36. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6873
Enzyme 37 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Enzyme 37 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 3
  2. 1-AGP acyltransferase 3
  3. 1-AGPAT 3
  4. Lysophosphatidic acid acyltransferase gamma
  5. LPAAT-gamma
Enzyme 37 Gene Name AGPAT3
Enzyme 37 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ
LVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKV
LAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRF
TETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSL
LGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFK
PARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTE
IEKGSSYGNQEFKKKE
Enzyme 37 Number of Residues 376
Enzyme 37 Molecular Weight 43380.6
Enzyme 37 Theoretical pI 8.91
Enzyme 37 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 37 General Function Involved in acyltransferase activity
Enzyme 37 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 37 Pathways
Enzyme 37 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • 11-31 124-144 308-330 335-357
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 11611541 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9NRZ7 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name PLCC_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1131 bp
ATGGGCCTGCTGGCCTTCCTGAAGACCCAGTTCGTGCTGCACCTGCTGGTCGGCTTTGTC
TTCGTGGTGAGTGGTCTGGTCATCAACTTCGTCCAGCTGTGCACGCTGGCGCTCTGGCCG
GTCAGCAAGCAGCTCTACCGCCGCCTCAACTGCCGCCTCGCCTACTCACTCTGGAGCCAA
CTGGTCATGCTGCTGGAGTGGTGGTCCTGCACGGAGTGTACACTGTTCACGGACCAGGCC
ACGGTAGAGCGCTTTGGGAAGGAGCACGCAGTCATCATCCTCAACCACAACTTCGAGATC
GACTTCCTCTGTGGGTGGACCATGTGTGAGCGCTTCGGAGTGCTGGGGAGCTCCAAGGTC
CTCGCTAAGAAGGAGCTGCTCTACGTGCCCCTCATCGGCTGGACGTGGTACTTTCTGGAG
ATTGTGTTCTGCAAGCGGAAGTGGGAGGAGGACCGGGACACCGTGGTCGAAGGGCTGAGG
CGCCTGTCGGACTACCCCGAGTACATGTGGTTTCTCCTGTACTGCGAGGGGACGCGCTTC
ACGGAGACCAAGCACCGCGTTAGCATGGAGGTGGCGGCTGCTAAGGGGCTTCCTGTCCTC
AAGTACCACCTGCTGCCGCGGACCAAGGGCTTCACCACCGCAGTCAAGTGCCTCCGGGGG
ACAGTCGCAGCTGTCTATGATGTAACCCTGAACTTCAGAGGAAACAAGAACCCGTCCCTG
CTGGGGATCCTCTACGGGAAGAAGTACGAGGCGGACATGTGCGTGAGGAGATTTCCTCTG
GAAGACATCCCGCTGGATGAAAAGGAAGCAGCTCAGTGGCTTCATAAACTGTACCAGGAG
AAGGACGCGCTCCAGGAGATATATAATCAGAAGGGCATGTTTCCAGGGGAGCAGTTTAAG
CCTGCCCGGAGGCCGTGGACCCTCCTGAACTTCCTGTCCTGGGCCACCATTCTCCTGTCT
CCCCTCTTCAGTTTTGTCTTGGGCGTCTTTGCCAGCGGATCACCTCTCCTGATCCTGACT
TTCTTGGGGTTTGTGGGAGCAGCTTCCTTTGGAGTTCGCAGACTGATAGGAGTAACTGAG
ATAGAAAAAGGCTCCAGCTACGGAAACCAAGAGTTTAAGAAAAAGGAATAA
Enzyme 37 GenBank Gene ID AB040138 Link Image
Enzyme 37 GeneCard ID AGPAT3 Link Image
Enzyme 37 GenAtlas ID AGPAT3 Link Image
Enzyme 37 HGNC ID HGNC:326 Link Image
Enzyme 37 Chromosome Location 2
Enzyme 37 Locus 21q22.3
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Leung DW: The structure and functions of human lysophosphatidic acid acyltransferases. Front Biosci. 2001 Aug 1;6:D944-53. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6875
Enzyme 38 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Enzyme 38 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 2
  2. 1-AGP acyltransferase 2
  3. 1-AGPAT 2
  4. Lysophosphatidic acid acyltransferase beta
  5. LPAAT-beta
Enzyme 38 Gene Name AGPAT2
Enzyme 38 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase beta
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENM
SIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAK
RELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGD
LLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAAD
VPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
Enzyme 38 Number of Residues 278
Enzyme 38 Molecular Weight 30914.1
Enzyme 38 Theoretical pI 9.22
Enzyme 38 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 38 General Function Lipid transport and metabolism
Enzyme 38 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 38 Pathways
Enzyme 38 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 1-21 30-50 122-142
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 2282590 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID O15120 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name PLCB_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >837 bp
ATGGAGCTGTGGCCGTGTCTGGCCGCGGCGCTGCTGTTGCTGCTGCTGCTGGTGCAGCTG
AGCCGCGCGGCCGAGTTCTACGCCAAGGTCGCCCTGTACTGCGCGCTGTGCTTCACGGTG
TCCGCCGTGGCCTCGCTCGTCTGCCTGCTGCGCCACGGCGGCCGGACGGTGGAGAACATG
AGCATCATCGGCTGGTTCGTGCGAAGCTTCAAGTACTTTTACGGGCTCCGCTTCGAGGTG
CGGGACCCGCGCAGGCTGCAGGAGGCCCGTCCCTGTGTCATCGTCTCCAACCACCAGAGC
ATCCTGGACATGATGGGCCTCATGGAGGTCCTTCCGGAGCGCTGCGTGCAGATCGCCAAG
CGGGAGCTGCTCTTCCTGGGGCCCGTGGGCCTCATCATGTACCTCGGGGGCGTCTTCTTC
ATCAACCGGCAGCGCTCTAGCACTGCCATGACAGTGATGGCCGACCTGGGCGAGCGCATG
GTCAGGGAGAACCTCAAAGTGTGGATCTATCCCGAGGGTACTCGCAACGACAATGGGGAC
CTGCTGCCTTTTAAGAAGGGCGCCTTCTACCTGGCAGTCCAGGCACAGGTGCCCATCGTC
CCCGTGGTGTACTCTTCCTTCTCCTCCTTCTACAACACCAAGAAGAAGTTCTTCACTTCA
GGAACAGTCACAGTGCAGGTGCTGGAAGCCATCCCCACCAGCGGCCTCACTGCGGCGGAC
GTCCCTGCGCTCGTGGACACCTGCCACCGGGCCATGAGGACCACCTTCCTCCACATCTCC
AAGACCCCCCAGGAGAACGGGGCCACTGCGGGGTCTGGCGTGCAGCCGGCCCAGTAG
Enzyme 38 GenBank Gene ID AF000237 Link Image
Enzyme 38 GeneCard ID AGPAT2 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID Not Available
Enzyme 38 Chromosome Location 9
Enzyme 38 Locus 9q34.3
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Eberhardt C, Gray PW, Tjoelker LW: Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3. J Biol Chem. 1997 Aug 8;272(32):20299-305. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Garg A: Acquired and inherited lipodystrophies. N Engl J Med. 2004 Mar 18;350(12):1220-34. [PubMed Link Image]
  7. Agarwal AK, Arioglu E, De Almeida S, Akkoc N, Taylor SI, Bowcock AM, Barnes RI, Garg A: AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nat Genet. 2002 May;31(1):21-3. Epub 2002 Apr 22. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6877
Enzyme 39 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
Enzyme 39 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 1
  2. 1-AGP acyltransferase 1
  3. 1-AGPAT 1
  4. Lysophosphatidic acid acyltransferase alpha
  5. LPAAT-alpha
  6. Protein G15
Enzyme 39 Gene Name AGPAT1
Enzyme 39 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRG
RNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGR
CVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGT
RNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTE
GLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
Enzyme 39 Number of Residues 283
Enzyme 39 Molecular Weight 31716.3
Enzyme 39 Theoretical pI 9.75
Enzyme 39 GO Classification
Function
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • O-acyltransferase activity
  • acylglycerol O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid biosynthetic process
  • phospholipid metabolic process
Component
  • cell part
  • membrane
Enzyme 39 General Function Involved in acyltransferase activity
Enzyme 39 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 39 Pathways
Enzyme 39 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • 7-27 38-58 128-148
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 55961399 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q99943 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name PLCA_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >852 bp
ATGGATTTGTGGCCAGGGGCATGGATGCTGCTGCTGCTGCTCTTCCTGCTGCTGCTCTTC
CTGCTGCCCACCCTGTGGTTCTGCAGCCCCAGTGCCAAGTACTTCTTCAAGATGGCCTTC
TACAATGGCTGGATCCTCTTCCTGGCTGTGCTCGCCATCCCTGTGTGTGCCGTGCGAGGA
CGCAACGTCGAGAACATGAAGATCTTGCGTCTAATGCTGCTCCACATCAAATACCTGTAC
GGGATCCGAGTGGAGGTGCGAGGGGCTCACCACTTCCCTCCCTCGCAGCCCTATGTTGTT
GTCTCCAACCACCAGAGCTCTCTCGATCTGCTTGGGATGATGGAGGTACTGCCAGGCCGC
TGTGTGCCCATTGCCAAGCGCGAGCTACTGTGGGCTGGCTCTGCCGGGCTGGCCTGCTGG
CTGGCAGGAGTCATCTTCATCGACCGGAAGCGCACGGGGGATGCCATCAGTGTCATGTCT
GAGGTCGCCCAGACCCTGCTCACCCAGGACGTGAGGGTCTGGGTGTTTCCTGAGGGAACG
AGAAACCACAATGGCTCCATGCTGCCCTTCAAACGTGGCGCCTTCCATCTTGCAGTGCAG
GCCCAGGTTCCCATTGTCCCCATAGTCATGTCCTCCTACCAAGACTTCTACTGCAAGAAG
GAGCGTCGCTTCACCTCGGGACAATGTCAGGTGCGGGTGCTGCCCCCAGTGCCCACGGAA
GGGCTGACACCAGATGACGTCCCAGCTCTGGCTGACAGAGTCCGGCACTCCATGCTCACT
GTTTTCCGGGAAATCTCCACTGATGGCCGGGGTGGTGGTGACTATCTGAAGAAGCCTGGG
GGCGGTGGGTGA
Enzyme 39 GenBank Gene ID AL662828 Link Image
Enzyme 39 GeneCard ID AGPAT1 Link Image
Enzyme 39 GenAtlas ID AGPAT1 Link Image
Enzyme 39 HGNC ID HGNC:324 Link Image
Enzyme 39 Chromosome Location 6
Enzyme 39 Locus 6p21.3
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. West J, Tompkins CK, Balantac N, Nudelman E, Meengs B, White T, Bursten S, Coleman J, Kumar A, Singer JW, Leung DW: Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. DNA Cell Biol. 1997 Jun;16(6):691-701. [PubMed Link Image]
  2. Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ: A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases. Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. [PubMed Link Image]
  3. Aguado B, Campbell RD: Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex. J Biol Chem. 1998 Feb 13;273(7):4096-105. [PubMed Link Image]
  4. Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 2003 Dec;13(12):2621-36. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6936
Enzyme 40 Name Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 40 Synonyms
  1. SBCAD
  2. 2-methyl branched chain acyl-CoA dehydrogenase
  3. 2-MEBCAD
  4. 2-methylbutyryl-coenzyme A dehydrogenase
  5. 2-methylbutyryl-CoA dehydrogenase
Enzyme 40 Gene Name ACADSB
Enzyme 40 Protein Sequence >Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDE
EMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLS
TVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAG
AGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRD
TPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQ
MLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAG
KPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ
LNTIAKHIDAEY
Enzyme 40 Number of Residues 432
Enzyme 40 Molecular Weight 47485.0
Enzyme 40 Theoretical pI 7.00
Enzyme 40 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 40 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 40 Specific Function Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein Not Available
Enzyme 40 UniProtKB/Swiss-Prot ID P45954 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name ACDSB_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1299 bp
ATGGAGGGCCTGGCAGTGCGGTTGCTGCGCGGCAGCAGGCTGCTAAGAAGAAATTTCCTG
ACTTGTTTGTCTTCTTGGAAGATTCCTCCTCATGTCTCAAAATCTTCCCAGTCAGAAGCT
CTACTCAATATAACAAATAATGGAATACACTTTGCTCCCCTGCAAACATTTACAGATGAG
GAAATGATGATAAAGAGTTCAGTTAAAAAATTTGCTCAGGAACAAATTGCACCTTTGGTT
TCAACCATGGATGAAAATTCGAAAATGGAGAAATCAGTAATACAAGGATTATTTCAACAA
GGGTTGATGGGTATTGAAGTTGACCCAGAATATGGAGGCACAGGAGCTTCTTTTTTATCC
ACTGTGCTCGTGATAGAGGAATTAGCCAAAGTTGATGCATCTGTGGCTGTCTTTTGTGAG
ATCCAGAACACATTAATTAACACACTGATTAGAAAACATGGAACAGAAGAACAAAAGGCC
ACCTATTTGCCTCAGCTCACTACAGAAAAAGTAGGAAGTTTCTGCCTTTCAGAGGCTGGA
GCAGGTAGTGACTCATTTGCTTTGAAGACCAGAGCTGATAAAGAGGGAGATTATTATGTC
CTCAATGGATCAAAGATGTGGATCAGCAGTGCTGAGCATGCAGGGCTCTTTCTGGTGATG
GCAAATGTAGACCCTACCATTGGATATAAGGGAATTACCTCCTTCTTAGTAGATCGTGAT
ACTCCGGGCCTTCATATAGGGAAACCTGAAAACAAATTGGGGCTCAGAGCTTCTTCCACC
TGCCCGTTAACATTCGAAAATGTCAAGGTTCCAGAAGCCAATATCTTGGGACAAATTGGA
CATGGCTATAAGTATGCCATAGGGAGTCTCAATGAAGGTAGAATAGGAATTGCTGCACAG
ATGCTGGGACTGGCGCAAGGATGTTTTGACTACACTATTCCATATATTAAAGAAAGGATA
CAATTTGGCAAAAGACTATTTGATTTTCAGGGCCTCCAACACCAAGTGGCTCACGTGGCC
ACCCAGCTGGAAGCTGCAAGATTACTAACATACAATGCTGCTAGGCTTTTAGAAGCTGGA
AAGCCATTCATAAAAGAAGCGTCAATGGCCAAATACTATGCATCAGAGATTGCAGGACAA
ACAACGAGTAAATGTATCGAGTGGATGGGGGGAGTAGGCTACACCAAAGATTACCCTGTG
GAGAAATACTTCCGAGATGCAAAGATTGGTACGATATATGAAGGAGCTTCCAACATCCAG
TTGAACACCATTGCAAAGCATATCGATGCAGAATACTGA
Enzyme 40 GenBank Gene ID U12778 Link Image
Enzyme 40 GeneCard ID ACADSB Link Image
Enzyme 40 GenAtlas ID ACADSB Link Image
Enzyme 40 HGNC ID HGNC:91 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 10q26.13
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Rozen R, Vockley J, Zhou L, Milos R, Willard J, Fu K, Vicanek C, Low-Nang L, Torban E, Fournier B: Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics. 1994 Nov 15;24(2):280-7. [PubMed Link Image]
  2. Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Gibson KM, Burlingame TG, Hogema B, Jakobs C, Schutgens RB, Millington D, Roe CR, Roe DS, Sweetman L, Steiner RD, Linck L, Pohowalla P, Sacks M, Kiss D, Rinaldo P, Vockley J: 2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism. Pediatr Res. 2000 Jun;47(6):830-3. [PubMed Link Image]
  7. Madsen PP, Kibaek M, Roca X, Sachidanandam R, Krainer AR, Christensen E, Steiner RD, Gibson KM, Corydon TJ, Knudsen I, Wanders RJ, Ruiter JP, Gregersen N, Andresen BS: Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping. Hum Genet. 2006 Feb;118(6):680-90. Epub 2005 Nov 30. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 7358
Enzyme 41 Name Very long-chain acyl-CoA synthetase
Enzyme 41 Synonyms
  1. VLACS
  2. VLCS
  3. Fatty acid transport protein 2
  4. FATP-2
  5. Fatty-acid-coenzyme A ligase, very long-chain 1
  6. Long-chain-fatty-acid--CoA ligase
  7. Solute carrier family 27 member 2
  8. THCA-CoA ligase
  9. Very long-chain-fatty-acid-CoA ligase
Enzyme 41 Gene Name SLC27A2
Enzyme 41 Protein Sequence >Very long-chain acyl-CoA synthetase
MLSAIYTVLAGLLFLPLLVNLCCPYFFQDIGYFLKVAAVGRRVRSYGKRRPARTILRAFL
EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWL
WLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIY
YVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQ
RIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDD
CRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYE
FYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKG
EVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDR
VGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGK
KLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAK
MYVPMTEDIYNAISAKTLKL
Enzyme 41 Number of Residues 620
Enzyme 41 Molecular Weight 70311.7
Enzyme 41 Theoretical pI 8.65
Enzyme 41 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 41 General Function Involved in catalytic activity
Enzyme 41 Specific Function Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes
Enzyme 41 Pathways
Enzyme 41 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • 5-27 107-127 262-282
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 227499619 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID O14975 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name S27A2_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1863 bp
ATGCTTTCCGCCATCTACACAGTCCTGGCGGGACTGCTGTTCCTGCCGCTCCTGGTGAAC
CTCTGCTGCCCATACTTCTTCCAGGACATAGGCTACTTCTTGAAGGTGGCCGCCGTGGGC
CGGAGGGTGCGCAGCTACGGGAAGCGGCGGCCGGCGCGCACCATCCTGCGGGCGTTCCTG
GAGAAAGCGCGCCAGACGCCACACAAGCCTTTTCTGCTCTTCCGCGACGAGACTCTCACC
TACGCGCAGGTGGACCGGCGCAGCAATCAAGTGGCCCGGGCGCTGCACGACCACCTCGGC
CTGCGCCAGGGAGACTGCGTGGCGCTCCTTATGGGTAACGAGCCGGCCTACGTGTGGCTG
TGGCTGGGGCTGGTGAAGCTGGGCTGTGCCATGGCGTGCCTCAATTACAACATCCGCGCG
AAGTCCCTGCTGCACTGCTTCCAGTGCTGCGGGGCGAAGGTGCTGCTGGTGTCGCCAGAA
CTACAAGCAGCTGTCGAAGAGATACTGCCAAGCCTTAAAAAAGATGATGTGTCCATCTAT
TATGTGAGCAGAACTTCTAACACAGATGGGATTGACTCTTTCCTGGACAAAGTGGATGAA
GTATCAACTGAACCTATCCCAGAGTCATGGAGGTCTGAAGTCACTTTTTCCACTCCTGCC
TTATACATTTATACTTCTGGAACCACAGGTCTTCCAAAAGCAGCCATGATCACTCATCAG
CGCATATGGTATGGAACTGGCCTCACTTTTGTAAGCGGATTGAAGGCAGATGATGTCATC
TATATCACTCTGCCCTTTTACCACAGTGCTGCACTACTGATTGGCATTCACGGATGTATT
GTGGCTGGTGCTACTCTTGCCTTGCGGACTAAATTTTCAGCCAGCCAGTTTTGGGATGAC
TGCAGAAAATACAACGTCACTGTCATTCAGTATATCGGTGAACTGCTTCGGTATTTATGC
AACTCACCACAGAAACCAAATGACCGTGATCATAAAGTGAGACTGGCACTGGGAAATGGC
TTACGAGGAGATGTGTGGAGACAATTTGTCAAGAGATTTGGGGACATATGCATCTATGAG
TTCTATGCTGCCACTGAAGGCAATATTGGATTTATGAATTATGCGAGAAAAGTTGGTGCT
GTTGGAAGAGTAAACTACCTACAGAAAAAAATCATAACTTATGACCTGATTAAATATGAT
GTGGAGAAAGATGAACCTGTCCGTGATGAAAATGGATATTGCGTCAGAGTTCCCAAAGGT
GAAGTTGGACTTCTGGTTTGCAAAATCACACAACTTACACCATTTAATGGCTATGCTGGA
GCAAAGGCTCAGACAGAGAAGAAAAAACTGAGAGATGTCTTTAAGAAAGGAGACCTCTAT
TTCAACAGTGGAGATCTCTTAATGGTTGACCATGAAAATTTCATCTATTTCCACGACAGA
GTTGGAGATACATTCCGGTGGAAAGGGGAAAATGTGGCCACCACTGAAGTTGCTGATACA
GTTGGACTGGTTGATTTTGTCCAAGAAGTAAATGTTTATGGAGTGCATGTGCCAGATCAT
GAGGGTCGCATTGGCATGGCCTCCATCAAAATGAAAGAAAACCATGAATTTGATGGAAAG
AAACTCTTTCAGCACATTGCTGATTACCTACCTAGTTATGCAAGGCCCCGGTTTCTAAGA
ATACAGGACACCATTGAGATCACTGGAACTTTTAAACACCGCAAAATGACCCTGGTGGAG
GAGGGCTTTAACCCTGCTGTCATCAAAGATGCCTTGTATTTCTTGGATGACACAGCAAAA
ATGTATGTGCCTATGACTGAGGACATCTATAATGCCATAAGTGCTAAAACCCTGAAACTC
TGA
Enzyme 41 GenBank Gene ID NM_003645.3 Link Image
Enzyme 41 GeneCard ID SLC27A2 Link Image
Enzyme 41 GenAtlas ID SLC27A2 Link Image
Enzyme 41 HGNC ID HGNC:10996 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 15q21.2
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Steinberg SJ, Wang SJ, Kim DG, Mihalik SJ, Watkins PA: Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism. Biochem Biophys Res Commun. 1999 Apr 13;257(2):615-21. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA: Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. J Biol Chem. 2002 Jul 5;277(27):24771-9. Epub 2002 Apr 29. [PubMed Link Image]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 7657
Enzyme 42 Name Peroxisome proliferator-activated receptor gamma
Enzyme 42 Synonyms
  1. PPAR-gamma
  2. Nuclear receptor subfamily 1 group C member 3
Enzyme 42 Gene Name PPARG
Enzyme 42 Protein Sequence >Peroxisome proliferator-activated receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC
RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR
ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE
QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS
LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII
LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL
LQVIKKTETDMSLHPLLQEIYKDLY
Enzyme 42 Number of Residues 505
Enzyme 42 Molecular Weight 57619.6
Enzyme 42 Theoretical pI 5.77
Enzyme 42 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 42 General Function Involved in DNA binding
Enzyme 42 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 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein Not Available
Enzyme 42 UniProtKB/Swiss-Prot ID P37231 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name PPARG_HUMAN Link Image
Enzyme 42 PDB ID 1I7I Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 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 42 GenBank Gene ID U79012 Link Image
Enzyme 42 GeneCard ID PPARG Link Image
Enzyme 42 GenAtlas ID PPARG Link Image
Enzyme 42 HGNC ID HGNC:9236 Link Image
Enzyme 42 Chromosome Location 3
Enzyme 42 Locus 3p25
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. 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]
  11. Zhou XP, Smith WM, Gimm O, Mueller E, Gao X, Sarraf P, Prior TW, Plass C, von Deimling A, Black PM, Yates AJ, Eng C: Over-representation of PPARgamma sequence variants in sporadic cases of glioblastoma multiforme: preliminary evidence for common low penetrance modifiers for brain tumour risk in the general population. J Med Genet. 2000 Jun;37(6):410-4. [PubMed Link Image]
  12. 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]
  13. Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ: ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor. Biochem Biophys Res Commun. 2004 Apr 23;317(1):54-9. [PubMed Link Image]
  14. Drori S, Girnun GD, Tou L, Szwaya JD, Mueller E, Xia K, Shivdasani RA, Spiegelman BM: Hic-5 regulates an epithelial program mediated by PPARgamma. Genes Dev. 2005 Feb 1;19(3):362-75. [PubMed Link Image]
  15. Uppenberg J, Svensson C, Jaki M, Bertilsson G, Jendeberg L, Berkenstam A: Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma. J Biol Chem. 1998 Nov 20;273(47):31108-12. [PubMed Link Image]
  16. Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998 Sep 10;395(6698):137-43. [PubMed Link Image]
  17. 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]
  18. Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed Link Image]
  19. Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure. 2001 Aug;9(8):699-706. [PubMed Link Image]
  20. Ebdrup S, Pettersson I, Rasmussen HB, Deussen HJ, Frost Jensen A, Mortensen SB, Fleckner J, Pridal L, Nygaard L, Sauerberg P: Synthesis and biological and structural characterization of the dual-acting peroxisome proliferator-activated receptor alpha/gamma agonist ragaglitazar. J Med Chem. 2003 Apr 10;46(8):1306-17. [PubMed Link Image]
  21. Ostberg T, Svensson S, Selen G, Uppenberg J, Thor M, Sundbom M, Sydow-Backman M, Gustavsson AL, Jendeberg L: A new class of peroxisome proliferator-activated receptor agonists with a novel binding epitope shows antidiabetic effects. J Biol Chem. 2004 Sep 24;279(39):41124-30. Epub 2004 Jul 15. [PubMed Link Image]
  22. Haffner CD, Lenhard JM, Miller AB, McDougald DL, Dwornik K, Ittoop OR, Gampe RT Jr, Xu HE, Blanchard S, Montana VG, Consler TG, Bledsoe RK, Ayscue A, Croom D: Structure-based design of potent retinoid X receptor alpha agonists. J Med Chem. 2004 Apr 8;47(8):2010-29. [PubMed Link Image]
  23. Shi GQ, Dropinski JF, McKeever BM, Xu S, Becker JW, Berger JP, MacNaul KL, Elbrecht A, Zhou G, Doebber TW, Wang P, Chao YS, Forrest M, Heck JV, Moller DE, Jones AB: Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic and lipid modulating activity. J Med Chem. 2005 Jun 30;48(13):4457-68. [PubMed Link Image]
  24. Li Y, Choi M, Suino K, Kovach A, Daugherty J, Kliewer SA, Xu HE: Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner. Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9505-10. Epub 2005 Jun 23. [PubMed Link Image]
  25. Hopkins CR, O'neil SV, Laufersweiler MC, Wang Y, Pokross M, Mekel M, Evdokimov A, Walter R, Kontoyianni M, Petrey ME, Sabatakos G, Roesgen JT, Richardson E, Demuth TP Jr: Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent PPAR-gamma binding agents with potential application to the treatment of osteoporosis. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5659-63. Epub 2006 Aug 21. [PubMed Link Image]
  26. Mahindroo N, Wang CC, Liao CC, Huang CF, Lu IL, Lien TW, Peng YH, Huang WJ, Lin YT, Hsu MC, Lin CH, Tsai CH, Hsu JT, Chen X, Lyu PC, Chao YS, Wu SY, Hsieh HP: Indol-1-yl acetic acids as peroxisome proliferator-activated receptor agonists: design, synthesis, structural biology, and molecular docking studies. J Med Chem. 2006 Feb 9;49(3):1212-6. [PubMed Link Image]
  27. Lu IL, Huang CF, Peng YH, Lin YT, Hsieh HP, Chen CT, Lien TW, Lee HJ, Mahindroo N, Prakash E, Yueh A, Chen HY, Goparaju CM, Chen X, Liao CC, Chao YS, Hsu JT, Wu SY: Structure-based drug design of a novel family of PPARgamma partial agonists: virtual screening, X-ray crystallography, and in vitro/in vivo biological activities. J Med Chem. 2006 May 4;49(9):2703-12. [PubMed Link Image]
  28. 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]
  29. 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]
  30. Deeb SS, Fajas L, Nemoto M, Pihlajamaki J, Mykkanen L, Kuusisto J, Laakso M, Fujimoto W, Auwerx J: A Pro12Ala substitution in PPARgamma2 associated with decreased receptor activity, lower body mass index and improved insulin sensitivity. Nat Genet. 1998 Nov;20(3):284-7. [PubMed Link Image]
  31. 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]
  32. Valve R, Sivenius K, Miettinen R, Pihlajamaki J, Rissanen A, Deeb SS, Auwerx J, Uusitupa M, Laakso M: Two polymorphisms in the peroxisome proliferator-activated receptor-gamma gene are associated with severe overweight among obese women. J Clin Endocrinol Metab. 1999 Oct;84(10):3708-12. [PubMed Link Image]
  33. 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]
  34. 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]
  35. Hegele RA, Cao H, Frankowski C, Mathews ST, Leff T: PPARG F388L, a transactivation-deficient mutant, in familial partial lipodystrophy. Diabetes. 2002 Dec;51(12):3586-90. [PubMed Link Image]
  36. 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]
  37. Masud S, Ye S: Effect of the peroxisome proliferator activated receptor-gamma gene Pro12Ala variant on body mass index: a meta-analysis. J Med Genet. 2003 Oct;40(10):773-80. [PubMed Link Image]
  38. Temelkova-Kurktschiev T, Hanefeld M, Chinetti G, Zawadzki C, Haulon S, Kubaszek A, Koehler C, Leonhardt W, Staels B, Laakso M: Ala12Ala genotype of the peroxisome proliferator-activated receptor gamma2 protects against atherosclerosis. J Clin Endocrinol Metab. 2004 Sep;89(9):4238-42. [PubMed Link Image]
  39. Kim KS, Choi SM, Shin SU, Yang HS, Yoon Y: Effects of peroxisome proliferator-activated receptor-gamma 2 Pro12Ala polymorphism on body fat distribution in female Korean subjects. Metabolism. 2004 Dec;53(12):1538-43. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 7694
Enzyme 43 Name Peroxisome proliferator-activated receptor alpha
Enzyme 43 Synonyms
  1. PPAR-alpha
  2. Nuclear receptor subfamily 1 group C member 1
Enzyme 43 Gene Name PPARA
Enzyme 43 Protein Sequence >Peroxisome proliferator-activated receptor alpha
MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSC
PGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACE
GCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSE
KAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFV
IHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANL
DLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFD
FAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDI
FLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY
Enzyme 43 Number of Residues 468
Enzyme 43 Molecular Weight 52224.6
Enzyme 43 Theoretical pI 6.20
Enzyme 43 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 43 General Function Involved in DNA binding
Enzyme 43 Specific Function Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl- 2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 216409688 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q07869 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PPARA_HUMAN Link Image
Enzyme 43 PDB ID 1K7L Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1407 bp
ATGGTGGACACGGAAAGCCCACTCTGCCCCCTCTCCCCACTCGAGGCCGGCGATCTAGAG
AGCCCGTTATCTGAAGAGTTCCTGCAAGAAATGGGAAACATCCAAGAGATTTCGCAATCC
ATCGGCGAGGATAGTTCTGGAAGCTTTGGCTTTACGGAATACCAGTATTTAGGAAGCTGT
CCTGGCTCAGATGGCTCGGTCATCACGGACACGCTTTCACCAGCTTCGAGCCCCTCCTCG
GTGACTTATCCTGTGGTCCCCGGCAGCGTGGACGAGTCTCCCAGTGGAGCATTGAACATC
GAATGTAGAATCTGCGGGGACAAGGCCTCAGGCTATCATTACGGAGTCCACGCGTGTGAA
GGCTGCAAGGGCTTCTTTCGGCGAACGATTCGACTCAAGCTGGTGTATGACAAGTGCGAC
CGCAGCTGCAAGATCCAGAAAAAGAACAGAAACAAATGCCAGTATTGTCGATTTCACAAG
TGCCTTTCTGTCGGGATGTCACACAACGCGATTCGTTTTGGACGAATGCCAAGATCTGAG
AAAGCAAAACTGAAAGCAGAAATTCTTACCTGTGAACATGACATAGAAGATTCTGAAACT
GCAGATCTCAAATCTCTGGCCAAGAGAATCTACGAGGCCTACTTGAAGAACTTCAACATG
AACAAGGTCAAAGCCCGGGTCATCCTCTCAGGAAAGGCCAGTAACAATCCACCTTTTGTC
ATACATGATATGGAGACACTGTGTATGGCTGAGAAGACGCTGGTGGCCAAGCTGGTGGCC
AATGGCATCCAGAACAAGGAGGCGGAGGTCCGCATCTTTCACTGCTGCCAGTGCACGTCA
GTGGAGACCGTCACGGAGCTCACGGAATTCGCCAAGGCCATCCCAGGCTTCGCAAACTTG
GACCTGAACGATCAAGTGACATTGCTAAAATACGGAGTTTATGAGGCCATATTCGCCATG
CTGTCTTCTGTGATGAACAAAGACGGGATGCTGGTAGCGTATGGAAATGGGTTTATAACT
CGTGAATTCCTAAAAAGCCTAAGGAAACCGTTCTGTGATATCATGGAACCCAAGTTTGAT
TTTGCCATGAAGTTCAATGCACTGGAACTGGATGACAGTGATATCTCCCTTTTTGTGGCT
GCTATCATTTGCTGTGGAGATCGTCCTGGCCTTCTAAACGTAGGACACATTGAAAAAATG
CAGGAGGGTATTGTACATGTGCTCAGACTCCACCTGCAGAGCAACCACCCGGACGATATC
TTTCTCTTCCCCAAACTTCTTCAAAAAATGGCAGACCTCCGGCAGCTGGTGACGGAGCAT
GCGCAGCTGGTGCAGATCATCAAGAAGACGGAGTCGGATGCTGCGCTGCACCCGCTACTG
CAGGAGATCTACAGGGACATGTACTGA
Enzyme 43 GenBank Gene ID AB307690 Link Image
Enzyme 43 GeneCard ID PPARA Link Image
Enzyme 43 GenAtlas ID PPARA Link Image
Enzyme 43 HGNC ID HGNC:9232 Link Image
Enzyme 43 Chromosome Location 2
Enzyme 43 Locus 22q12-q13.1|22q13.31
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Sher T, Yi HF, McBride OW, Gonzalez FJ: cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry. 1993 Jun 1;32(21):5598-604. [PubMed Link Image]
  2. Mukherjee R, Jow L, Noonan D, McDonnell DP: Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators. J Steroid Biochem Mol Biol. 1994 Nov;51(3-4):157-66. [PubMed Link Image]
  3. Tugwood JD, Aldridge TC, Lambe KG, Macdonald N, Woodyatt NJ: Peroxisome proliferator-activated receptors: structures and function. Ann N Y Acad Sci. 1996 Dec 27;804:252-65. [PubMed Link Image]
  4. Kobayashi T, Kodani Y, Nozawa A, Endo Y, Sawasaki T: DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system. FEBS Lett. 2008 Aug 6;582(18):2737-44. Epub 2008 Jul 11. [PubMed Link Image]
  5. Cho MC, Lee S, Choi HS, Yang Y, Tae Hong J, Kim SJ, Yoon DY: Optimization of an enzyme-linked immunosorbent assay to screen ligand of Peroxisome proliferator-activated receptor alpha. Immunopharmacol Immunotoxicol. 2009;31(3):459-67. [PubMed Link Image]
  6. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  9. Li H, Gomes PJ, Chen JD: RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8479-84. [PubMed Link Image]
  10. 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]
  11. Fu J, Gaetani S, Oveisi F, Lo Verme J, Serrano A, Rodriguez De Fonseca F, Rosengarth A, Luecke H, Di Giacomo B, Tarzia G, Piomelli D: Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-alpha. Nature. 2003 Sep 4;425(6953):90-3. [PubMed Link Image]
  12. Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed Link Image]
  13. Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure. 2001 Aug;9(8):699-706. [PubMed Link Image]
  14. Xu HE, Stanley TB, Montana VG, Lambert MH, Shearer BG, Cobb JE, McKee DD, Galardi CM, Plunket KD, Nolte RT, Parks DJ, Moore JT, Kliewer SA, Willson TM, Stimmel JB: Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha. Nature. 2002 Feb 14;415(6873):813-7. [PubMed Link Image]
  15. Oon Han H, Kim SH, Kim KH, Hur GC, Joo Yim H, Chung HK, Ho Woo S, Dong Koo K, Lee CS, Sung Koh J, Kim GT: Design and synthesis of oxime ethers of alpha-acyl-beta-phenylpropanoic acids as PPAR dual agonists. Bioorg Med Chem Lett. 2007 Feb 15;17(4):937-41. Epub 2006 Nov 18. [PubMed Link Image]
  16. Sierra ML, Beneton V, Boullay AB, Boyer T, Brewster AG, Donche F, Forest MC, Fouchet MH, Gellibert FJ, Grillot DA, Lambert MH, Laroze A, Le Grumelec C, Linget JM, Montana VG, Nguyen VL, Nicodeme E, Patel V, Penfornis A, Pineau O, Pohin D, Potvain F, Poulain G, Ruault CB, Saunders M, Toum J, Xu HE, Xu RX, Pianetti PM: Substituted 2-[(4-aminomethyl)phenoxy]-2-methylpropionic acid PPARalpha agonists. 1. Discovery of a novel series of potent HDLc raising agents. J Med Chem. 2007 Feb 22;50(4):685-95. Epub 2007 Jan 23. [PubMed Link Image]
  17. Oyama T, Toyota K, Waku T, Hirakawa Y, Nagasawa N, Kasuga JI, Hashimoto Y, Miyachi H, Morikawa K: Adaptability and selectivity of human peroxisome proliferator-activated receptor (PPAR) pan agonists revealed from crystal structures. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):786-95. Epub 2009 Jul 10. [PubMed Link Image]
  18. Benardeau A, Benz J, Binggeli A, Blum D, Boehringer M, Grether U, Hilpert H, Kuhn B, Marki HP, Meyer M, Puntener K, Raab S, Ruf A, Schlatter D, Mohr P: Aleglitazar, a new, potent, and balanced dual PPARalpha/gamma agonist for the treatment of type II diabetes. Bioorg Med Chem Lett. 2009 May 1;19(9):2468-73. Epub 2009 Mar 14. [PubMed Link Image]
  19. Artis DR, Lin JJ, Zhang C, Wang W, Mehra U, Perreault M, Erbe D, Krupka HI, England BP, Arnold J, Plotnikov AN, Marimuthu A, Nguyen H, Will S, Signaevsky M, Kral J, Cantwell J, Settachatgull C, Yan DS, Fong D, Oh A, Shi S, Womack P, Powell B, Habets G, West BL, Zhang KY, Milburn MV, Vlasuk GP, Hirth KP, Nolop K, Bollag G, Ibrahim PN, Tobin JF: Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent. Proc Natl Acad Sci U S A. 2009 Jan 6;106(1):262-7. Epub 2008 Dec 30. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 7848
Enzyme 44 Name Peroxisome proliferator-activated receptor delta
Enzyme 44 Synonyms
  1. PPAR-delta
  2. NUCI
  3. Nuclear hormone receptor 1
  4. NUC1
  5. Nuclear receptor subfamily 1 group C member 2
  6. Peroxisome proliferator-activated receptor beta
  7. PPAR-beta
Enzyme 44 Gene Name PPARD
Enzyme 44 Protein Sequence >Peroxisome proliferator-activated receptor delta
MEQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYTDLSRSSSPPSLLDQLQM
GCDGASCGSLNMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCERSCKIQKK
NRNKCQYCRFQKCLALGMSHNAIRFGRMPEAEKRKLVAGLTANEGSQYNPQVADLKAFSK
HIYNAYLKNFNMTKKKARSILTGKASHTAPFVIHDIETLWQAEKGLVWKQLVNGLPPYKE
ISVHVFYRCQCTTVETVRELTEFAKSIPSFSSLFLNDQVTLLKYGVHEAIFAMLASIVNK
DGLLVANGSGFVTREFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGD
RPGLMNVPRVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRI
KKTETETSLHPLLQEIYKDMY
Enzyme 44 Number of Residues 441
Enzyme 44 Molecular Weight 49903.0
Enzyme 44 Theoretical pI 7.65
Enzyme 44 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 44 General Function Involved in DNA binding
Enzyme 44 Specific Function Ligand-activated transcription factor. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID Q03181 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name PPARD_HUMAN Link Image
Enzyme 44 PDB ID 1Y0S Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1326 bp
ATGGAGCAGCCACAGGAGGAAGCCCCTGAGGTCCGGGAAGAGGAGGAGAAAGAGGAAGTG
GCAGAGGCAGAAGGAGCCCCAGAGCTCAATGGGGGACCACAGCATGCACTTCCTTCCAGC
AGCTACACAGACCTCTCCCGGAGCTCCTCGCCACCCTCACTGCTGGACCAACTGCAGATG
GGCTGTGACGGGGCCTCATGCGGCAGCCTCAACATGGAGTGCCGGGTGTGCGGGGACAAG
GCATCGGGCTTCCACTACGGTGTTCATGCATGTGAGGGGTGCAAGGGCTTCTTCCGTCGT
ACGATCCGCATGAAGCTGGAGTACGAGAAGTGTGAGCGCAGCTGCAAGATTCAGAAGAAG
AACCGCAACAAGTGCCAGTACTGCCGCTTCCAGAAGTGCCTGGCACTGGGCATGTCACAC
AACGCTATCCGTTTTGGTCGGATGCCGGAGGCTGAGAAGAGGAAGCTGGTGGCAGGGCTG
ACTGCAAACGAGGGGAGCCAGTACAACCCACAGGTGGCCGACCTGAAGGCCTTCTCCAAG
CACATCTACAATGCCTACCTGAAAAACTTCAACATGACCAAAAAGAAGGCCCGCAGCATC
CTCACCGGCAAAGCCAGCCACACGGCGCCCTTTGTGATCCACGACATCGAGACATTGTGG
CAGGCAGAGAAGGGGCTGGTGTGGAAGCAGTTGGTGAATGGCCTGCCTCCCTACAAGGAG
ATCAGCGTGCACGTCTTCTACCGCTGCCAGTGCACCACAGTGGAGACCGTGCGGGAGCTC
ACTGAGTTCGCCAAGAGCATCCCCAGCTTCAGCAGCCTCTTCCTCAACGACCAGGTTACC
CTTCTCAAGTATGGCGTGCACGAGGCCATCTTCGCCATGCTGGCCTCTATCGTCAACAAG
GACGGGCTGCTGGTAGCCAACGGCAGTGGCTTTGTCACCCGTGAGTTCCTGCGCAGCCTC
CGCAAACCCTTCAGTGATATCATTGAGCCTAAGTTTGAATTTGCTGTCAAGTTCAACGCC
CTGGAACTTGATGACAGTGACCTGGCCCTATTCATTGCGGCCATCATTCTGTGTGGAGAC
CGGCCAGGCCTCATGAACGTTCCACGGGTGGAGGCTATCCAGGACACCATCCTGCGTGCC
CTCGAATTCCACCTGCAGGCCAACCACCCTGATGCCCAGTACCTCTTCCCCAAGCTGCTG
CAGAAGATGGCTGACCTGCGGCAACTGGTCACCGAGCACGCCCAGATGATGCAGCGGATC
AAGAAGACCGAAACCGAGACCTCGCTGCACCCTCTGCTCCAGGAGATCTACAAGGACATG
TACTAA
Enzyme 44 GenBank Gene ID L07592 Link Image
Enzyme 44 GeneCard ID PPARD Link Image
Enzyme 44 GenAtlas ID PPARD Link Image
Enzyme 44 HGNC ID HGNC:9235 Link Image
Enzyme 44 Chromosome Location 6
Enzyme 44 Locus 6p21.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Schmidt A, Endo N, Rutledge SJ, Vogel R, Shinar D, Rodan GA: Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids. Mol Endocrinol. 1992 Oct;6(10):1634-41. [PubMed Link Image]
  2. Skogsberg J, Kannisto K, Roshani L, Gagne E, Hamsten A, Larsson C, Ehrenborg E: Characterization of the human peroxisome proliferator activated receptor delta gene and its expression. Int J Mol Med. 2000 Jul;6(1):73-81. [PubMed Link Image]
  3. Kobayashi T, Kodani Y, Nozawa A, Endo Y, Sawasaki T: DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system. FEBS Lett. 2008 Aug 6;582(18):2737-44. Epub 2008 Jul 11. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. van der Veen JN, Kruit JK, Havinga R, Baller JF, Chimini G, Lestavel S, Staels B, Groot PH, Groen AK, Kuipers F: Reduced cholesterol absorption upon PPARdelta activation coincides with decreased intestinal expression of NPC1L1. J Lipid Res. 2005 Mar;46(3):526-34. Epub 2004 Dec 16. [PubMed Link Image]
  8. Xu HE, Lambert MH, Montana VG, Parks DJ, Blanchard SG, Brown PJ, Sternbach DD, Lehmann JM, Wisely GB, Willson TM, Kliewer SA, Milburn MV: Molecular recognition of fatty acids by peroxisome proliferator-activated receptors. Mol Cell. 1999 Mar;3(3):397-403. [PubMed Link Image]
  9. Takada I, Yu RT, Xu HE, Lambert MH, Montana VG, Kliewer SA, Evans RM, Umesono K: Alteration of a single amino acid in peroxisome proliferator-activated receptor-alpha (PPAR alpha) generates a PPAR delta phenotype. Mol Endocrinol. 2000 May;14(5):733-40. [PubMed Link Image]
  10. Epple R, Azimioara M, Russo R, Xie Y, Wang X, Cow C, Wityak J, Karanewsky D, Bursulaya B, Kreusch A, Tuntland T, Gerken A, Iskandar M, Saez E, Martin Seidel H, Tian SS: 3,4,5-Trisubstituted isoxazoles as novel PPARdelta agonists. Part 2. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5488-92. Epub 2006 Aug 22. [PubMed Link Image]
  11. Fyffe SA, Alphey MS, Buetow L, Smith TK, Ferguson MA, Sorensen MD, Bjorkling F, Hunter WN: Recombinant human PPAR-beta/delta ligand-binding domain is locked in an activated conformation by endogenous fatty acids. J Mol Biol. 2006 Mar 3;356(4):1005-13. Epub 2006 Jan 4. [PubMed Link Image]
  12. Fyffe SA, Alphey MS, Buetow L, Smith TK, Ferguson MA, Sorensen MD, Bjorkling F, Hunter WN: Reevaluation of the PPAR-beta/delta ligand binding domain model reveals why it exhibits the activated form. Mol Cell. 2006 Jan 6;21(1):1-2. [PubMed Link Image]
  13. Pettersson I, Ebdrup S, Havranek M, Pihera P, Korinek M, Mogensen JP, Jeppesen CB, Johansson E, Sauerberg P: Design of a partial PPARdelta agonist. Bioorg Med Chem Lett. 2007 Aug 15;17(16):4625-9. Epub 2007 May 27. [PubMed Link Image]
  14. Shearer BG, Patel HS, Billin AN, Way JM, Winegar DA, Lambert MH, Xu RX, Leesnitzer LM, Merrihew RV, Huet S, Willson TM: Discovery of a novel class of PPARdelta partial agonists. Bioorg Med Chem Lett. 2008 Sep 15;18(18):5018-22. Epub 2008 Aug 9. [PubMed Link Image]
  15. Oyama T, Toyota K, Waku T, Hirakawa Y, Nagasawa N, Kasuga JI, Hashimoto Y, Miyachi H, Morikawa K: Adaptability and selectivity of human peroxisome proliferator-activated receptor (PPAR) pan agonists revealed from crystal structures. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):786-95. Epub 2009 Jul 10. [PubMed Link Image]
  16. Connors RV, Wang Z, Harrison M, Zhang A, Wanska M, Hiscock S, Fox B, Dore M, Labelle M, Sudom A, Johnstone S, Liu J, Walker NP, Chai A, Siegler K, Li Y, Coward P: Identification of a PPARdelta agonist with partial agonistic activity on PPARgamma. Bioorg Med Chem Lett. 2009 Jul 1;19(13):3550-4. Epub 2009 May 9. [PubMed Link Image]
  17. Artis DR, Lin JJ, Zhang C, Wang W, Mehra U, Perreault M, Erbe D, Krupka HI, England BP, Arnold J, Plotnikov AN, Marimuthu A, Nguyen H, Will S, Signaevsky M, Kral J, Cantwell J, Settachatgull C, Yan DS, Fong D, Oh A, Shi S, Womack P, Powell B, Habets G, West BL, Zhang KY, Milburn MV, Vlasuk GP, Hirth KP, Nolop K, Bollag G, Ibrahim PN, Tobin JF: Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent. Proc Natl Acad Sci U S A. 2009 Jan 6;106(1):262-7. Epub 2008 Dec 30. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 7861
Enzyme 45 Name Acyl-CoA-binding protein
Enzyme 45 Synonyms
  1. ACBP
  2. Diazepam-binding inhibitor
  3. DBI
  4. Endozepine
  5. EP
Enzyme 45 Gene Name DBI
Enzyme 45 Protein Sequence >Acyl-CoA-binding protein
MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWN
ELKGTSKEDAMKAYINKVEELKKKYGI
Enzyme 45 Number of Residues 87
Enzyme 45 Molecular Weight 10044.4
Enzyme 45 Theoretical pI 6.54
Enzyme 45 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 45 General Function Involved in acyl-CoA binding
Enzyme 45 Specific Function Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 73746603 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P07108 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name ACBP_HUMAN Link Image
Enzyme 45 PDB ID 1NVL Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >252 bp
GCTGAGTTTGAGAAAGCTGCAGAGGAGGTTAGGCACCTTAAGACCAAGCCAGCAGATGAT
GAGATGCTGTTCATCTATGGCCGCTACAAACAAGCAACTGTGGGCGACATAAATACAGAA
CGGCCCGGGATGTTGGACTTCACAGGCAAGGCCAAGTGGGATGCCTGGAATGAGCTGAAA
GGGACTACCAAGGAAGATGCCATGAAAGCTTACATCAACAAAGTAGAAGAGCTAAAGAAA
AAATACGGGATA
Enzyme 45 GenBank Gene ID DQ150443 Link Image
Enzyme 45 GeneCard ID DBI Link Image
Enzyme 45 GenAtlas ID DBI Link Image
Enzyme 45 HGNC ID HGNC:2690 Link Image
Enzyme 45 Chromosome Location 2
Enzyme 45 Locus 2q12-q21
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Gray PW, Glaister D, Seeburg PH, Guidotti A, Costa E: Cloning and expression of cDNA for human diazepam binding inhibitor, a natural ligand of an allosteric regulatory site of the gamma-aminobutyric acid type A receptor. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7547-51. [PubMed Link Image]
  2. Webb NR, Rose TM, Malik N, Marquardt H, Shoyab M, Todaro GJ, Lee DC: Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand. DNA. 1987 Feb;6(1):71-9. [PubMed Link Image]
  3. Nitz I, Doring F, Schrezenmeir J, Burwinkel B: Identification of new acyl-CoA binding protein transcripts in human and mouse. Int J Biochem Cell Biol. 2005 Nov;37(11):2395-405. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Marquardt H, Todaro GJ, Shoyab M: Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor. J Biol Chem. 1986 Jul 25;261(21):9727-31. [PubMed Link Image]
  7. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  8. Apfel R, Lottspeich F, Hoppe J, Behl C, Durr G, Bogdahn U: Purification and analysis of growth regulating proteins secreted by a human melanoma cell line. Melanoma Res. 1992 Dec;2(5-6):327-36. [PubMed Link Image]
  9. Kolmer M, Rovio A, Alho H: The characterization of two diazepam binding inhibitor (DBI) transcripts in humans. Biochem J. 1995 Mar 1;306 ( Pt 2):327-30. [PubMed Link Image]
  10. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Taskinen JP, van Aalten DM, Knudsen J, Wierenga RK: High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand. Proteins. 2007 Jan 1;66(1):229-38. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 8205
Enzyme 46 Name Fatty acid-binding protein, heart
Enzyme 46 Synonyms
  1. Fatty acid-binding protein 3
  2. Heart-type fatty acid-binding protein
  3. H-FABP
  4. Mammary-derived growth inhibitor
  5. MDGI
  6. Muscle fatty acid-binding protein
  7. M-FABP
Enzyme 46 Gene Name FABP3
Enzyme 46 Protein Sequence >Fatty acid-binding protein, heart
MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKN
TEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTH
GTAVCTRTYEKEA
Enzyme 46 Number of Residues 133
Enzyme 46 Molecular Weight 14857.9
Enzyme 46 Theoretical pI 6.80
Enzyme 46 GO Classification
Function
  • binding
  • lipid binding
  • transporter activity
Process
  • establishment of localization
  • transport
Component
Enzyme 46 General Function Involved in negative regulation of cell proliferation
Enzyme 46 Specific Function FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 189054293 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P05413 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name FABPH_HUMAN Link Image
Enzyme 46 PDB ID 1G5W Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >402 bp
ATGGTGGACGCTTTCCTGGGCACCTGGAAGCTAGTGGACAGCAAGAATTTCGATGACTAC
ATGAAGTCACTCGGTGTGGGTTTTGCTACCAGGCAGGTGGCCAGCATGACCAAGCCTACC
ACAATCATCGAAAAGAATGGGGACATTCTCACCCTAAAAACACACAGCACCTTCAAGAAC
ACAGAGATCAGCTTTAAGTTGGGGGTGGAGTTCGATGAGACAACAGCAGATGACAGGAAG
GTCAAGTCCATTGTGACACTGGATGGAGGGAAACTTGTTCACCTGCAGAAATGGGACGGG
CAAGAGACCACACTTGTGCGGGAGCTAATTGATGGAAAACTCATCCTGACACTCACCCAC
GGCACTGCAGTTTGCACTCGCACTTACGAGAAAGAGGCATGA
Enzyme 46 GenBank Gene ID AK314122 Link Image
Enzyme 46 GeneCard ID FABP3 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 1p33-p32
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Peeters RA, Veerkamp JH, Geurts van Kessel A, Kanda T, Ono T: Cloning of the cDNA encoding human skeletal-muscle fatty-acid-binding protein, its peptide sequence and chromosomal localization. Biochem J. 1991 May 15;276 ( Pt 1):203-7. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Offner GD, Brecher P, Sawlivich WB, Costello CE, Troxler RF: Characterization and amino acid sequence of a fatty acid-binding protein from human heart. Biochem J. 1988 May 15;252(1):191-8. [PubMed Link Image]
  6. Borchers T, Hojrup P, Nielsen SU, Roepstorff P, Spener F, Knudsen J: Revision of the amino acid sequence of human heart fatty acid-binding protein. Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):127-33. [PubMed Link Image]
  7. Troxler RF, Offner GD, Jiang JW, Wu BL, Skare JC, Milunsky A, Wyandt HE: Localization of the gene for human heart fatty acid binding protein to chromosome 1p32-1p33. Hum Genet. 1993 Dec;92(6):563-6. [PubMed Link Image]
  8. Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [PubMed Link Image]
  9. Zanotti G, Scapin G, Spadon P, Veerkamp JH, Sacchettini JC: Three-dimensional structure of recombinant human muscle fatty acid-binding protein. J Biol Chem. 1992 Sep 15;267(26):18541-50. [PubMed Link Image]
  10. Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC: Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids. Structure. 1994 Jun 15;2(6):523-34. [PubMed Link Image]
  11. Lucke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Ruterjans H: Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP). Biochem J. 2001 Mar 1;354(Pt 2):259-66. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 8524
Enzyme 47 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Enzyme 47 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 5
  2. 1-AGP acyltransferase 5
  3. 1-AGPAT 5
  4. Lysophosphatidic acid acyltransferase epsilon
  5. LPAAT-epsilon
Enzyme 47 Gene Name AGPAT5
Enzyme 47 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQS
MVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLK
EGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPE
QTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQ
RRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPD
PERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWV
TIKA
Enzyme 47 Number of Residues 364
Enzyme 47 Molecular Weight 42071.8
Enzyme 47 Theoretical pI 9.41
Enzyme 47 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 47 General Function Involved in acyltransferase activity
Enzyme 47 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 47 Pathways
Enzyme 47 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • 15-35 61-81 344-364
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 14161585 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9NUQ2 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name PLCE_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1095 bp
ATGCTGCTGTCCCTGGTGCTCCACACGTACTCCATGCGCTACCTGCTGCCCAGCGTCGTG
CTCCTGGGCACGGCGCCCACCTACGTGTTGGCCTGGGGGGTCTGGCGGCTGCTCTCCGCC
TTCCTGCCCGCCCGCTTCTACCAAGCGCTGGACGACCGGCTCTACTGCGTCTACCAGAGC
ATGGTGCTCTTCTTCTTCGAGAATTACACCGGGGTCCAGATATTGCTATATGGAGATTTG
CCAAAAAATAAAGAAAATATAATATATTTAGCAAATCATCAAAGCACAGTTGACTGGATT
GTTGCTGACATCTTGGCCATCAGGCAGAATGCGCTAGGACATGTGCGCTACGTGCTGAAA
GAAGGGTTAAAATGGCTGCCATTGTATGGGTGTTACTTTGCTCAGCATGGAGGAATCTAT
GTAAAGCGCAGTGCCAAATTTAACGAGAAAGAGATGCGAAACAAGTTGCAGAGCTACGTG
GACGCAGGAACTCCAATGTATCTTGTGATTTTTCCAGAAGGTACAAGGTATAATCCAGAG
CAAACAAAAGTCCTTTCAGCTAGTCAGGCATTTGCTGCCCAACGTGGCCTTGCAGTATTA
AAACATGTGCTAACACCACGAATAAAGGCAACTCACGTTGCTTTTGATTGCATGAAGAAT
TATTTAGATGCAATTTATGATGTTACGGTGGTTTATGAAGGGAAAGACGATGGAGGGCAG
CGAAGAGAGTCACCGACCATGACGGAATTTCTCTGCAAAGAATGTCCAAAAATTCATATT
CACATTGATCGTATCGACAAAAAAGATGTCCCAGAAGAACAAGAACATATGAGAAGATGG
CTGCATGAACGTTTCGAAATCAAAGATAAGATGCTTATAGAATTTTATGAGTCACCAGAT
CCAGAAAGAAGAAAAAGATTTCCTGGGAAAAGTGTTAATTCCAAATTAAGTATCAAGAAG
ACTTTACCATCAATGTTGATCTTAAGTGGTTTGACTGCAGGCATGCTTATGACCGATGCT
GGAAGGAAGCTGTATGTGAACACCTGGATATATGGAACCCTACTTGGCTGCCTGTGGGTT
ACTATTAAAGCATAG
Enzyme 47 GenBank Gene ID AF375789 Link Image
Enzyme 47 GeneCard ID AGPAT5 Link Image
Enzyme 47 GenAtlas ID AGPAT5 Link Image
Enzyme 47 HGNC ID HGNC:20886 Link Image
Enzyme 47 Chromosome Location 8
Enzyme 47 Locus 8p23.1
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 8587
Enzyme 48 Name Bile acyl-CoA synthetase
Enzyme 48 Synonyms
  1. BACS
  2. Bile acid-CoA ligase
  3. BA-CoA ligase
  4. BAL
  5. Cholate--CoA ligase
  6. Fatty acid transport protein 5
  7. FATP-5
  8. Fatty-acid-coenzyme A ligase, very long-chain 3
  9. Solute carrier family 27 member 5
  10. Very long-chain acyl-CoA synthetase homolog 2
  11. VLCS-H2
  12. VLCSH2
  13. Very long-chain acyl-CoA synthetase-related protein
  14. VLACS-related
  15. VLACSR
Enzyme 48 Gene Name SLC27A5
Enzyme 48 Protein Sequence >Bile acyl-CoA synthetase
MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWV
PHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAF
ERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVL
ASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILP
KLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTG
LPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP
KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQ
QRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDN
QGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMD
REGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQ
LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVD
PLFVLDNRAQSFRPLTAEMYQAVCEGTWRL
Enzyme 48 Number of Residues 690
Enzyme 48 Molecular Weight 75384.4
Enzyme 48 Theoretical pI 7.70
Enzyme 48 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 48 General Function Involved in catalytic activity
Enzyme 48 Specific Function Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol
Enzyme 48 Pathways
Enzyme 48 Reactions
  • (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN:R02794]
  • (2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN:R04580]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • 31-51 56-76
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 4768277 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q9Y2P5 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name S27A5_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >2073 bp
ATGGGTGTCAGGCAACAGTTGGCCTTGCTGCTGCTGCTGCTGCTCCTGCTCTGGGGCCTG
GGGCAGCCAGTGTGGCCAGTCGCTGTGGCCTTGACCCTGCGCTGGCTCCTGGGGGATCCC
ACATGTTGCGTGCTACTTGGGCTGGCCATGTTAGCACGGCCCTGGCTCGGCCCCTGGGTG
CCCCATGGGCTGAGCCTGGCAGCTGCGGCCCTGGCACTAACCCTCCTGCCAGCACGGCTG
CCCCCAGGACTACGCTGGCTGCCGGCTGATGTGATCTTCTTGGCCAAGATCCTCCACCTG
GGCCTGAAGATCAGGGGATGCTTGAGCCGGCAGCCGCCTGACACCTTTGTAGATGCCTTC
GAGCGGCGAGCACGAGCGCAGCCTGGCAGGGCACTCTTGGTGTGGACGGGGCCTGGGGCC
GGCTCAGTCACCTTTGGTGAGCTGGATGCCCGGGCCTGCCAGGCGGCATGGGCCCTGAAG
GCTGAGCTGGGTGACCCTGCGAGCCTGTGTGCCGGGGAGCCTACTGCCCTCCTTGTGCTG
GCTTCCCAGGCCGTTCCAGCCCTGTGTATGTGGCTGGGGCTGGCCAAGCTGGGCTGCCCA
ACAGCCTGGATCAACCCGCATGGCCGGGGGATGCCCCTGGCGCACTCTGTGCTGAGCTCT
GGGGCCCGGGTGCTGGTGGTGGACCCAGACCTCCGGGAGAGCCTGGAGGAGATCCTTCCC
AAGCTGCAGGCTGAGAACATCCGCTGCTTCTACCTCAGCCATACCTCCCCTACACCAGGG
GTGGGGGCTCTGGGGGCTGCCCTGGATGCAGCGCCCTCCCACCCAGTGCCTGCTGACCTG
CGTGCTGGGATCACATGGAGAAGCCCTGCCCTCTTCATCTATACCTCGGGGACCACTGGC
CTCCCGAAGCCAGCCATCCTCACGCATGAGCGGGTACTGCAGATGAGCAAGATGCTGTCC
TTATCTGGGGCCACAGCTGATGATGTGGTTTACACGGTCCTGCCTCTGTACCACGTGATG
GGACTTGTCGTTGGGATCCTCGGCTGCTTAGATCTCGGAGCCACCTGTGTTCTGGCCCCC
AAGTTCTCTACTTCCTGCTTCTGGGATGACTGTCGGCAGCATGGCGTGACAGTGATCCTG
TATGTGGGCGAGCTCCTGCGGTACTTGTGTAACATTCCCCAGCAACCAGAGGACCGGACA
CATACAGTCCGCCTGGCAATGGGCAATGGACTACGGGCTGATGTGTGGGAGACCTTCCAG
CAGCGCTTCGGTCCTATTCGGATCTGGGAAGTCTACGGCTCCACAGAAGGCAACATGGGC
TTAGTCAACTATGTGGGGCGCTGCGGGGCCCTGGGCAAGATGAGCTGCCTCCTCCGAATG
CTGTCCCCCTTTGAGCTGGTGCAGTTCGACATGGAGGCGGCGGAGCCTGTGAGGGACAAT
CAGGGCTTCTGCATCCCTGTAGGGCTAGGGGAGCCGGGGCTGCTGCTGACCAAGGTGGTA
AGCCAGCAACCCTTCGTGGGCTACCGCGGCCCCCGAGAGCTGTCGGAACGGAAGCTGGTG
CGCAACGTGCGGCAATCGGGCGACGTTTACTACAACACCGGGGACGTACTGGCCATGGAC
CGCGAAGGCTTCCTCTACTTCCGCGACCGCCTCGGGGACACCTTCCGATGGAAGGGCGAG
AACGTGTCCACGCACGAGGTGGAGGGCGTGTTGTCGCAGGTGGACTTCTTGCAACAGGTT
AACGTGTATGGCGTGTGCGTGCCAGGTTGTGAGGGTAAGGTGGGCATGGCTGCTGTGCAG
CTAGCCCCCGGCCAGACTTTCGACGGGGAGAAGTTGTACCAGCACGTTCGCGCTTGGCTC
CCTGCCTACGCTACCCCCCATTTCATCCGCATCCAGGACGCCATGGAGGTCACCAGCACG
TTCAAACTGATGAAGACCCGGTTGGTGCGTGAGGGCTTCAATGTGGGGATCGTGGTTGAC
CCTCTGTTTGTACTGGACAACCGGGCCCAGTCCTTCCGGCCCCTGACGGCAGAAATGTAC
CAGGCTGTGTGTGAGGGAACCTGGAGGCTCTGA
Enzyme 48 GenBank Gene ID AF064255 Link Image
Enzyme 48 GeneCard ID SLC27A5 Link Image
Enzyme 48 GenAtlas ID SLC27A5 Link Image
Enzyme 48 HGNC ID HGNC:10999 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 19q13.43
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA: Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. Mol Genet Metab. 1999 Sep;68(1):32-42. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Steinberg SJ, Mihalik SJ, Kim DG, Cuebas DA, Watkins PA: The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase. J Biol Chem. 2000 May 26;275(21):15605-8. [PubMed Link Image]
  4. Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA: Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. J Biol Chem. 2002 Jul 5;277(27):24771-9. Epub 2002 Apr 29. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 8614
Enzyme 49 Name Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Enzyme 49 Synonyms
  1. Branched-chain alpha-keto acid dehydrogenase complex component E2
  2. BCKAD-E2
  3. BCKADE2
  4. Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
  5. Dihydrolipoamide branched chain transacylase
  6. Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Enzyme 49 Gene Name DBT
Enzyme 49 Protein Sequence >Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAAL
RGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKK
LYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRL
AMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPIL
VSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFA
RGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVK
NVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAI
GALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD
LK
Enzyme 49 Number of Residues 482
Enzyme 49 Molecular Weight 53486.6
Enzyme 49 Theoretical pI 8.75
Enzyme 49 GO Classification
Function
  • acyltransferase activity
  • binding
  • catalytic activity
  • cofactor binding
  • dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity
  • protein binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • acyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • fatty-acyl-CoA biosynthetic process
  • fatty-acyl-CoA metabolic process
  • metabolic process
Component
Enzyme 49 General Function Involved in acyltransferase activity
Enzyme 49 Specific Function The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions
  • 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine [RN:R02662]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 189053756 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID P11182 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name ODB2_HUMAN Link Image
Enzyme 49 PDB ID 1K8O Link Image
Enzyme 49 PDB File Show
Enzyme 49 3D Structure
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1449 bp
ATGGCTGCAGTCCGTATGCTGAGAACCTGGAGCAGGAATGCGGGGAAGCTGATTTGTGTT
CGCTATTTTCAAACATGTGGTAATGTTCATGTTTTGAAGCCAAATTATGTGTGTTTCTTT
GGTTATCCTTCATTCAAGTATAGTCATCCACATCACTTCCTGAAAACAACTGCTGCTCTC
CGTGGACAGGTTGTTCAGTTCAAGCTCTCAGACATTGGAGAAGGGATTAGAGAAGTAACT
GTTAAAGAATGGTATGTAAAAGAAGGAGATACAGTGTCTCAGTTTGATAGCATCTGTGAA
GTTCAAAGTGATAAAGCTTCTGTTACCATCACTAGTCGTTATGATGGAGTCATTAAAAAA
CTCTATTATAATCTAGACGATATTGCCTATGTGGGGAAGCCATTAGTAGACATAGAAACG
GAAGCTTTAAAAGATTCAGAAGAAGATGTTGTTGAAACTCCTGCAGTGTCTCATGATGAA
CATACACACCAAGAGATAAAGGGCCGAAAAACACTGGCAACTCCTGCAGTTCGCCGTCTG
GCAATGGAAAACAATATTAAGCTGAGTGAAGTTGTTGGCTCAGGAAAAGATGGCAGAATA
CTTAAAGAAGATATCCTCAACTATTTGGAAAAGCAGACAGGAGCTATATTGCCTCCTTCA
CCCAAAGTTGAAATTATGCCACCTCCACCAAAGCCAAAAGACATGACTGTTCCTATACTA
GTATCAAAACCTCCGGTATTCACAGGCAAAGACAAAACAGAACCCATAAAAGGCTTTCAA
AAAGCAATGGTCAAGACTATGTCTGCAGCCCTGAAGATACCTCATTTTGGTTATTGTGAT
GAGATTGACCTTACTGAACTGGTTAAGCTCCGAGAAGAATTAAAACCCATTGCATTTGCT
CGTGGAATTAAACTCTCCTTTATGCCTTTCTTCTTAAAGGCTGCTTCCTTGGGATTACTA
CAGTTTCCTATCCTTAACGCTTCTGTGGATGAAAACTGCCAGAATATAACATATAAGGCT
TCTCATAACATTGGGATAGCAATGGATACTGAGCAGGGTTTGATTGTCCCTAATGTGAAA
AATGTTCAGATCTGCTCTATATTTGACATCGCCACTGAACTGAACCGCCTCCAGAAATTG
GGCTCTGTGGGTCAGCTCAGCACCACTGATCTTACAGGAGGAACATTTACTCTTTCCAAC
ATTGGATCAATTGGTGGTACCTTTGCCAAACCAGTGATAATGCCACCTGAAGTAGCCATT
GGGGCCCTTGGATCAATTAAGGCCATTCCCCGATTTAACCAGAAAGGAGAAGTATATAAG
GCACAGATAATGAATGTGAGCTGGTCAGCTGATCACAGAGTTATTGATGGTGCTACAATG
TCACGCTTCTCCAATTTGTGGAAATCCTATTTAGAAAACCCAGCTTTTATGCTACTAGAT
CTGAAATGA
Enzyme 49 GenBank Gene ID AK313191 Link Image
Enzyme 49 GeneCard ID DBT Link Image
Enzyme 49 GenAtlas ID DBT Link Image
Enzyme 49 HGNC ID HGNC:2698 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1p31
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT: The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex. Biochim Biophys Acta. 1992 Oct 20;1132(3):319-21. [PubMed Link Image]
  2. Hummel KB, Litwer S, Bradford AP, Aitken A, Danner DJ, Yeaman SJ: Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure. J Biol Chem. 1988 May 5;263(13):6165-8. [PubMed Link Image]
  3. Danner DJ, Litwer S, Herring WJ, Pruckler J: Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase. J Biol Chem. 1989 May 5;264(13):7742-6. [PubMed Link Image]
  4. Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I: Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex. Biochem Biophys Res Commun. 1989 Jun 30;161(3):1035-41. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Lau KS, Griffin TA, Hu CW, Chuang DT: Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry. 1988 Mar 22;27(6):1972-81. [PubMed Link Image]
  9. Lau KS, Herring WJ, Chuang JL, McKean M, Danner DJ, Cox RP, Chuang DT: Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene. J Biol Chem. 1992 Nov 25;267(33):24090-6. [PubMed Link Image]
  10. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Chang CF, Chou HT, Chuang JL, Chuang DT, Huang TH: Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. J Biol Chem. 2002 May 3;277(18):15865-73. Epub 2002 Feb 11. [PubMed Link Image]
  13. Fisher CW, Lau KS, Fisher CR, Wynn RM, Cox RP, Chuang DT: A 17-bp insertion and a Phe215----Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34. Biochem Biophys Res Commun. 1991 Jan 31;174(2):804-9. [PubMed Link Image]
  14. Tsuruta M, Mitsubuchi H, Mardy S, Miura Y, Hayashida Y, Kinugasa A, Ishitsu T, Matsuda I, Indo Y: Molecular basis of intermittent maple syrup urine disease: novel mutations in the E2 gene of the branched-chain alpha-keto acid dehydrogenase complex. J Hum Genet. 1998;43(2):91-100. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 8626
Enzyme 50 Name 2-acylglycerol O-acyltransferase 2
Enzyme 50 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 2
  2. MGAT2
  3. hMGAT2
  4. Diacylglycerol O-acyltransferase candidate 5
  5. hDC5
  6. Diacylglycerol acyltransferase 2-like protein 5
  7. Monoacylglycerol O-acyltransferase 2
Enzyme 50 Gene Name MOGAT2
Enzyme 50 Protein Sequence >2-acylglycerol O-acyltransferase 2
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
Enzyme 50 Number of Residues 334
Enzyme 50 Molecular Weight 38195.3
Enzyme 50 Theoretical pI 9.77
Enzyme 50 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 50 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 50 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity
Enzyme 50 Pathways
Enzyme 50 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • 23-37 38-59 103-123
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 37537527 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q3SYC2 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name MOGT2_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1005 bp
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
Enzyme 50 GenBank Gene ID NM_025098.2 Link Image
Enzyme 50 GeneCard ID MOGAT2 Link Image
Enzyme 50 GenAtlas ID MOGAT2 Link Image
Enzyme 50 HGNC ID HGNC:23248 Link Image
Enzyme 50 Chromosome Location 1
Enzyme 50 Locus 11q13.5
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 5. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Lockwood JF, Cao J, Burn P, Shi Y: Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E927-37. Epub 2003 Jun 24. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 8676
Enzyme 51 Name Long-chain fatty acid transport protein 3
Enzyme 51 Synonyms
  1. FATP-3
  2. Fatty acid transport protein 3
  3. Solute carrier family 27 member 3
  4. Very long-chain acyl-CoA synthetase homolog 3
  5. VLCS-3
Enzyme 51 Gene Name SLC27A3
Enzyme 51 Protein Sequence >Long-chain fatty acid transport protein 3
MGVCQRTRAPWKEKSQLERAALGFRKGGSGMFASGWNQTVPIEEAGSMAALLLLPLLLLL
PLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEGPEGGCSLAWRLAE
LAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGGDSGEGSAGEGERA
APGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEFLWLWFGLAKAGLR
TAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAG
ISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQ
LCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQ
YIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVA
TINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVS
QQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGE
NVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENL
PPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQAVGAYLPLTTARY
SALLAGNLRI
Enzyme 51 Number of Residues 730
Enzyme 51 Molecular Weight 78643.4
Enzyme 51 Theoretical pI 7.53
Enzyme 51 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 51 General Function Involved in catalytic activity
Enzyme 51 Specific Function Has acyl-CoA ligase activity for long-chain and very- long-chain fatty acids. Does not exhibit fatty acid transport activity
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 50-70 369-389
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 13236579 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q5K4L6 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name S27A3_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2193 bp
ATGGGCGTGTGCCAGCGCACGCGCGCTCCCTGGAAGGAGAAGTCTCAGCTAGAACGAGCG
GCCCTAGGTTTTCGGAAGGGAGGATCAGGGATGTTTGCGAGCGGCTGGAACCAGACGGTG
CCGATAGAGGAAGCGGGCTCCATGGCTGCCCTCCTGCTGCTGCCCCTGCTGCTGTTGCTA
CCGCTGCTGCTGCTGAAGCTACACCTCTGGCCGCAGTTGCGCTGGCTTCCGGCGGACTTG
GCCTTTGCGGTGCGAGCTCTGTGCTGCAAAAGGGCTCTTCGAGCTCGCGCCCTGGCCGCG
GCTGCCGCCGACCCGGAAGGTCCCGAGGGGGGCTGCAGCCTGGCCTGGCGCCTCGCGGAA
CTGGCCCAGCAGCGCGCCGCGCACACCTTTCTCATTCACGGCTCGCGGCGCTTTAGCTAC
TCAGAGGCGGAGCGCGAGAGTAACAGGGCTGCACGCGCCTTCCTACGTGCGCTAGGCTGG
GACTGGGGACCCGACGGCGGCGACAGCGGCGAGGGGAGCGCTGGAGAAGGCGAGCGGGCA
GCGCCGGGAGCCGGAGATGCAGCGGCCGGAAGCGGCGCGGAGTTTGCCGGAGGGGACGGT
GCCGCCAGAGGTGGAGGAGCCGCCGCCCCTCTGTCACCTGGAGCAACTGTGGCGCTGCTC
CTCCCCGCTGGCCCAGAGTTTCTGTGGCTCTGGTTCGGGCTGGCCAAGGCCGGCCTGCGC
ACTGCCTTTGTGCCCACCGCCCTGCGCCGGGGCCCCCTGCTGCACTGCCTCCGCAGCTGC
GGCGCGCGCGCGCTGGTGCTGGCGCCAGAGTTTCTGGAGTCCCTGGAGCCGGACCTGCCC
GCCCTGAGAGCCATGGGGCTCCACCTGTGGGCTGCAGGCCCAGGAACCCACCCTGCTGGA
ATTAGCGATTTGCTGGCTGAAGTGTCCGCTGAAGTGGATGGGCCAGTGCCAGGATACCTC
TCTTCCCCCCAGAGCATAACAGACACGTGCCTGTACATCTTCACCTCTGGCACCACGGGC
CTCCCCAAGGCTGCTCGGATCAGTCATCTGAAGATCCTGCAATGCCAGGGCTTCTATCAG
CTGTGTGGTGTCCACCAGGAAGATGTGATCTACCTCGCCCTCCCACTCTACCACATGTCC
GGTTCCCTGCTGGGCATCGTGGGCTGCATGGGCATTGGGGCCACAGTGGTGCTGAAATCC
AAGTTCTCGGCTGGTCAGTTCTGGGAAGATTGCCAGCAGCACAGGGTGACGGTGTTCCAG
TACATTGGGGAGCTGTGCCGATACCTTGTCAACCAGCCCCCGAGCAAGGCAGAACGTGGC
CATAAGGTCCGGCTGGCAGTGGGCAGCGGGCTGCGCCCAGATACCTGGGAGCGTTTTGTG
CGGCGCTTCGGGCCCCTGCAGGTGCTGGAGACATATGGACTGACAGAGGGCAACGTGGCC
ACCATCAACTACACAGGACAGCGGGGCGCTGTGGGGCGTGCTTCCTGGCTTTACAAGCAT
ATCTTCCCCTTCTCCTTGATTCGCTATGATGTCACCACAGGAGAGCCAATTCGGGACCCC
CAGGGGCACTGTATGGCCACATCTCCAGGTGAGCCAGGGCTGCTGGTGGCCCCGGTAAGC
CAGCAGTCCCCATTCCTGGGCTATGCTGGCGGGCCAGAGCTGGCCCAGGGGAAGTTGCTA
AAGGATGTCTTCCGGCCTGGGGATGTTTTCTTCAACACTGGGGACCTGCTGGTCTGCGAT
GACCAAGGTTTTCTCCGCTTCCATGATCGTACTGGAGACACCTTCAGGTGGAAGGGGGAG
AATGTGGCCACAACCGAGGTGGCAGAGGTCTTCGAGGCCCTAGATTTTCTTCAGGAGGTG
AACGTCTATGGAGTCACTGTGCCAGGGCATGAAGGCAGGGCTGGAATGGCAGCCCTAGTT
CTGCGTCCCCCCCACGCTTTGGACCTTATGCAGCTCTACACCCACGTGTCTGAGAACTTG
CCACCTTATGCCCGGCCCCGATTCCTCAGGCTCCAGGAGTCTTTGGCCACCACAGAGACC
TTCAAACAGCAGAAAGTTCGGATGGCAAATGAGGGCTTCGACCCCAGCACCCTGTCTGAC
CCACTGTACGTTCTGGACCAGGCTGTAGGTGCCTACCTGCCCCTCACAACTGCCCGGTAC
AGCGCCCTCCTGGCAGGAAACCTTCGAATCTGA
Enzyme 51 GenBank Gene ID NM_024330.1 Link Image
Enzyme 51 GeneCard ID SLC27A3 Link Image
Enzyme 51 GenAtlas ID SLC27A3 Link Image
Enzyme 51 HGNC ID HGNC:10997 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 1q21.3
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 8735
Enzyme 52 Name Long-chain fatty acid transport protein 1
Enzyme 52 Synonyms
  1. FATP-1
  2. Fatty acid transport protein 1
  3. Solute carrier family 27 member 1
Enzyme 52 Gene Name SLC27A1
Enzyme 52 Protein Sequence >Long-chain fatty acid transport protein 1
MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSV
LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLF
RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI
FGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGM
DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIG
VGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL
AVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR
LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSV
FSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY
GVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ
KTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL
Enzyme 52 Number of Residues 646
Enzyme 52 Molecular Weight 71107.5
Enzyme 52 Theoretical pI 8.63
Enzyme 52 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 52 General Function Lipid transport and metabolism
Enzyme 52 Specific Function Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • 14-34
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 38524616 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q6PCB7 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name S27A1_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >1941 bp
ATGCGGGCTCCGGGTGCGGGCGCGGCCTCGGTGGTCTCGCTGGCGCTGTTGTGGCTGCTG
GGGCTGCCGTGGACCTGGAGCGCGGCAGCGGCGCTCGGCGTGTACGTGGGCAGCGGCGGC
TGGCGCTTCCTGCGCATCGTCTGCAAGACCGCGAGGCGAGACCTCTTCGGTCTCTCTGTG
CTGATCCGCGTGCGCCTGGAGCTGCGGCGGCACCAGCGTGCCGGCCACACCATCCCGCGC
ATCTTTCAGGCGGTAGTGCAGCGACAGCCCGAGCGCCTGGCGCTGGTGGATGCCGGGACC
GGCGAGTGCTGGACCTTTGCGCAGCTGGACGCCTACTCCAATGCGGTAGCCAACCTCTTC
CGCCAGCTGGGCTTCGCGCCGGGCGACGTGGTGGCCATCTTCCTGGAGGGCCGGCCGGAG
TTCGTGGGGCTGTGGCTGGGCCTGGCCAAGGCGGGCATGGAGGCCGCGCTGCTCAACGTG
AACCTGCGGCGCGAGCCCCTGGCCTTCTGCCTGGGCACCTCGGGCGCTAAGGCCCTGATC
TTTGGAGGAGAAATGGTGGCGGCGGTGGCCGAAGTGAGCGGGCATCTGGGGAAAAGTTTG
ATCAAGTTCTGCTCTGGAGACTTGGGGCCCGAGGGCATCTTGCCGGACACCCACCTCCTG
GACCCGCTGCTGAAGGAGGCCTCTACTGCCCCCTTGGCACAGATCCCCAGCAAGGGCATG
GACGATCGTCTTTTCTACATCTACACGTCGGGGACCACCGGGCTGCCCAAGGCTGCCATT
GTCGTGCACAGCAGGTACTACCGCATGGCAGCCTTCGGCCACCACGCCTACCGCATGCAG
GCGGCTGACGTGCTCTATGACTGCCTGCCCCTGTACCACTCGGCAGGAAACATCATCGGC
GTGGGGCAGTGTCTCATCTATGGGCTGACAGTCGTCCTCCGCAAGAAATTCTCGGCCAGC
CGCTTCTGGGACGACTGCATCAAGTACAACTGCACGGTGGTTCAGTACATCGGGGAGATC
TGCCGCTACCTGCTGAAGCAGCCGGTGCGCGAGGCGGAGAGGCGACACCGCGTGCGCCTG
GCGGTGGGGAACGGGCTGCGTCCTGCCATCTGGGAGGAGTTCACGGAGCGCTTCGGCGTA
CGCCAAATCGGGGAGTTCTACGGCGCCACCGAGTGCAACTGCAGCATTGCCAACATGGAC
GGCAAGGTCGGCTCCTGTGGTTTCAACAGCCGCATCCTGCCCCACGTGTACCCCATCCGG
CTGGTGAAGGTCAATGAGGACACAATGGAGCTGCTGCGGGATGCCCAGGGCCTCTGCATC
CCCTGCCAGGCCGGGGAGCCTGGCCTCCTTGTGGGTCAGATCAACCAACAGGACCCGCTG
CGCCGCTTCGATGGCTATGTCAGCGAGAGCGCCACCAGCAAGAAGATCGCCCACAGCGTC
TTCAGCAAGGGCGACAGCGCCTACCTCTCAGGTGACGTGCTAGTGATGGATGAGCTGGGC
TACATGTACTTCCGGGACCGTAGCGGGGACACCTTCCGCTGGCGAGGGGAGAACGTCTCC
ACCACCGAGGTGGAGGGCGTGCTGAGCCGCCTGCTGGGCCAGACAGACGTGGCCGTCTAT
GGGGTGGCTGTTCCAGGAGTGGAGGGTAAGGCAGGGATGGCGGCCGTCGCAGACCCCCAC
AGCCTGCTGGACCCCAACGCGATATACCAGGAGCTGCAGAAGGTGCTGGCACCCTATGCC
CGGCCCATCTTCCTGCGCCTCCTGCCCCAGGTGGACACCACAGGCACCTTCAAGATCCAG
AAGACGAGGCTGCAGCGAGAGGGCTTTGACCCACGCCAGACCTCAGACCGGCTCTTCTTC
CTGGACCTGAAGCAGGGCCACTACCTGCCCTTAAATGAGGCAGTCTACACTCGCATCTGC
TCGGGCGCCTTCGCCCTCTGA
Enzyme 52 GenBank Gene ID NM_198580.1 Link Image
Enzyme 52 GeneCard ID SLC27A1 Link Image
Enzyme 52 GenAtlas ID Not Available
Enzyme 52 HGNC ID Not Available
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 19p13.11
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Martin G, Nemoto M, Gelman L, Geffroy S, Najib J, Fruchart JC, Roevens P, de Martinville B, Deeb S, Auwerx J: The human fatty acid transport protein-1 (SLC27A1; FATP-1) cDNA and gene: organization, chromosomal localization, and expression. Genomics. 2000 Jun 15;66(3):296-304. [PubMed Link Image]
  4. Hatch GM, Smith AJ, Xu FY, Hall AM, Bernlohr DA: FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells. J Lipid Res. 2002 Sep;43(9):1380-9. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 8802
Enzyme 53 Name Acyl-CoA dehydrogenase family member 10
Enzyme 53 Synonyms
  1. ACAD-10
Enzyme 53 Gene Name ACAD10
Enzyme 53 Protein Sequence >Acyl-CoA dehydrogenase family member 10
MCVRSCFQSPRLQWVWRTAFLKHTQRRHQGSHRWTHLGGSTYRAVIFDMGGVLIPSPGRV
AAEWEVQNRIPSGTILKALMEGGENGPWMRFMRAEITAEGFLREFGRLCSEMLKTSVPVD
SFFSLLTSERVAKQFPVMTEAITQIRAKGLQTAVLSNNFYLPNQKSFLPLDRKQFDVIVE
SCMEGICKPDPRIYKLCLEQLGLQPSESIFLDDLGTNLKEAARLGIHTIKVNDPETAVKE
LEALLGFTLRVGVPNTRPVKKTMEIPKDSLQKYLKDLLGIQTTGPLELLQFDHGQSNPTY
YIRLANRDLVLRKKPPGTLLPSAHAIEREFRIMKALANAGVPVPNVLDLCEDSSVIGTPF
YVMEYCPGLIYKDPSLPGLEPSHRRAIYTAMNTVLCKIHSVDLQAVGLEDYGKQGDYIPR
QVRTWVKQYRASETSTIPAMERLIEWLPLHLPRQQRTTVVHGDFRLDNLVFHPEEPEVLA
VLDWELSTLGDPLADVAYSCLAHYLPSSFPVLRGINDCDLTQLGIPAAEEYFRMYCLQMG
LPPTENWNFYMAFSFFRVAAILQGVYKRSLTGQASSTYAEQTGKLTEFVSNLAWDFAVKE
GFRVFKEMPFTNPLTRSYHTWARPQSQWCPTGSRSYSSVPEASPAHTSRGGLVISPESLS
PPVRELYHRLKHFMEQRVYPAEPELQSHQASAARWSPSPLIEDLKEKAKAEGLWNLFLPL
EADPEKKYGAGLTNVEYAHLCELMGTSLYAPEVCNCSAPDTGNMELLVRYGTEAQKARWL
IPLLEGKARSCFAMTEPQVASSDATNIEASIREEDSFYVINGHKWWITGILDPRCQLCVF
MGKTDPHAPRHRQQSVLLVPMDTPGIKIIRPLTVYGLEDAPGGHGEVRFEHVRVPKENMV
LGPGRGFEIAQGRLGPGRIHHCMRLIGFSERALALMKARVKSRLAFGKPLVEQGTVLADI
AQSRVEIEQARLLVLRAAHLMDLAGNKAAALDIAMIKMVAPSMASRVIDRAIQAFGAAGL
SSDYPLAQFFTWARALRFADGPDEVHRATVAKLELKHRI
Enzyme 53 Number of Residues 1059
Enzyme 53 Molecular Weight 118833.0
Enzyme 53 Theoretical pI 8.13
Enzyme 53 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hydrolase activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 53 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 53 Specific Function May function as oxidoreductase
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 48976061 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID Q6JQN1 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name ACD10_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >3180 bp
ATGTGTGTCAGGAGCTGTTTCCAGTCCCCCCGTCTCCAGTGGGTGTGGAGAACAGCCTTC
CTGAAACACACCCAGCGCAGGCACCAGGGGTCCCACCGATGGACACACCTTGGAGGCAGC
ACCTACAGAGCGGTGATTTTCGACATGGGCGGAGTTCTCATTCCTTCTCCAGGGAGAGTC
GCTGCAGAATGGGAGGTACAGAATCGTATCCCTTCTGGAACTATATTAAAGGCCTTGATG
GAAGGTGGTGAAAATGGGCCCTGGATGAGATTTATGAGAGCAGAAATAACAGCAGAGGGT
TTTTTACGAGAATTTGGGAGACTTTGCTCTGAAATGTTAAAGACCTCCGTGCCTGTGGAC
TCATTTTTCTCTCTGTTGACCAGTGAGCGAGTGGCAAAGCAGTTCCCAGTGATGACTGAG
GCCATAACTCAAATTCGGGCAAAAGGTCTTCAGACTGCAGTCTTGAGCAATAATTTTTAT
CTTCCCAACCAGAAAAGCTTTTTGCCCCTGGACCGGAAACAGTTTGATGTGATTGTGGAG
TCCTGCATGGAAGGGATCTGTAAGCCAGACCCTAGGATCTACAAGCTGTGCTTGGAGCAG
CTCGGCCTGCAGCCCTCTGAGTCCATCTTTCTTGATGACCTTGGAACAAATCTAAAAGAA
GCTGCCAGACTTGGTATTCACACCATTAAGGTTAATGACCCAGAGACTGCAGTAAAGGAA
TTAGAAGCTCTCTTGGGTTTTACATTGAGAGTAGGTGTTCCAAACACTCGGCCTGTGAAA
AAGACGATGGAAATTCCGAAAGATTCCTTGCAGAAGTACCTCAAAGACTTACTGGGTATC
CAGACCACAGGCCCATTGGAACTACTTCAGTTTGATCACGGGCAGTCAAATCCAACTTAC
TACATCAGGCTGGCTAATCGTGATCTAGTTCTGAGGAAGAAGCCCCCAGGGACACTCCTT
CCATCTGCCCATGCCATAGAGAGGGAGTTCAGGATTATGAAAGCCCTTGCAAATGCTGGA
GTACCTGTCCCTAACGTTCTTGATCTCTGTGAAGATTCAAGTGTCATTGGCACCCCCTTC
TATGTGATGGAGTACTGCCCAGGTCTCATCTACAAAGACCCTTCCCTGCCAGGCTTGGAG
CCCAGCCACAGACGAGCCATATACACTGCCATGAACACAGTCCTGTGCAAAATTCACAGT
GTGGATCTGCAGGCTGTGGGACTTGAAGACTATGGGAAGCAAGGGGACTATATTCCACGC
CAGGTACGAACCTGGGTTAAGCAGTATCGAGCTTCCGAAACTAGCACCATCCCAGCCATG
GAGAGGCTGATCGAATGGCTGCCCCTCCATCTTCCCCGTCAGCAGAGGACCACAGTGGTG
CACGGGGACTTCAGGCTCGACAACCTGGTGTTTCATCCAGAAGAGCCAGAGGTGCTTGCT
GTCCTTGACTGGGAACTTTCTACCTTGGGCGACCCCCTTGCTGATGTGGCCTACAGCTGC
CTGGCTCATTACCTGCCATCCAGTTTTCCCGTGCTGAGAGGTATTAATGACTGTGACTTG
ACACAGCTGGGAATCCCTGCTGCAGAGGAGTATTTCAGGATGTACTGTCTCCAAATGGGG
CTCCCTCCCACTGAGAACTGGAACTTCTATATGGCTTTTTCCTTTTTCCGTGTGGCTGCA
ATCCTACAGGGAGTCTACAAGCGATCACTCACAGGGCAAGCAAGCTCCACATATGCGGAA
CAAACTGGAAAGCTGACCGAATTTGTGTCTAACCTGGCGTGGGATTTCGCAGTCAAAGAA
GGGTTCCGGGTTTTCAAAGAGATGCCCTTCACAAATCCGTTAACAAGGTCCTACCACACG
TGGGCCAGGCCCCAGTCCCAGTGGTGCCCCACAGGCAGCAGGAGTTATAGCTCCGTTCCA
GAAGCTTCCCCAGCTCATACCTCAAGGGGAGGTCTGGTTATCTCTCCAGAGAGCCTCTCT
CCACCTGTCAGAGAGCTGTATCACCGGCTGAAGCACTTCATGGAGCAACGTGTGTACCCT
GCAGAGCCAGAGCTGCAGAGTCACCAGGCCTCAGCAGCCAGGTGGAGCCCCTCCCCACTG
ATCGAAGACCTCAAGGAGAAAGCCAAAGCTGAAGGACTTTGGAACCTTTTCCTACCCTTA
GAGGCTGATCCCGAGAAAAAATACGGAGCAGGACTGACCAATGTGGAATATGCACATCTG
TGTGAGCTCATGGGCACGTCCCTGTATGCCCCCGAGGTATGTAACTGCTCTGCGCCTGAC
ACGGGCAACATGGAGCTGCTGGTGAGGTATGGCACCGAAGCGCAGAAGGCTCGCTGGCTG
ATTCCTCTGCTGGAGGGGAAAGCCCGCTCCTGTTTTGCTATGACCGAGCCCCAGGTTGCC
TCTTCAGATGCCACCAACATTGAGGCTTCCATCAGAGAGGAGGACAGCTTCTATGTCATA
AACGGTCACAAATGGTGGATCACAGGCATCCTGGATCCTCGTTGCCAACTCTGTGTGTTT
ATGGGAAAAACAGACCCACATGCACCAAGACACCGGCAGCAGTCTGTGCTCTTGGTTCCC
ATGGATACCCCAGGGATAAAAATCATCCGGCCTCTGACGGTGTATGGACTGGAAGATGCA
CCAGGTGGCCATGGTGAAGTCCGATTTGAGCACGTGCGTGTGCCCAAAGAGAACATGGTC
CTGGGCCCTGGCCGAGGCTTTGAGATCGCCCAGGGCAGACTGGGCCCCGGCAGGATCCAT
CACTGCATGAGGCTGATCGGGTTCTCAGAGAGGGCCCTGGCACTCATGAAGGCCCGCGTG
AAGTCCCGCTTGGCTTTTGGGAAGCCCCTGGTGGAGCAGGGCACAGTGCTGGCGGACATC
GCGCAGTCGCGCGTGGAGATTGAGCAGGCACGGCTGCTGGTGCTGAGAGCTGCCCACCTC
ATGGACCTGGCAGGAAACAAGGCTGCAGCCTTGGATATAGCCATGATTAAAATGGTCGCC
CCGTCCATGGCCTCCCGAGTGATTGATCGTGCGATTCAGGCCTTTGGAGCAGCAGGCCTG
AGCAGCGACTACCCACTGGCTCAGTTCTTCACCTGGGCCCGAGCCCTGCGCTTTGCCGAC
GGCCCTGACGAGGTGCACCGGGCCACGGTGGCCAAGCTAGAGCTGAAGCACCGCATTTAG
Enzyme 53 GenBank Gene ID NM_025247.5 Link Image
Enzyme 53 GeneCard ID ACAD10 Link Image
Enzyme 53 GenAtlas ID ACAD10 Link Image
Enzyme 53 HGNC ID HGNC:21597 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 12q24.12
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Ye X, Ji C, Zhou C, Zeng L, Gu S, Ying K, Xie Y, Mao Y: Cloning and characterization of a human cDNA ACAD10 mapped to chromosome 12q24.1. Mol Biol Rep. 2004 Sep;31(3):191-5. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 8816
Enzyme 54 Name Acyl-CoA dehydrogenase family member 11
Enzyme 54 Synonyms
  1. ACAD-11
Enzyme 54 Gene Name ACAD11
Enzyme 54 Protein Sequence >Acyl-CoA dehydrogenase family member 11
MKPGATGESDLAEVLPQHKFDSKSLEAYLNQHLSGFGAEREATLTIAQYRAGKSNPTFYL
QKGFQTYVLRKKPPGSLLPKAHQIDREFKVQKALFSIGFPVPKPILYCSDTSVIGTEFYV
MEHVQGRIFRDLTIPGLSPAERSAIYVATVETLAQLRSLNIQSLQLEGYGIGAGYCKRQV
STWTKQYQAAAHQDIPAMQQLSEWLMKNLPDNDNEENLIHGDFRLDNIVFHPKECRVIAV
LDWELSTIGHPLSDLAHFSLFYFWPRTVPMINQGSYSENSGIPSMEELISIYCRCRGINS
ILPNWNFFLALSYFKMAGIAQGVYSRYLLGNNSSEDSFLFANIVQPLAETGLQLSKRTFS
TVLPQIDTTGQLFVQTRKGQEVLIKVKHFMKQHILPAEKEVTEFYVQNENSVDKWGKPLV
IDKLKEMAKVEGLWNLFLPAVSGLSHVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLH
LYGSEEQKKQWLEPLLQGNITSCFCMTEPDVASSDATNIECSIQRDEDSYVINGKKWWSS
GAGNPKCKIAIVLGRTQNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNFHGGHFE
IHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAF
KKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAMIKVAAPRAVSK
IVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELRDQAKRLTAKI
Enzyme 54 Number of Residues 780
Enzyme 54 Molecular Weight 87282.7
Enzyme 54 Theoretical pI 8.21
Enzyme 54 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 54 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 54 Specific Function May function as oxidoreductase (Probable)
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 38490142 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID Q709F0 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name ACD11_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >2343 bp
ATGAAGCCAGGTGCTACTGGCGAGTCCGATTTGGCCGAAGTGCTGCCCCAGCACAAGTTC
GACAGCAAGTCCCTGGAGGCCTACCTAAACCAGCACTTGTCTGGCTTTGGGGCCGAACGT
GAGGCTACGCTGACCATTGCCCAGTACAGAGCAGGAAAGTCCAATCCAACCTTTTATCTC
CAGAAGGGCTTTCAAACATATGTGCTCAGGAAAAAACCACCAGGTTCACTTCTTCCTAAA
GCACATCAGATTGATAGAGAATTTAAAGTCCAGAAAGCCTTGTTTTCAATTGGATTCCCC
GTTCCCAAGCCTATACTGTACTGCAGTGATACTTCTGTCATTGGAACAGAATTTTACGTA
ATGGAACATGTGCAGGGTCGAATCTTCCGTGATTTAACAATTCCTGGACTTAGCCCAGCA
GAACGTTCAGCCATATATGTGGCCACGGTAGAAACATTGGCTCAGTTACATTCCTTGAAT
ATACAGTCACTGCAGCTGGAAGGATATGGTATAGGTGCTGGGTACTGCAAAAGACAGGTA
TCAACCTGGACAAAGCAATATCAAGCTGCAGCTCATCAGGACATCCCTGCCATGCAACAG
CTATCGGAGTGGCTAATGAAGAACTTGCCCGATAATGACAATGAAGAGAATTTGATTCAT
GGAGATTTCAGACTAGATAACATAGTTTTCCACCCTAAAGAGTGTCGAGTTATAGCAGTG
CTGGATTGGGAGCTGTCAACCATTGGTCATCCTTTGTCAGACTTAGCTCATTTTTCCCTG
TTCTACTTTTGGCCAAGGACAGTTCCAATGATAAATCAAGGTTCTTATAGTGAAAACTCA
GGGATACCATCAATGGAAGAACTGATTTCAATATATTGCCGCTGCAGGGGAATTAATTCT
ATTCTTCCTAACTGGAATTTCTTTCTTGCCCTTTCATATTTTAAGATGGCTGGAATAGCA
CAGGGAGTATATAGCAGATATCTTCTGGGAAATAATTCATCTGAGGATAGCTTTTTATTT
GCCAATATTGTGCAACCTCTGGCAGAAACTGGACTACAACTCTCCAAACGAACTTTCAGT
ACTGTACTACCACAGATTGATACTACTGGACAGTTGTTTGTACAGACTCGGAAAGGTCAG
GAAGTTCTTATTAAGGTGAAGCATTTCATGAAACAACACATTCTTCCAGCTGAAAAGGAG
GTAACTGAGTTCTATGTTCAAAATGAAAATTCAGTGGACAAGTGGGGAAAACCTTTAGTG
ATTGATAAACTCAAGGAAATGGCCAAAGTCGAGGGTCTCTGGAACTTGTTTTTGCCAGCT
GTCAGCGGACTCAGCCACGTGGACTATGCCTTGATTGCTGAAGAAACAGGAAAATGCTTT
TTTGCTCCAGATGTCTTTAACTGCCAAGCACCAGACACAGGGAATATGGAGGTTCTGCAC
CTGTATGGAAGTGAGGAACAGAAGAAACAGTGGCTTGAGCCTCTTCTTCAAGGGAACATT
ACCTCTTGCTTCTGTATGACAGAACCTGATGTAGCTTCAAGTGATGCCACGAATATTGAA
TGCAGCATCCAACGAGATGAAGATAGCTATGTAATTAACGGCAAAAAATGGTGGAGCAGT
GGAGCTGGGAATCCCAAGTGCAAAGTTGCAATTGTTTTGGGAAGAACTCAAAATACTTCT
CTCTCCAGACACAAACAGCACAGCATGATTCTTGTTCCCATGAACACACCTGGAGTAAAA
ATAATAAGGCCTTTGTCAGTTTTTGGCTACACAGATAATTTTCATGGAGGACATTTTGAG
ATCCATTTTAATCAAGTGCGAGTTCCTGCCACAAATCTAATACTAGGTGAAGGTAGGGGA
TTTGAAATTTCCCAAGGCCGCCTTGGACCTGGCAGAATCCACCACTGTATGAGAACAGTA
GGTTTGGCGGAACGCGCTTTGCAGATCATGTGTGAGCGGGCAACACAAAGGATAGCTTTC
AAGAAGAAGTTGTATGCACATGAGGTTGTGGCTCACTGGATTGCTGAAAGCCGCATTGCC
ATTGAGAAGATCCGCTTGTTGACTCTGAAAGCTGCTCACAGCATGGACACTCTGGGCAGT
GCTGGCGCTAAGAAAGAGATTGCAATGATCAAAGTGGCTGCCCCACGGGCTGTCAGCAAA
ATCGTTGACTGGGCCATCCAGGTGTGCGGAGGTGCTGGTGTTTCCCAGGATTACCCTCTG
GCTAACATGTATGCTATAACCCGAGTTTTGCGTTTAGCAGATGGACCTGACGAAGTTCAT
CTTTCAGCAATCGCAACAATGGAGCTGCGGGACCAAGCCAAAAGACTGACAGCCAAGATA
TAA
Enzyme 54 GenBank Gene ID AJ608287 Link Image
Enzyme 54 GeneCard ID ACAD11 Link Image
Enzyme 54 GenAtlas ID ACAD11 Link Image
Enzyme 54 HGNC ID HGNC:30211 Link Image
Enzyme 54 Chromosome Location 3
Enzyme 54 Locus 3q22.1
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 8871
Enzyme 55 Name Glycerol-3-phosphate acyltransferase 4
Enzyme 55 Synonyms
  1. GPAT4
  2. 1-acylglycerol-3-phosphate O-acyltransferase 6
  3. 1-AGP acyltransferase 6
  4. 1-AGPAT 6
  5. Acyl-CoA:glycerol-3-phosphate acyltransferase 4
  6. Lysophosphatidic acid acyltransferase zeta
  7. LPAAT-zeta
Enzyme 55 Gene Name AGPAT6
Enzyme 55 Protein Sequence >Glycerol-3-phosphate acyltransferase 4
MFLLLPFDSLIVNLLGISLTVLFTLLLVFIIVPAIFGVSFGIRKLYMKSLLKIFAWATLR
MERGAKEKNHQLYKPYTNGIIAKDPTSLEEEIKEIRRSGSSKALDNTPEFELSDIFYFCR
KGMETIMDDEVTKRFSAEELESWNLLSRTNYNFQYISLRLTVLWGLGVLIRYCFLLPLRI
ALAFTGISLLVVGTTVVGYLPNGRFKEFMSKHVHLMCYRICVRALTAIITYHDRENRPRN
GGICVANHTSPIDVIILASDGYYAMVGQVHGGLMGVIQRAMVKACPHVWFERSEVKDRHL
VAKRLTEHVQDKSKLPILIFPEGTCINNTSVMMFKKGSFEIGATVYPVAIKYDPQFGDAF
WNSSKYGMVTYLLRMMTSWAIVCSVWYLPPMTREADEDAVQFANRVKSAIARQGGLVDLL
WDGGLKREKVKDTFKEEQQKLYSKMIVGNHKDRSRS
Enzyme 55 Number of Residues 456
Enzyme 55 Molecular Weight 52070.6
Enzyme 55 Theoretical pI 9.56
Enzyme 55 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 55 General Function Involved in acyltransferase activity
Enzyme 55 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long- chain fatty acyl-CoAs
Enzyme 55 Pathways
Enzyme 55 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • 1-37
Enzyme 55 Transmembrane Regions
  • 156-176 180-200
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 30142570 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q86UL3 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name GPAT4_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1371 bp
ATGTTCCTGTTGCTGCCTTTTGATAGCCTGATTGTCAACCTTCTGGGCATCTCCCTGACT
GTCCTCTTCACCCTCCTTCTCGTTTTCATCATAGTGCCAGCCATTTTTGGAGTCTCCTTT
GGTATCCGCAAACTCTACATGAAAAGTCTGTTAAAAATCTTTGCGTGGGCTACCTTGAGA
ATGGAGCGAGGAGCCAAGGAGAAGAACCACCAGCTTTACAAGCCCTACACCAACGGAATC
ATTGCAAAGGATCCCACTTCACTAGAAGAAGAGATCAAAGAGATTCGTCGAAGTGGTAGT
AGTAAGGCTCTGGACAACACTCCAGAGTTCGAGCTCTCTGACATTTTCTACTTTTGCCGG
AAAGGAATGGAGACCATTATGGATGATGAGGTGACAAAGAGATTCTCAGCAGAAGAACTG
GAGTCCTGGAACCTGCTGAGCAGAACCAATTATAACTTCCAGTACATCAGCCTTCGGCTC
ACGGTCCTGTGGGGGTTAGGAGTGCTGATTCGGTACTGCTTTCTGCTGCCGCTCAGGATA
GCACTGGCTTTCACAGGGATTAGCCTTCTGGTGGTGGGCACAACTGTGGTGGGATACTTG
CCAAATGGGAGGTTTAAGGAGTTCATGAGTAAACATGTTCACTTAATGTGTTACCGGATC
TGCGTGCGAGCGCTGACAGCCATCATCACCTACCATGACAGGGAAAACAGACCAAGAAAT
GGTGGCATCTGTGTGGCCAATCATACCTCACCGATCGATGTGATCATCTTGGCCAGCGAT
GGCTATTATGCCATGGTGGGTCAAGTGCACGGGGGACTCATGGGTGTGATTCAGAGAGCC
ATGGTGAAGGCCTGCCCACACGTCTGGTTTGAGCGCTCGGAAGTGAAGGATCGCCACCTG
GTGGCTAAGAGACTGACTGAACATGTGCAAGATAAAAGCAAGCTGCCTATCCTCATCTTC
CCAGAAGGAACCTGCATCAATAATACATCGGTGATGATGTTCAAAAAGGGAAGTTTTGAA
ATTGGAGCCACAGTTTACCCTGTTGCTATCAAGTATGACCCTCAATTTGGCGATGCCTTC
TGGAACAGCAGCAAATACGGGATGGTGACGTACCTGCTGCGAATGATGACCAGCTGGGCC
ATTGTCTGCAGCGTGTGGTACCTGCCTCCCATGACTAGAGAGGCAGATGAAGATGCTGTC
CAGTTTGCGAATAGGGTGAAATCTGCCATTGCCAGGCAGGGAGGACTTGTGGACCTGCTG
TGGGATGGGGGCCTGAAGAGGGAGAAGGTGAAGGACACGTTCAAGGAGGAGCAGCAGAAG
CTGTACAGCAAGATGATCGTGGGGAACCACAAGGACAGGAGCCGCTCCTGA
Enzyme 55 GenBank Gene ID AF406612 Link Image
Enzyme 55 GeneCard ID AGPAT6 Link Image
Enzyme 55 GenAtlas ID AGPAT6 Link Image
Enzyme 55 HGNC ID HGNC:20880 Link Image
Enzyme 55 Chromosome Location 8
Enzyme 55 Locus 8p11.21
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Li D, Yu L, Wu H, Shan Y, Guo J, Dang Y, Wei Y, Zhao S: Cloning and identification of the human LPAAT-zeta gene, a novel member of the lysophosphatidic acid acyltransferase family. J Hum Genet. 2003;48(8):438-42. Epub 2003 Aug 19. [PubMed Link Image]
  2. Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G: AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase. J Biol Chem. 2008 Apr 11;283(15):10048-57. Epub 2008 Jan 31. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 9777
Enzyme 56 Name Acyl-coenzyme A synthetase ACSM1, mitochondrial
Enzyme 56 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 1
  2. Butyrate--CoA ligase 1
  3. Butyryl-coenzyme A synthetase 1
  4. Lipoate-activating enzyme
  5. Middle-chain acyl-CoA synthetase 1
Enzyme 56 Gene Name ACSM1
Enzyme 56 Protein Sequence >Acyl-coenzyme A synthetase ACSM1, mitochondrial
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM
Enzyme 56 Number of Residues 577
Enzyme 56 Molecular Weight 65272.7
Enzyme 56 Theoretical pI 8.40
Enzyme 56 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 56 General Function Involved in catalytic activity
Enzyme 56 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 56 Pathways
Enzyme 56 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 15487302 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID Q08AH1 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name ACSM1_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >1734 bp
ATGCAGTGGCTAATGAGGTTCCGGACCCTCTGGGGCATCCACAAATCCTTCCACAACATC
CACCCTGCCCCTTCACAGCTGCGCTGCCGGTCTTTATCAGAATTTGGAGCCCCAAGATGG
AATGACTATGAAGTACCGGAGGAATTTAACTTTGCAAGTTATGTACTGGACTACTGGGCT
CAAAAGGAGAAGGAGGGCAAGAGAGGTCCAAATCCAGCTTTTTGGTGGGTGAATGGCCAA
GGGGATGAAGTAAAGTGGAGCTTCAGAGAGATGGGAGACCTAACCCGCCGTGTAGCCAAC
GTCTTCACACAGACCTGTGGCCTACAACAGGGAGACCATCTGGCCTTGATGCTGCCTCGA
GTTCCTGAGTGGTGGCTGGTGGCTGTGGGCTGCATGCGAACAGGGATCATCTTCATTCCT
GCGACCATCCTGTTGAAGGCCAAAGACATTCTCTATCGACTACAGTTGTCTAAAGCCAAG
GGCATTGTGACCATAGATGCCCTTGCCTCAGAGGTGGACTCCATAGCTTCTCAGTGCCCC
TCTCTGAAAACCAAGCTCCTGGTGTCTGATCACAGCCGTGAAGGGTGGCTGGACTTCCGA
TCGCTGGTTAAATCAGCATCCCCAGAACACACCTGTGTTAAGTCAAAGACCTTGGACCCA
ATGGTCATCTTCTTCACCAGTGGGACCACAGGCTTCCCCAAGATGGCAAAACACTCCCAT
GGGTTGGCCTTACAACCCTCCTTCCCAGGAAGTAGGAAATTACGGAGCCTGAAGACATCT
GATGTCTCCTGGTGCCTGTCGGACTCAGGATGGATTGTGGCTACCATTTGGACCCTGGTA
GAACCATGGACAGCGGGTTGTACAGTCTTTATCCACCATCTGCCACAGTTTGACACCAAG
GTCATCATACAGACATTGTTGAAATACCCCATTAACCACTTTTGGGGGGTATCATCTATA
TATCGAATGATTCTGCAGCAGGATTTCACCAGCATCAGGTTCCCTGCCCTGGAGCACTGC
TATACTGGCGGGGAGGTCGTGTTGCCCAAGGATCAGGAGGAGTGGAAAAGACGGACGGGC
CTTCTGCTCTACGAGAACTATGGGCAGTCGGAAACGGGACTAATTTGTGCCACCTACTGG
GGAATGAAGATCAAGCCGGGTTTCATGGGGAAGGCCACTCCACCCTATGACGTCCAGGTC
ATTGATGACAAGGGCAGCATCCTGCCACCTAACACAGAAGGAAACATTGGCATCAGAATC
AAACCTGTCAGGCCTGTGAGCCTCTTCATGTGCTATGAGGGTGACCCAGAGAAGACAGCT
AAAGTGGAATGTGGGGACTTCTACAACACTGGGGACAGAGGAAAGATGGATGAAGAGGGC
TACATTTGTTTCCTGGGGAGGAGTGATGACATCATTAATGCCTCTGGGTATCGCATCGGG
CCTGCAGAGGTTGAAAGCGCTTTGGTGGAGCACCCAGCGGTGGCGGAGTCAGCCGTGGTG
GGCAGCCCAGACCCGATTCGAGGGGAGGTGGTGAAGGCCTTTATTGTCCTGACCCCACAG
TTCCTGTCCCATGACAAGGATCAGCTGACCAAGGAACTGCAGCAGCATGTCAAGTCAGTG
ACAGCCCCATACAAGTACCCAAGGAACGTGGAGTTTGTCTCAGAGCTGCCAAAAACCATC
ACTGGCAAGATTGAACGGAAGGAACTTCGGAAAAAGGAGACTGGTCAGATGTAA
Enzyme 56 GenBank Gene ID AB059429 Link Image
Enzyme 56 GeneCard ID ACSM1 Link Image
Enzyme 56 GenAtlas ID ACSM1 Link Image
Enzyme 56 HGNC ID HGNC:18049 Link Image
Enzyme 56 Chromosome Location 1
Enzyme 56 Locus 16p12.3
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 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]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 10076
Enzyme 57 Name Diacylglycerol O-acyltransferase 2
Enzyme 57 Synonyms
  1. Diglyceride acyltransferase 2
Enzyme 57 Gene Name DGAT2
Enzyme 57 Protein Sequence >Diacylglycerol O-acyltransferase 2
MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLN
RSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKG
GRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATE
VSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGG
AAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQ
KKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHT
MYMEALVKLFDKHKTKFGLPETEVLEVN
Enzyme 57 Number of Residues 388
Enzyme 57 Molecular Weight 43830.5
Enzyme 57 Theoretical pI 9.80
Enzyme 57 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 57 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 57 Specific Function Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides. Probably plays a central role in cytosolic lipid accumulation
Enzyme 57 Pathways
Enzyme 57 Reactions
  • acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol [RN:R02251]
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • 76-96 98-117
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 22506631 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID Q96PD7 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name DGAT2_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1167 bp
ATGAAGACCCTCATAGCCGCCTACTCCGGGGTCCTGCGCGGCGAGCGTCAGGCCGAGGCT
GACCGGAGCCAGCGCTCTCACGGAGGACCTGCGCTGTCGCGCGAGGGGTCTGGGAGATGG
GGCACTGGATCCAGCATCCTCTCCGCCCTCCAGGACCTCTTCTCTGTCACCTGGCTCAAT
AGGTCCAAGGTGGAAAAGCAGCTACAGGTCATCTCAGTGCTCCAGTGGGTCCTGTCCTTC
CTTGTACTGGGAGTGGCCTGCAGTGCCATCCTCATGTACATATTCTGCACTGATTGCTGG
CTCATCGCTGTGCTCTACTTCACTTGGCTGGTGTTTGACTGGAACACACCCAAGAAAGGT
GGCAGGAGGTCACAGTGGGTCCGAAACTGGGCTGTGTGGCGCTACTTTCGAGACTACTTT
CCCATCCAGCTGGTGAAGACACACAACCTGCTGACCACCAGGAACTATATCTTTGGATAC
CACCCCCATGGTATCATGGGCCTGGGTGCCTTCTGCAACTTCAGCACAGAGGCCACAGAA
GTGAGCAAGAAGTTCCCAGGCATACGGCCTTACCTGGCTACACTGGCAGGCAACTTCCGA
ATGCCTGTGTTGAGGGAGTACCTGATGTCTGGAGGTATCTGCCCTGTCAGCCGGGACACC
ATAGACTATTTGCTTTCAAAGAATGGGAGTGGCAATGCTATCATCATCGTGGTCGGGGGT
GCGGCTGAGTCTCTGAGCTCCATGCCTGGCAAGAATGCAGTCACCCTGCGGAACCGCAAG
GGCTTTGTGAAACTGGCCCTGCGTCATGGAGCTGACCTGGTTCCCATCTACTCCTTTGGA
GAGAATGAAGTGTACAAGCAGGTGATCTTCGAGGAGGGCTCCTGGGGCCGATGGGTCCAG
AAGAAGTTCCAGAAATACATTGGTTTCGCCCCATGCATCTTCCATGGTCGAGGCCTCTTC
TCCTCCGACACCTGGGGGCTGGTGCCCTACTCCAAGCCCATCACCACTGTTGTGGGAGAG
CCCATCACCATCCCCAAGCTGGAGCACCCAACCCAGCAAGACATCGACCTGTACCACACC
ATGTACATGGAGGCCCTGGTGAAGCTCTTCGACAAGCACAAGACCAAGTTCGGCCTCCCG
GAGACTGAGGTCCTGGAGGTGAACTGA
Enzyme 57 GenBank Gene ID AB048286 Link Image
Enzyme 57 GeneCard ID DGAT2 Link Image
Enzyme 57 GenAtlas ID DGAT2 Link Image
Enzyme 57 HGNC ID HGNC:16940 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 11q13.5
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [PubMed Link Image]
  2. Wakimoto K, Chiba H, Michibata H, Seishima M, Kawasaki S, Okubo K, Mitsui H, Torii H, Imai Y: A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice. Biochem Biophys Res Commun. 2003 Oct 17;310(2):296-302. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 10119
Enzyme 58 Name 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
Enzyme 58 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 4
  2. 1-AGP acyltransferase 4
  3. 1-AGPAT 4
  4. Lysophosphatidic acid acyltransferase delta
  5. LPAAT-delta
Enzyme 58 Gene Name AGPAT4
Enzyme 58 Protein Sequence >1-acyl-sn-glycerol-3-phosphate acyltransferase delta
MDLAGLLKSQFLCHLVFCYVFIASGLIINTIQLFTLLLWPINKQLFRKINCRLSYCISSQ
LVMLLEWWSGTECTIFTDPRAYLKYGKENAIVVLNHKFEIDFLCGWSLSERFGLLGGSKV
LAKKELAYVPIIGWMWYFTEMVFCSRKWEQDRKTVATSLQHLRDYPEKYFFLIHCEGTRF
TEKKHEISMQVARAKGLPRLKHHLLPRTKGFAITVRSLRNVVSAVYDCTLNFRNNENPTL
LGVLNGKKYHADLYVRRIPLEDIPEDDDECSAWLHKLYQEKDAFQEEYYRTGTFPETPMV
PPRRPWTLVNWLFWASLVLYPFFQFLVSMIRSGSSLTLASFILVFFVASVGVRWMIGVTE
IDKGSAYGNSDSKQKLND
Enzyme 58 Number of Residues 378
Enzyme 58 Molecular Weight 44020.9
Enzyme 58 Theoretical pI 8.90
Enzyme 58 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 58 General Function Involved in acyltransferase activity
Enzyme 58 Specific Function Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone
Enzyme 58 Pathways
Enzyme 58 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • 11-31 125-145 307-327 338-358
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 8886005 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID Q9NRZ5 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name PLCD_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1137 bp
ATGGACCTCGCGGGACTGCTGAAGTCTCAGTTCCTGTGCCACCTGGTCTTCTGCTACGTC
TTTATTGCCTCAGGGCTAATCATCAACACCATTCAGCTCTTCACTCTCCTCCTCTGGCCC
ATTAACAAGCAGCTCTTCCGGAAGATCAACTGCAGACTGTCCTATTGCATCTCAAGCCAG
CTGGTGATGCTGCTGGAGTGGTGGTCGGGCACGGAATGCACCATCTTCACGGACCCGCGC
GCCTACCTCAAGTATGGGAAGGAAAATGCCATCGTGGTTCTCAACCACAAGTTTGAAATT
GACTTTCTGTGTGGCTGGAGCCTGTCCGAACGCTTTGGGCTGTTAGGGGGCTCCAAGGTC
CTGGCCAAGAAAGAGCTGGCCTATGTCCCAATTATCGGCTGGATGTGGTACTTCACCGAG
ATGGTCTTCTGTTCGCGCAAGTGGGAGCAGGATCGCAAGACGGTTGCCACCAGTTTGCAG
CACCTCCGGGACTACCCCGAGAAGTATTTTTTCCTGATTCACTGTGAGGGCACACGGTTC
ACGGAGAAGAAGCATGAGATCAGCATGCAGGTGGCCCGGGCCAAGGGGCTGCCTCGCCTC
AAGCATCACCTGTTGCCACGAACCAAGGGCTTCGCCATCACCGTGAGGAGCTTGAGAAAT
GTAGTTTCAGCTGTATATGACTGTACACTCAATTTCAGAAATAATGAAAATCCAACACTG
CTGGGAGTCCTAAACGGAAAGAAATACCATGCAGATTTGTATGTTAGGAGGATCCCACTG
GAAGACATCCCTGAAGACGATGACGAGTGCTCGGCCTGGCTGCACAAGCTCTACCAGGAG
AAGGATGCCTTTCAGGAGGAGTACTACAGGACGGGCACCTTCCCAGAGACGCCCATGGTG
CCCCCCCGGCGGCCCTGGACCCTCGTGAACTGGCTGTTTTGGGCCTCGCTGGTGCTCTAC
CCTTTCTTCCAGTTCCTGGTCAGCATGATCAGGAGCGGGTCTTCCCTGACGCTGGCCAGC
TTCATCCTCGTCTTCTTTGTGGCCTCCGTGGGAGTTCGATGGATGATTGGTGTGACGGAA
ATTGACAAGGGCTCTGCCTACGGCAACTCTGACAGCAAGCAGAAACTGAATGACTGA
Enzyme 58 GenBank Gene ID AF156776 Link Image
Enzyme 58 GeneCard ID AGPAT4 Link Image
Enzyme 58 GenAtlas ID AGPAT4 Link Image
Enzyme 58 HGNC ID HGNC:20885 Link Image
Enzyme 58 Chromosome Location 6
Enzyme 58 Locus 6q26
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Leung DW: The structure and functions of human lysophosphatidic acid acyltransferases. Front Biosci. 2001 Aug 1;6:D944-53. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 10239
Enzyme 59 Name 2-acylglycerol O-acyltransferase 1
Enzyme 59 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 1
  2. MGAT1
  3. Diacylglycerol O-acyltransferase candidate 2
  4. hDC2
  5. Diacylglycerol acyltransferase 2-like protein 1
  6. Monoacylglycerol O-acyltransferase 1
Enzyme 59 Gene Name MOGAT1
Enzyme 59 Protein Sequence >2-acylglycerol O-acyltransferase 1
MKVEFAPLNIQLARRLQTVAVLQWVLKYLLLGPMSIGITVMLIIHNYLFLYIPYLMWLYF
DWHTPERGGRRSSWIKNWTLWKHFKDYFPIHLIKTQDLDPSHNYIFGFHPHGIMAVGAFG
NFSVNYSDFKDLFPGFTSYLHVLPLWFWCPVFREYVMSVGLVSVSKKSVSYMVSKEGGGN
ISVIVLGGAKESLDAHPGKFTLFIRQRKGFVKIALTHGASLVPVVSFGENELFKQTDNPE
GSWIRTVQNKLQKIMGFALPLFHARGVFQYNFGLMTYRKAIHTVVGRPIPVRQTLNPTQE
QIEELHQTYMEELRKLFEEHKGKYGIPEHETLVLK
Enzyme 59 Number of Residues 335
Enzyme 59 Molecular Weight 38812.2
Enzyme 59 Theoretical pI 9.96
Enzyme 59 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 59 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 59 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine
Enzyme 59 Pathways
Enzyme 59 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • 18-38 40-60 132-152
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 148746191 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q96PD6 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name MOGT1_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >1008 bp
ATGAAGGTAGAGTTTGCACCGCTCAACATCCAGCTGGCGCGGCGGCTGCAGACGGTGGCC
GTGCTGCAGTGGGTCCTGAAATACCTGCTGCTCGGGCCGATGTCCATTGGAATCACTGTG
ATGCTGATCATACACAACTATTTGTTCCTTTACATCCCTTATTTGATGTGGCTTTACTTT
GACTGGCATACCCCAGAGCGAGGAGGCAGGAGATCCAGCTGGATCAAAAATTGGACTCTT
TGGAAACACTTTAAGGACTATTTTCCAATTCATCTTATCAAAACTCAAGATTTGGATCCA
AGTCACAACTATATATTTGGGTTTCACCCCCATGGAATAATGGCAGTTGGAGCCTTTGGG
AATTTTTCTGTAAATTATTCTGACTTCAAGGACCTGTTTCCTGGCTTTACTTCATATCTT
CACGTGCTGCCACTTTGGTTCTGGTGTCCTGTCTTTCGAGAATATGTGATGAGTGTTGGG
CTGGTTTCAGTTTCCAAGAAAAGTGTGTCCTACATGGTAAGCAAGGAGGGAGGTGGAAAC
ATCTCTGTCATTGTCCTTGGGGGTGCAAAAGAATCACTGGATGCTCATCCTGGAAAGTTC
ACTCTGTTCATCCGCCAGCGGAAAGGATTTGTTAAAATTGCTTTGACCCATGGCGCCTCT
CTGGTCCCAGTGGTTTCTTTTGGTGAAAATGAACTGTTTAAACAAACTGACAACCCTGAA
GGATCATGGATTAGAACTGTTCAGAATAAACTGCAGAAGATCATGGGGTTTGCTTTGCCC
CTGTTTCATGCCAGGGGAGTTTTTCAGTACAATTTTGGCCTAATGACCTATAGGAAAGCC
ATCCACACTGTTGTTGGCCGCCCGATCCCTGTTCGTCAGACTCTGAACCCGACCCAGGAG
CAGATTGAGGAGTTACATCAGACCTATATGGAGGAACTTAGGAAATTGTTTGAGGAACAC
AAAGGAAAGTATGGCATTCCAGAGCACGAGACTCTTGTTTTAAAATGA
Enzyme 59 GenBank Gene ID NM_058165.2 Link Image
Enzyme 59 GeneCard ID MOGAT1 Link Image
Enzyme 59 GenAtlas ID MOGAT1 Link Image
Enzyme 59 HGNC ID HGNC:18210 Link Image
Enzyme 59 Chromosome Location 2
Enzyme 59 Locus 2q36.1
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Cases S, Stone SJ, Zhou P, Yen E, Tow B, Lardizabal KD, Voelker T, Farese RV Jr: Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem. 2001 Oct 19;276(42):38870-6. Epub 2001 Jul 31. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 10872
Enzyme 60 Name Isobutyryl-CoA dehydrogenase, mitochondrial
Enzyme 60 Synonyms
  1. Activator-recruited cofactor 42 kDa component
  2. ARC42
  3. Acyl-CoA dehydrogenase family member 8
  4. ACAD-8
Enzyme 60 Gene Name ACAD8
Enzyme 60 Protein Sequence >Isobutyryl-CoA dehydrogenase, mitochondrial
MLWSGCRRFGARLGCLPGGLRVLVQTGHRSLTSCIDPSMGLNEEQKEFQKVAFDFAAREM
APNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT
AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQG
DHYILNGSKAFISGAGESDIYVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNS
QPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAAHASVILTRDHLN
VRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD
ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE
Enzyme 60 Number of Residues 415
Enzyme 60 Molecular Weight 45069.4
Enzyme 60 Theoretical pI 7.91
Enzyme 60 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 60 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 60 Specific Function Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein Not Available
Enzyme 60 UniProtKB/Swiss-Prot ID Q9UKU7 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name ACAD8_HUMAN Link Image
Enzyme 60 PDB ID 1RX0 Link Image
Enzyme 60 PDB File Show
Enzyme 60 3D Structure
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >1248 bp
ATGCTGTGGAGCGGCTGCCGGCGTTTCGGGGCGCGCCTCGGCTGCCTGCCCGGCGGTCTC
CGGGTCCTCGTCCAGACCGGCCACCGGAGCTTGACCTCCTGCATCGACCCTTCCATGGGA
CTTAATGAAGAGCAGAAAGAATTTCAAAAAGTGGCCTTTGACTTTGCTGCCCGAGAGATG
GCTCCAAATATGGCAGAGTGGGACCAGAAGGAGCTGTTCCCAGTGGATGTGATGCGGAAG
GCAGCCCAGCTAGGCTTCGGAGGGGTCTACATACAAACAGATGTGGGCGGGTCTGGGCTG
TCACGTCTTGATACCTCTGTCATTTTTGAAGCCTTGGCTACAGGCTGCACCAGCACCACA
GCCTATATAAGCATCCACAACATGTGTGCCTGGATGATTGATAGCTTCGGAAATGAGGAA
CAGAGGCACAAATTTTGCCCACCGCTCTGTACCATGGAGAAGTTTGCTTCCTACTGCCTC
ACTGAACCAGGAAGTGGGAGTGATGCTGCCTCTCTTCTGACCTCCGCTAAGAAACAGGGA
GATCATTACATCCTCAATGGCTCCAAGGCCTTCATCAGTGGTGCTGGTGAGTCAGACATC
TATGTGGTCATGTGCCGAACAGGAGGACCAGGCCCCAAGGGCATCTCATGCATAGTTGTT
GAGAAGGGGACCCCTGGCCTCAGCTTTGGCAAGAAGGAGAAAAAGGTGGGGTGGAACTCC
CAGCCAACACGAGCTGTGATCTTCGAAGACTGTGCTGTCCCTGTGGCCAACAGAATTGGG
AGCGAGGGGCAGGGCTTCCTCATTGCCGTGAGAGGACTGAACGGAGGGAGGATCAATATT
GCTTCCTGCTCCCTGGGGGCTGCCCACGCCTCTGTCATCCTCACCCGAGACCACCTCAAT
GTCCGGAAGCAGTTTGGAGAGCCTCTGGCCAGTAACCAGTACTTGCAATTCACACTGGCT
GATATGGCAACAAGGCTGGTGGCCGCGCGGCTGATGGTCCGCAATGCAGCAGTGGCTCTG
CAGGAGGAGAGGAAGGATGCAGTGGCCTTGTGCTCCATGGCCAAGCTCTTTGCTACAGAT
GAATGCTTTGCCATCTGCAACCAGGCCTTGCAGATGCACGGGGGCTACGGCTACCTGAAG
GATTACGCTGTTCAGCAGTACGTGCGGGACTCCAGGGTCCACCAGATTCTAGAAGGTAGC
AATGAAGTGATGAGGATACTGATCTCTAGAAGCCTGCTTCAGGAGTAG
Enzyme 60 GenBank Gene ID AF126245 Link Image
Enzyme 60 GeneCard ID ACAD8 Link Image
Enzyme 60 GenAtlas ID ACAD8 Link Image
Enzyme 60 HGNC ID HGNC:87 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 11q25
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Telford EA, Moynihan LM, Markham AF, Lench NJ: Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family. Biochim Biophys Acta. 1999 Sep 3;1446(3):371-6. [PubMed Link Image]
  2. Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Naar AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R: Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature. 1999 Apr 29;398(6730):828-32. [PubMed Link Image]
  6. Battaile KP, Nguyen TV, Vockley J, Kim JJ: Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases. J Biol Chem. 2004 Apr 16;279(16):16526-34. Epub 2004 Jan 28. [PubMed Link Image]
  7. Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J: Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. Mol Genet Metab. 2002 Sep-Oct;77(1-2):68-79. [PubMed Link Image]
  8. Sass JO, Sander S, Zschocke J: Isobutyryl-CoA dehydrogenase deficiency: isobutyrylglycinuria and ACAD8 gene mutations in two infants. J Inherit Metab Dis. 2004;27(6):741-5. [PubMed Link Image]
  9. Pedersen CB, Bischoff C, Christensen E, Simonsen H, Lund AM, Young SP, Koeberl DD, Millington DS, Roe CR, Roe DS, Wanders RJ, Ruiter JP, Keppen LD, Stein Q, Knudsen I, Gregersen N, Andresen BS: Variations in IBD (ACAD8) in children with elevated C4-carnitine detected by tandem mass spectrometry newborn screening. Pediatr Res. 2006 Sep;60(3):315-20. Epub 2006 Jul 20. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 10874
Enzyme 61 Name Acyl-CoA dehydrogenase family member 9, mitochondrial
Enzyme 61 Synonyms
  1. ACAD-9
Enzyme 61 Gene Name ACAD9
Enzyme 61 Protein Sequence >Acyl-CoA dehydrogenase family member 9, mitochondrial
MSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVRAFAKELFLGKIKKKEVFPFPEVS
QDELNEINQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGF
SNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCL
TEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKD
KITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNIL
NSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMT
YLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTR
ILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVD
LGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINL
YGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKK
VSQQILEKRAYICAHPLDRTC
Enzyme 61 Number of Residues 621
Enzyme 61 Molecular Weight 68759.7
Enzyme 61 Theoretical pI 8.05
Enzyme 61 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 61 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 61 Specific Function Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA then on stearoyl-CoA. Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0)
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 18028283 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q9H845 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name ACAD9_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >1866 bp
ATGAGCGGCTGCGGGCTCTTCCTGCGCACCACGGCTGCGGCTCGTGCCTGCCGGGGTCTG
GTGGTCTCTACCGCGAACCGGCGGCTACTGCGCACCAGCCCGCCTGTACGAGCTTTCGCC
AAAGAGCTTTTCCTAGGCAAAATCAAGAAGAAAGAAGTTTTCCCATTTCCAGAAGTTAGC
CAAGATGAACTTAATGAAATCAATCAGTTCTTGGGACCCGTGGAAAAATTCTTCACTGAA
GAGGTGGACTCCCGAAAAATTGACCAGGAAGGGAAAATCCCAGATGAAACTTTGGAGAAA
TTGAAGAGCCTAGGGCTTTTTGGGCTGCAAGTCCCAGAAGAATATGGTGGCCTGGGCTTC
TCCAACACCATGTACTCAAGACTAGGGGAGATCATCAGCATGGATGGGTCCATCACTGTG
ACCCTGGCAGCGCACCAGGCTATTGGCCTCAAGGGGATCATCTTGGCTGGCACTGAGGAG
CAGAAAGCCAAATACTTGCCTAAACTGGCGTCCGGGGAGCACATTGCAGCCTTCTGCCTC
ACGGAGCCAGCCAGTGGGAGCGATGCAGCCTCAATCCGGAGCAGAGCCACACTAAGTGAA
GACAAGAAGCACTACATCCTCAATGGCTCCAAGGTCTGGATTACTAATGGAGGACTGGCC
AATATTTTTACTGTGTTTGCAAAGACTGAGGTCGTTGATTCTGATGGATCAGTGAAAGAC
AAAATCACAGCATTCATAGTAGAAAGAGACTTTGGTGGAGTCACTAATGGGAAACCCGAA
GATAAATTAGGCATTCGGGGCTCCAACACTTGTGAAGTCCATTTTGAAAACACCAAGATA
CCTGTGGAAAACATCCTTGGAGAGGTCGGAGATGGGTTTAAGGTGGCCATGAACATCCTC
AACAGCGGCCGGTTCAGCATGGGCAGCGTCGTGGCTGGGCTGCTCAAGAGATTGATTGAA
ATGACTGCTGAGTACGCCTGCACAAGGAAACAGTTTAACAAGAGGCTCAGTGAATTTGGA
TTGATTCAGGAGAAATTTGCACTGATGGCTCAGAAGGCTTACGTCATGGAGAGTATGACC
TACCTCACAGCAGGGATGCTGGACCAACCTGGCTTTCCCGACTGCTCCATCGAGGCAGCC
ATGGTGAAGGTGTTCAGCTCCGAGGCCGCCTGGCAGTGTGTGAGTGAGGTGCTGCAGATC
CTCGGGGGCTTGGGCTACACAAGGGACTATCCGTACGAGCGCATATTGCGTGACACCCGC
ATCCTCCTCATCTTCGAGGGAACCAATGAGATTCTCCGGATGTACATCGCCCTGACGGGT
CTGCAGCATGCCGGCCGCATCCTGACTACCAGGATCCATGAGCTTAAACAGGCCAAAGTG
AGCACAGTCATGGATACCGTTGGCCGGAGGCTTCGGGACTCGCTGGGCCGAACTGTGGAC
CTGGGGCTGACAGGCAACCATGGAGTTGTGCACCCCAGTCTTGCGGACAGTGCCAACAAG
TTTGAGGAGAACACCTACTGCTTCGGCCGGACCGTGGAGACACTGCTGCTCCGCTTTGGC
AAGACCATCATGGAGGAGCAGCTGGTACTGAAGCGGGTGGCCAACATCCTCATCAACCTG
TATGGCATGACGGCCGTGCTGTCGCGGGCCAGCCGCTCCATCCGCATTGGGCTCCGCAAC
CACGACCACGAGGTTCTCTTGGCCAACACCTTCTGCGTGGAAGCTTACTTGCAGAATCTC
TTCAGCCTCTCTCAGCTGGACAAGTATGCTCCAGAAAACCTAGATGAGCAGATTAAGAAA
GTGTCCCAGCAGATCCTTGAGAAGCGAGCCTATATCTGTGCCCACCCTCTGGACAGGACA
TGCTGA
Enzyme 61 GenBank Gene ID AF327351 Link Image
Enzyme 61 GeneCard ID ACAD9 Link Image
Enzyme 61 GenAtlas ID ACAD9 Link Image
Enzyme 61 HGNC ID HGNC:21497 Link Image
Enzyme 61 Chromosome Location 3
Enzyme 61 Locus 3q21.3
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X: Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1033-42. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. He M, Rutledge SL, Kelly DR, Palmer CA, Murdoch G, Majumder N, Nicholls RD, Pei Z, Watkins PA, Vockley J: A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency. Am J Hum Genet. 2007 Jul;81(1):87-103. Epub 2007 Jun 4. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 12492
Enzyme 62 Name Long-chain fatty acid transport protein 4
Enzyme 62 Synonyms
  1. FATP-4
  2. Fatty acid transport protein 4
  3. Solute carrier family 27 member 4
Enzyme 62 Gene Name SLC27A4
Enzyme 62 Protein Sequence >Long-chain fatty acid transport protein 4
MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLL
KVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQA
RGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFG
SEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDK
LFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQ
CLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALG
NGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVR
VNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKK
GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE
VPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTE
LRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
Enzyme 62 Number of Residues 643
Enzyme 62 Molecular Weight 72063.6
Enzyme 62 Theoretical pI 8.58
Enzyme 62 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 62 General Function Involved in catalytic activity
Enzyme 62 Specific Function Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • 20-42 139-156
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 40807357 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q6P1M0 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name S27A4_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >1932 bp
ATGCTGCTTGGAGCCTCTCTGGTGGGGGTGCTGCTGTTCTCCAAGCTGGTGCTGAAACTG
CCCTGGACCCAGGTGGGATTCTCCCTGTTGTTCCTCTACTTGGGATCTGGCGGCTGGCGC
TTCATCCGGGTCTTCATCAAGACCATCAGGCGCGATATCTTTGGCGGCCTGGTCCTCCTG
AAGGTGAAGGCAAAGGTGCGACAGTGCCTGCAGGAGCGGCGGACAGTGCCCATTTTGTTT
GCCTCTACCGTTCGGCGCCACCCCGACAAGACGGCCCTGATCTTCGAGGGCACAGATACC
CACTGGACCTTCCGCCAGCTGGATGAGTACTCAAGCAGTGTAGCCAACTTCCTGCAGGCC
CGGGGCCTGGCCTCGGGCGATGTGGCTGCCATCTTCATGGAGAACCGCAATGAGTTCGTG
GGCCTATGGCTGGGCATGGCCAAGCTCGGTGTGGAGGCAGCCCTCATCAACACCAACCTG
CGGCGGGATGCTCTGCTCCACTGCCTCACCACCTCGCGCGCACGGGCCCTTGTCTTTGGC
AGCGAAATGGCCTCAGCCATCTGTGAGGTCCATGCCAGCCTGGACCCCTCGCTCAGCCTC
TTCTGCTCTGGCTCCTGGGAGCCCGGTGCGGTGCCTCCAAGCACAGAACACCTGGACCCT
CTGCTGAAAGATGCTCCCAAGCACCTTCCCAGTTGCCCTGACAAGGGCTTCACAGATAAA
CTGTTCTACATCTACACATCCGGCACCACAGGGCTGCCCAAGGCCGCCATCGTGGTGCAC
AGCAGGTATTACCGCATGGCTGCCCTGGTGTACTATGGATTCCGCATGCGGCCCAACGAC
ATCGTCTATGACTGCCTCCCCCTCTACCACTCAGCAGGAAACATCGTGGGAATCGGCCAG
TGCCTGCTGCATGGCATGACGGTGGTGATTCGGAAGAAGTTCTCAGCCTCCCGGTTCTGG
GACGATTGTATCAAGTACAACTGCACGATTGTGCAGTACATTGGTGAACTGTGCCGCTAC
CTCCTGAACCAGCCACCGCGGGAGGCAGAAAACCAGCACCAGGTTCGCATGGCACTAGGC
AATGGCCTCCGGCAGTCCATCTGGACCAACTTTTCCAGCCGCTTCCACATACCCCAGGTG
GCTGAGTTCTACGGGGCCACAGAGTGCAACTGTAGCCTGGGCAACTTCGACAGCCAGGTG
GGGGCCTGTGGTTTCAATAGCCGCATCCTGTCCTTCGTGTACCCCATCCGGTTGGTACGT
GTCAACGAGGACACCATGGAGCTGATCCGGGGGCCCGACGGCGTCTGCATTCCCTGCCAG
CCAGGTGAGCCGGGCCAGCTGGTGGGCCGCATCATCCAGAAAGACCCCCTGCGCCGCTTC
GATGGCTACCTCAACCAGGGCGCCAACAACAAGAAGATTGCCAAGGATGTCTTCAAGAAG
GGGGACCAGGCCTACCTTACTGGTGATGTGCTGGTGATGGACGAGCTGGGCTACCTGTAC
TTCCGAGACCGCACTGGGGACACGTTCCGCTGGAAAGGTGAGAACGTGTCCACCACCGAG
GTGGAAGGCACACTCAGCCGCCTGCTGGACATGGCTGACGTGGCCGTGTATGGTGTCGAG
GTGCCAGGAACCGAGGGCCGGGCCGGAATGGCTGCTGTGGCCAGCCCCACTGGCAACTGT
GACCTGGAGCGCTTTGCTCAGGTCTTGGAGAAGGAACTGCCCCTGTATGCGCGCCCCATC
TTCCTGCGCCTCCTGCCTGAGCTGCACAAAACAGGAACCTACAAGTTCCAGAAGACAGAG
CTACGGAAGGAGGGCTTTGACCCGGCTATTGTGAAAGACCCGCTGTTCTATCTAGATGCC
CAGAAGGGCCGCTACGTCCCGCTGGACCAAGAGGCCTACAGCCGCATCCAGGCAGGCGAG
GAGAAGCTGTGA
Enzyme 62 GenBank Gene ID NM_005094.3 Link Image
Enzyme 62 GeneCard ID SLC27A4 Link Image
Enzyme 62 GenAtlas ID SLC27A4 Link Image
Enzyme 62 HGNC ID HGNC:10998 Link Image
Enzyme 62 Chromosome Location 9
Enzyme 62 Locus 9q34.11
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Fitscher BA, Riedel HD, Young KC, Stremmel W: Tissue distribution and cDNA cloning of a human fatty acid transport protein (hsFATP4). Biochim Biophys Acta. 1998 Dec 22;1443(3):381-5. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gertow K, Bellanda M, Eriksson P, Boquist S, Hamsten A, Sunnerhagen M, Fisher RM: Genetic and structural evaluation of fatty acid transport protein-4 in relation to markers of the insulin resistance syndrome. J Clin Endocrinol Metab. 2004 Jan;89(1):392-9. [PubMed Link Image]
  6. Klar J, Schweiger M, Zimmerman R, Zechner R, Li H, Torma H, Vahlquist A, Bouadjar B, Dahl N, Fischer J: Mutations in the fatty acid transport protein 4 gene cause the ichthyosis prematurity syndrome. Am J Hum Genet. 2009 Aug;85(2):248-53. Epub 2009 Jul 23. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 12889
Enzyme 63 Name Fatty acyl-CoA reductase 1
Enzyme 63 Synonyms
  1. Male sterility domain-containing protein 2
Enzyme 63 Gene Name FAR1
Enzyme 63 Protein Sequence >Fatty acyl-CoA reductase 1
MVSIPEYYEGKNVLLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEVL
SGKLFDRLRDENPDFREKIIAINSELTQPKLALSEEDKEVIIDSTNIIFHCAATVRFNEN
LRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDS
LEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPF
PGWIDNFNGPSGLFIAAGKGILRTIRASNNALADLVPVDVVVNMSLAAAWYSGVNRPRNI
MVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAP
AFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTENVNMLMNQLNPEDKKT
FNIDVRQLHWAEYIENYCLGTKKYVLNEEMSGLPAARKHLNKLRNIRYGFNTILVILIWR
IFIARSQMARNIWYFVVSLCYKFLSYFRASSTMRY
Enzyme 63 Number of Residues 515
Enzyme 63 Molecular Weight 59356.3
Enzyme 63 Theoretical pI 9.52
Enzyme 63 GO Classification
Function
  • binding
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 63 General Function Involved in catalytic activity
Enzyme 63 Specific Function Catalyzes the reduction of saturated fatty acyl-CoA with chain length C16 or C18 to fatty alcohols
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • 466-483
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 37182687 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q8WVX9 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name FACR1_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >1548 bp
ATGGTTTCAATCCCAGAATACTATGAAGGCAAGAACGTCCTCCTCACAGGAGCTACCGGT
TTTCTAGGGAAGGTGCTTCTGGAAAAGTTGCTGAGGTCTTGTCCTAAGGTGAATTCAGTA
TATGTTTTGGTGAGGCAGAAAGCTGGACAGACACCACAAGAGCGAGTGGAAGAAGTCCTT
AGTGGCAAGCTTTTTGACAGATTGAGAGATGAAAATCCAGATTTTAGAGAGAAAATTATA
GCAATCAACAGCGAACTCACCCAACCTAAACTGGCTCTCAGTGAAGAAGATAAAGAGGTG
ATCATAGATTCTACCAATATTATATTCCACTGTGCAGCTACAGTAAGGTTTAATGAAAAT
TTAAGAGATGCTGTTCAGTTAAATGTGATTGCAACGCGACAGCTTATTCTCCTTGCACAA
CAAATGAAGAATCTGGAAGTGTTCATGCATGTATCAACAGCATATGCCTACTGTAATCGC
AAGCATATTGATGAAGTAGTCTATCCACCACCTGTGGATCCCAAGAAGCTGATTGATTCT
TTAGAGTGGATGGATGATGGCCTAGTAAATGATATCACGCCAAAATTGATAGGAGACAGA
CCTAATACATACATATACACAAAAGCATTGGCAGAATATGTTGTACAACAAGAAGGAGCA
AAACTAAATGTGGCAATTGTAAGGCCATCGATTGTTGGTGCCAGTTGGAAAGAACCTTTT
CCAGGATGGATTGATAACTTTAATGGACCAAGTGGTCTCTTTATTGCGGCAGGGAAAGGA
ATTCTTCGAACAATACGTGCCTCCAACAATGCCCTTGCAGATCTTGTTCCTGTAGATGTA
GTTGTCAACATGAGTCTTGCGGCAGCCTGGTATTCCGGAGTTAATAGACCAAGAAACATC
ATGGTGTATAATTGTACAACAGGCAGCACTAATCCTTTCCACTGGGGTGAAGTTGAGTAC
CATGTAATTTCCACTTTCAAGAGGAATCCTCTCGAACAGGCCTTCAGACGGCCCAATGTA
AATCTAACCTCCAATCATCTTTTATATCATTACTGGATTGCTGTAAGCCATAAGGCCCCA
GCATTCCTGTATGATATCTACCTCAGGATGACTGGAAGAAGCCCAAGGATGATGAAAACA
ATAACTCGTCTTCACAAAGCTATGGTGTTTCTTGAATATTTCACAAGTAATTCTTGGGTT
TGGAATACTGAGAATGTCAATATGTTAATGAATCAACTAAACCCTGAAGATAAAAAGACC
TTCAATATTGATGTACGGCAGTTACATTGGGCAGAATATATAGAGAACTACTGCTTGGGA
ACTAAGAAGTACGTATTGAATGAAGAAATGTCTGGCCTCCCTGCAGCCAGAAAACATCTG
AACAAGTTGCGGAATATACGTTATGGTTTTAATACTATCCTTGTGATCCTCATCTGGCGC
ATTTTTATTGCAAGATCACAAATGGCAAGAAATATCTGGTACTTTGTGGTTAGTCTGTGT
TACAAGTTTTTGTCATACTTCCGAGCATCCAGCACTATGAGATACTGA
Enzyme 63 GenBank Gene ID AY358784 Link Image
Enzyme 63 GeneCard ID FAR1 Link Image
Enzyme 63 GenAtlas ID FAR1 Link Image
Enzyme 63 HGNC ID HGNC:26222 Link Image
Enzyme 63 Chromosome Location 1
Enzyme 63 Locus 11p15.2
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Cheng JB, Russell DW: Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J Biol Chem. 2004 Sep 3;279(36):37789-97. Epub 2004 Jun 27. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 12890
Enzyme 64 Name Fatty acyl-CoA reductase 2
Enzyme 64 Synonyms
  1. Male sterility domain-containing protein 1
Enzyme 64 Gene Name FAR2
Enzyme 64 Protein Sequence >Fatty acyl-CoA reductase 2
MSTIAAFYGGKSILITGATGFLGKVLMEKLFRTSPDLKVIYILVRPKAGQTLQQRVFQIL
DSKLFEKVKEVCPNVHEKIRAIYADLNQNDFAISKEDMQELLSCTNIIFHCAATVRFDDT
LRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKIIDS
LEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPF
PGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKST
LVYHITSGNMNPCNWHKMGVQVLATFEKIPFERPFRRPNANFTSNSFTSQYWNAVSHRAP
AIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRV
FNFDVRQLNWLEYIENYVLGVKKYLLKEDMAGIPKAKQRLKRLRNIHYLFNTALFLIAWR
LLIARSQMARNVWFFIVSFCYKFLSYFRASSTLKV
Enzyme 64 Number of Residues 515
Enzyme 64 Molecular Weight 59437.9
Enzyme 64 Theoretical pI 9.79
Enzyme 64 GO Classification
Function
  • binding
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 64 General Function Involved in catalytic activity
Enzyme 64 Specific Function Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 but low activity can be observed with C10-C14 substrates
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • 465-484 491-510
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 7022510 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q96K12 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name FACR2_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >1548 bp
ATGTCCACAATTGCAGCTTTCTATGGCGGCAAGTCCATCCTCATCACGGGGGCCACAGGC
TTTCTGGGCAAAGTGCTAATGGAGAAGCTGTTTCGCACCAGCCCAGACCTGAAAGTCATT
TACATCCTTGTGAGGCCCAAGGCTGGCCAGACACTGCAGCAGAGGGTTTTCCAGATCCTA
GACAGTAAGCTATTTGAGAAAGTCAAAGAAGTTTGTCCAAATGTGCATGAGAAGATCAGA
GCTATTTATGCAGATCTCAATCAGAATGACTTTGCCATCAGCAAAGAGGACATGCAGGAG
CTTCTCTCCTGTACAAACATAATATTTCACTGTGCAGCCACTGTACGCTTTGACGACACT
CTCAGACATGCTGTGCAACTTAACGTCACTGCCACCCGGCAGCTCTTGCTTATGGCTAGT
CAGATGCCAAAGCTGGAAGCCTTTATACATATCTCTACTGCCTATTCAAATTGTAACCTG
AAGCACATCGATGAAGTTACCTATCCGTGCCCTGTGGAGCCAAAAAAAATCATTGATTCC
CTTGAGTGGTTAGACGATGCTATTATTGACGAGATTACACCCAAGCTGATCAGAGATTGG
CCCAATATTTATACCTACACCAAGGCCTTGGGAGAAATGGTGGTGCAGCAAGAGAGCAGG
AACCTGAACATTGCCATCATAAGGCCCTCCATTGTGGGAGCAACTTGGCAGGAGCCTTTC
CCAGGTTGGGTTGATAATATAAATGGACCTAATGGAATCATTATTGCGACTGGGAAAGGG
TTTCTTCGGGCCATAAAAGCTACTCCAATGGCTGTGGCAGACGTAATTCCAGTTGATACA
GTCGTCAATCTCATGCTAGCTGTAGGATGGTATACTGCAGTTCACAGACCTAAGTCAACA
TTAGTCTACCACATTACATCTGGTAACATGAATCCCTGCAATTGGCACAAAATGGGAGTC
CAAGTCTTGGCAACCTTTGAAAAAATCCCATTTGAGAGACCTTTCAGGAGGCCAAATGCT
AATTTTACCAGCAACAGCTTCACATCACAGTACTGGAATGCGGTCAGCCACCGGGCCCCT
GCCATTATCTATGACTGCTATCTGCGGCTCACTGGAAGGAAGCCCAGGATGACAAAGCTC
ATGAATCGGCTTTTAAGAACTGTTTCCATGTTGGAGTATTTCATCAACCGGAGTTGGGAA
TGGAGCACGTACAATACAGAAATGCTGATGTCTGAGCTGAGTCCTGAAGACCAGAGGGTA
TTCAACTTTGACGTGCGCCAGTTGAACTGGTTGGAATACATTGAAAATTATGTTTTGGGA
GTTAAAAAATACTTATTGAAAGAGGATATGGCTGGGATCCCAAAGGCAAAGCAACGCTTA
AAAAGGCTCCGAAATATTCACTACCTCTTTAATACTGCCCTCTTCCTTATCGCCTGGCGC
CTTCTCATTGCAAGATCTCAGATGGCTCGGAATGTCTGGTTCTTCATTGTAAGCTTCTGT
TATAAATTCCTCTCCTACTTTAGAGCATCCAGCACGCTCAAAGTTTAA
Enzyme 64 GenBank Gene ID AK001324 Link Image
Enzyme 64 GeneCard ID FAR2 Link Image
Enzyme 64 GenAtlas ID FAR2 Link Image
Enzyme 64 HGNC ID HGNC:25531 Link Image
Enzyme 64 Chromosome Location 1
Enzyme 64 Locus 12p11.22
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cheng JB, Russell DW: Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J Biol Chem. 2004 Sep 3;279(36):37789-97. Epub 2004 Jun 27. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 12897
Enzyme 65 Name Acyl-CoA wax alcohol acyltransferase 1
Enzyme 65 Synonyms
  1. Diacylglycerol O-acyltransferase 2-like protein 3
  2. Diacylglycerol acyltransferase 2
  3. Long-chain-alcohol O-fatty-acyltransferase 1
Enzyme 65 Gene Name AWAT1
Enzyme 65 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 1
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPE
RGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEA
TGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVG
GVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKF
QSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHA
LYMDALHKLFDQHKTHYGCSETQKLFFL
Enzyme 65 Number of Residues 328
Enzyme 65 Molecular Weight 37758.8
Enzyme 65 Theoretical pI 9.02
Enzyme 65 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 65 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 65 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20)
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • 12-32 34-53
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 123227401 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q58HT5 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name AWAT1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >987 bp
ATGGCTCATTCCAAGCAGCCTAGTCACTTCCAGAGTCTGATGCTTCTGCAGTGGCCTTTG
AGCTACCTTGCCATCTTTTGGATCTTGCAGCCATTGTTCGTCTACCTGCTGTTTACATCC
TTGTGGCCGCTACCAGTGCTTTACTTTGCCTGGTTGTTCCTGGACTGGAAGACCCCAGAG
CGAGGTGGCAGGCGTTCGGCCTGGGTAAGGAACTGGTGTGTCTGGACCCACATCAGGGAC
TATTTCCCCATTACGATCCTGAAGACAAAGGACCTATCACCTGAGCACAACTACCTCATG
GGGGTTCACCCCCATGGCCTCCTGACCTTTGGCGCCTTCTGCAACTTCTGCACTGAGGCC
ACAGGCTTCTCGAAGACCTTCCCAGGCATCACTCCTCACTTGGCCACGCTGTCCTGGTTC
TTCAAGATCCCCTTTGTTAGGGAGTACCTCATGGCCAAAGGTGTGTGCTCTGTGAGCCAG
CCAGCCATCAACTATCTGCTGAGCCATGGCACTGGCAACCTCGTGGGCATTGTAGTGGGA
GGTGTGGGTGAGGCCCTGCAAAGTGTGCCCAACACCACCACCCTCATCCTCCAGAAGCGC
AAGGGGTTCGTGCGCACAGCCCTCCAGCATGGGGCTCATCTGGTCCCCACCTTCACTTTT
GGGGAAACTGAGGTGTATGATCAGGTGCTGTTCCATAAGGATAGCAGGATGTACAAGTTC
CAGAGCTGCTTCCGCCGTATCTTTGGTTTCTACTGTTGTGTCTTCTATGGACAAAGCTTC
TGTCAAGGCTCCACTGGGCTCCTGCCATACTCCAGGCCTATTGTCACTGTGGTTGGGGAG
CCTCTGCCACTGCCCCAAATTGAAAAGCCAAGCCAGGAGATGGTGGACAAATACCATGCA
CTTTATATGGATGCTCTGCACAAACTGTTCGACCAGCATAAGACCCACTATGGCTGCTCA
GAGACCCAAAAGCTGTTTTTCCTGTGA
Enzyme 65 GenBank Gene ID AL357752 Link Image
Enzyme 65 GeneCard ID AWAT1 Link Image
Enzyme 65 GenAtlas ID AWAT1 Link Image
Enzyme 65 HGNC ID HGNC:23252 Link Image
Enzyme 65 Chromosome Location Not Available
Enzyme 65 Locus Not Available
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 12898
Enzyme 66 Name Acyl-CoA wax alcohol acyltransferase 2
Enzyme 66 Synonyms
  1. Diacylglycerol O-acyltransferase 2-like protein 4
  2. Diacylglycerol O-acyltransferase candidate 4
  3. hDC4
  4. Long-chain-alcohol O-fatty-acyltransferase 2
  5. Multifunctional O-acyltransferase
  6. Wax synthase
  7. hWS
Enzyme 66 Gene Name AWAT2
Enzyme 66 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 2
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII
Enzyme 66 Number of Residues 333
Enzyme 66 Molecular Weight 38093.2
Enzyme 66 Theoretical pI 9.69
Enzyme 66 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 66 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 66 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • 15-35 38-58 130-150
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 49854214 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID Q6E213 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name AWAT2_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1002 bp
ATGCTCTTGCCCTCTAAGAAGGACCTCAAGACTGCCCTGGATGTCTTTGCTGTTTTCCAG
TGGTCCTTCAGTGCCTTGCTTATCACAACCACTGTGATTGCTGTCAACCTCTACCTGGTG
GTGTTCACACCATACTGGCCTGTCACTGTGCTTATTCTTACCTGGCTGGCTTTTGACTGG
AAGACCCCTCAGCGAGGCGGCCGCCGGTTTACCTGTGTGAGGCACTGGCGCCTGTGGAAA
CACTACAGCGATTATTTCCCTCTCAAGCTTCTGAAGACTCATGACATCTGCCCCAGCCGC
AACTACATCCTCGTCTGCCACCCTCATGGGCTCTTTGCCCATGGATGGTTTGGCCACTTT
GCCACAGAGGCCTCAGGCTTCTCCAAGATATTTCCTGGCATCACCCCTTACATACTCACA
CTGGGAGCCTTTTTCTGGATGCCTTTCCTCAGAGAATATGTAATGTCTACAGGGGCCTGC
TCTGTGAGTCGATCCTCCATTGACTTTCTGCTGACTCATAAAGGCACAGGCAACATGGTC
ATTGTGGTGATTGGTGGACTGGCTGAGTGCAGATACAGCCTGCCAGGTTCTTCTACCCTG
GTGTTGAAGAACCGGTCTGGCTTTGTGCGCATGGCCCTTCAGCATGGGGTGCCTCTAATA
CCTGCCTATGCCTTTGGGGAGACGGACCTCTATGATCAGCACATTTTCACTCCTGGTGGC
TTTGTCAACCGCTTCCAGAAGTGGTTCCAGAGCATGGTACACATCTACCCTTGTGCTTTC
TATGGACGTGGCTTCACCAAGAACTCCTGGGGCCTTCTGCCCTATAGTCGGCCTGTAACC
ACCATCGTCGGGGAGCCTCTACCAATGCCCAAGATTGAGAATCCAAGCCAGGAGATCGTG
GCTAAATATCACACACTCTATATTGATGCCCTACGTAAACTGTTTGACCAGCATAAGACC
AAGTTTGGTATCTCAGAGACCCAGGAGCTGGAGATAATTTGA
Enzyme 66 GenBank Gene ID AY605053 Link Image
Enzyme 66 GeneCard ID AWAT2 Link Image
Enzyme 66 GenAtlas ID AWAT2 Link Image
Enzyme 66 HGNC ID HGNC:23251 Link Image
Enzyme 66 Chromosome Location Not Available
Enzyme 66 Locus Not Available
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Cheng JB, Russell DW: Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. J Biol Chem. 2004 Sep 3;279(36):37798-807. Epub 2004 Jun 27. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
  4. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
  5. Yen CL, Brown CH 4th, Monetti M, Farese RV Jr: A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. J Lipid Res. 2005 Nov;46(11):2388-97. Epub 2005 Aug 16. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 12899
Enzyme 67 Name Diacylglycerol O-acyltransferase 2-like protein 6
Enzyme 67 Synonyms
  1. Diacylglycerol O-acyltransferase candidate 3
  2. hDC3
Enzyme 67 Gene Name DGAT2L6
Enzyme 67 Protein Sequence >Diacylglycerol O-acyltransferase 2-like protein 6
MAFFSRLNLQEGLQTFFVLQWIPVYIFLGAIPILLIPYFLLFSKFWPLAVLSLAWLTYDW
NTHSQGGRRSAWVRNWTLWKYFRNYFPVKLVKTHDLSPKHNYIIANHPHGILSFGVFINF
ATEATGIARIFPSITPFVGTLERIFWIPIVREYVMSMGVCPVSSSALKYLLTQKGSGNAV
VIVVGGAAEALLCRPGASTLFLKQRKGFVKMALQTGAYLVPSYSFGENEVFNQETFPEGT
WLRLFQKTFQDTFKKILGLNFCTFHGRGFTRGSWGFLPFNRPITTVVGEPLPIPRIKRPN
QKTVDKYHALYISALRKLFDQHKVEYGLPETQELTIT
Enzyme 67 Number of Residues 337
Enzyme 67 Molecular Weight 38592.9
Enzyme 67 Theoretical pI 10.34
Enzyme 67 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 67 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 67 Specific Function Probable acyltransferase uses fatty acyl-CoA as substrate. Has no wax synthase activity to produce wax esters
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions Not Available
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • 22-42 102-122
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 34526048 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID Q6ZPD8 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name DG2L6_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1014 bp
ATGGCTTTCTTCTCCCGACTGAATCTCCAGGAGGGCCTCCAAACCTTCTTTGTTTTGCAA
TGGATCCCAGTCTATATATTTTTAGGAGCTATTCCCATTCTCCTTATACCCTACTTTCTG
TTATTCAGTAAGTTCTGGCCCTTGGCTGTGCTCTCCTTAGCCTGGCTCACCTATGATTGG
AACACCCACAGTCAAGGTGGCAGGCGTTCAGCTTGGGTACGAAACTGGACCCTATGGAAG
TATTTCCGAAATTACTTCCCAGTAAAGCTGGTGAAGACTCATGATCTTTCTCCCAAACAC
AACTACATCATTGCCAATCACCCCCATGGCATTCTCTCTTTTGGTGTCTTCATCAACTTT
GCCACTGAGGCCACTGGCATTGCTCGGATTTTCCCATCCATCACTCCCTTTGTAGGGACC
TTAGAAAGGATATTTTGGATCCCAATTGTGCGAGAATATGTGATGTCAATGGGTGTGTGC
CCTGTGAGTAGCTCAGCCTTGAAGTACTTGCTGACCCAGAAAGGCTCAGGCAATGCCGTG
GTTATTGTGGTGGGTGGAGCTGCTGAAGCTCTCTTGTGCCGACCAGGAGCCTCCACTCTC
TTCCTCAAGCAGCGTAAAGGTTTTGTGAAGATGGCACTGCAAACAGGGGCATACCTTGTC
CCTTCATATTCCTTTGGTGAGAACGAAGTTTTCAATCAGGAGACCTTCCCTGAGGGCACG
TGGTTAAGGTTGTTCCAAAAAACCTTCCAGGACACATTCAAAAAAATCCTGGGACTAAAT
TTCTGTACCTTCCATGGCCGGGGCTTCACTCGCGGATCCTGGGGCTTCCTGCCTTTCAAT
CGGCCCATTACCACTGTTGTTGGGGAACCCCTTCCAATTCCCAGGATTAAGAGGCCAAAC
CAGAAGACAGTAGACAAGTATCACGCACTCTACATCAGTGCCCTGCGCAAGCTCTTTGAC
CAACACAAAGTTGAATATGGCCTCCCTGAGACCCAAGAGCTGACAATTACATAA
Enzyme 67 GenBank Gene ID AK129500 Link Image
Enzyme 67 GeneCard ID DGAT2L6 Link Image
Enzyme 67 GenAtlas ID DGAT2L6 Link Image
Enzyme 67 HGNC ID HGNC:23250 Link Image
Enzyme 67 Chromosome Location Not Available
Enzyme 67 Locus Not Available
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
  4. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 12900
Enzyme 68 Name Putative diacylglycerol O-acyltransferase 2-like protein 7
Enzyme 68 Synonyms Not Available
Enzyme 68 Gene Name DGAT2L7
Enzyme 68 Protein Sequence >Putative diacylglycerol O-acyltransferase 2-like protein 7
MLAVLYLLVKTAKLGTSWNYLFDFHPHRVLVVGAFANFCTEPTGCSCLFPKLPPHLLMLP
CWFHLLFFQDYIMSGASALPPGLVSFVKAPLPQWWPGGCPGVGGPLQALEAKPGQLSLPI
RNQKRLVKSALELGENELFQQFPNPQSSWVQRTQEALRPLLSVALQLFLGRRGLPLPFRA
PIRTVVGSAIPVQQSPPPSPAQVDTLQARYVGRLTQLFEEHQARYGVPADRHLVLTEARP
TAWPRLSAG
Enzyme 68 Number of Residues 249
Enzyme 68 Molecular Weight 27571.0
Enzyme 68 Theoretical pI 9.99
Enzyme 68 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 68 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 68 Specific Function Probable acyltransferase uses fatty acyl-CoA as substrate
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • 1-17
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein Not Available
Enzyme 68 UniProtKB/Swiss-Prot ID Q6IED9 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name DG2L7_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence Not Available
Enzyme 68 GenBank Gene ID Not Available
Enzyme 68 GeneCard ID DGAT2L7 Link Image
Enzyme 68 GenAtlas ID Not Available
Enzyme 68 HGNC ID Not Available
Enzyme 68 Chromosome Location 7
Enzyme 68 Locus 7q22.1
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. 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]
  2. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 12903
Enzyme 69 Name 2-acylglycerol O-acyltransferase 3
Enzyme 69 Synonyms
  1. Acyl-CoA:monoacylglycerol acyltransferase 3
  2. MGAT3
  3. Diacylglycerol O-acyltransferase candidate 7
  4. hDC7
  5. Diacylglycerol acyltransferase 2-like protein 7
  6. Monoacylglycerol O-acyltransferase 3
Enzyme 69 Gene Name MOGAT3
Enzyme 69 Protein Sequence >2-acylglycerol O-acyltransferase 3
MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYL
VWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMC
TGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQ
PQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRL
KAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQR
LHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI
Enzyme 69 Number of Residues 341
Enzyme 69 Molecular Weight 38729.8
Enzyme 69 Theoretical pI 8.70
Enzyme 69 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 69 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 69 Specific Function Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes
Enzyme 69 Pathways
Enzyme 69 Reactions
  • acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • 29-49 50-70 137-157
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 29124967 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q86VF5 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name MOGT3_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >1026 bp
ATGGGAGTTGCCACAACCCTGCAGCCCCCAACCACTTCCAAAACCTTGCAGAAGCAGCAT
CTAGAAGCAGTGGGCGCCTACCAATATGTGCTCACTTTCCTCTTCATGGGCCCTTTCTTC
TCCCTTCTTGTCTTTGTCCTCCTCTTCACGTCACTCTGGCCCTTCTCTGTTTTTTACTTG
GTGTGGCTCTATGTGGACTGGGACACACCCAACCAAGGTGGAAGGCGTTCGGAGTGGATA
AGGAACCGGGCAATTTGGAGACAACTAAGGGATTATTATCCTGTCAAGCTGGTGAAAACA
GCAGAGCTGCCCCCGGATCGGAACTACGTGCTGGGCGCCCACCCTCATGGGATCATGTGT
ACAGGCTTCCTCTGTAATTTCTCCACCGAGAGCAATGGCTTCTCCCAGCTCTTCCCGGGG
CTCCGGCCCTGGTTAGCCGTGCTGGCTGGCCTCTTCTACCTCCCGGTCTATCGCGACTAC
ATCATGTCCTTTGGACTCTGTCCGGTGAGCCGCCAGAGCCTGGACTTCATCCTGTCCCAG
CCCCAGCTCGGGCAGGCCGTGGTCATCATGGTGGGGGGTGCGCACGAGGCCCTGTATTCA
GTCCCCGGGGAGCACTGCCTTACGCTCCAGAAGCGCAAAGGCTTCGTGCGCCTGGCGCTG
AGGCACGGGGCGTCCCTGGTGCCCGTGTACTCCTTTGGGGAGAATGACATCTTTAGACTT
AAGGCTTTTGCCACAGGCTCCTGGCAGCATTGGTGCCAGCTCACCTTCAAGAAGCTCATG
GGCTTCTCTCCTTGCATCTTCTGGGGTCGCGGTCTCTTCTCAGCCACCTCCTGGGGCCTG
CTGCCCTTTGCTGTGCCCATCACCACTGTGGTGGGCCGCCCCATCCCCGTCCCCCAGCGC
CTCCACCCCACCGAGGAGGAAGTCAATCACTATCACGCCCTCTACATGACGGCCCTGGAG
CAGCTCTTCGAGGAGCACAAGGAAAGCTGTGGGGTCCCCGCTTCCACCTGCCTCACCTTC
ATCTAG
Enzyme 69 GenBank Gene ID AY229854 Link Image
Enzyme 69 GeneCard ID MOGAT3 Link Image
Enzyme 69 GenAtlas ID MOGAT3 Link Image
Enzyme 69 HGNC ID HGNC:23249 Link Image
Enzyme 69 Chromosome Location 7
Enzyme 69 Locus 7q22.1
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Cheng D, Nelson TC, Chen J, Walker SG, Wardwell-Swanson J, Meegalla R, Taub R, Billheimer JT, Ramaker M, Feder JN: Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption. J Biol Chem. 2003 Apr 18;278(16):13611-4. Epub 2003 Mar 3. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 12907
Enzyme 70 Name Lysophospholipid acyltransferase 5
Enzyme 70 Synonyms
  1. LPLAT 5
  2. 1-acylglycerophosphocholine O-acyltransferase
  3. 1-acylglycerophosphoserine O-acyltransferase
  4. Lysophosphatidylcholine acyltransferase
  5. LPCAT
  6. Lyso-PC acyltransferase
  7. Lysophosphatidylcholine acyltransferase 3
  8. Lyso-PC acyltransferase 3
  9. Lysophosphatidylserine acyltransferase
  10. LPSAT
  11. Lyso-PS acyltransferase
  12. Membrane-bound O-acyltransferase domain-containing protein 5
  13. O-acyltransferase domain-containing protein 5
Enzyme 70 Gene Name LPCAT3
Enzyme 70 Protein Sequence >Lysophospholipid acyltransferase 5
MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRH
YLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCF
QMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRG
VPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFY
LVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGL
GFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKE
LSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFY
YLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRK
EKLKKME
Enzyme 70 Number of Residues 487
Enzyme 70 Molecular Weight 56034.5
Enzyme 70 Theoretical pI 8.87
Enzyme 70 GO Classification Not Available
Enzyme 70 General Function Involved in 1-acylglycerophosphocholine O-acyltransfera
Enzyme 70 Specific Function Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3- phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero- 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn- glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle
Enzyme 70 Pathways Not Available
Enzyme 70 Reactions
  • acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318]
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • 44-64 84-104 111-131 180-200 227-247 285-305 364-384 422-442 453-473
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 42542394 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID Q6P1A2 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name MBOA5_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >1464 bp
ATGGCGTCCTCAGCGGAGGGGGACGAGGGGACTGTGGTGGCGCTGGCGGGGGTTCTGCAG
TCGGGTTTCCAGGAGCTGAGCCTTAACAAGTTGGCGACGTCCCTGGGCGCGTCAGAACAG
GCGCTGCGGCTGATCATCTCCATCTTCCTGGGTTACCCCTTTGCTTTGTTTTATCGGCAT
TACCTTTTCTACAAGGAGACCTACCTCATCCACCTCTTCCATACCTTTACAGGCCTCTCA
ATTGCTTATTTTAACTTTGGAAACCAGCTCTACCACTCCCTGCTGTGTATTGTGCTTCAG
TTCCTCATCCTTCGACTAATGGGCCGCACCATCACTGCCGTCCTCACTACCTTTTGCTTC
CAGATGGCCTACCTTCTGGCTGGATACTATTACACTGCCACCGGCAACTACGATATCAAG
TGGACAATGCCACATTGTGTTCTGACTTTGAAGCTGATTGGTTTGGCTGTTGACTACTTT
GACGGAGGGAAAGATCAGAATTCCTTGTCCTCTGAGCAACAGAAATATGCCATACGTGGT
GTTCCTTCCCTGCTGGAAGTTGCTGGTTTCTCCTACTTCTATGGGGCCTTCTTGGTAGGG
CCCCAGTTCTCAATGAATCACTACATGAAGCTGGTGCAGGGAGAGCTGATTGACATACCA
GGAAAGATACCAAACAGCATCATTCCTGCTCTCAAGCGCCTGAGTCTGGGCCTTTTCTAC
CTAGTGGGCTACACACTGCTCAGCCCCCACATCACAGAAGACTATCTCCTCACTGAAGAC
TATGACAACCACCCCTTCTGGTTCCGCTGCATGTACATGCTGATCTGGGGCAAGTTTGTG
CTGTACAAATATGTCACCTGTTGGCTGGTCACAGAAGGAGTATGCATTTTGACGGGCCTG
GGCTTCAATGGCTTTGAAGAAAAGGGCAAGGCAAAGTGGGATGCCTGTGCCAACATGAAG
GTGTGGCTCTTTGAAACAAACCCCCGCTTCACTGGCACCATTGCCTCATTCAACATCAAC
ACCAACGCCTGGGTGGCCCGCTACATCTTCAAACGACTCAAGTTCCTTGGAAATAAAGAA
CTCTCTCAGGGTCTCTCGTTGCTATTCCTGGCCCTCTGGCACGGCCTGCACTCAGGATAC
CTGGTCTGCTTCCAGATGGAATTCCTCATTGTTATTGTGGAAAGACAGGCTGCCAGGCTC
ATTCAAGAGAGCCCCACCCTGAGCAAGCTGGCCGCCATTACTGTCCTCCAGCCCTTCTAC
TATTTGGTGCAACAGACCATCCACTGGCTCTTCATGGGTTACTCCATGACTGCCTTCTGC
CTCTTCACGTGGGACAAATGGCTTAAGGTGTATAAATCCATCTATTTCCTTGGCCACATC
TTCTTCCTGAGCCTACTATTCATATTGCCTTATATTCACAAAGCAATGGTGCCAAGGAAA
GAGAAGTTAAAGAAGATGGAATAA
Enzyme 70 GenBank Gene ID NM_005768.5 Link Image
Enzyme 70 GeneCard ID LPCAT3 Link Image
Enzyme 70 GenAtlas ID LPCAT3 Link Image
Enzyme 70 HGNC ID HGNC:30244 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 12p13
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Zhao Y, Chen YQ, Bonacci TM, Bredt DS, Li S, Bensch WR, Moller DE, Kowala M, Konrad RJ, Cao G: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J Biol Chem. 2008 Mar 28;283(13):8258-65. Epub 2008 Jan 14. [PubMed Link Image]
  7. Gijon MA, Riekhof WR, Zarini S, Murphy RC, Voelker DR: Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils. J Biol Chem. 2008 Oct 31;283(44):30235-45. Epub 2008 Sep 3. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 12909
Enzyme 71 Name Lysophosphatidylcholine acyltransferase 1
Enzyme 71 Synonyms
  1. LPC acyltransferase 1
  2. LPCAT-1
  3. LysoPC acyltransferase 1
  4. 1-acylglycerophosphocholine O-acyltransferase
  5. 1-alkylglycerophosphocholine O-acetyltransferase
  6. Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
  7. Acetyl-CoA:lyso-PAF acetyltransferase
  8. Lyso-PAF acetyltransferase
  9. LysoPAFAT
  10. Acyltransferase-like 2
  11. Phosphonoformate immuno-associated protein 3
Enzyme 71 Gene Name LPCAT1
Enzyme 71 Protein Sequence >Lysophosphatidylcholine acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
Enzyme 71 Number of Residues 534
Enzyme 71 Molecular Weight 59150.7
Enzyme 71 Theoretical pI 5.82
Enzyme 71 GO Classification
Function
  • acyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 71 General Function Involved in acyltransferase activity
Enzyme 71 Specific Function Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology
Enzyme 71 Pathways
Enzyme 71 Reactions
  • acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 58-78
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 100811832 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q8NF37 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name PCAT1_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >1605 bp
ATGAGGCTGCGGGGATGCGGACCCCGGGCCGCCCCTGCCTCCAGCGCAGGGGCCAGCGAC
GCTCGGCTGCTGGCGCCCCCGGGGCGGAACCCCTTCGTGCACGAGCTGCGCCTCAGCGCC
CTGCAGAAGGCCCAGGTGGCCCTCATGACACTGACGCTCTTCCCGGTCCGGCTCCTGGTT
GCCGCTGCCATGATGCTGCTGGCCTGGCCCCTCGCACTTGTCGCATCCCTGGGCTCTGCG
GAGAAGGAACCCGAGCAGCCCCCGGCCCTGTGGAGGAAGGTTGTGGACTTCCTGCTGAAG
GCCATCATGCGCACCATGTGGTTCGCCGGCGGCTTCCACCGGGTGGCCGTGAAGGGGCGG
CAGGCGCTGCCCACCGAGGCGGCCATCCTCACGCTCGCGCCTCACTCGTCCTACTTCGAC
GCCATCCCTGTGACCATGACGATGTCCTCCATCGTGATGAAGGCAGAGAGCAGAGACATC
CCGATCTGGGGAACTCTGATCCAGTATATACGGCCTGTGTTCGTGTCCCGGTCAGACCAG
GATTCTCGCAGGAAAACAGTAGAAGAAATCAAGAGACGGGCGCAGTCCAACGGAAAGTGG
CCACAGATAATGATTTTTCCAGAAGGAACTTGTACAAACAGGACCTGCCTAATTACCTTC
AAACCTGGTGCATTCATCCCTGGAGCGCCCGTCCAGCCTGTGGTTTTACGATATCCAAAT
AAACTGGACACCATCACATGGACGTGGCAAGGACCTGGAGCGCTGGAAATCCTGTGGCTC
ACGCTGTGTCAGTTTCACAACCAAGTGGAAATCGAGTTCCTTCCTGTGTACAGCCCTTCT
GAGGAGGAGAAGAGGAACCCCGCGCTGTATGCCAGCAACGTGCGGCGAGTCATGGCCGAG
GCCTTGGGTGTCTCCGTGACTGACTACACGTTCGAGGACTGCCAGCTGGCCCTGGCGGAA
GGACAGCTCCGTCTCCCCGCTGACACTTGCCTTTTAGAATTTGCCAGGCTCGTGCGGGGC
CTCGGGCTAAAACCAGAAAAGCTTGAAAAAGATCTGGACAGATACTCAGAAAGAGCCAGG
ATGAAGGGAGGAGAGAAGATAGGTATTGCGGAGTTTGCCGCCTCCCTGGAAGTCCCCGTT
TCTGACTTGCTGGAAGACATGTTTTCACTGTTCGACGAGAGCGGCAGCGGCGAGGTGGAC
CTGCGAGAGTGTGTGGTTGCCCTGTCTGTCGTCTGCCGGCCGGCCCGGACCCTGGACACC
ATCCAGCTGGCTTTCAAGATGTACGGAGCGCAAGAGGACGGCAGCGTCGGCGAAGGTGAC
CTGTCCTGCATCCTCAAGACGGCCCTGGGGGTGGCAGAGCTCACCGTGACCGACCTATTC
CGAGCCATTGACCAAGAGGAGAAGGGGAAGATCACATTCGCTGACTTCCACAGGTTTGCA
GAAATGTACCCTGCCTTCGCAGAGGAATACCTGTACCCGGATCAGACACATTTCGAAAGC
TGTGCAGAGACCTCACCTGCGCCAATCCCAAACGGCTTCTGTGCCGATTTCAGCCCGGAA
AACTCAGACGCTGGGCGGAAGCCTGTTCGCAAGAAGCTGGATTAG
Enzyme 71 GenBank Gene ID AB244719 Link Image
Enzyme 71 GeneCard ID LPCAT1 Link Image
Enzyme 71 GenAtlas ID LPCAT1 Link Image
Enzyme 71 HGNC ID HGNC:25718 Link Image
Enzyme 71 Chromosome Location 5
Enzyme 71 Locus 5p15.33
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Nakanishi H, Shindou H, Hishikawa D, Harayama T, Ogasawara R, Suwabe A, Taguchi R, Shimizu T: Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production. J Biol Chem. 2006 Jul 21;281(29):20140-7. Epub 2006 May 16. [PubMed Link Image]
  2. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Chen X, Hyatt BA, Mucenski ML, Mason RJ, Shannon JM: Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11724-9. Epub 2006 Jul 24. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 12931
Enzyme 72 Name Lysocardiolipin acyltransferase 1
Enzyme 72 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 8
  2. 1-AGP acyltransferase 8
  3. 1-AGPAT 8
  4. Acyl-CoA:lysocardiolipin acyltransferase 1
Enzyme 72 Gene Name LCLAT1
Enzyme 72 Protein Sequence >Lysocardiolipin acyltransferase 1
MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSI
FMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVII
MNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKS
HFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTF
VVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDL
QLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAM
CLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
Enzyme 72 Number of Residues 414
Enzyme 72 Molecular Weight 48919.8
Enzyme 72 Theoretical pI 8.80
Enzyme 72 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 72 General Function Involved in acyltransferase activity
Enzyme 72 Specific Function Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages
Enzyme 72 Pathways
Enzyme 72 Reactions
  • acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02241]
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • 47-67 86-106 340-360 362-382
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 42558246 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID Q6UWP7 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name LCLT1_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >1245 bp
ATGCATTCCAGGGGAAGGGAAATTGTGGTGCTTCTGAACCCATGGTCAATTAACGAGGCA
GTTTCTAGCTACTGCACGTACTTCATAAAGCAGGACTCTAAAAGCTTTGGAATCATGGTG
TCATGGAAAGGGATTTACTTTATACTGACTCTGTTTTGGGGAAGCTTTTTTGGAAGCATT
TTCATGCTGAGTCCCTTTTTACCTTTGATGTTTGTAAACCCATCTTGGTATCGCTGGATC
AACAACCGCCTTGTGGCAACATGGCTCACCCTACCTGTGGCATTATTGGAGACCATGTTT
GGTGTAAAAGTGATTATAACTGGGGATGCATTTGTTCCTGGAGAAAGAAGTGTCATTATC
ATGAACCATCGGACAAGAATGGACTGGATGTTCCTGTGGAATTGCCTGATGCGATATAGC
TACCTCAGATTGGAGAAAATTTGCCTCAAAGCGAGTCTCAAAGGTGTTCCTGGATTTGGT
TGGGCCATGCAGGCTGCTGCCTATATCTTCATTCATAGGAAATGGAAGGATGACAAGAGC
CATTTCGAAGACATGATTGATTACTTTTGTGATATTCACGAACCACTTCAACTCCTCATA
TTCCCAGAAGGGACTGATCTCACAGAAAACAGCAAGTCTCGAAGTAATGCATTTGCTGAA
AAAAATGGACTTCAGAAATATGAATATGTTTTACATCCAAGAACTACAGGCTTTACTTTT
GTGGTAGACCGTCTAAGAGAAGGTAAGAACCTTGATGCTGTCCATGATATCACTGTGGCG
TATCCTCACAACATTCCTCAATCAGAGAAGCACCTCCTCCAAGGAGACTTTCCCAGGGAA
ATCCACTTTCACGTCCACCGGTATCCAATAGACACCCTCCCCACATCCAAGGAGGACCTT
CAACTCTGGTGCCACAAACGGTGGGAAGAGAAAGAAGAGAGGCTGCGTTCCTTCTATCAA
GGGGAGAAGAATTTTTATTTTACCGGACAGAGTGTCATTCCACCTTGCAAGTCTGAACTC
AGGGTCCTTGTGGTCAAATTGCTCTCTATACTGTATTGGACCCTGTTCAGCCCTGCAATG
TGCCTACTCATATATTTGTACAGTCTTGTTAAGTGGTATTTTATAATCACCATTGTAATC
TTTGTGCTGCAAGAGAGAATATTTGGTGGACTGGAGATCATAGAACTTGCATGTTACCGA
CTTTTACACAAACAGCCACATTTAAATTCAAAGAAAAATGAGTAA
Enzyme 72 GenBank Gene ID NM_182551.3 Link Image
Enzyme 72 GeneCard ID LCLAT1 Link Image
Enzyme 72 GenAtlas ID LCLAT1 Link Image
Enzyme 72 HGNC ID HGNC:26756 Link Image
Enzyme 72 Chromosome Location 2
Enzyme 72 Locus 2p23.1
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Agarwal AK, Barnes RI, Garg A: Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity. Arch Biochem Biophys. 2006 May 15;449(1-2):64-76. Epub 2006 Mar 29. [PubMed Link Image]
  4. Zhao Y, Chen YQ, Li S, Konrad RJ, Cao G: The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids. J Lipid Res. 2009 May;50(5):945-56. Epub 2008 Dec 15. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 12935
Enzyme 73 Name Lysophospholipid acyltransferase LPCAT4
Enzyme 73 Synonyms
  1. 1-acylglycerol-3-phosphate O-acyltransferase 7
  2. 1-AGP acyltransferase 7
  3. 1-AGPAT 7
  4. Acyltransferase-like 3
  5. Lysophosphatidylcholine acyltransferase 4
  6. Lysophosphatidylethanolamine acyltransferase 2
Enzyme 73 Gene Name LPCAT4
Enzyme 73 Protein Sequence >Lysophospholipid acyltransferase LPCAT4
MSQGSPGDWAPLDPTPGPPASPNPFVHELHLSRLQRVKFCLLGALLAPIRVLLAFIVLFL
LWPFAWLQVAGLSEEQLQEPITGWRKTVCHNGVLGLSRLLFFLLGFLRIRVRGQRASRLQ
APVLVAAPHSTFFDPIVLLPCDLPKVVSRAENLSVPVIGALLRFNQAILVSRHDPASRRR
VVEEVRRRATSGGKWPQVLFFPEGTCSNKKALLKFKPGAFIAGVPVQPVLIRYPNSLDTT
SWAWRGPGVLKVLWLTASQPCSIVDVEFLPVYHPSPEESRDPTLYANNVQRVMAQALGIP
ATECEFVGSLPVIVVGRLKVALEPQLWELGKVLRKAGLSAGYVDAGAEPGRSRMISQEEF
ARQLQLSDPQTVAGAFGYFQQDTKGLVDFRDVALALAALDGGRSLEELTRLAFELFAEEQ
AEGPNRLLYKDGFSTILHLLLGSPHPAATALHAELCQAGSSQGLSLCQFQNFSLHDPLYG
KLFSTYLRPPHTSRGTSQTPNASSPGNPTALANGTVQAPKQKGD
Enzyme 73 Number of Residues 524
Enzyme 73 Molecular Weight 57218.6
Enzyme 73 Theoretical pI 9.24
Enzyme 73 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 73 General Function Involved in acyltransferase activity
Enzyme 73 Specific Function Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1- alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl- phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors
Enzyme 73 Pathways
Enzyme 73 Reactions Not Available
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • 40-62 87-107
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 87116681 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID Q643R3 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name LPCT4_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >1575 bp
ATGAGCCAGGGAAGTCCGGGGGACTGGGCCCCCCTAGATCCCACCCCCGGACCCCCAGCA
TCCCCCAACCCCTTCGTGCATGAGTTACATCTCTCTCGCCTCCAGAGGGTTAAGTTCTGC
CTCCTGGGGGCATTGCTGGCCCCCATCCGAGTGCTTCTGGCCTTTATCGTCCTCTTTCTC
CTCTGGCCCTTTGCCTGGCTTCAAGTGGCCGGTCTTAGTGAGGAGCAGCTTCAGGAGCCA
ATTACAGGATGGAGGAAGACTGTGTGCCACAACGGGGTGCTAGGCCTGAGCCGCCTGCTG
TTTTTCCTGCTGGGCTTCCTCCGGATTCGCGTTCGTGGCCAGCGAGCCTCTCGCCTTCAA
GCCCCTGTCCTTGTTGCTGCCCCACACTCCACTTTCTTTGACCCCATTGTTCTGCTGCCC
TGTGACCTGCCCAAAGTTGTGTCCCGAGCTGAGAACCTTTCCGTTCCTGTCATTGGAGCC
CTTCTTCGATTCAACCAAGCCATCCTGGTATCCCGGCATGACCCGGCTTCTCGACGCAGA
GTGGTGGAGGAGGTCCGAAGGCGGGCCACCTCAGGAGGCAAGTGGCCGCAGGTGCTATTC
TTTCCTGAGGGCACCTGTTCCAACAAGAAGGCTTTGCTTAAGTTCAAACCAGGAGCCTTC
ATCGCAGGGGTGCCTGTGCAGCCTGTCCTCATCCGCTACCCCAACAGTCTGGACACCACC
AGCTGGGCATGGAGGGGTCCTGGAGTACTCAAAGTCCTCTGGCTCACAGCCTCTCAGCCC
TGCAGCATTGTGGATGTGGAGTTCCTTCCTGTGTATCACCCCAGCCCTGAGGAGAGCAGG
GACCCCACCCTCTATGCCAACAATGTTCAGAGGGTCATGGCACAGGCTCTGGGCATTCCA
GCCACCGAATGTGAGTTTGTAGGGAGCTTACCTGTGATTGTGGTGGGCCGGCTGAAGGTG
GCGTTGGAACCACAGCTCTGGGAACTGGGAAAAGTGCTTCGGAAGGCTGGGCTGTCCGCT
GGCTATGTGGACGCTGGGGCAGAGCCAGGCCGGAGTCGAATGATCAGCCAGGAAGAGTTT
GCCAGGCAGCTACAGCTCTCTGATCCTCAGACGGTGGCTGGTGCCTTTGGCTACTTCCAG
CAGGATACCAAGGGTTTGGTGGACTTCCGAGATGTGGCCCTTGCACTAGCAGCTCTGGAT
GGGGGCAGGAGCCTGGAAGAGCTAACTCGTCTGGCCTTTGAGCTCTTTGCTGAAGAGCAA
GCAGAGGGTCCCAACCGCCTGCTGTACAAAGACGGCTTCAGCACCATCCTGCACCTGCTG
CTGGGTTCACCCCACCCTGCTGCCACAGCTTTGCATGCTGAGCTGTGCCAGGCAGGATCC
AGCCAAGGCCTCTCCCTCTGTCAGTTCCAGAACTTCTCCCTCCATGACCCACTCTATGGG
AAACTCTTCAGCACCTACCTGCGCCCCCCACACACCTCTCGAGGCACCTCCCAGACACCA
AATGCCTCATCCCCAGGCAACCCCACTGCTCTGGCCAATGGGACTGTGCAAGCACCCAAG
CAGAAGGGAGACTGA
Enzyme 73 GenBank Gene ID NM_153613.2 Link Image
Enzyme 73 GeneCard ID LPCAT4 Link Image
Enzyme 73 GenAtlas ID LPCAT4 Link Image
Enzyme 73 HGNC ID HGNC:30059 Link Image
Enzyme 73 Chromosome Location 1
Enzyme 73 Locus 15q14
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Ye GM, Chen C, Huang S, Han DD, Guo JH, Wan B, Yu L: Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7. DNA Seq. 2005 Oct;16(5):386-90. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cao J, Shan D, Revett T, Li D, Wu L, Liu W, Tobin JF, Gimeno RE: Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2. J Biol Chem. 2008 Jul 4;283(27):19049-57. Epub 2008 May 5. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 12936
Enzyme 74 Name Glycerol-3-phosphate acyltransferase 3
Enzyme 74 Synonyms
  1. GPAT-3
  2. 1-acylglycerol-3-phosphate O-acyltransferase 9
  3. 1-AGP acyltransferase 9
  4. 1-AGPAT 9
  5. Acyl-CoA:glycerol-3-phosphate acyltransferase 3
  6. hGPAT3
  7. Lung cancer metastasis-associated protein 1
  8. Lysophosphatidic acid acyltransferase theta
  9. LPAAT-theta
  10. MAG-1
Enzyme 74 Gene Name AGPAT9
Enzyme 74 Protein Sequence >Glycerol-3-phosphate acyltransferase 3
MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKE
SILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEE
LVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQ
LPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTT
DGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILI
FPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSW
AIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQ
KNYSKMIVGNGSLS
Enzyme 74 Number of Residues 434
Enzyme 74 Molecular Weight 48704.8
Enzyme 74 Theoretical pI 9.15
Enzyme 74 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 74 General Function Involved in acyltransferase activity
Enzyme 74 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Overexpression activates the mTOR pathway
Enzyme 74 Pathways
Enzyme 74 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • 14-34 137-157 161-181
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 21362092 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q53EU6 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name GPAT3_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >1305 bp
ATGGAGGGCGCAGAGCTGGCCGGGAAGATCCTTTCCACCTGGCTGACGCTGGTTCTCGGC
TTCATCCTTTTACCTTCGGTCTTCGGAGTGTCTCTGGGCATCTCCGAGATCTACATGAAG
ATCCTAGTGAAAACTTTAGAGTGGGCCACAATACGAATTGAAAAAGGAACCCCAAAGGAG
TCGATTCTTAAAAACTCTGCTTCTGTTGGTATTATCCAAAGAGATGAGTCACCCATGGAA
AAAGGGCTCTCTGGTCTACGAGGAAGGGACTTTGAGCTGTCTGACGTGTTTTATTTCTCC
AAGAAGGGATTGGAAGCCATTGTAGAAGATGAAGTGACCCAGAGGTTTTCCTCAGAGGAG
CTAGTGTCATGGAATCTCCTCACAAGAACCAATGTAAATTTCCAGTACATCAGTCTGCGG
CTCACTATGGTGTGGGTGCTGGGCGTCATAGTGCGCTATTGTGTCCTACTGCCTCTGAGG
GTTACCTTGGCTTTCATTGGGATCAGTTTGCTGGTTATAGGAACTACACTGGTTGGGCAG
CTGCCAGACAGCAGCCTCAAAAACTGGCTGAGTGAACTGGTCCATCTGACTTGCTGCCGG
ATCTGTGTGCGAGCCCTCTCTGGTACCATTCATTATCATAACAAGCAGTACAGACCCCAG
AAGGGAGGCATTTGTGTTGCCAACCATACTTCCCCCATTGATGTTTTAATCTTGACAACG
GATGGATGTTATGCTATGGTTGGCCAGGTTCATGGCGGCTTGATGGGAATTATTCAGAGA
GCTATGGTCAAGGCTTGTCCTCATGTCTGGTTTGAACGCTCAGAAATGAAGGATCGACAC
CTGGTTACTAAGAGACTAAAAGAACATATTGCTGATAAGAAGAAACTACCCATACTAATT
TTTCCTGAAGGAACTTGCATCAACAATACTTCAGTCATGATGTTTAAAAAGGGGAGCTTT
GAAATTGGAGGAACCATACATCCAGTTGCAATTAAGTATAACCCTCAGTTCGGTGATGCA
TTTTGGAACAGTAGTAAATACAACATGGTGAGCTACCTGCTTCGAATGATGACCAGCTGG
GCCATCGTCTGTGACGTGTGGTACATGCCCCCCATGACCAGAGAGGAAGGAGAAGATGCA
GTCCAGTTTGCTAACAGGGTTAAGTCTGCTATTGCTATACAAGGAGGCCTGACTGAACTT
CCCTGGGATGGAGGACTAAAGAGAGCAAAGGTGAAGGACATCTTTAAGGAAGAGCAGCAG
AAAAATTACAGCAAGATGATTGTGGGCAATGGATCTCTCAGCTAA
Enzyme 74 GenBank Gene ID NM_032717.3 Link Image
Enzyme 74 GeneCard ID AGPAT9 Link Image
Enzyme 74 GenAtlas ID AGPAT9 Link Image
Enzyme 74 HGNC ID HGNC:28157 Link Image
Enzyme 74 Chromosome Location 4
Enzyme 74 Locus 4q21.23
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Tang W, Yuan J, Chen X, Gu X, Luo K, Li J, Wan B, Wang Y, Yu L: Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway. J Biochem Mol Biol. 2006 Sep 30;39(5):626-35. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  6. Cao J, Li JL, Li D, Tobin JF, Gimeno RE: Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis. Proc Natl Acad Sci U S A. 2006 Dec 26;103(52):19695-700. Epub 2006 Dec 14. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 12971
Enzyme 75 Name Glycine N-acyltransferase
Enzyme 75 Synonyms
  1. Acyl-CoA:glycine N-acyltransferase
  2. AAc
  3. Aralkyl acyl-CoA N-acyltransferase
  4. Aralkyl acyl-CoA:amino acid N-acyltransferase
  5. HRP-1(CLP)
Enzyme 75 Gene Name GLYAT
Enzyme 75 Protein Sequence >Glycine N-acyltransferase
MMLPLQGAQMLQMLEKSLRKSLPASLKVYGTVFHINHGNPFNLKAVVDKWPDFNTVVVCP
QEQDMTDDLDHYTNTYQIYSKDPQNCQEFLGSPELINWKQHLQIQSSQPSLNEAIQNLAA
IKSFKVKQTQRILYMAAETAKELTPFLLKSKILSPSGGKPKAINQEMFKLSSMDVTHAHL
VNKFWHFGGNERSQRFIERCIQTFPTCCLLGPEGTPVCWDLMDQTGEMRMAGTLPEYRLH
GLVTYVIYSHAQKLGKLGFPVYSHVDYSNEAMQKMSYTLQHVPIPRSWNQWNCVPL
Enzyme 75 Number of Residues 296
Enzyme 75 Molecular Weight 33897.0
Enzyme 75 Theoretical pI 8.28
Enzyme 75 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine N-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 75 General Function Involved in glycine N-acyltransferase activity
Enzyme 75 Specific Function Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions
  • acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 111038137 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q6IB77 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name GLYAT_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >891 bp
ATGATGTTACCATTGCAAGGTGCCCAGATGCTGCAGATGCTGGAGAAATCCTTGAGGAAG
AGCCTCCCAGCATCCTTAAAGGTTTATGGAACTGTCTTTCACATAAACCATGGAAATCCA
TTCAATCTGAAGGCTGTGGTGGACAAGTGGCCTGATTTTAATACAGTGGTTGTCTGCCCT
CAGGAGCAGGATATGACAGATGACCTTGATCACTATACCAATACTTACCAAATCTACTCC
AAAGATCCCCAAAACTGTCAGGAATTCCTTGGATCACCAGAACTCATCAACTGGAAACAG
CATTTACAGATTCAAAGTTCACAGCCTAGCCTGAATGAGGCTATACAAAATCTTGCAGCC
ATTAAGTCCTTCAAAGTCAAACAAACACAACGCATTCTCTATATGGCAGCTGAAACAGCC
AAGGAACTGACTCCTTTCCTGCTGAAATCAAAGATTTTATCTCCCAATGGTGGCAAACCC
AAGGCCATCAACCAAGAGATGTTTAAACTCTCATCCATGGATGTTACCCATGCTCACTTG
GTGAATAAATTCTGGCATTTTGGTGGTAATGAGAGGAGCCAGAGATTCATTGAGCGCTGC
ATTCAGACCTTTCCCACCTGCTGTCTCCTGGGGCCTGAGGGGACCCCTGTGTGCTGGGAT
CTAATGGACCAGACTGGAGAGATGAGAATGGCAGGCACCTTGCCGGAATACCGGCTCCAT
GGCCTTGTGACGTATGTCATCTATTCCCACGCCCAGAAATTGGGCAAACTTGGGTTTCCT
GTCTATTCTCATGTAGACTACAGCAATGAAGCTATGCAAAAAATGAGTTACACACTGCAA
CATGTTCCCATTCCCAGAAGCTGGAACCAGTGGAACTGTGTACCTCTGTGA
Enzyme 75 GenBank Gene ID NM_201648.2 Link Image
Enzyme 75 GeneCard ID GLYAT Link Image
Enzyme 75 GenAtlas ID GLYAT Link Image
Enzyme 75 HGNC ID HGNC:13734 Link Image
Enzyme 75 Chromosome Location 1
Enzyme 75 Locus 11q12.1
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. van der Westhuizen FH, Pretorius PJ, Erasmus E: The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase. J Biochem Mol Toxicol. 2000;14(2):102-9. [PubMed Link Image]
  2. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Mawal YR, Qureshi IA: Purification to homogeneity of mitochondrial acyl coa:glycine n-acyltransferase from human liver. Biochem Biophys Res Commun. 1994 Dec 15;205(2):1373-9. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 12972
Enzyme 76 Name Glycine N-acyltransferase-like protein 1
Enzyme 76 Synonyms
  1. Acyl-CoA:glycine N-acyltransferase-like protein 1
Enzyme 76 Gene Name GLYATL1
Enzyme 76 Protein Sequence >Glycine N-acyltransferase-like protein 1
MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQ
KQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFS
KSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSG
LVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRR
TGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLV
PF
Enzyme 76 Number of Residues 302
Enzyme 76 Molecular Weight 35100.9
Enzyme 76 Theoretical pI 6.86
Enzyme 76 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine N-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 76 General Function Involved in glycine N-acyltransferase activity
Enzyme 76 Specific Function Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines
Enzyme 76 Pathways Not Available
Enzyme 76 Reactions
  • acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein Not Available
Enzyme 76 UniProtKB/Swiss-Prot ID Q969I3 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name GLYL1_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >909 bp
ATGATCCTACTGAATAACTCCCATAAGCTGCTGGCCCTATACAAATCCTTGGCCAGGAGC
ATCCCTGAGTCCCTGAAGGTGTATGGCTCTGTGTATCACATCAATCACGGGAACCCCTTC
AACATGGAGGTGCTGGTGGATTCCTGGCCTGAATATCAGATGGTTATTATCCGGCCTCAA
AAGCAGGAGATGACTGATGACATGGATTCATACACAAACGTATATCGTATGTTCTCCAAA
GAGCCTCAAAAATCAGAAGAAGTTTTGAAAAATTGTGAGATCGTAAACTGGAAACAGAGA
CTCCAAATCCAAGGTCTTCAAGAAAGTTTAGGTGAGGGGATAAGAGTGGCTACATTTTCA
AAGTCAGTGAAAGTAGAGCATTCGAGAGCACTCCTCTTGGTTACGGAAGATATTCTGAAG
CTCAATGCCTCCAGTAAAAGCAAGCTTGGAAGCTGGGCTGAGACAGGCCACCCAGATGAT
GAATTTGAAAGTGAAACTCCCAACTTTAAGTATGCCCAGCTGGATGTCTCTTATTCTGGG
CTGGTAAATGACAACTGGAAGCGAGGGAAGAATGAGAGGAGCCTGCATTACATCAAGCGC
TGCATAGAAGACCTGCCAGCAGCCTGTATGCTCGGCCCAGAGGGAGTCCCGGTCTCATGG
GTAACCATGGACCCTTCTTGTGAAGTAGGAATGGCCTACAGCATGGAAAAATACCGAAGG
ACAGGCAACATGGCACGAGTGATGGTGCGATACATGAAATATCTGCGTCAGAAGAATATT
CCATTTTACATCTCTGTGTTGGAAGAAAATGAAGACTCCCGCAGATTTGTGGGGCAGTTT
GGTTTCTTTGAGGCCTCCTGTGAGTGGCACCAATGGACTTGCTACCCACAGAATCTAGTT
CCATTTTAG
Enzyme 76 GenBank Gene ID DQ084381 Link Image
Enzyme 76 GeneCard ID GLYATL1 Link Image
Enzyme 76 GenAtlas ID GLYATL1 Link Image
Enzyme 76 HGNC ID HGNC:30519 Link Image
Enzyme 76 Chromosome Location 1
Enzyme 76 Locus 11q12.1
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 12973
Enzyme 77 Name Glycine N-acyltransferase-like protein 2
Enzyme 77 Synonyms
  1. Acyl-CoA:glycine N-acyltransferase-like protein 2
Enzyme 77 Gene Name GLYATL2
Enzyme 77 Protein Sequence >Glycine N-acyltransferase-like protein 2
MLVLHNSQKLQILYKSLEKSIPESIKVYGAIFNIKDKNPFNMEVLVDAWPDYQIVITRPQ
KQEMKDDQDHYTNTYHIFTKAPDKLEEVLSYSNVISWEQTLQIQGCQEGLDEAIRKVATS
KSVQVDYMKTILFIPELPKKHKTSSNDKMELFEVDDDNKEGNFSNMFLDASHAGLVNEHW
AFGKNERSLKYIERCLQDFLGFGVLGPEGQLVSWIVMEQSCELRMGYTVPKYRHQGNMLQ
IGYHLEKYLSQKEIPFYFHVADNNEKSLQALNNLGFKICPCGWHQWKCTPKKYC
Enzyme 77 Number of Residues 294
Enzyme 77 Molecular Weight 34277.1
Enzyme 77 Theoretical pI 6.67
Enzyme 77 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycine N-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 77 General Function Involved in glycine N-acyltransferase activity
Enzyme 77 Specific Function Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines
Enzyme 77 Pathways Not Available
Enzyme 77 Reactions
  • acyl-CoA + glycine = CoA + N-acylglycine [RN:R00395]
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 29243559 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q8WU03 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name GLYL2_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >885 bp
ATGCTTGTGCTTCATAACTCTCAGAAGCTGCAGATTCTGTATAAATCCTTAGAAAAGAGC
ATCCCTGAATCCATAAAGGTATATGGCGCCATTTTCAACATAAAAGATAAAAACCCTTTC
AACATGGAGGTGCTGGTAGATGCCTGGCCAGATTACCAGATCGTCATTACCCGGCCTCAG
AAACAGGAGATGAAAGATGACCAGGATCATTATACCAACACTTACCACATCTTCACCAAA
GCTCCTGACAAATTAGAGGAAGTCCTGTCATACTCCAATGTAATCAGCTGGGAGCAAACT
TTGCAGATCCAAGGTTGCCAAGAGGGCTTGGATGAAGCAATAAGAAAGGTTGCAACTTCA
AAATCAGTGCAGGTAGATTACATGAAAACCATCCTCTTTATACCGGAATTACCAAAGAAA
CACAAGACCTCAAGTAATGACAAGATGGAGTTATTTGAAGTGGATGATGATAACAAGAAA
GGAAACTTTTCAAACATGTTCTTAGATGCTTCACATGCAGGTCTTGTGAATGAACACTGG
GCCTTTGGGAAAAATGAGAGGAGCTTGAAATATATTGAACGCTGCCTCCAGGATTTTCTA
GGATTTGGCGTGCTGGGTCCAGAGGGCCAGCTTGTCTCTTGGATTGTGATGGAACGGTCC
TGTGAGTTGAGAATGGGTTATACTGTCCCCAAATACAGACACCAAGGCAACATGTTGCAA
ATTGGTTACCATCTTGAAAAGTATCTTTCTCAGAAAGAAATCCCATTTTATTTCCATGTG
GCAGATAATAATGAGAAAAGCCTACAGGCACTGAACAATTTGGGGTTTAAGATTTGTCCC
TGTGGCTGGCATCAGTGGAAATGCACCCCCAAGAAATGTTGTTGA
Enzyme 77 GenBank Gene ID AF426250 Link Image
Enzyme 77 GeneCard ID GLYATL2 Link Image
Enzyme 77 GenAtlas ID GLYATL2 Link Image
Enzyme 77 HGNC ID HGNC:24178 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 11q12.1
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 13010
Enzyme 78 Name Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
Enzyme 78 Synonyms
  1. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase, isoform CRA_b
  2. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase variant
Enzyme 78 Gene Name EHHADH
Enzyme 78 Protein Sequence >Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAG
ADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQV
GLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEE
AIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAA
VQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSV
GVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSG
PKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIAS
STDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFV
GNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLT
GPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFL
SRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHK
GGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPS
SKL
Enzyme 78 Number of Residues 723
Enzyme 78 Molecular Weight 79496
Enzyme 78 Theoretical pI 9.54
Enzyme 78 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
Enzyme 78 General Function Lipid transport and metabolism
Enzyme 78 Specific Function Not Available
Enzyme 78 Pathways Not Available
Enzyme 78 Reactions Not Available
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • None
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 62021246 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID Q58EZ5 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name Q58EZ5_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence Not Available
Enzyme 78 GenBank Gene ID BC038948 Link Image
Enzyme 78 GeneCard ID Q58EZ5 Link Image
Enzyme 78 GenAtlas ID EHHADH Link Image
Enzyme 78 HGNC ID HGNC:3247 Link Image
Enzyme 78 Chromosome Location Not Available
Enzyme 78 Locus Not Available
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 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]
  2. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  3. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 13022
Enzyme 79 Name Putative uncharacterized protein
Enzyme 79 Synonyms Not Available
Enzyme 79 Gene Name HADHA
Enzyme 79 Protein Sequence >Putative uncharacterized protein
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 79 Number of Residues 763
Enzyme 79 Molecular Weight 83000
Enzyme 79 Theoretical pI Not Available
Enzyme 79 GO Classification Not Available
Enzyme 79 General Function Not Available
Enzyme 79 Specific Function Not Available
Enzyme 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function Not Available
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein Not Available
Enzyme 79 UniProtKB/Swiss-Prot ID B2R7L4 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name B2R7L4_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence Not Available
Enzyme 79 GenBank Gene ID Not Available
Enzyme 79 GeneCard ID B2R7L4 Link Image
Enzyme 79 GenAtlas ID Not Available
Enzyme 79 HGNC ID Not Available
Enzyme 79 Chromosome Location Not Available
Enzyme 79 Locus Not Available
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References Not Available
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 13026
Enzyme 80 Name Peroxisomal 3,2-trans-enoyl-CoA isomerase
Enzyme 80 Synonyms
  1. pECI
  2. DRS-1
  3. Delta(3),delta(2)-enoyl-CoA isomerase
  4. D3,D2-enoyl-CoA isomerase
  5. Diazepam-binding inhibitor-related protein 1
  6. DBI-related protein 1
  7. Dodecenoyl-CoA isomerase
  8. Hepatocellular carcinoma-associated antigen 88
  9. Renal carcinoma antigen NY-REN-1
Enzyme 80 Gene Name PECI
Enzyme 80 Protein Sequence >Peroxisomal 3,2-trans-enoyl-CoA isomerase
MAMAYLAWRLARRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNE
VKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSP
SLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAAS
KDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIA
VVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEML
IFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNALRISKEVIRKREREKL
HAVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
Enzyme 80 Number of Residues 394
Enzyme 80 Molecular Weight 43584.8
Enzyme 80 Theoretical pI 9.42
Enzyme 80 GO Classification
Function
  • acyl-CoA binding
  • binding
  • catalytic activity
  • fatty acid binding
  • lipid binding
Process
  • metabolic process
Component
Enzyme 80 General Function Involved in acyl-CoA binding
Enzyme 80 Specific Function Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates
Enzyme 80 Pathways
Enzyme 80 Reactions
  • (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA [RN:R04100]
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 260274832 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID O75521 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name PECI_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >1185 bp
ATGGCGATGGCGTACTTGGCTTGGAGACTGGCGCGGCGTTCGTGTCCGAGTTCTCTGCAG
GTCACTAGTTTCCCGGTAGTTCAGCTGCACATGAATAGAACAGCAATGAGAGCCAGTCAG
AAGGACTTTGAAAATTCAATGAATCAAGTGAAACTCTTGAAAAAGGATCCAGGAAACGAA
GTGAAGCTAAAACTCTACGCGCTATATAAGCAGGCCACTGAAGGACCTTGTAACATGCCC
AAACCAGGTGTATTTGACTTGATCAACAAGGCCAAATGGGACGCATGGAATGCCCTTGGC
AGCCTGCCCAAGGAAGCTGCCAGGCAGAACTATGTGGATTTGGTGTCCAGTTTGAGTCCT
TCATTGGAATCCTCTAGTCAGGTGGAGCCTGGAACAGACAGGAAATCAACTGGGTTTGAA
ACTCTGGTGGTGACCTCCGAAGATGGCATCACAAAGATCATGTTCAACCGGCCCAAAAAG
AAAAATGCCATAAACACTGAGATGTATCATGAAATTATGCGTGCACTTAAAGCTGCCAGC
AAGGATGACTCAATCATCACTGTTTTAACAGGAAATGGTGACTATTACAGTAGTGGGAAT
GATCTGACTAACTTCACTGATATTCCCCCTGGTGGAGTAGAGGAGAAAGCTAAAAATAAT
GCCGTTTTACTGAGGGAATTTGTGGGCTGTTTTATAGATTTTCCTAAGCCTCTGATTGCA
GTGGTCAATGGTCCAGCTGTGGGCATCTCCGTCACCCTCCTTGGGCTATTCGATGCCGTG
TATGCATCTGACAGGGCAACATTTCATACACCATTTAGTCACCTAGGCCAAAGTCCGGAA
GGATGCTCCTCTTACACTTTTCCGAAGATAATGAGCCCAGCCAAGGCAACAGAGATGCTT
ATTTTTGGAAAGAAGTTAACAGCGGGAGAGGCATGTGCTCAAGGACTTGTTACTGAAGTT
TTCCCTGATAGCACTTTTCAGAAAGAAGTCTGGACCAGGCTGAAGGCATTTGCAAAGCTT
CCCCCAAATGCCTTGAGAATTTCAAAAGAGGTAATCAGGAAAAGAGAGAGAGAAAAACTA
CACGCTGTTAATGCTGAAGAATGCAATGTCCTTCAGGGAAGATGGCTATCAGATGAATGC
ACAAATGCTGTGGTGAACTTCTTATCCAGAAAATCAAAACTGTGA
Enzyme 80 GenBank Gene ID NM_206836.2 Link Image
Enzyme 80 GeneCard ID PECI Link Image
Enzyme 80 GenAtlas ID PECI Link Image
Enzyme 80 HGNC ID HGNC:14601 Link Image
Enzyme 80 Chromosome Location 6
Enzyme 80 Locus 6p24.3
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Suk K, Kim YH, Hwang DY, Ihm SH, Yoo HJ, Lee MS: Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor. Biochim Biophys Acta. 1999 May 31;1454(1):126-31. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Geisbrecht BV, Zhang D, Schulz H, Gould SJ: Characterization of PECI, a novel monofunctional Delta(3), Delta(2)-enoyl-CoA isomerase of mammalian peroxisomes. J Biol Chem. 1999 Jul 30;274(31):21797-803. [PubMed Link Image]
  7. Wang Y, Han KJ, Pang XW, Vaughan HA, Qu W, Dong XY, Peng JR, Zhao HT, Rui JA, Leng XS, Cebon J, Burgess AW, Chen WF: Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies. J Immunol. 2002 Jul 15;169(2):1102-9. [PubMed Link Image]
  8. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  9. Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S: Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep. 2000 Sep;1(3):287-92. [PubMed Link Image]
  10. Feng X, Chuhjo T, Sugimori C, Kotani T, Lu X, Takami A, Takamatsu H, Yamazaki H, Nakao S: Diazepam-binding inhibitor-related protein 1: a candidate autoantigen in acquired aplastic anemia patients harboring a minor population of paroxysmal nocturnal hemoglobinuria-type cells. Blood. 2004 Oct 15;104(8):2425-31. Epub 2004 Jun 24. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 13066
Enzyme 81 Name Acyl-CoA synthetase family member 4
Enzyme 81 Synonyms
  1. Protein NRPS998
Enzyme 81 Gene Name AASDH
Enzyme 81 Protein Sequence >Acyl-CoA synthetase family member 4
MTLQELVHKAASCYMDRVAVCFDECNNQLPVYYTYKTVVNAASELSNFLLLHCDFQGIRE
IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKFK
SFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNLMLNDGKEKYEKEKIKSISSEHVNEEKA
EEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL
TFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQL
IKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPE
KTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL
GTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE
KLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY
INLKSENKLSGKEDLWEKLQYLWKSTLNLPEDLLRVPDESLFLNSGGDSLKSIRLLSEIE
KLVGTSVPGLLEIILSSSILEIYNHILQTVVPDEDVTFRKSCATKRKLSDINQEEASGTS
LHQKAIMTFTCHNEINAFVVLSRGSQILSLNSTRFLTKLGHCSSACPSDSVSQTNIQNLK
GLNSPVLIGKSKDPSCVAKVSEEGKPAIGTQKMELHVRWRSDTGKCVDASPLVVIPTFDK
SSTTVYIGSHSHRMKAVDFYSGKVKWEQILGDRIESSACVSKCGNFIVVGCYNGLVYVLK
SNSGEKYWMFTTEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFS
SPCLNLIPHHLYFATLGGLLLAVNPATGNVIWKHSCGKPLFSSPQCCSQYICIGCVDGNL
LCFTHFGEQVWQFSTSGPIFSSPCTSPSEQKIFFGSHDCFIYCCNMKGHLQWKFETTSRV
YATPFAFHNYNGSNEMLLAAASTDGKVWILESQSGQLQSVYELPGEVFSSPVVLESMLII
GCRDNYVYCLDLLGGNQK
Enzyme 81 Number of Residues 1098
Enzyme 81 Molecular Weight 122596.1
Enzyme 81 Theoretical pI 7.26
Enzyme 81 GO Classification
Function
  • acyl carrier activity
  • binding
  • catalytic activity
  • cofactor binding
  • substrate-specific transporter activity
  • transporter activity
Process
  • metabolic process
Component
Enzyme 81 General Function Involved in acyl carrier activity
Enzyme 81 Specific Function Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 45580730 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q4L235 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name ACSF4_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >3297 bp
ATGACTCTTCAGGAATTGGTGCATAAGGCTGCCTCCTGTTATATGGACAGAGTAGCTGTA
TGTTTTGATGAATGCAACAACCAGCTTCCAGTTTACTACACCTACAAGACTGTGGTTAAT
GCTGCTTCTGAATTATCAAATTTTCTGCTGTTACACTGTGACTTTCAAGGAATTCGGGAA
ATTGGTCTCTACTGCCAACCTGGGATAGACTTACCCTCTTGGATTTTAGGAATTCTCCAA
GTCCCGGCTGCTTATGTACCTATCGAGCCAGATTCACCACCGTCATTATCAACTCATTTT
ATGAAAAAATGTAATCTAAAGTATATCCTTGTTGAAAAAAAACAAATTAATAAATTTAAA
TCTTTTCATGAAACATTATTGAACTATGATACATTTACAGTGGAACATAATGACCTAGTG
CTCTTCAGACTTCACTGGAAAAATACTGAGGTGAACTTGATGCTAAATGATGGAAAAGAG
AAATATGAAAAAGAAAAAATAAAAAGCATAAGTTCTGAGCATGTCAATGAAGAAAAAGCA
GAAGAACACATGGATCTGAGGCTAAAGCATTGCTTAGCCTATGTTCTACATACATCAGGG
ACTACAGGGATACCGAAGATTGTCAGAGTGCCTCATAAGTGTATAGTACCAAATATCCAG
CATTTTCGGGTACTTTTTGACATCACACAAGAAGATGTTTTGTTTCTGGCTTCACCTCTG
ACCTTCGATCCTTCTGTTGTGGAAATATTTCTTGCTCTATCAAGTGGTGCCTCTCTGCTT
ATTGTACCAACTTCCGTCAAGTTGCTCCCATCAAAATTAGCCAGCGTTCTCTTTTCCCAT
CATAGAGTGACTGTTTTGCAGGCAACACCAACATTGCTTAGAAGATTTGGATCTCAGCTT
ATCAAGTCAACTGTTTTGTCAGCCACTACTTCTCTTCGAGTATTAGCCCTTGGTGGTGAA
GCGTTTCCATCATTGACAGTTCTCAGAAGCTGGAGAGGAGAAGGCAATAAAACACAAATA
TTTAATGTTTATGGTATCACAGAGGTATCAAGTTGGGCGACCATTTATAGGATTCCAGAG
AAGACTCTTAACTCTACTCTCAAATGTGAATTGCCTGTACAACTGGGATTTCCACTTCTT
GGAACAGTAGTTGAAGTCAGAGATACTAATGGCTTCACAATTCAGGAAGGCAGTGGCCAA
GTATTTTTAGGTGGCAGAAACAGAGTGTGTTTTCTTGATGATGAAGTGACAGTACCACTT
GGCACAATGCGAGCTACAGGAGACTTTGTGACTGTGAAAGATGGAGAGATTTTTTTTTTG
GGACGAAAAGACAGTCAGATCAAACGTCATGGCAAACGTCTTAACATTGAACTTGTGCAA
CAGGTTGCTGAAGAGCTTCAGCAAGTGGAGTCTTGTGCAGTTACATGGTATAATCAGGAA
AAATTAATTCTCTTCATGGTGTCTAAAGATGCTTCAGTAAAAGAATACATCTTTAAAGAA
CTGCAGAAATATCTTCCAAGTCATGCAGTCCCGGATGAGCTTGTATTGATCGACTCTCTA
CCATTTACATCCCACGGCAAAATTGATGTTTCTGAGTTAAACAAGATATATTTAAACTAC
ATAAACTTGAAGTCTGAGAATAAGCTCAGTGGGAAAGAGGACCTTTGGGAAAAATTACAG
TATTTGTGGAAGTCTACTCTGAATCTCCCAGAAGATCTTTTGAGGGTTCCTGATGAGTCA
CTCTTCTTAAATAGTGGTGGAGATTCCTTAAAGTCCATCCGGCTCCTCAGTGAGATTGAA
AAACTTGTTGGTACATCAGTACCTGGGCTTCTGGAAATTATTCTCAGCAGTTCCATTTTA
GAGATTTATAATCACATCCTTCAAACAGTGGTTCCAGATGAAGATGTGACATTCAGGAAG
AGTTGTGCCACAAAAAGGAAACTCAGCGACATTAATCAAGAGGAAGCCAGTGGAACATCT
TTACATCAGAAAGCCATCATGACTTTCACTTGCCACAATGAGATTAATGCTTTTGTTGTA
CTGAGCAGAGGGAGTCAAATTTTGTCTCTGAATTCCACTAGGTTTTTAACAAAGTTAGGA
CATTGCTCTTCAGCCTGTCCTTCTGACTCAGTTTCACAGACCAACATTCAAAATTTGAAA
GGCTTAAATTCTCCAGTTCTTATTGGGAAGTCAAAAGATCCATCCTGTGTTGCAAAAGTT
TCTGAAGAGGGGAAACCTGCGATAGGGACTCAGAAAATGGAGTTACATGTGAGGTGGAGG
TCAGACACAGGCAAATGTGTAGATGCTTCACCGCTGGTTGTAATACCCACTTTTGATAAG
TCATCTACAACTGTGTACATTGGTTCCCATTCTCATAGAATGAAGGCAGTTGACTTTTAC
TCTGGGAAGGTAAAATGGGAACAGATTTTGGGAGATCGAATTGAATCCTCAGCATGTGTA
TCTAAGTGTGGAAACTTTATTGTGGTGGGCTGTTATAATGGATTAGTTTATGTTCTGAAA
AGTAATAGTGGAGAAAAATACTGGATGTTTACTACTGAAGATGCTGTCAAAAGCTCGGCA
ACCATGGATCCAACCACAGGACTCATTTACATTGGATCTCATGACCAGCACGCATATGCT
TTAGATATTTATAGAAAGAAGTGTGTTTGGAAGTCAAAATGTGGAGGAACTGTCTTTTCC
TCTCCGTGTTTGAACCTGATTCCACATCATTTGTATTTTGCTACATTGGGAGGACTTTTA
CTGGCTGTAAATCCTGCTACTGGGAACGTTATTTGGAAACATTCCTGTGGAAAACCACTC
TTCTCTTCCCCACAATGTTGCTCACAGTATATTTGTATTGGCTGTGTAGATGGGAATTTA
CTCTGCTTTACTCACTTTGGAGAACAGGTTTGGCAGTTCTCTACCAGTGGACCAATCTTT
TCATCCCCGTGTACCTCACCATCAGAGCAAAAAATATTTTTTGGTTCCCATGATTGCTTT
ATCTACTGTTGTAACATGAAAGGTCACCTGCAGTGGAAATTTGAAACTACTTCAAGGGTC
TATGCAACACCGTTTGCTTTCCATAACTACAATGGCAGCAATGAAATGTTGCTGGCAGCA
GCATCTACTGATGGGAAAGTGTGGATCTTGGAATCTCAGAGTGGACAATTGCAAAGTGTT
TATGAACTTCCTGGAGAAGTCTTCTCTTCTCCTGTGGTCCTGGAATCAATGCTCATTATT
GGGTGTAGAGATAATTATGTTTATTGTCTGGATTTATTGGGTGGCAATCAAAAATAA
Enzyme 81 GenBank Gene ID NM_181806.2 Link Image
Enzyme 81 GeneCard ID AASDH Link Image
Enzyme 81 GenAtlas ID AASDH Link Image
Enzyme 81 HGNC ID HGNC:23993 Link Image
Enzyme 81 Chromosome Location 4
Enzyme 81 Locus 4q12
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Wang L, Jil C, Xu Y, Xu J, Dai J, Wu Q, Wu M, Zou X, Sun L, Gu S, Xie Y, Mao Y: Cloning and characterization of a novel human homolog* of mouse U26, a putative PQQ-dependent AAS dehydrogenase. Mol Biol Rep. 2005 Mar;32(1):47-53. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 13971
Enzyme 82 Name Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 82 Synonyms
  1. VLCAD
Enzyme 82 Gene Name ACADVL
Enzyme 82 Protein Sequence >Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDAL
TRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPA
KNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA
HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY
YTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKM
GIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV
DHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKI
FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDK
GKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRAL
EQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEK
MLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF
Enzyme 82 Number of Residues 655
Enzyme 82 Molecular Weight 70389.6
Enzyme 82 Theoretical pI 9.10
Enzyme 82 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 82 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 82 Specific Function Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accomodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons
Enzyme 82 Pathways Not Available
Enzyme 82 Reactions Not Available
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • None
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 12653261 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID P49748 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name ACADV_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >1968 bp
ATGCAGGCGGCTCGGATGGCCGCGAGCTTGGGGCGGCAGCTGCTGAGGCTCGGGGGCGGA
AGCTCGCGGCTCACGGCGCTCCTGGGGCAGCCCCGGCCCGGCCCTGCCCGGCGGCCCTAT
GCCGGGGGTGCCGCTCAGCTGGCTCTGGACAAGTCAGATTCCCACCCCTCTGACGCTCTG
ACCAGGAAAAAACCGGCCAAGGCGGAATCTAAGTCCTTTGCTGTGGGAATGTTCAAAGGC
CAGCTCACCACAGATCAGGTGTTCCCATACCCGTCCGTGCTCAACGAAGAGCAGACACAG
TTTCTTAAAGAGCTGGTGGAGCCTGTGTCCCGTTTCTTCGAGGAAGTGAACGATCCCGCC
AAGAATGACGCTCTGGAGATGGTGGAGGAGACCACTTGGCAGGGCCTCAAGGAGCTGGGG
GCCTTTGGTCTGCAAGTGCCCAGTGAGCTGGGTGGTGTGGGCCTTTGCAACACCCAGTAC
GCCCGTTTGGTGGAGATCGTGGGCATGCATGACCTTGGCGTGGGCATTACCCTGGGGGCC
CATCAGAGCATCGGTTTCAAAGGCATCCTGCTCTTTGGCACAAAGGCCCAGAAAGAAAAA
TACCTCCCCAAGCTGGCATCTGGGGAGACTGTGGCCGCTTTCTGTCTAACCGAGCCCTCA
AGCGGGTCAGATGCAGCCTCCATCCGAACCTCTGCTGTGCCCAGCCCCTGTGGAAAATAC
TATACCCTCAATGGAAGCAAGCTTTGGATCAGTAATGGGGGCCTAGCAGACATCTTCACG
GTCTTTGCCAAGACACCAGTTACAGATCCAGCCACAGGAGCCGTGAAGGAGAAGATCACA
GCTTTTGTGGTGGAGAGGGGCTTCGGGGGCATTACCCATGGGCCCCCTGAGAAGAAGATG
GGCATCAAGGCTTCAAACACAGCAGAGGTGTTCTTTGATGGAGTACGGGTGCCATCGGAG
AACGTGCTGGGTGAGGTTGGGAGTGGCTTCAAGGTTGCCATGCACATCCTCAACAATGGA
AGGTTTGGCATGGCTGCGGCCCTGGCAGGTACCATGAGAGGCATCATTGCTAAGGCGGTA
GATCATGCCACTAATCGTACCCAGTTTGGGGAGAAAATTCACAACTTTGGGCTGATCCAG
GAGAAGCTGGCACGGATGGTTATGCTGCAGTATGTAACTGAGTCCATGGCTTACATGGTG
AGTGCTAACATGGACCAGGGAGCCACGGACTTCCAGATAGAGGCCGCCATCAGCAAAATC
TTTGGCTCGGAGGCAGCCTGGAAGGTGACAGATGAATGCATCCAAATCATGGGGGGTATG
GGCTTCATGAAGGAACCTGGAGTAGAGCGTGTGCTCCGAGATCTTCGCATCTTCCGGATC
TTTGAGGGGACAAATGACATTCTTCGGCTGTTTGTGGCTCTGCAGGGCTGTATGGACAAA
GGAAAGGAGCTCTCTGGGCTTGGCAGTGCTCTAAAGAATCCCTTTGGGAATGCTGGCCTC
CTGCTAGGAGAGGCAGGCAAACAGCTGAGGCGGCGGGCAGGGCTGGGCAGCGGCCTGAGT
CTCAGCGGACTTGTCCACCCGGAGTTGAGTCGGAGTGGCGAGCTGGCAGTACGGGCTCTG
GAGCAGTTTGCCACTGTGGTGGAGGCCAAGCTGATAAAACACAAGAAGGGGATTGTCAAT
GAACAGTTTCTGCTGCAGCGGCTGGCAGACGGGGCCATCGACCTCTATGCCATGGTGGTG
GTTCTCTCGAGGGCCTCAAGATCCCTGAGTGAGGGCCACCCCACGGCCCAGCATGAGAAA
ATGCTCTGTGACACCTGGTGTATCGAGGCTGCAGCTCGGATCCGAGAGGGCATGGCCGCC
CTGCAGTCTGACCCCTGGCAGCAAGAGCTCTACCGCAACTTCAAAAGCATCTCCAAGGCC
TTGGTGGAGCGGGGTGGTGTGGTCACCAGCAACCCACTTGGCTTCTGA
Enzyme 82 GenBank Gene ID BC000399 Link Image
Enzyme 82 GeneCard ID ACADVL Link Image
Enzyme 82 GenAtlas ID ACADVL Link Image
Enzyme 82 HGNC ID HGNC:92 Link Image
Enzyme 82 Chromosome Location 1
Enzyme 82 Locus 17p13.1
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Aoyama T, Souri M, Ueno I, Kamijo T, Yamaguchi S, Rhead WJ, Tanaka K, Hashimoto T: Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients. Am J Hum Genet. 1995 Aug;57(2):273-83. [PubMed Link Image]
  2. Andresen BS, Bross P, Vianey-Saban C, Divry P, Zabot MT, Roe CR, Nada MA, Byskov A, Kruse TA, Neve S, Kristiansen K, Knudsen I, Corydon MJ, Gregersen N: Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene. Hum Mol Genet. 1996 Apr;5(4):461-72. [PubMed Link Image]
  3. Orii KO, Aoyama T, Souri M, Orii KE, Kondo N, Orii T, Hashimoto T: Genomic DNA organization of human mitochondrial very-long-chain acyl-CoA dehydrogenase and mutation analysis. Biochem Biophys Res Commun. 1995 Dec 26;217(3):987-92. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T: Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J Clin Invest. 1995 Jun;95(6):2465-73. [PubMed Link Image]
  6. Andresen BS, Olpin S, Poorthuis BJ, Scholte HR, Vianey-Saban C, Wanders R, Ijlst L, Morris A, Pourfarzam M, Bartlett K, Baumgartner ER, deKlerk JB, Schroeder LD, Corydon TJ, Lund H, Winter V, Bross P, Bolund L, Gregersen N: Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency. Am J Hum Genet. 1999 Feb;64(2):479-94. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. McAndrew RP, Wang Y, Mohsen AW, He M, Vockley J, Kim JJ: Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J Biol Chem. 2008 Apr 4;283(14):9435-43. Epub 2008 Jan 28. [PubMed Link Image]
  9. Souri M, Aoyama T, Orii K, Yamaguchi S, Hashimoto T: Mutation analysis of very-long-chain acyl-coenzyme A dehydrogenase (VLCAD) deficiency: identification and characterization of mutant VLCAD cDNAs from four patients. Am J Hum Genet. 1996 Jan;58(1):97-106. [PubMed Link Image]
  10. Smelt AH, Poorthuis BJ, Onkenhout W, Scholte HR, Andresen BS, van Duinen SG, Gregersen N, Wintzen AR: Very long chain acyl-coenzyme A dehydrogenase deficiency with adult onset. Ann Neurol. 1998 Apr;43(4):540-4. [PubMed Link Image]
  11. Mathur A, Sims HF, Gopalakrishnan D, Gibson B, Rinaldo P, Vockley J, Hug G, Strauss AW: Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death. Circulation. 1999 Mar 16;99(10):1337-43. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 13972
Enzyme 83 Name Acyl-coenzyme A oxidase-like protein
Enzyme 83 Synonyms
  1. Acyl-CoA oxidase-like protein
Enzyme 83 Gene Name ACOXL
Enzyme 83 Protein Sequence >Acyl-coenzyme A oxidase-like protein
MRALTVQRVKFAMDLPLLKRAGQDLAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWL
FGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVID
TPCENAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDENGSLYPGVTAIDMMY
KEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRL
AVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIEHQTQTLRLMPHLATALALTFV
SRYAGALLDEDVFQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENR
ISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYTKQYEEKPLFGLLQNWAESVGDKLRTS
FLAFNMDTVDDLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDFFHAWNSCLHHVASLS
LAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTR
IRNQERC
Enzyme 83 Number of Residues 547
Enzyme 83 Molecular Weight 61795.0
Enzyme 83 Theoretical pI 8.68
Enzyme 83 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleoside binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 83 General Function Involved in oxidoreductase activity, acting on the CH-CH group of donors
Enzyme 83 Specific Function Not Available
Enzyme 83 Pathways Not Available
Enzyme 83 Reactions Not Available
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 119570743 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q9NUZ1 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name ACOXL_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >1778 bp


>1743 BP
ATGAGAGCTTTGACAGTTCAGAGAGTGAAGTTTGCCATGGACCTGCCTCTGTTAAAACGT
GCAGGTCAGGATCTGGCAGAGAAAACAAAGAATTTTGTCAGCCGAAGCCTTGTCATAGGA
GAAGTCCTCTCCATGGCGGACATGGCCACAGGAGTGAAGTGCGGAATAATTTATTGGCTA
TTTGGTGGTGCTATCAGGAATCTCGGAAGCCCTGAACATGTTACTAAGTGGTTTCAGCCA
CTCCAGGAGCAGAAATACACTGGGATGTTTGCAATGACCGAGAGGGGCCATGGGAGCAAC
GCGAGAGGGATCCAGACCGAAGCCACCTTTGACCTCTCTGCCCAGGAGTTTGTAATTGAC
ACGCCGTGTGAAAATGCGGAGAAGATGTATATTGGAAATGCCATGTACGGGAATTATGCA
GCTGTCTTTGCCCAGCTCATCATAGATGGAAGATCTCAAGGGCCCCACTGTTTCATCGTT
CCTGTCCGGGATGAAAACGGAAGCTTGTACCCAGGAGTCACAGCTATTGATATGATGTAC
AAGGAGGGTCTGCATGGTGTGGACAATGGGATATTAATATTTGACAAGGTTCGGATACCC
AGGGAGAACCTGCTGGATAAGTTTGGTTCCGTGGCTCCAGATGGACAGTACCATTCGCCT
ATTAGGAACAAGAGTGCAAGATTCAATGCCATGCTGGCAGCACTGACCCCTTCGAGATTA
GCTGTGGCTTTCCAAGCTATGGGTGCCATGAAGCTTGGGTTGACGATAGCCATTCGCTAT
AGCCACAGCCGGAGGCAGTTTGGGCCCAAAACCAAGGAAGAGGTGAAGATCATTGAGCAC
CAAACACAGACCCTGCGGCTGATGCCCCACCTGGCCACAGCCTTGGCCCTGACCTTCGTC
AGCAGGTATGCTGGGGCCCTCCTGGATGAGGATGTCTTCCAGGGAAAGGAGCTGGTCAAC
AGTCGCTCGCTGCAGGCTCTGGTGGCGGGGCTGAAGGCCTACAGCACCTGGGAGAACATC
CGCTGCCTGCAGGACTGCCGCGAGTGCACTGGAGGCATGGTTGTGGGGCGGGAACTGCTG
GCCCAATACACCAAACAGTATGAAGAAAAACCACTCTTTGGCCTGCTCCAAAACTGGGCT
GAATCTGTGGGGGACAAGCTGAGAACCAGTTTCCTGGCATTTAACATGGACACAGTTGAT
GATCTCGCCTTTCTGTTGAAAGCAGTGAAATTTCGTGAAAGGGTTCTTCAGCGGGGTTTG
GTGGCCAGAATTTATTATAAGGTAAAGACCAAGAAGGAGGATTTTTTCCATGCCTGGAAC
TCGTGTCTGCACCACGTGGCTTCTCTGTCCCTGGCACACACTCACCGAGTTACCTTAGAG
CAGTTCTCCCTAGCAGTGAAGAGCTGTCCTGACCAAGAGGACCAGACTTTGTTAATGAAG
TTTTGTCTGTTGTATGGAACCAAGCTGGTGTTTCAGGAGCGGGCCTGGTATTTAGAACAT
AAATACTTGACTCCCATGGCCAGCACGAGGATCAGGAATCAGTTGCTGGATTTGTGCGAC
TCGGTGAAGGATGATGCCCGGAGGGTGATCTCGACCTTTAACATTCCACACACCTACCTC
CACGCACCAATCGCCGGAATCTCCAACCCGCGGGCCGCGTGGGCTTTCTACCCTGCACCG
CTGCAGCCGCGGCCACGGGAAGAGGCGCGCTCCCGGCGGCCCAAGCTGGGAGCCAAGCTC
TAA
Enzyme 83 GenBank Gene ID CH471237 Link Image
Enzyme 83 GeneCard ID ACOXL Link Image
Enzyme 83 GenAtlas ID ACOXL Link Image
Enzyme 83 HGNC ID HGNC:25621 Link Image
Enzyme 83 Chromosome Location 2
Enzyme 83 Locus 2q13
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 14011
Enzyme 84 Name Acyl-coenzyme A synthetase ACSM6, mitochondrial
Enzyme 84 Synonyms Not Available
Enzyme 84 Gene Name ACSM6
Enzyme 84 Protein Sequence >Acyl-coenzyme A synthetase ACSM6, mitochondrial
MLGRFQPFSLVRSFRLGFEACCYPNQKCATQTIRPPDSRCLVQAVSQNFNFAKDVLDQWS
QLEKDGLRGPYPALWKVSAKGEEDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPP
TPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCP
TLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQ
YGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPE
TVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRIT
KLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR
IKLNQPASLYCPHMVSWEEYASARGHMLYLTGDRGIMDEDGYFWWSGRVDDVANALGQRL
Enzyme 84 Number of Residues 480
Enzyme 84 Molecular Weight 53584.5
Enzyme 84 Theoretical pI 8.50
Enzyme 84 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 84 General Function Involved in catalytic activity
Enzyme 84 Specific Function ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 84 Pathways Not Available
Enzyme 84 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 195947378 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID Q6P461 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name ACSM6_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >1443 bp
ATGCTAGGCCGATTTCAACCCTTCTCCTTGGTCCGGAGTTTCAGACTGGGATTTGAAGCC
TGCTGCTATCCAAACCAAAAATGTGCTACTCAGACCATCAGACCCCCTGACTCCAGGTGC
CTAGTCCAAGCAGTTTCTCAGAACTTTAATTTTGCAAAGGATGTGTTGGATCAGTGGTCC
CAGCTGGAAAAGGACGGACTCAGAGGGCCTTACCCCGCCCTCTGGAAGGTTAGTGCCAAA
GGAGAAGAGGACAAATGGAGCTTTGAAAGGATGACTCAACTCTCCAAGAAGGCCGCCAGC
ATCCTCTCAGACACCTGTGCCCTTAGCCATGGAGACCGGCTGATGATAATCTTGCCCCCA
ACACCTGAAGCCTACTGGATCTGCCTGGCCTGTGTGCGCTTGGGAATCACCTTTGTGCCT
GGGAGCCCCCAGCTGACTGCCAAGAAAATTCGCTATCAATTACGCATGTCTAAGGCCCAG
TGCATTGTGGCTAATGAAGCTATGGCCCCAGTTGTAAACTCTGCCGTGTCCGACTGCCCC
ACCTTGAAAACCAAGCTCCTGGTGTCAGATAAGAGCTATGATGGGTGGTTGGATTTCAAG
AAGTTGATTCAAGTTGCCCCTCCAAAGCAGACCTACATGAGGACCAAAAGCCAAGATCCA
ATGGCCATATTCTTCACCAAGGGTACAACAGGAGCTCCCAAAATGGTCGAGTATTCCCAG
TATGGTTTGGGAATGGGATTCAGCCAGGCTTCCAGACGGTGGATGGATCTCCAGCCAACA
GATGTCTTGTGGAGTCTGGGTGATGCCTTTGGTGGATCTTTATCCCTGAGCGCTGTCTTG
GGAACTTGGTTCCAAGGAGCCTGTGTGTTTCTGTGTCACATGCCAACCTTCTGCCCTGAG
ACTGTTCTAAATGTCCTGTCCAGATTTCCCATCACCACTCTATCTGCAAATCCAGAGATG
TACCAGGAACTGCTTCAGCACAAGTGTTTCACCAGCTACAGATTCAAGAGTCTGAAGCAG
TGTGTGGCTGCAGGAGGACCCATCAGCCCTGGGGTGATTGAGGACTGGAAACGCATCACT
AAGTTGGACATCTATGAAGGCTATGGGCAGACGGAAACTGGTCTACTCTGTGCCACTTCC
AAAACAATAAAATTGAAGCCAAGCTCTCTGGGGAAGCCATTGCCACCTTATATTGTCCAG
ATTGTGGATGAAAACTCAAATCTCCTGCCTCCAGGGGAAGAAGGAAATATTGCAATCCGC
ATAAAACTAAACCAACCTGCTTCTCTGTACTGTCCACACATGGTGAGCTGGGAGGAATAT
GCTTCAGCAAGAGGCCACATGCTTTACCTCACAGGTGACAGAGGGATCATGGATGAAGAC
GGCTACTTCTGGTGGTCTGGTAGAGTTGATGATGTTGCCAATGCATTGGGTCAGAGATTG
TGA
Enzyme 84 GenBank Gene ID NM_207321.2 Link Image
Enzyme 84 GeneCard ID ACSM6 Link Image
Enzyme 84 GenAtlas ID ACSM6 Link Image
Enzyme 84 HGNC ID HGNC:31665 Link Image
Enzyme 84 Chromosome Location Not Available
Enzyme 84 Locus Not Available
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 14420
Enzyme 85 Name Acyl-coenzyme A synthetase ACSM2A, mitochondrial
Enzyme 85 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 2A
  2. Butyrate--CoA ligase 2A
  3. Butyryl-coenzyme A synthetase 2A
  4. Middle-chain acyl-CoA synthetase 2A
Enzyme 85 Gene Name ACSM2A
Enzyme 85 Protein Sequence >Acyl-coenzyme A synthetase ACSM2A, mitochondrial
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN
ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ
Enzyme 85 Number of Residues 577
Enzyme 85 Molecular Weight 64222.7
Enzyme 85 Theoretical pI 8.20
Enzyme 85 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 85 General Function Involved in catalytic activity
Enzyme 85 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 85 Pathways
Enzyme 85 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein 58082049 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID Q08AH3 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name ACS2A_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 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 85 GenBank Gene ID NM_001010845.2 Link Image
Enzyme 85 GeneCard ID ACSM2A Link Image
Enzyme 85 GenAtlas ID ACSM2A Link Image
Enzyme 85 HGNC ID HGNC:32017 Link Image
Enzyme 85 Chromosome Location 1
Enzyme 85 Locus 16p12.3
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW: Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A. J Mol Biol. 2009 May 22;388(5):997-1008. Epub 2009 Apr 1. [PubMed Link Image]
  6. Iwai N, Mannami T, Tomoike H, Ono K, Iwanaga Y: An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors. Hypertension. 2003 May;41(5):1041-6. Epub 2003 Mar 24. [PubMed Link Image]
  7. Lindner I, Rubin D, Helwig U, Nitz I, Hampe J, Schreiber S, Schrezenmeir J, Doring F: The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population. Mol Nutr Food Res. 2006 Mar;50(3):270-4. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 14421
Enzyme 86 Name Acyl-coenzyme A synthetase ACSM2B, mitochondrial
Enzyme 86 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 2B
  2. Butyrate--CoA ligase 2B
  3. Butyryl-coenzyme A synthetase 2B
  4. Middle-chain acyl-CoA synthetase 2B
  5. Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A
Enzyme 86 Gene Name ACSM2B
Enzyme 86 Protein Sequence >Acyl-coenzyme A synthetase ACSM2B, mitochondrial
MHWLRKVQGLCTLWGTQMSSRTLYINSRQLVSLQWGHQEVPAKFNFASDVLDHWADMEKA
GKRLPSPALWWVNGKGKELMWNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWW
LVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIK
LLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGL
KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTL
SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF
YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPI
GIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN
ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY
PRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKARAQ
Enzyme 86 Number of Residues 577
Enzyme 86 Molecular Weight 64270.8
Enzyme 86 Theoretical pI 8.38
Enzyme 86 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 86 General Function Involved in catalytic activity
Enzyme 86 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 86 Pathways
Enzyme 86 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 51555772 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q68CK6 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name ACS2B_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >1734 bp
ATGCATTGGCTGCGAAAAGTTCAGGGACTTTGCACCCTGTGGGGTACTCAGATGTCCAGC
CGCACTCTCTACATTAATAGTAGGCAACTGGTGTCCCTGCAGTGGGGCCACCAGGAAGTT
CCGGCCAAGTTTAACTTTGCTAGTGATGTGTTGGATCACTGGGCTGACATGGAGAAGGCT
GGCAAGCGACTCCCAAGCCCAGCCCTGTGGTGGGTGAATGGGAAGGGGAAGGAATTAATG
TGGAATTTCAGAGAACTGAGTGAAAACAGCCAGCAGGCAGCCAACGTCCTCTCGGGAGCC
TGTGGCCTGCAGCGTGGGGATCGTGTGGCAGTGATGCTGCCCCGAGTGCCTGAGTGGTGG
CTGGTGATCCTGGGCTGCATTCGAGCAGGTCTCATCTTTATGCCTGGAACCATCCAGATG
AAATCCACTGACATACTGTATAGGTTGCAGATGTCTAAGGCCAAGGCTATTGTTGCTGGG
GATGAAGTCATCCAAGAAGTGGACACAGTGGCATCTGAATGTCCTTCTCTGAGAATTAAG
CTACTGGTGTCTGAGAAAAGCTGCGATGGGTGGCTGAACTTCAAGAAACTACTAAATGAG
GCATCCACCACTCATCACTGTGTGGAGACTGGAAGCCAGGAAGCATCTGCCATCTACTTC
ACTAGTGGGACCAGTGGTCTTCCCAAGATGGCAGAACATTCCTACTCGAGCCTGGGCCTC
AAGGCCAAGATGGATGCTGGTTGGACAGGCCTGCAAGCCTCTGATATAATGTGGACCATA
TCAGACACAGGTTGGATACTGAACATCTTGGGCTCACTTTTGGAATCTTGGACATTAGGA
GCATGCACATTTGTTCATCTCTTGCCAAAGTTTGACCCACTGGTTATTCTAAAGACACTC
TCCAGTTATCCAATCAAGAGTATGATGGGTGCCCCTATTGTTTACCGGATGTTGCTACAG
CAGGATCTTTCCAGTTACAAGTTCCCCCATCTACAGAACTGCCTCGCTGGAGGGGAGTCC
CTTCTTCCAGAAACTCTGGAGAACTGGAGGGCCCAGACAGGACTGGACATCCGAGAATTC
TATGGCCAGACAGAAACGGGATTAACTTGCATGGTTTCCAAGACAATGAAAATCAAACCA
GGATACATGGGAACGGCTGCTTCCTGTTATGATGTACAGGTTATAGATGATAAGGGCAAC
GTCCTGCCCCCCGGCACAGAAGGAGACATTGGCATCAGGGTCAAACCCATCAGGCCTATA
GGCATCTTCTCTGGCTATGTGGAAAATCCCGACAAGACAGCAGCCAACATTCGAGGAGAC
TTTTGGCTCCTTGGAGACCGGGGAATCAAAGATGAAGATGGGTATTTCCAGTTTATGGGA
CGGGCAGATGATATCATTAACTCCAGCGGGTACCGGATTGGACCCTCGGAGGTAGAGAAT
GCACTGATGAAGCACCCTGCTGTGGTTGAGACGGCTGTGATCAGCAGCCCAGACCCCGTC
CGAGGAGAGGTGGTGAAGGCATTTGTGATCCTGGCCTCGCAGTTCCTATCCCATGACCCA
GAACAGCTCACCAAGGAGCTGCAGCAGCATGTGAAGTCAGTGACAGCCCCATACAAGTAC
CCAAGAAAGATAGAGTTTGTCTTGAACCTGCCCAAGACTGTCACAGGGAAAATTCAACGA
ACCAAACTTCGAGACAAGGAGTGGAAGATGTCCGGAAAAGCCCGTGCGCAGTGA
Enzyme 86 GenBank Gene ID AB073604 Link Image
Enzyme 86 GeneCard ID ACSM2B Link Image
Enzyme 86 GenAtlas ID ACSM2B Link Image
Enzyme 86 HGNC ID HGNC:30931 Link Image
Enzyme 86 Chromosome Location 1
Enzyme 86 Locus 16p12.3
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Vessey DA, Lau E, Kelley M, Warren RS: Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria. J Biochem Mol Toxicol. 2003;17(1):1-6. [PubMed Link Image]
  2. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Vessey DA, Kelley M, Warren RS: Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids. Biochim Biophys Acta. 1999 Aug 5;1428(2-3):455-62. [PubMed Link Image]
  5. Boomgaarden I, Vock C, Klapper M, Doring F: Comparative analyses of disease risk genes belonging to the acyl-CoA synthetase medium-chain (ACSM) family in human liver and cell lines. Biochem Genet. 2009 Oct;47(9-10):739-48. Epub 2009 Jul 26. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 14422
Enzyme 87 Name Acyl-coenzyme A synthetase ACSM3, mitochondrial
Enzyme 87 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 3
  2. Butyrate--CoA ligase 3
  3. Butyryl-coenzyme A synthetase 3
  4. Middle-chain acyl-CoA synthetase 3
  5. Protein SA homolog
Enzyme 87 Gene Name ACSM3
Enzyme 87 Protein Sequence >Acyl-coenzyme A synthetase ACSM3, mitochondrial
MLARVTRKMLRHAKCFQRLAIFGSVRALHKDNRTATPQNFSNYESMKQDFKLGIPEYFNF
AKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRG
DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPA
VDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG
YPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFT
HHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDV
TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPG
QEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDV
ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIK
EIQEHVKKTTAPYKYPRKVEFIQELPKTISGKTKRNELRKKEWKTI
Enzyme 87 Number of Residues 586
Enzyme 87 Molecular Weight 66152.2
Enzyme 87 Theoretical pI 9.45
Enzyme 87 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 87 General Function Involved in catalytic activity
Enzyme 87 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 87 Pathways
Enzyme 87 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • None
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 42544132 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q53FZ2 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name ACSM3_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >1761 bp
ATGCTAGCTCGTGTCACCAGGAAGATGCTACGTCATGCCAAGTGTTTTCAGCGCCTAGCA
ATTTTTGGTTCTGTGAGGGCACTGCATAAAGATAATAGAACAGCAACCCCTCAGAATTTC
TCCAACTATGAATCCATGAAACAGGACTTCAAACTGGGGATTCCAGAGTATTTCAACTTT
GCTAAAGATGTCCTGGACCAATGGACTGATAAGGAAAAGGCTGGAAAGAAACCTTCAAAT
CCAGCCTTCTGGTGGATCAACAGAAATGGAGAAGAGATGCGATGGAGTTTTGAGGAACTG
GGATCTCTGTCCAGAAAATTTGCCAATATACTTTCAGAAGCCTGTTCCCTACAAAGAGGA
GATCGGGTAATTCTGATTCTGCCCAGGGTCCCAGAGTGGTGGCTTGCAAATGTGGCCTGT
CTGCGAACAGGGACAGTTTTAATTCCAGGAACCACTCAGCTGACCCAGAAAGACATTCTC
TACAGACTACAATCTTCAAAAGCAAACTGCATTATCACCAATGATGTTTTAGCCCCAGCA
GTAGACGCTGTTGCATCCAAATGTGAAAATCTGCACTCCAAGCTGATTGTATCAGAGAAC
TCCAGAGAGGGGTGGGGGAACCTCAAGGAGTTGATGAAACATGCCAGTGACAGCCACACC
TGTGTGAAGACAAAACACAATGAGATCATGGCCATATTCTTTACCAGTGGAACAAGTGGA
TATCCGAAAATGACTGCACACACCCACAGCAGTTTTGGTTTAGGATTATCTGTAAATGGA
AGGTTCTGGCTAGATTTGACACCCTCAGATGTGATGTGGAATACCTCAGATACGGGCTGG
GCAAAGTCTGCATGGAGTAGTGTTTTTTCTCCGTGGATCCAGGGAGCATGTGTATTCACA
CACCATTTACCCCGTTTTGAGCCGACTTCTATCTTGCAAACACTCTCCAAGTACCCCATC
ACAGTCTTCTGTTCAGCACCAACTGTATACCGAATGCTTGTACAGAATGATATAACCAGC
TATAAGTTTAAAAGCTTAAAGCACTGTGTGAGTGCTGGGGAACCAATTACCCCTGACGTG
ACTGAAAAATGGAGAAACAAGACGGGCCTGGATATCTACGAAGGATATGGACAGACTGAA
ACGGTGCTAATCTGTGGAAATTTTAAGGGAATGAAAATTAAACCTGGCTCAATGGGAAAA
CCTTCTCCTGCTTTCGATGTTAAGATTGTAGATGTAAATGGCAATGTTCTACCTCCTGGA
CAAGAAGGAGATATTGGCATTCAAGTTCTACCCAACCGACCATTTGGCCTTTTTACTCAT
TACGTAGATAATCCTTCAAAAACAGCTTCAACTCTACGAGGCAATTTCTATATCACTGGG
GACAGAGGATATATGGATAAAGATGGGTATTTCTGGTTTGTTGCAAGAGCAGATGATGTC
ATATTATCCTCTGGCTATCGAATTGGACCATTTGAGGTAGAAAATGCCCTGAATGAACAC
CCTTCAGTTGCAGAGTCAGCTGTTGTCAGCAGCCCAGACCCCATCAGAGGAGAGGTAGTA
AAGGCTTTTGTCGTTCTAAATCCTGATTACAAGTCACATGATCAAGAACAACTAATAAAG
GAGATTCAGGAGCATGTTAAAAAAACTACAGCACCTTACAAATATCCCAGAAAGGTAGAA
TTTATTCAAGAGCTGCCAAAGACTATCAGTGGGAAGACAAAAAGAAATGAACTGAGGAAG
AAAGAATGGAAGACAATTTAA
Enzyme 87 GenBank Gene ID NM_005622.3 Link Image
Enzyme 87 GeneCard ID ACSM3 Link Image
Enzyme 87 GenAtlas ID ACSM3 Link Image
Enzyme 87 HGNC ID HGNC:10522 Link Image
Enzyme 87 Chromosome Location 1
Enzyme 87 Locus 16p13.11
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
  6. Telgmann R, Brand E, Nicaud V, Hagedorn C, Beining K, Schonfelder J, Brink-Spalink V, Schmidt-Petersen K, Matanis T, Vischer P, Nofer JR, Hasenkamp S, Plouin PF, Drouet L, Cambien F, Paul M, Tiret L, Brand-Herrmann SM: SAH gene variants are associated with obesity-related hypertension in Caucasians: the PEGASE Study. J Hypertens. 2007 Mar;25(3):557-64. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 14424
Enzyme 88 Name Acyl-coenzyme A synthetase ACSM5, mitochondrial
Enzyme 88 Synonyms Not Available
Enzyme 88 Gene Name ACSM5
Enzyme 88 Protein Sequence >Acyl-coenzyme A synthetase ACSM5, mitochondrial
MRPWLRHLVLQALRNSRAFCGSHGKPAPLPVPQKIVATWEAISLGRQLVPEYFNFAHDVL
DVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMML
VLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIS
AECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMV
EHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV
DAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH
QTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVA
VRIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSY
RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHV
KRVTAPYKYPRKVAFVSELPKTVSGKIQRSKLRSQEWGK
Enzyme 88 Number of Residues 579
Enzyme 88 Molecular Weight 64759.6
Enzyme 88 Theoretical pI 8.52
Enzyme 88 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 88 General Function Involved in catalytic activity
Enzyme 88 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 88 Pathways
Enzyme 88 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • None
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 38505220 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q6NUN0 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name ACSM5_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >1740 bp
ATGAGACCATGGCTGAGACACCTAGTCCTCCAGGCACTGAGGAACTCCAGGGCATTCTGT
GGGTCTCATGGGAAGCCAGCACCTCTACCTGTTCCTCAGAAGATCGTGGCCACCTGGGAA
GCCATCAGCCTGGGAAGGCAGCTGGTGCCTGAGTACTTCAACTTCGCCCATGATGTGCTG
GATGTGTGGAGTCGGCTGGAAGAGGCTGGACACCGCCCCCCAAATCCTGCCTTCTGGTGG
GTCAATGGCACAGGAGCAGAGATCAAGTGGAGCTTTGAGGAGCTGGGGAAGCAGTCCAGG
AAGGCAGCCAATGTGCTGGGGGGTGCATGCGGCCTGCAGCCTGGGGACAGAATGATGCTG
GTACTCCCACGGCTCCCGGAGTGGTGGCTGGTCAGTGTGGCTTGCATGCGGACAGGGACT
GTGATGATTCCGGGTGTGACTCAGCTGACAGAGAAGGACCTCAAGTACCGGCTGCAGGCG
TCCAGGGCCAAGTCCATTATCACCAGTGACTCCCTAGCTCCAAGGGTGGATGCCATCAGT
GCCGAATGCCCCTCCCTCCAGACCAAGCTGCTGGTGTCAGACAGCAGTCGGCCAGGCTGG
TTGAACTTCAGGGAACTCCTCCGGGAGGCTTCTACAGAGCACAACTGCATGAGGACAAAG
AGTCGAGACCCGCTGGCCATCTACTTTACCAGCGGAACCACCGGGGCCCCCAAGATGGTC
GAGCACTCCCAGAGCAGCTACGGACTGGGTTTTGTGGCCAGCGGAAGACGGTGGGTGGCC
TTGACCGAATCTGACATCTTCTGGAACACGACTGACACTGGCTGGGTGAAGGCAGCCTGG
ACTCTCTTCTCTGCCTGGCCTAATGGATCTTGCATTTTTGTGCATGAGCTGCCCCGAGTT
GATGCCAAAGTTATCCTGAATACTCTCTCCAAATTCCCGATAACCACCCTCTGCTGTGTC
CCAACCATCTTTCGGCTGCTTGTGCAGGAGGATCTGACCAGGTACCAGTTTCAGAGCCTG
AGGCACTGTCTGACCGGAGGAGAGGCCCTCAACCCTGACGTGAGGGAGAAGTGGAAACAC
CAGACTGGTGTGGAGCTGTACGAAGGCTATGGCCAGTCTGAAACGGTTGTCATCTGTGCC
AATCCAAAAGGCATGAAAATCAAGTCTGGATCCATGGGGAAGGCGTCCCCACCCTACGAT
GTGCAGATTGTGGATGATGAGGGCAACGTCCTGCCTCCTGGAGAAGAGGGGAATGTTGCC
GTCCGTATCAGACCCACTCGGCCCTTCTGTTTCTTCAATTGCTATTTGGACAATCCTGAG
AAGACAGCTGCATCAGAACAAGGGGACTTTTACATCACAGGGGACCGAGCTCGCATGGAC
AAGGATGGCTACTTTTGGTTCATGGGAAGAAACGACGATGTGATCAATTCTTCAAGCTAC
CGGATCGGGCCTGTTGAAGTGGAAAGTGCCCTGGCAGAGCATCCTGCTGTCCTGGAGTCG
GCTGTGGTCAGCAGCCCAGACCCCATCAGGGGAGAGGTGGTAAAGGCATTTATAGTCCTT
ACTCCAGCCTACTCCTCTCATGACCCAGAGGCACTAACGCGGGAACTCCAGGAGCATGTG
AAAAGGGTGACTGCTCCATACAAATACCCCAGGAAGGTGGCCTTTGTTTCAGAACTGCCA
AAGACGGTTTCTGGAAAGATCCAAAGGAGTAAATTGCGAAGTCAGGAGTGGGGGAAATGA
Enzyme 88 GenBank Gene ID NM_017888.2 Link Image
Enzyme 88 GeneCard ID ACSM5 Link Image
Enzyme 88 GenAtlas ID ACSM5 Link Image
Enzyme 88 HGNC ID HGNC:26060 Link Image
Enzyme 88 Chromosome Location 1
Enzyme 88 Locus 16p12.3
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Iwai N, Mannami T, Tomoike H, Ono K, Iwanaga Y: An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors. Hypertension. 2003 May;41(5):1041-6. Epub 2003 Mar 24. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 14506
Enzyme 89 Name Peroxisomal coenzyme A diphosphatase NUDT7
Enzyme 89 Synonyms
  1. Nucleoside diphosphate-linked moiety X motif 7
  2. Nudix motif 7
Enzyme 89 Gene Name NUDT7
Enzyme 89 Protein Sequence >Peroxisomal coenzyme A diphosphatase NUDT7
MSRLGLPEEPVRNSLLDDAKARLRKYDIGGKYSHLPYNKYSVLLPLVAKEGKLHLLFTVR
SEKLRRAPGEVCFPGGKRDPTDMDDAATALREAQEEVGLRPHQVEVVCCLVPCLIDTDTL
ITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGHRFINHIFEYTNP
EDGVTYQIKGMTANLAVLVAFIILEKKPTFEVQFNLNDVLASSEELFLKVHKKATSRL
Enzyme 89 Number of Residues 238
Enzyme 89 Molecular Weight 26941.9
Enzyme 89 Theoretical pI 7.06
Enzyme 89 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • magnesium ion binding
  • manganese ion binding
  • metal ion binding
  • transition metal ion binding
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside diphosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
Component
Enzyme 89 General Function Involved in hydrolase activity
Enzyme 89 Specific Function Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. CoA into 3',5'-ADP and 4'- phosphopantetheine. Has no activity toward NDP-sugars, CDP- alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand
Enzyme 89 Pathways Not Available
Enzyme 89 Reactions Not Available
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 157785656 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID P0C024 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name NUDT7_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >717 bp
ATGTCACGACTTGGTCTTCCCGAGGAGCCAGTCAGAAACAGTTTGCTAGATGATGCTAAG
GCCCGCTTAAGAAAGTATGATATTGGAGGCAAATATTCTCACTTGCCATATAACAAATAC
TCCGTCCTTTTGCCATTGGTGGCTAAAGAAGGAAAACTCCATTTGTTGTTCACCGTCCGG
TCAGAGAAGCTAAGAAGGGCCCCTGGAGAAGTTTGCTTCCCTGGAGGTAAGCGTGACCCT
ACAGACATGGATGATGCAGCCACAGCTCTCCGGGAAGCCCAGGAGGAAGTGGGTCTCCGT
CCTCACCAAGTGGAAGTTGTCTGCTGCCTGGTGCCATGTCTTATTGATACAGATACATTG
ATAACTCCATTTGTGGGTTTAATAGACCACAACTTCCAGGCCCAGCCGAATCCTGCTGAA
GTTAAGGATGTATTCCTGGTGCCTCTGGCCTATTTCCTGCATCCACAGGTCCATGACCAG
CATTACGTCACACGTCTTGGTCACCGTTTTATTAATCATATCTTTGAGTACACAAACCCT
GAAGACGGTGTCACTTACCAGATCAAGGGAATGACGGCAAACCTTGCAGTGTTGGTGGCC
TTTATCATTTTGGAAAAAAAACCCACCTTTGAGGTTCAATTTAATCTTAATGATGTATTA
GCATCCTCTGAAGAGTTATTCCTGAAGGTTCATAAAAAAGCTACAAGCAGGTTATGA
Enzyme 89 GenBank Gene ID NM_001105663.1 Link Image
Enzyme 89 GeneCard ID NUDT7 Link Image
Enzyme 89 GenAtlas ID NUDT7 Link Image
Enzyme 89 HGNC ID HGNC:8054 Link Image
Enzyme 89 Chromosome Location 1
Enzyme 89 Locus 16q23.1
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  2. Gasmi L, McLennan AG: The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem J. 2001 Jul 1;357(Pt 1):33-8. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 14869
Enzyme 90 Name Acyl-coenzyme A synthetase ACSM4, mitochondrial
Enzyme 90 Synonyms Not Available
Enzyme 90 Gene Name ACSM4
Enzyme 90 Protein Sequence >Acyl-coenzyme A synthetase ACSM4, mitochondrial
MKIFFRYQTFRFIWLTKPPGRRLHKDHQLWTPLTLADFEAINRCNRPLPKNFNFAADVLD
QWSQKEKTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANVLTKPCGLQRGDRLAVI
LPRIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVL
ECPDLKTKLLVSPQSWNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQ
HSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQF
DTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRV
QTGLELYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIA
LRLKPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGY
RIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHV
KKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR
Enzyme 90 Number of Residues 580
Enzyme 90 Molecular Weight 65702.2
Enzyme 90 Theoretical pI 8.76
Enzyme 90 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 90 General Function Involved in catalytic activity
Enzyme 90 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 90 Pathways Not Available
Enzyme 90 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 122937307 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID P0C7M7 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name ACSM4_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >1743 bp
ATGAAGATTTTTTTCCGCTACCAGACATTTAGATTCATCTGGCTCACCAAGCCACCTGGC
CGGCGCTTACACAAAGATCACCAGCTTTGGACGCCTCTGACTCTTGCTGACTTTGAAGCC
ATAAATCGCTGTAACAGGCCATTGCCTAAAAACTTTAACTTTGCTGCAGATGTGCTGGAC
CAGTGGTCCCAAAAGGAGAAGACAGGGGAGAGACCAGCTAACCCAGCCCTGTGGTGGGTG
AATGGCAAAGGGGATGAGGTAAAATGGAGCTTCAGAGAACTGGGCTCCTTGTCCCGAAAA
GCTGCCAACGTGCTCACCAAGCCCTGTGGCCTGCAGAGAGGAGACCGTTTGGCCGTGATT
CTGCCCAGAATCCCTGAGTGGTGGCTGGTCAATGTAGCTTGCATACGAACAGGGATCATC
TTCATGCCGGGAACAATCCAGCTGACAGCAAAAGACATCCTCTACCGGCTGCGAGCATCC
AAGGCCAAGTGCATTGTGGCCAGTGAGGAGGTGGCCCCAGCGGTGGAGTCCATTGTATTG
GAGTGTCCTGACCTTAAGACAAAACTCCTGGTGTCTCCACAAAGCTGGAATGGGTGGCTC
AGCTTCCAGGAGTTATTTCAATTCGCCTCTGAAGAGCACAGCTGTGTGGAAACAGGAAGT
CAAGAACCAATGACCATTTATTTCACCAGTGGGACCACAGGCTTTCCTAAAATGGCCCAG
CACTCTCAGAGCAGCCTCGGCATTGGGTTCACCCTCTGCGGAAGGTATTGGCTGGACTTG
AAGTCCTCAGATATCATATGGAATATGTCTGACACGGGCTGGGTCAAGGCCGCCATTGGC
AGTGTGTTTTCTTCCTGGCTGTGTGGAGCCTGTGTTTTTGTGCATCGAATGGCACAGTTT
GACACTGACACCTTCCTAGACACACTTACTACTTATCCCATCACGACCCTGTGCAGTCCT
CCCACTGTGTACCGGATGCTCGTGCAAAAAGACCTTAAGAGATATAAATTCAAGAGTCTG
CGGCACTGCTTGACCGGAGGGGAGCCACTCAACCCAGAAGTGCTGGAGCAGTGGAGGGTG
CAAACTGGGCTGGAGCTATATGAGGGCTATGGACAGACGGAAGTGGGAATGATTTGTGCC
AATCAGAAAGGCCAAGAAATTAAACCAGGTTCAATGGGGAAAGGAATGCTGCCCTATGAT
GTCCAGATTATAGATGAAAATGGCAATGTTCTACCACCTGGCAAAGAAGGGGAAATTGCC
CTCAGACTCAAACCTACACGGCCCTTCTGTTTCTTCTCTAAATATGTGGACAATCCACAG
AAAACTGCTGCCACGATAAGAGGAGATTTTTATGTCACTGGAGACAGAGGAGTGATGGAC
AGTGATGGGTATTTCTGGTTTGTCGGCAGAGCTGATGATGTCATTATATCCTCTGGGTAC
CGTATTGGGCCATTTGAAGTGGAGAGTGCACTCATTGAGCATCCAGCAGTTGTTGAATCG
GCTGTTGTCAGTAGTCCAGATCAAATCCGCGGAGAGGTGGTGAAAGCTTTTGTTGTCTTA
GCTGCACCCTTTAAGTCCTACAACCCAGAGAAATTAACTCTTGAACTTCAGGATCATGTG
AAAAAATCAACTGCACCTTACAAATATCCAAGAAAGGTGGAATTTGTTCAAGAACTCCCA
AAGACAATCACTGGGAAAATCAAACGCAACGTTTTAAGAGACCAAGAATGGAGAGGAAGA
TAG
Enzyme 90 GenBank Gene ID NM_001080454.1 Link Image
Enzyme 90 GeneCard ID ACSM4 Link Image
Enzyme 90 GenAtlas ID ACSM4 Link Image
Enzyme 90 HGNC ID HGNC:32016 Link Image
Enzyme 90 Chromosome Location 1
Enzyme 90 Locus 12p13.31
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  2. Watkins PA, Maiguel D, Jia Z, Pevsner J: Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J Lipid Res. 2007 Dec;48(12):2736-50. Epub 2007 Aug 30. [PubMed Link Image]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 16856
Enzyme 91 Name Glycerol-3-phosphate acyltransferase 2, mitochondrial
Enzyme 91 Synonyms
  1. GPAT-2
  2. xGPAT1
Enzyme 91 Gene Name GPAT2
Enzyme 91 Protein Sequence >Glycerol-3-phosphate acyltransferase 2, mitochondrial
MATMLEGRCQTQPRSSPSGREASLWSSGFGMKLEAVTPFLGKYRPFVGRCCQTCTPKSWE
SLFHRSITDLGFCNVILVKEENTRFRGWLVRRLCYFLWSLEQHIPPCQDVPQKIMESTGV
QNLLSGRVPGGTGEGQVPDLVKKEVQRILGHIQAPPRPFLVRLFSWALLRFLNCLFLNVQ
LHKGQMKMVQKAAQAGLPLVLLSTHKTLLDGILLPFMLLSQGLGVLRVAWDSRACSPALR
ALLRKLGGLFLPPEASLSLDSSEGLLARAVVQAVIEQLLVSGQPLLIFLEEPPGALGPRL
SALGQAWVGFVVQAVQVGIVPDALLVPVAVTYDLVPDAPCDIDHASAPLGLWTGALAVLR
SLWSRWGCSHRICSRVHLAQPFSLQEYIVSARSCWGGRQTLEQLLQPIVLGQCTAVPDTE
KEQEWTPITGPLLALKEEDQLLVRRLSCHVLSASVGSSAVMSTAIMATLLLFKHQKLLGE
FSWLTEEILLRGFDVGFSGQLRSLLQHSLSLLRAHVALLRIRQGDLLVVPQPGPGLTHLA
QLSAELLPVFLSEAVGACAVRGLLAGRVPPQGPWELQGILLLSQNELYRQILLLMHLLPQ
DLLLLKPCQSSYCYCQEVLDRLIQCGLLVAEETPGSRPACDTGRQRLSRKLLWKPSGDFT
DSDSDDFGEADGRYFRLSQQSHCPDFFLFLCRLLSPLLKAFAQAAAFLRQGQLPDTELGY
TEQLFQFLQATAQEEGIFECADPKLAISAVWTFRDLGVLQQTPSPAGPRLHLSPTFASLD
NQEKLEQFIRQFICS
Enzyme 91 Number of Residues 795
Enzyme 91 Molecular Weight 87834.5
Enzyme 91 Theoretical pI 7.63
Enzyme 91 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • metabolic process
Component
Enzyme 91 General Function Involved in acyltransferase activity
Enzyme 91 Specific Function Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis
Enzyme 91 Pathways Not Available
Enzyme 91 Reactions
  • acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate [RN:R00851]
Enzyme 91 Pfam Domain Function Not Available
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • 159-179 452-472
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 116812614 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q6NUI2 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name GPAT2_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >2388 bp
ATGGCCACCATGTTGGAAGGCAGATGCCAAACTCAGCCAAGGAGCAGCCCCAGTGGCCGA
GAGGCTAGCCTGTGGTCGTCAGGCTTTGGGATGAAGCTGGAGGCTGTCACTCCATTCCTG
GGGAAGTATCGCCCCTTTGTGGGTCGCTGTTGCCAGACCTGCACCCCCAAGAGCTGGGAG
TCCCTCTTCCACAGAAGCATAACGGACCTAGGCTTCTGCAATGTGATCCTGGTGAAGGAG
GAGAACACAAGGTTTCGGGGCTGGCTGGTTCGGAGGCTCTGCTATTTCCTGTGGTCCCTG
GAGCAGCACATCCCCCCCTGCCAGGATGTCCCACAGAAGATCATGGAAAGCACCGGGGTG
CAGAACCTCCTCTCAGGGAGGGTCCCAGGAGGCACTGGGGAAGGCCAGGTGCCTGACCTT
GTGAAGAAGGAGGTACAGCGCATCCTGGGTCACATCCAGGCCCCACCCCGTCCCTTCCTG
GTCAGGCTGTTCAGCTGGGCGCTGCTGAGGTTCCTGAACTGCCTGTTCCTGAATGTGCAG
CTCCACAAGGGTCAGATGAAGATGGTCCAGAAGGCCGCCCAGGCAGGCTTGCCGCTTGTC
CTCCTCTCTACTCACAAAACCCTCCTGGATGGGATCCTGCTGCCCTTTATGCTGCTCTCC
CAGGGCCTGGGTGTGCTTCGTGTGGCCTGGGACTCCCGCGCCTGCTCCCCTGCCCTCAGA
GCTCTGCTGAGGAAGCTTGGGGGGCTTTTCCTGCCCCCAGAGGCCAGCCTCTCCCTGGAC
AGCTCTGAGGGGCTCCTTGCCAGGGCTGTGGTCCAGGCGGTCATAGAGCAGCTGCTGGTT
AGTGGGCAGCCCCTGCTCATCTTCCTGGAGGAACCTCCTGGGGCTCTGGGGCCACGGCTG
TCAGCCCTGGGCCAGGCTTGGGTGGGGTTTGTGGTGCAGGCAGTCCAGGTGGGCATCGTC
CCAGATGCTCTGCTGGTACCAGTGGCCGTCACCTATGACCTGGTTCCGGATGCACCGTGT
GACATAGACCATGCCTCGGCCCCCCTGGGGCTGTGGACAGGAGCTCTGGCTGTCCTACGT
AGCTTGTGGAGCCGCTGGGGCTGCAGCCACCGGATCTGCTCCCGGGTGCACCTAGCTCAG
CCCTTTTCCCTGCAGGAATACATCGTCAGTGCCAGAAGCTGCTGGGGCGGCAGACAGACC
CTGGAGCAGCTACTGCAGCCCATCGTGCTGGGCCAATGTACTGCTGTCCCAGACACTGAG
AAGGAGCAGGAGTGGACCCCCATAACTGGGCCTCTCCTGGCCCTCAAGGAAGAGGACCAG
CTCCTGGTCAGGAGACTGAGCTGTCATGTCCTGAGTGCCAGTGTAGGGAGCTCTGCGGTG
ATGAGCACGGCCATTATGGCAACGCTGCTGCTCTTCAAGCATCAGAAGCTCCTGGGGGAG
TTCTCCTGGCTGACGGAGGAGATACTGTTGCGTGGCTTTGATGTAGGCTTCTCTGGGCAG
CTGCGGAGCCTGCTGCAGCACTCACTGAGCCTGCTGCGGGCGCACGTGGCCCTGCTGCGC
ATCCGTCAGGGTGACTTGCTGGTGGTGCCGCAGCCTGGCCCAGGCCTCACACACCTGGCA
CAACTGAGTGCTGAGCTGCTGCCCGTCTTCCTGAGCGAGGCTGTGGGCGCCTGTGCAGTG
CGGGGGCTGCTGGCAGGCAGAGTGCCGCCCCAGGGGCCCTGGGAGCTGCAGGGCATATTG
CTGCTGAGCCAGAATGAGCTGTACCGCCAGATCCTGCTGCTGATGCACCTGCTGCCGCAA
GACCTGCTGCTGCTAAAGCCCTGCCAGTCTTCCTACTGCTACTGTCAGGAGGTGCTGGAC
CGGCTCATCCAATGCGGGCTCCTGGTTGCTGAGGAGACCCCAGGCTCCCGGCCAGCCTGT
GACACAGGGCGACAGCGATTGAGCAGAAAGCTGCTGTGGAAACCGAGTGGGGACTTTACT
GATAGTGACAGTGATGACTTCGGAGAGGCTGACGGCCGGTACTTCAGGCTCAGCCAGCAG
TCACACTGCCCAGATTTCTTTCTTTTCCTCTGCCGCCTGCTCAGCCCGCTGCTCAAGGCC
TTTGCACAGGCTGCCGCCTTCCTCCGCCAGGGCCAGCTGCCCGATACTGAGTTGGGCTAC
ACAGAGCAGCTGTTCCAGTTCCTGCAGGCCACCGCCCAGGAAGAAGGGATCTTCGAGTGT
GCGGACCCAAAGCTCGCCATCAGTGCTGTCTGGACCTTCAGAGACCTAGGGGTTCTGCAG
CAGACGCCGAGCCCTGCAGGCCCCAGGCTCCACCTGTCCCCTACTTTTGCCAGCCTGGAC
AATCAGGAAAAACTAGAACAGTTCATCCGGCAGTTCATTTGTAGCTAG
Enzyme 91 GenBank Gene ID NM_207328.2 Link Image
Enzyme 91 GeneCard ID GPAT2 Link Image
Enzyme 91 GenAtlas ID GPAT2 Link Image
Enzyme 91 HGNC ID HGNC:27168 Link Image
Enzyme 91 Chromosome Location 2
Enzyme 91 Locus 2q11.1
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 17317
Enzyme 92 Name Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
Enzyme 92 Synonyms Not Available
Enzyme 92 Gene Name Not Available
Enzyme 92 Protein Sequence >Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
MNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINK
AKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGI
TKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPP
GGVEEKARNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHT
PFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEV
WTRLKAFAKLPPNALRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSR
KSKL
Enzyme 92 Number of Residues 364
Enzyme 92 Molecular Weight 40210.7
Enzyme 92 Theoretical pI 9.12
Enzyme 92 GO Classification
Function
  • acyl-CoA binding
  • binding
  • catalytic activity
  • fatty acid binding
  • lipid binding
Process
  • metabolic process
Component
Enzyme 92 General Function Involved in acyl-CoA binding
Enzyme 92 Specific Function Not Available
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions Not Available
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • None
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 62897567 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID Q53GC8 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name Q53GC8_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >1095 bp
ATGAATAGAACAGCAATGAGAGCCAGTCAGAAGGACTTTGAAAATTCAATGAATCAAGTG
AAACTCTTGAAAAAGGATCCAGGAAACGAAGTGAAGCTAAAACTCTACGCGCTATATAAG
CAGGCCACTGAAGGACCTTGTAACATGCCCAAACCAGGTGTATTTGACTTGATCAACAAG
GCCAAATGGGACGCATGGAATGCCCTTGGCAGCCTGCCCAAGGAAGCTGCCAGGCAGAAC
TATGTGGATTTGGTGTCCAGTTTGAGTCCTTCATTGGAATCCTCTAGTCAGGTGGAGCCT
GGAACAGACAGGAAATCAACTGGGTTTGAAACTCTGGTGGTGACCTCCGAAGATGGCATC
ACAAAGATCATGTTCAACCGGCCCAAAAAGAAAAATGCCATAAACACTGAGATGTATCAT
GAAATTATGCGTGCACTTAAAGCTGCCAGCAAGGATGACTCAATCATCACTGTTTTAACA
GGAAATGGTGACTATTACAGTAGTGGGAATGATCTGACTAACTTCACTGATATTCCCCCT
GGTGGAGTAGAGGAGAAAGCTAGAAATAATGCCGTTTTACTGAGGGAATTTGTGGGCTGT
TTTATAGATTTTCCTAAGCCTCTGATTGCAGTGGTCAATGGTCCAGCTGTGGGCATCTCC
GTCACCCTCCTTGGGCTATTCGATGCCGTGTATGCATCTGACAGGGCAACATTTCATACA
CCATTTAGTCACCTAGGCCAAAGTCCGGAAGGATGCTCCTCTTACACTTTTCCGAAGATA
ATGAGCCCAGCCAAGGCAACAGAGATGCTTATTTTTGGAAAGAAGTTAACAGCGGGAGAG
GCATGTGCTCAAGGACTTGTTACTGAAGTTTTCCCTGATAGCACTTTTCAGAAAGAAGTC
TGGACCAGGCTGAAGGCATTTGCAAAGCTTCCCCCAAATGCCTTGAGAATTTCAAAAGAG
GTAATCAGGAAAAGAGAGAGAGAAAAACTACACGCTGTTAATGCTGAAGAATGCAATGTC
CTTCAGGGAAGATGGCTATCAGATGAATGCACAAATGCTGTGGTGAACTTCTTATCCAGA
AAATCAAAACTGTGA
Enzyme 92 GenBank Gene ID AK223003 Link Image
Enzyme 92 GeneCard ID Not Available
Enzyme 92 GenAtlas ID Not Available
Enzyme 92 HGNC ID HGNC:14601 Link Image
Enzyme 92 Chromosome Location Not Available
Enzyme 92 Locus Not Available
Enzyme 92 SNPs Not Available
Enzyme 92 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 17318
Enzyme 93 Name cDNA FLJ56683, highly similar to Peroxisomal 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8)
Enzyme 93 Synonyms Not Available
Enzyme 93 Gene Name Not Available
Enzyme 93 Protein Sequence >cDNA FLJ56683, highly similar to Peroxisomal 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8)
MNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINK
AKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGI
TKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPP
GGVEEKAKNNAVLLR
Enzyme 93 Number of Residues 195
Enzyme 93 Molecular Weight 21565.3
Enzyme 93 Theoretical pI 9.26
Enzyme 93 GO Classification
Function
  • acyl-CoA binding
  • binding
  • catalytic activity
  • fatty acid binding
  • lipid binding
Process
  • metabolic process
Component
Enzyme 93 General Function Involved in acyl-CoA binding
Enzyme 93 Specific Function Not Available
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions Not Available
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 194386022 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID B4DLL3 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name B4DLL3_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >588 bp
ATGAATAGAACAGCAATGAGAGCCAGTCAGAAGGACTTTGAAAATTCAATGAATCAAGTG
AAACTCTTGAAAAAGGATCCAGGAAACGAAGTGAAGCTAAAACTCTACGCGCTATATAAG
CAGGCCACTGAAGGACCTTGTAACATGCCCAAACCAGGTGTATTTGACTTGATCAACAAG
GCCAAATGGGACGCATGGAATGCCCTTGGCAGCCTGCCCAAGGAAGCTGCCAGGCAGAAC
TATGTGGATTTGGTGTCCAGTTTGAGTCCTTCATTGGAATCCTCTAGTCAGGTGGAGCCT
GGAACAGACAGGAAATCAACTGGGTTTGAAACTCTGGTGGTGACCTCCGAAGATGGCATC
ACAAAGATCATGTTCAACCGGCCCAAAAAGAAAAATGCCATAAACACTGAGATGTATCAT
GAAATTATGCGTGCACTTAAAGCTGCCAGCAAGGATGACTCAATCATCACTGTTTTAACA
GGAAATGGTGACTATTACAGTAGTGGGAATGATCTGACTAACTTCACTGATATTCCCCCT
GGTGGAGTAGAGGAGAAAGCTAAAAATAATGCCGTTTTACTGAGGTAA
Enzyme 93 GenBank Gene ID AK297049 Link Image
Enzyme 93 GeneCard ID Not Available
Enzyme 93 GenAtlas ID Not Available
Enzyme 93 HGNC ID HGNC:14601 Link Image
Enzyme 93 Chromosome Location Not Available
Enzyme 93 Locus Not Available
Enzyme 93 SNPs Not Available
Enzyme 93 General References Not Available
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 17319
Enzyme 94 Name Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
Enzyme 94 Synonyms Not Available
Enzyme 94 Gene Name Not Available
Enzyme 94 Protein Sequence >Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
MNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINK
AKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGI
TKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPP
GGVGEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHT
PFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEV
WTRLKAFAKLPPNALRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSR
KSKL
Enzyme 94 Number of Residues 364
Enzyme 94 Molecular Weight 40110.7
Enzyme 94 Theoretical pI 9.28
Enzyme 94 GO Classification
Function
  • acyl-CoA binding
  • binding
  • catalytic activity
  • fatty acid binding
  • lipid binding
Process
  • metabolic process
Component
Enzyme 94 General Function Involved in acyl-CoA binding
Enzyme 94 Specific Function Not Available
Enzyme 94 Pathways Not Available
Enzyme 94 Reactions Not Available
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 62896793 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID Q53HG3 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name Q53HG3_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >1095 bp
ATGAATAGAACAGCAATGAGAGCCAGTCAGAAGGACTTTGAAAATTCAATGAATCAAGTG
AAACTCTTGAAAAAGGATCCAGGAAACGAAGTGAAGCTAAAACTCTACGCGCTATATAAG
CAGGCCACTGAAGGACCTTGTAACATGCCCAAACCAGGTGTATTTGACTTGATCAACAAG
GCCAAATGGGACGCATGGAATGCCCTTGGCAGCCTGCCCAAGGAAGCTGCCAGGCAGAAC
TATGTGGATTTGGTGTCCAGTTTGAGTCCTTCATTGGAATCCTCTAGTCAGGTGGAGCCT
GGAACAGACAGGAAATCAACTGGGTTTGAAACTCTGGTGGTGACCTCCGAAGATGGCATC
ACAAAGATCATGTTCAACCGGCCCAAAAAGAAAAATGCCATAAACACTGAGATGTATCAT
GAAATTATGCGTGCACTTAAAGCTGCCAGCAAGGATGACTCAATCATCACTGTTTTAACA
GGAAATGGTGACTATTACAGTAGTGGGAATGATCTGACTAACTTCACTGATATTCCCCCT
GGTGGAGTAGGGGAGAAAGCTAAAAATAATGCCGTTTTACTGAGGGAATTTGTGGGCTGT
TTTATAGATTTTCCTAAGCCTCTGATTGCAGTGGTCAATGGTCCAGCTGTGGGCATCTCC
GTCACCCTCCTTGGGCTATTCGATGCCGTGTATGCATCTGACAGGGCAACATTTCATACA
CCATTTAGTCACCTAGGCCAAAGTCCGGAAGGATGCTCCTCTTACACTTTTCCGAAGATA
ATGAGCCCAGCCAAGGCAACAGAGATGCTTATTTTTGGAAAGAAGTTAACAGCGGGAGAG
GCATGTGCTCAAGGACTTGTTACTGAAGTTTTCCCTGATAGCACTTTTCAGAAAGAAGTC
TGGACCAGGCTGAAGGCATTTGCAAAGCTTCCCCCAAATGCCTTGAGAATTTCAAAAGAG
GTAATCAGGAAAAGAGAGAGAGAAAAACTACACGCTGTTAATGCTGAAGAATGCAATGTC
CTTCAGGGAAGATGGCTATCAGATGAATGCACAAATGCTGTGGTGAACTTCTTATCCAGA
AAATCAAAACTGTGA
Enzyme 94 GenBank Gene ID AK222617 Link Image
Enzyme 94 GeneCard ID Not Available
Enzyme 94 GenAtlas ID Not Available
Enzyme 94 HGNC ID HGNC:14601 Link Image
Enzyme 94 Chromosome Location Not Available
Enzyme 94 Locus Not Available
Enzyme 94 SNPs Not Available
Enzyme 94 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 17320
Enzyme 95 Name Nef-associated protein 1
Enzyme 95 Synonyms
  1. Thioesterase NAP1
Enzyme 95 Gene Name C9orf156
Enzyme 95 Protein Sequence >Nef-associated protein 1
MRGLEESGPRPTATPCGCVKPALETGNLLTEPVGYLESCFSAKNGTPRQPSICSYSRACL
RIRKRIFNNPEHSLMGLEQFSHVWILFVFHKNGHLSCKAKVQPPRLNGAKTGVFSTRSPH
RPNAIGLTLAKLEKVEGGAIYLSGIDMIHGTPVLDIKPYIAEYDSPQNVMEPLADFNLQN
NQHTPNTVSQSDSKTDSCDQRQLSGCDEPQPHHSTKRKPKCPEDRTSEENYLTHSDTARI
QQAFPMHREIAVDFGLESRRDQSSSVAEEQIGPYCPEKSFSEKGTDKKLERVEGAAVLQG
SRAETQPMAPHCPAGRADGAPRSVVPAWVTEAPVATLEVRFTPHAEMDLGQLSSQDVGQA
SFKYFQSAEEAKRAIEAVLSADPRSVYRRKLCQDRLFYFTVDIAHVTCWFGDGFAEVLRI
KPASEPVHMTGPVGSLVSLGS
Enzyme 95 Number of Residues 441
Enzyme 95 Molecular Weight 48586.5
Enzyme 95 Theoretical pI 7.18
Enzyme 95 GO Classification Not Available
Enzyme 95 General Function Involved in hydrolase activity
Enzyme 95 Specific Function Hydrolyzes acyl-CoA thioesters (in vitro). Has a preference for substrates with medium chain length (C10-C14). Inactive towards substrates with C18 or C20 aliphatic chains. Its physiological function is not known
Enzyme 95 Pathways Not Available
Enzyme 95 Reactions Not Available
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 7020150 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID Q9BU70 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name NAP1_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >1326 bp
ATGCGCGGCTTGGAGGAGCCGGGGCCTCGGCCTACAGCGACCCCGTGCGGCTGCGTGAAG
CCGGCTCTGGAGACAGGGAATCTTTTAACTGAGCCAGTCGGCTACTTGGAATCTTGTTTC
TCGGCCAAGAATGGTACTCCAAGACAGCCATCCATTTGTAGCTATTCTCGAGCCTGTTTG
AGGATTAGAAAGAGGATCTTTAATAATCCTGAACATTCCTTGATGGGCCTAGAACAGTTT
TCTCATGTTTGGATTTTGTTTGTTTTTCACAAAAATGGTCATTTGAGCTGTAAGGCAAAA
GTGCAGCCTCCTAGACTGAATGGTGCAAAGACTGGAGTTTTTTCCACAAGGAGCCCTCAT
CGTCCCAATGCAATAGGACTGACCCTGGCCAAGCTGGAAAAGGTAGAAGGTGGAGCTATA
TACCTTTCTGGAATTGACATGATACATGGCACACCCGTACTAGACATCAAGCCCTACATA
GCTGAGTATGACTCACCGCAAAATGTGATGGAGCCTTTAGCAGACTTTAATTTACAGAAT
AACCAACATACACCAAACACTGTGTCCCAGTCTGACAGCAAGACTGACAGCTGTGACCAG
CGACAGCTCTCAGGGTGTGATGAGCCACAACCCCACCATAGCACTAAGAGGAAACCTAAA
TGTCCTGAAGACAGAACTTCAGAAGAAAACTACCTGACACACAGTGACACAGCCAGAATT
CAGCAAGCATTTCCTATGCACAGGGAGATAGCAGTGGATTTTGGTTTGGAATCAAGACGT
GATCAGAGTTCCAGCGTGGCAGAAGAACAAATTGGCCCATATTGCCCAGAGAAGAGCTTT
TCAGAGAAAGGTACAGACAAGAAGCTAGAAAGAGTGGAAGGAGCAGCAGTCTTGCAAGGA
AGCAGGGCAGAGACACAGCCCATGGCCCCTCACTGCCCTGCTGGAAGGGCTGATGGAGCT
CCCCGCAGCGTGGTTCCTGCCTGGGTGACAGAGGCTCCTGTGGCCACTTTAGAAGTGCGG
TTTACTCCTCATGCCGAGATGGACCTTGGGCAGCTCAGTTCACAAGATGTTGATCAGGCG
TCATTTAAATATTTTCAGTCAGCAGAGGAAGCAAAGCGTGCCATTGAGGCTGTGCTGTCA
GCGGATCCTCGGTCTGTGTACCGCCGGAAGCTTTGCCAGGACCGCCTTTTCTACTTTACT
GTAGACATAGCGCATGTCACTTGCTGGTTTGGTGATGGCTTTGCAGAGGTGCTGAGGATC
AAGCCGGCTTCTGAGCCTGTTCATATGACTGGCCCTGTGGGGTCCTTGGTGTCTCTAGGG
TCTTAA
Enzyme 95 GenBank Gene ID AK000213 Link Image
Enzyme 95 GeneCard ID C9orf156 Link Image
Enzyme 95 GenAtlas ID C9orf156 Link Image
Enzyme 95 HGNC ID HGNC:30967 Link Image
Enzyme 95 Chromosome Location 9
Enzyme 95 Locus 9q22.33
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  5. Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 17321
Enzyme 96 Name Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
Enzyme 96 Synonyms Not Available
Enzyme 96 Gene Name Not Available
Enzyme 96 Protein Sequence >Peroxisomal D3,D2-enoyl-CoA isomerase isoform 1 variant
EQLEIRLQKCEGWEQIEISLPNCSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLL
KKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVD
LVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIM
RALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLR
Enzyme 96 Number of Residues 232
Enzyme 96 Molecular Weight 25830.2
Enzyme 96 Theoretical pI 7.34
Enzyme 96 GO Classification
Function
  • acyl-CoA binding
  • binding
  • catalytic activity
  • fatty acid binding
  • lipid binding
Process
  • metabolic process
Component
Enzyme 96 General Function Involved in acyl-CoA binding
Enzyme 96 Specific Function Not Available
Enzyme 96 Pathways Not Available
Enzyme 96 Reactions Not Available
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 62089420 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q59E94 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name Q59E94_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >699 bp
GAACAATTAGAAATCAGGCTGCAGAAATGTGAGGGTTGGGAACAAATAGAAATCAGTCTG
CCTAATTGTAGTTCTCTGCAGGTCACTAGTTTCCCGGTAGTTCAGCTGCACATGAATAGA
ACAGCAATGAGAGCCAGTCAGAAGGACTTTGAAAATTCAATGAATCAAGTGAAACTCTTG
AAAAAGGATCCAGGAAACGAAGTGAAGCTAAAACTCTACGCGCTATATAAGCAGGCCACT
GAAGGACCTTGTAACATGCCCAAACCAGGTGTATTTGACTTGATCAACAAGGCCAAATGG
GACGCATGGAATGCCCTTGGCAGCCTGCCCAAGGAAGCTGCCAGGCAGAACTATGTGGAT
TTGGTGTCCAGTTTGAGTCCTTCATTGGAATCCTCTAGTCAGGTGGAGCCTGGAACAGAC
AGGAAATCAACTGGGTTTGAAACTCTGGTGGTGACCTCCGAAGATGGCATCACAAAGATC
ATGTTCAACCGGCCCAAAAAGAAAAATGCCATAAACACTGAGATGTATCATGAAATTATG
CGTGCACTTAAAGCTGCCAGCAAGGATGACTCAATCATCACTGTTTTAACAGGAAATGGT
GACTATTACAGTAGTGGGAATGATCTGACTAACTTCACTGATATTCCCCCTGGTGGAGTA
GAGGAGAAAGCTAAAAATAATGCCGTTTTACTGAGGTAA
Enzyme 96 GenBank Gene ID AB209917 Link Image
Enzyme 96 GeneCard ID Not Available
Enzyme 96 GenAtlas ID Not Available
Enzyme 96 HGNC ID HGNC:14601 Link Image
Enzyme 96 Chromosome Location Not Available
Enzyme 96 Locus Not Available
Enzyme 96 SNPs Not Available
Enzyme 96 General References Not Available
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 17322
Enzyme 97 Name Acyl-coenzyme A thioesterase 9, mitochondrial
Enzyme 97 Synonyms
  1. Acyl-CoA thioesterase 9
  2. Acyl-CoA thioester hydrolase 9
Enzyme 97 Gene Name ACOT9
Enzyme 97 Protein Sequence >Acyl-coenzyme A thioesterase 9, mitochondrial
MRRAALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHEVRDKLREIVGASTNWRDHVKA
MEERKLLHSFLAKSQDGLPPRRMKDSYIEVLLPLGSEPELREKYLTVQNTVRFGRILEDL
DSLGVLICYMHNKIHSAKMSPLSIVTALVDKIDMCKKSLSPEQDIKFSGHVSWVGKTSME
VKMQMFQLHGDEFCPVLDATFVMVARDSENKGPAFVNPLIPESPEEEELFRQGELNKGRR
IAFSSTSLLKMAPSAEERTTIHEMFLSTLDPKTISFRSRVLPSNAVWMENSKLKSLEICH
PQERNIFNRIFGGFLMRKAYELAWATACSFGGSRPFVVAVDDIMFQKPVEVGSLLFLSSQ
VCFTQNNYIQVRVHSEVASLQEKQHTTTNVFHFTFMSEKEVPLVFPKTYGESMLYLDGQR
HFNSMSGPATLRKDYLVEP
Enzyme 97 Number of Residues 439
Enzyme 97 Molecular Weight 49901.3
Enzyme 97 Theoretical pI 8.82
Enzyme 97 GO Classification Not Available
Enzyme 97 General Function Lipid transport and metabolism
Enzyme 97 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 81295404 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID Q9Y305 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name ACOT9_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >1320 bp
ATGAGGCGGGCAGCACTGCGGCTTTGTGCCTTGGGCAAAGGGCAGCTTACTCCTGGAAGA
GGACTGACTCAAGGACCCCAGAACCCCAAGAAACAGGGAATCTTCCACATTCATGAAGTT
CGAGATAAGTTGCGGGAGATAGTAGGAGCATCCACAAACTGGAGAGACCATGTGAAGGCA
ATGGAAGAAAGGAAATTACTTCATAGTTTCTTGGCTAAATCACAGGATGGACTGCCTCCT
AGGAGAATGAAGGACAGTTATATTGAAGTTCTCTTGCCTTTGGGCAGTGAGCCTGAATTA
CGAGAGAAATATTTGACTGTTCAAAACACCGTAAGATTTGGCAGGATTCTTGAGGATCTT
GACAGCTTGGGAGTTCTTATTTGTTACATGCACAACAAAATCCACTCCGCCAAGATGTCT
CCTTTATCGATAGTTACAGCCCTGGTGGATAAGATTGATATGTGTAAGAAGAGCTTGAGC
CCAGAACAGGACATTAAGTTCAGTGGCCATGTTAGCTGGGTCGGGAAGACATCCATGGAA
GTGAAGATGCAAATGTTCCAGTTACATGGTGATGAATTTTGTCCTGTTTTGGATGCAACA
TTTGTAATGGTGGCTCGTGATTCTGAAAATAAAGGGCCGGCATTTGTAAATCCACTCATC
CCTGAAAGCCCAGAGGAAGAGGAGCTCTTTAGACAAGGGGAATTGAACAAGGGGAGAAGA
ATTGCCTTCAGCTCCACGTCGTTACTGAAAATGGCCCCCAGCGCTGAGGAGAGGACCACC
ATACATGAGATGTTTCTCAGCACACTGGATCCAAAGACTATAAGTTTTCGGAGTCGAGTT
TTACCCTCTAATGCAGTGTGGATGGAGAATTCAAAACTGAAGAGTTTGGAAATTTGCCAC
CCTCAGGAGCGGAACATTTTCAATCGGATCTTTGGTGGTTTCCTTATGAGGAAGGCATAT
GAACTTGCGTGGGCTACTGCTTGTAGCTTTGGTGGTTCTCGACCGTTTGTGGTAGCAGTA
GATGACATCATGTTTCAGAAACCTGTTGAGGTTGGCTCATTGCTCTTTCTTTCTTCACAG
GTATGCTTTACTCAGAATAATTATATTCAAGTCAGAGTACACAGTGAAGTGGCCTCCCTG
CAGGAGAAGCAGCATACAACCACCAATGTCTTTCATTTCACGTTCATGTCGGAAAAAGAA
GTGCCATTGGTTTTCCCAAAAACATATGGAGAGTCCATGTTGTACTTAGATGGGCAGCGG
CATTTCAACTCCATGAGTGGCCCAGCGACCTTGAGAAAGGACTACCTTGTGGAGCCCTAA
Enzyme 97 GenBank Gene ID NM_001033583.2 Link Image
Enzyme 97 GeneCard ID ACOT9 Link Image
Enzyme 97 GenAtlas ID ACOT9 Link Image
Enzyme 97 HGNC ID HGNC:17152 Link Image
Enzyme 97 Chromosome Location Not Available
Enzyme 97 Locus Not Available
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  5. Jones S, Zhang X, Parsons DW, Lin JC, Leary RJ, Angenendt P, Mankoo P, Carter H, Kamiyama H, Jimeno A, Hong SM, Fu B, Lin MT, Calhoun ES, Kamiyama M, Walter K, Nikolskaya T, Nikolsky Y, Hartigan J, Smith DR, Hidalgo M, Leach SD, Klein AP, Jaffee EM, Goggins M, Maitra A, Iacobuzio-Donahue C, Eshleman JR, Kern SE, Hruban RH, Karchin R, Papadopoulos N, Parmigiani G, Vogelstein B, Velculescu VE, Kinzler KW: Core signaling pathways in human pancreatic cancers revealed by global genomic analyses. Science. 2008 Sep 26;321(5897):1801-6. Epub 2008 Sep 4. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 17323
Enzyme 98 Name Acyl-CoA synthetase family member 3, mitochondrial
Enzyme 98 Synonyms Not Available
Enzyme 98 Gene Name ACSF3
Enzyme 98 Protein Sequence >Acyl-CoA synthetase family member 3, mitochondrial
MLPHVVLTFRRLGCALASCRLAPARHRGSGLLHTAPVARSDRSAPVFTRALAFGDRIALV
DQHGRHTYRELYSRSLRLSQEICRLCGCVGGDLREERVSFLCANDASYVVAQWASWMSGG
VAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVE
EPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILH
VLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKL
MEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEI
GMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREACSYTIHAEGDERGTKVTPGFEE
KEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSVDIIKTG
GYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNV
LAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFHPS
Enzyme 98 Number of Residues 576
Enzyme 98 Molecular Weight 64129.6
Enzyme 98 Theoretical pI 8.47
Enzyme 98 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 98 General Function Involved in catalytic activity
Enzyme 98 Specific Function Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. May have some preference toward very-long-chain substrates
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions Not Available
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 187761345 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID Q4G176 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name ACSF3_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1731 bp
ATGCTGCCCCATGTGGTGCTCACCTTCCGGCGCCTGGGCTGCGCCTTGGCGTCCTGCCGG
CTGGCGCCTGCGAGACACAGAGGAAGTGGTCTTCTGCACACAGCCCCAGTGGCCCGCTCG
GACAGGAGCGCCCCGGTGTTCACCCGTGCCCTGGCCTTTGGGGACAGAATCGCCCTGGTT
GACCAGCACGGCCGCCACACGTACAGGGAGCTTTATTCCCGCAGCCTTCGCCTGTCCCAG
GAGATCTGCAGGCTCTGCGGGTGTGTCGGCGGGGACCTCCGGGAGGAGAGGGTCTCCTTC
CTATGCGCTAACGATGCCTCCTACGTCGTGGCCCAGTGGGCGTCATGGATGAGTGGCGGT
GTGGCAGTCCCCCTCTACAGGAAGCATCCCGCGGCCCAGCTGGAGTATGTCATCTGCGAC
TCCCAGAGCTCTGTGGTCCTTGCCAGCCAGGAGTACCTGGAGCTCCTGAGCCCGGTGGTC
AGGAAGCTGGGGGTCCCGCTGCTGCCGCTCACACCAGCCATCTACACTGGAGCAGTAGAG
GAACCGGCAGAGGTCCCGGTCCCAGAGCAGGGATGGAGGAACAAGGGCGCCATGATCATC
TACACCAGTGGGACCACGGGGAGGCCCAAGGGCGTGCTGAGCACGCACCAAAACATCAGG
GCTGTGGTGACCGGGCTGGTCCACAAGTGGGCATGGACCAAAGACGACGTGATCCTCCAC
GTGCTCCCGCTGCACCACGTCCATGGTGTGGTCAACGCGCTGCTCTGTCCTCTCTGGGTG
GGAGCCACCTGTGTGATGATGCCTGAGTTCAGCCCTCAGCAGGTTTGGGAAAAGTTCTTA
AGTTCTGAAACGCCGCGGATCAATGTCTTTATGGCAGTGCCTACAATATACACCAAGCTG
ATGGAGTACTACGACAGGCATTTTACCCAGCCGCACGCCCAGGATTTCTTGCGTGCAGTT
TGTGAAGAAAAAATTAGGCTGATGGTCTCAGGCTCAGCTGCCCTGCCCCTCCCAGTGCTG
GAGAAGTGGAAGAACATCACGGGCCACACCCTGCTGGAGCGGTATGGCATGACCGAGATC
GGCATGGCTCTGTCCGGGCCCCTGACCACTGCCGTGCGCCTGCCAGGTTCCGTGGGGACC
CCACTGCCTGGAGTACAGGTGCGCATTGTCTCAGAAAACCCACAGAGGGAAGCCTGCTCC
TACACCATCCACGCAGAGGGAGACGAGAGGGGGACCAAGGTGACCCCAGGGTTTGAAGAA
AAGGAGGGGGAGCTGCTGGTGAGGGGACCCTCCGTGTTTCGAGAATACTGGAATAAACCA
GAAGAAACTAAGAGTGCATTCACCCTGGATGGCTGGTTTAAGACAGGGGACACCGTGGTG
TTTAAGGATGGCCAGTACTGGATCCGAGGCCGGACCTCAGTGGACATCATCAAGACTGGA
GGCTACAAGGTCAGCGCCCTGGAGGTGGAGTGGCACCTGCTGGCCCACCCCAGCATCACA
GATGTGGCTGTGATTGGAGTTCCGGATATGACATGGGGCCAGCGGGTCACTGCTGTGGTG
ACCCTCCGAGAAGGACACTCACTGTCCCACAGGGAGCTCAAAGAGTGGGCCAGAAATGTC
CTGGCCCCGTACGCGGTGCCCTCGGAGCTGGTGCTGGTGGAGGAGATCCCGCGGAACCAG
ATGGGCAAGATTGACAAGAAGGCGCTCATCAGGCACTTCCACCCCTCATGA
Enzyme 98 GenBank Gene ID NM_001127214.1 Link Image
Enzyme 98 GeneCard ID ACSF3 Link Image
Enzyme 98 GenAtlas ID ACSF3 Link Image
Enzyme 98 HGNC ID HGNC:27288 Link Image
Enzyme 98 Chromosome Location 1
Enzyme 98 Locus 16q24.3
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Watkins PA, Maiguel D, Jia Z, Pevsner J: Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J Lipid Res. 2007 Dec;48(12):2736-50. Epub 2007 Aug 30. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 17324
Enzyme 99 Name Acyl-coenzyme A thioesterase 1
Enzyme 99 Synonyms
  1. Acyl-CoA thioesterase 1
  2. CTE-I
  3. CTE-Ib
  4. Inducible cytosolic acyl-coenzyme A thioester hydrolase
  5. Long chain acyl-CoA thioester hydrolase
  6. Long chain acyl-CoA hydrolase
Enzyme 99 Gene Name ACOT1
Enzyme 99 Protein Sequence >Acyl-coenzyme A thioesterase 1
MAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLL
CRVRHERYFLPPGVRREPVRAGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAG
KGFAVMALAYYNYEDLPKTMETLHLEYFEEAVNYLLSHPEVKGPGVGLLGISKGGELCLS
MASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPL
EGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGH
YIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSK
V
Enzyme 99 Number of Residues 421
Enzyme 99 Molecular Weight 46277.0
Enzyme 99 Theoretical pI 7.37
Enzyme 99 GO Classification
Function
  • CoA hydrolase activity
  • acyl-CoA thioesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • palmitoyl-CoA hydrolase activity
  • thiolester hydrolase activity
Process
  • acyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 99 General Function Involved in thiolester hydrolase activity
Enzyme 99 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active towards fatty acyl-CoA with chain-lengths of C12-C16
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 121934111 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID Q86TX2 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name ACOT1_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1266 bp
ATGGCGGCGACGCTGATCCTGGAGCCCGCGGGCCGCTGCTGCTGGGACGAACCGGTGCGA
ATCGCCGTGCGCGGCCTAGCCCCGGAGCAGCCGGTCACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTTTTCCAGGCCCACGCGCGCTACCGCGCCGACACCCTTGGCGAGCTG
GACCTGGAGCGCGCGCCCGCGCTGGGCGGCAGCTTCGCGGGGCTTGAGCCCATGGGGCTG
CTCTGGGCCTTGGAGCCCGAGAAACCCTTGGTGCGGCTGGTGAAGCGCGACGTGCGAACG
CCCTTGGCCGTGGAGCTGGAGGTGCTGGATGGCCACGACCCCGACCCCGGGCGGCTGCTG
TGCCGGGTGCGGCACGAGCGCTACTTCCTCCCGCCCGGGGTGCGGCGCGAGCCGGTGCGC
GCGGGCCGGGTGCGAGGCACGCTCTTCCTGCCGCCAGAACCTGGGCCCTTTCCTGGCATT
GTGGACATGTTCGGAACTGGAGGTGGCCTGCTGGAGTATCGGGCTAGTCTGCTGGCTGGG
AAGGGTTTTGCTGTGATGGCTCTGGCTTACTATAACTATGAAGACCTCCCCAAGACCATG
GAGACGCTCCATCTGGAGTACTTTGAAGAAGCTGTGAACTACTTGCTCAGTCATCCTGAG
GTAAAAGGTCCAGGAGTTGGGCTGCTTGGAATTTCCAAAGGGGGTGAGCTCTGCCTTTCC
ATGGCCTCTTTCCTGAAGGGCATCACGGCTGCTGTCGTCATCAACGGCTCTGTGGCCAAT
GTTGGGGGAACCTTACGCTACAAGGGCGAGACCCTGCCCCCTGTGGGCGTCAACAGAAAT
CGCATCAAGGTGACCAAAGATGGCTATGCAGACATTGTGGATGTCCTGAACAGCCCTTTG
GAAGGACCTGACCAGAAGAGCTTCATTCCTGTGGAAAGGGCAGAGAGCACCTTCCTGTTC
CTGGTAGGTCAGGATGACCACAACTGGAAGAGTGAGTTCTATGCTAATGAGGCCTGTAAA
CGCTTGCAGGCCCATGGGAGGAGAAAGCCCCAGATCATCTGTTACCCAGAGACAGGGCAC
TATATTGAGCCTCCTTACTTCCCCCTGTGTCGGGCTTCCCTGCATGCCTTGGTGGGCAGT
CCTATTATCTGGGGAGGGGAGCCCAGGGCTCATGCCATGGCTCAGGTGGATGCTTGGAAA
CAACTCCAGACTTTCTTCCACAAACACTTGGGTGGCCACGAGGGGACAATCCCATCAAAA
GTGTAA
Enzyme 99 GenBank Gene ID BC127748 Link Image
Enzyme 99 GeneCard ID ACOT1 Link Image
Enzyme 99 GenAtlas ID ACOT1 Link Image
Enzyme 99 HGNC ID HGNC:33128 Link Image
Enzyme 99 Chromosome Location Not Available
Enzyme 99 Locus Not Available
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 17325
Enzyme 100 Name Cytosolic acyl coenzyme A thioester hydrolase-like
Enzyme 100 Synonyms
  1. Acyl-CoA thioesterase 7-like
Enzyme 100 Gene Name ACOT7L
Enzyme 100 Protein Sequence >Cytosolic acyl coenzyme A thioester hydrolase-like
MIKEAGAIISTRHCNPQNGDRCVAALARVECTHFLWPMCIGEVAHVSAEITYTSKHSVEV
QVNMMSENILTGAKKLTNKATLWYAPLSLTNVDKVLEEPPVVYFRQEQEEEGQKRYKTQK
LERMETNWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHSFVHEGVTMKVMDEVA
GILAARHCKTNLVTASMEAINFDNKIRKGCIKTISGRMTFTSNKSVEIEVLVDADCVVDS
SQKRYRAASVFT
Enzyme 100 Number of Residues 252
Enzyme 100 Molecular Weight 28164.1
Enzyme 100 Theoretical pI 7.18
Enzyme 100 GO Classification Not Available
Enzyme 100 General Function Lipid transport and metabolism
Enzyme 100 Specific Function Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions
  • palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 34531349 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID Q6ZUV0 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name BACHL_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >759 bp
ATGATCAAAGAGGCGGGCGCCATCATCAGCACCCGGCATTGCAATCCGCAGAACGGGGAT
CGCTGTGTGGCCGCTCTGGCTCGGGTCGAGTGCACCCACTTCCTGTGGCCCATGTGCATC
GGTGAGGTGGCCCACGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTG
CAGGTCAACATGATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCC
ACCCTCTGGTATGCGCCCCTGTCGCTGACGAACGTGGACAAGGTCCTCGAAGAGCCTCCT
GTTGTGTATTTCCGGCAGGAGCAGGAGGAGGAGGGCCAGAAGCGGTACAAAACCCAGAAG
CTGGAGCGCATGGAGACCAACTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCA
GAGCCGAACACTGTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGAC
TGTACCCTGCACAGCTTCGTGCATGAAGGGGTGACCATGAAGGTCATGGACGAGGTCGCC
GGGATCTTGGCTGCACGCCACTGCAAGACCAACCTCGTCACAGCCTCCATGGAGGCCATT
AATTTTGACAACAAGATCAGAAAAGGCTGCATCAAGACCATCTCCGGACGCATGACCTTC
ACGAGCAATAAGTCCGTAGAGATCGAGGTCTTGGTGGATGCCGACTGTGTTGTGGACAGC
TCTCAGAAGCGCTACAGGGCCGCCAGTGTCTTCACCTAA
Enzyme 100 GenBank Gene ID AK125299 Link Image
Enzyme 100 GeneCard ID ACOT7L Link Image
Enzyme 100 GenAtlas ID Not Available
Enzyme 100 HGNC ID Not Available
Enzyme 100 Chromosome Location Not Available
Enzyme 100 Locus Not Available
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Jiang RC, Qin HD, Zeng MS, Huang W, Feng BJ, Zhang F, Chen HK, Jia WH, Chen LZ, Feng QS, Zhang RH, Yu XJ, Zheng MZ, Zeng YX: A functional variant in the transcriptional regulatory region of gene LOC344967 cosegregates with disease phenotype in familial nasopharyngeal carcinoma. Cancer Res. 2006 Jan 15;66(2):693-700. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 17326
Enzyme 101 Name Acyl-CoA synthetase family member 2, mitochondrial
Enzyme 101 Synonyms Not Available
Enzyme 101 Gene Name ACSF2
Enzyme 101 Protein Sequence >Acyl-CoA synthetase family member 2, mitochondrial
MAVYVGMLRLGRLCAGSSGVLGARAALSRSWQEARLQGVRFLSSREVDRMVSTPIGGLSY
VQGCTKKHLNSKTVGQCLETTAQRVPEREALVVLHEDVRLTFAQLKEEVDKAASGLLSIG
LCKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYVLKKVGCKALVFPKQ
FKTQQYYNVLKQICPEVENAQPGALKSQRLPDLTTVISVDAPLPGTLLLDEVVAAGSTRQ
HLDQLQYNQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNSNILGERLKLHEKTPEQ
LRMILPNPLYHCLGSVAGTMMCLMYGATLILASPIFNGKKALEAISRERGTFLYGTPTMF
VDILNQPDFSSYDISTMCGGVIAGSPAPPELIRAIINKINMKDLVVAYGTTENSPVTFAH
FPEDTVEQKAESVGRIMPHTEARIMNMEAGTLAKLNTPGELCIRGYCVMLGYWGEPQKTE
EAVDQDKWYWTGDVATMNEQGFCKIVGRSKDMIIRGGENIYPAELEDFFHTHPKVQEVQV
VGVKDDRMGEEICACIRLKDGEETTVEEIKAFCKGKISHFKIPKYIVFVTNYPLTISGKI
QKFKLREQMERHLNL
Enzyme 101 Number of Residues 615
Enzyme 101 Molecular Weight 68124.4
Enzyme 101 Theoretical pI 7.60
Enzyme 101 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 101 General Function Involved in catalytic activity
Enzyme 101 Specific Function Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipodyte differentiation
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 10436885 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q96CM8 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name ACSF2_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >1848 bp
ATGGCTGTCTACGTCGGGATGCTGCGCCTGGGGAGGCTGTGCGCCGGGAGCTCGGGGGTG
CTGGGGGCCCGGGCCGCCCTCTCTCGGAGTTGGCAGGAAGCCAGGTTGCAGGGTGTCCGC
TTCCTCAGTTCCAGAGAGGTGGATCGCATGGTCTCCACGCCCATCGGAGGCCTCAGCTAC
GTTCAGGGGTGCACCAAAAAGCATCTTAACAGCAAGACTGTGGGCCAGTGCCTGGAGACC
ACAGCACAGAGGGTCCCAGAACGAGAGGCCTTGGTCGTCCTCCATGAAGACGTCAGGTTG
ACCTTTGCCCAACTCAAGGAGGAGGTGGACAAAGCTGCTTCTGGCCTCCTGAGCATTGGC
CTCTGCAAAGGTGACCGGCTGGGCATGTGGGGACCTAACTCCTATGCATGGGTGCTCATG
CAGTTGGCCACCGCCCAGGCGGGCATCATTCTGGTGTCTGTGAACCCAGCCTACCAGGCT
ATGGAACTGGAGTATGTCCTCAAGAAGGTGGGCTGCAAGGCCCTTGTGTTCCCCAAGCAA
TTCAAGACCCAGCAATACTACAACGTCCTGAAGCAGATCTGTCCAGAAGTGGAGAATGCC
CAGCCAGGGGCCTTGAAGAGTCAGAGGCTCCCAGATCTGACCACAGTCATCTCGGTGGAT
GCCCCTTTGCCGGGGACCCTGCTCCTGGATGAAGTGGTGGCGGCTGGCAGCACACGGCAG
CATCTGGACCAGCTCCAATACAACCAGCAGTTCCTGTCCTGCCATGACCCCATCAACATC
CAGTTCACCTCGGGGACAACAGGCAGCCCCAAGGGGGCCACCCTCTCCCACTACAACATT
GTCAACAACTCCAACATTTTAGGAGAGCGCCTGAAACTGCATGAGAAGACACCAGAGCAG
TTGCGGATGATCCTGCCCAACCCCCTGTACCATTGCCTGGGTTCCGTGGCAGGCACAATG
ATGTGTCTGATGTACGGTGCCACCCTCATCCTGGCCTCTCCCATCTTCAATGGCAAGAAG
GCACTGGAGGCCATCAGCAGAGAGAGAGGCACCTTCCTGTATGGTACCCCCACGATGTTC
GTGGACATTCTGAACCAGCCAGACTTCTCCAGTTATGACATCTCGACCATGTGTGGAGGT
GTCATTGCTGGGTCCCCTGCACCTCCAGAGTTGATCCGAGCCATCATCAACAAGATAAAT
ATGAAGGACCTGGTGGTTGCTTATGGAACCACAGAGAACAGTCCCGTGACATTCGCGCAC
TTCCCTGAGGACACTGTGGAGCAGAAGGCAGAAAGCGTGGGCAGAATTATGCCTCACACG
GAGGCCCGGATCATGAACATGGAGGCAGGGACGCTGGCAAAGCTGAACACGCCCGGGGAG
CTGTGCATCCGAGGGTACTGCGTCATGCTGGGCTACTGGGGTGAGCCTCAGAAGACAGAG
GAAGCAGTGGATCAGGACAAGTGGTATTGGACAGGAGATGTCGCCACAATGAATGAGCAG
GGCTTCTGCAAGATCGTGGGCCGCTCTAAGGATATGATCATCCGGGGTGGTGAGAACATC
TACCCCGCAGAGCTCGAGGACTTCTTTCACACACACCCGAAGGTGCAGGAAGTGCAGGTG
GTGGGAGTGAAGGACGATCGGATGGGGGAAGAGATTTGTGCCTGCATTCGGCTGAAGGAC
GGGGAGGAGACCACGGTGGAGGAGATAAAAGCTTTCTGCAAAGGGAAGATCTCTCACTTC
AAGATTCCGAAGTACATCGTGTTTGTCACAAACTACCCCCTCACCATTTCAGGAAAGATC
CAGAAATTCAAACTTCGAGAGCAGATGGAACGACATCTAAATCTGTGA
Enzyme 101 GenBank Gene ID AK024573 Link Image
Enzyme 101 GeneCard ID ACSF2 Link Image
Enzyme 101 GenAtlas ID ACSF2 Link Image
Enzyme 101 HGNC ID HGNC:26101 Link Image
Enzyme 101 Chromosome Location 1
Enzyme 101 Locus 17q21.33
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Perera RJ, Marcusson EG, Koo S, Kang X, Kim Y, White N, Dean NM: Identification of novel PPARgamma target genes in primary human adipocytes. Gene. 2006 Mar 15;369:90-9. Epub 2005 Dec 27. [PubMed Link Image]
  5. Watkins PA, Maiguel D, Jia Z, Pevsner J: Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J Lipid Res. 2007 Dec;48(12):2736-50. Epub 2007 Aug 30. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 17327
Enzyme 102 Name Acyl-coenzyme A thioesterase 11
Enzyme 102 Synonyms
  1. Acyl-CoA thioesterase 11
  2. Acyl-CoA thioester hydrolase 11
  3. Adipose-associated thioesterase
  4. Brown fat-inducible thioesterase
  5. BFIT
Enzyme 102 Gene Name ACOT11
Enzyme 102 Protein Sequence >Acyl-coenzyme A thioesterase 11
MIQNVGNHLRRGLASVFSNRTSRKSALRAGNDSAMADGEGYRNPTEVQMSQLVLPCHTNQ
RGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFN
SSMEVGIQVASEDLCSEKQWNVCKALATFVARREITKVKLKQITPRTEEEKMEHSVAAER
RRMRLVYADTIKDLLANCAIQGDLESRDCSRMVPAEKTRVESVELVLPPHANHQGNTFGG
QIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGV
CVEAYRQEAETHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRL
DRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLED
DKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALG
GHTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQ
LTKCCWVRVSLTELVSASGFYSWGLESRSKGRRSDGWNGKLAGGHLSTLKAIPVAKINSR
FGYLQDT
Enzyme 102 Number of Residues 607
Enzyme 102 Molecular Weight 68491.6
Enzyme 102 Theoretical pI 8.43
Enzyme 102 GO Classification Not Available
Enzyme 102 General Function Lipid transport and metabolism
Enzyme 102 Specific Function Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 22165355 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID Q8WXI4 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name ACO11_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >1824 bp
ATGATCCAGAATGTCGGAAATCACCTGCGACGGGGCTTGGCCTCTGTGTTCTCCAACCGC
ACATCCCGGAAGTCAGCCTTACGTGCGGGGAACGACAGTGCCATGGCAGACGGCGAGGGA
TACCGGAACCCCACGGAGGTGCAGATGAGCCAGCTGGTGCTGCCCTGCCACACCAACCAA
CGTGGTGAGCTGAGCGTCGGGCAGCTGCTCAAGTGGATTGACACCACGGCTTGCCTGTCC
GCGGAGAGGCACGCTGGCTGCCCCTGTGTCACAGCTTCCATGGATGACATCTATTTTGAG
CACACCATTAGTGTTGGACAAGTGGTGAATATCAAGGCCAAGGTGAACCGGGCCTTCAAC
TCCAGCATGGAGGTGGGCATCCAGGTGGCCTCGGAGGACCTGTGCTCTGAGAAGCAGTGG
AATGTGTGCAAGGCCTTGGCCACCTTCGTGGCCCGCCGAGAGATCACCAAGGTGAAGCTG
AAGCAGATCACGCCGCGGACAGAAGAGGAGAAGATGGAGCACAGTGTGGCGGCTGAGCGC
CGGCGCATGCGCCTTGTCTATGCAGACACCATCAAGGACCTCCTGGCCAACTGCGCCATT
CAGGGCGATCTGGAGAGCAGAGACTGTAGCCGCATGGTGCCGGCTGAGAAGACCCGTGTG
GAGAGTGTGGAGCTGGTCCTGCCTCCCCACGCCAATCACCAGGGCAACACCTTTGGGGGC
CAGATCATGGCCTGGATGGAGAATGTGGCCACCATTGCAGCCAGCCGGCTCTGCCGTGCC
CACCCTACGCTGAAGGCCATTGAAATGTTCCACTTCCGAGGCCCGTCCCAGGTCGGCGAC
CGTCTGGTGCTCAAAGCCATCGTGAACAATGCCTTCAAACATAGCATGGAGGTGGGCGTG
TGCGTGGAGGCCTATCGCCAGGAGGCTGAGACCCACCGGCGCCACATCAACAGTGCCTTT
ATGACCTTTGTGGTCCTGGACGCAGATGACCAGCCCCAGTTGCTGCCCTGGATTCGGCCC
CAGCCCGGCGATGGTGAGCGGCGGTACCGAGAGGCCAGTGCCAGAAAGAAGATCCGCCTG
GACAGGAAGTACATCGTGTCCTGTAAGCAGACAGAGGTGCCCCTCTCCGTCCCCTGGGAC
CCTAGCAACCAGGTGTACCTGAGCTACAATAACGTCTCCTCCTTGAAGATGCTTGTGGCC
AAGGACAACTGGGTGCTGTCCTCGGAGATCAGTCAGGTCCGCCTGTACACTCTGGAGGAT
GACAAGTTCCTCTCCTTCCACATGGAGATGGTGGTGCATGTGGATGCAGCCCAGGCCTTC
CTGCTGCTCTCGGACCTGCGTCAGAGGCCAGAGTGGGACAAGCACTACCGGAGCGTGGAG
CTAGTGCAGCAGGTAGACGAGGACGACGCCATCTACCACGTCACCAGCCCTGCCCTCGGA
GGTCACACAAAGCCCCAGGACTTCGTGATCCTGGCCTCGAGGCGGAAGCCTTGTGACAAT
GGGGACCCCTATGTCATCGCGCTGAGGTCGGTCACGCTGCCCACACACCGAGAGACGCCA
GAGTACAGACGCGGAGAGACCCTCTGCTCAGGCTTCTGCCTCTGGCGCGAGGGGGACCAG
CTGACCAAGTGCTGCTGGGTTAGGGTCTCCCTGACTGAGCTGGTCTCGGCAAGTGGCTTC
TATTCCTGGGGGCTCGAATCCAGGTCAAAGGGTCGCAGGAGCGACGGTTGGAATGGAAAA
CTAGCTGGAGGACACCTGAGTACTCTTAAAGCAATCCCCGTGGCCAAAATCAACAGCCGA
TTTGGATACCTTCAAGACACCTGA
Enzyme 102 GenBank Gene ID NM_015547.3 Link Image
Enzyme 102 GeneCard ID ACOT11 Link Image
Enzyme 102 GenAtlas ID ACOT11 Link Image
Enzyme 102 HGNC ID HGNC:18156 Link Image
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 1p32.3
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Adams SH, Chui C, Schilbach SL, Yu XX, Goddard AD, Grimaldi JC, Lee J, Dowd P, Colman S, Lewin DA: BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity. Biochem J. 2001 Nov 15;360(Pt 1):135-42. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 17328
Enzyme 103 Name Long-chain-fatty-acid--CoA ligase ACSBG2
Enzyme 103 Synonyms
  1. Acyl-CoA synthetase bubblegum family member 2
  2. Bubblegum-related protein
  3. PRTD-NY3
Enzyme 103 Gene Name ACSBG2
Enzyme 103 Protein Sequence >Long-chain-fatty-acid--CoA ligase ACSBG2
MTGTPKTQEGAKDLEVDMNKTEVTPRLWTTCRDGEVLLRLSKHGPGHETPMTIPEFFRES
VNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFI
TAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKA
IIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV
MLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADA
LKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKK
MLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELY
GLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESET
ETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPII
SNAMLVGDKLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQD
PLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQ
IDHMYH
Enzyme 103 Number of Residues 666
Enzyme 103 Molecular Weight 74353.8
Enzyme 103 Theoretical pI 8.66
Enzyme 103 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 103 General Function Involved in catalytic activity
Enzyme 103 Specific Function Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 32968194 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q5FVE4 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name ACBG2_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >2001 bp
ATGACTGGAACCCCAAAGACTCAAGAAGGAGCTAAAGATCTTGAAGTAGACATGAATAAA
ACAGAAGTTACTCCCAGGCTGTGGACCACCTGTCGAGATGGAGAAGTCCTTCTGAGGCTA
TCCAAACACGGACCAGGCCATGAGACCCCGATGACCATCCCTGAATTTTTTCGAGAGTCA
GTCAACCGATTTGGAACTTATCCAGCCCTCGCATCCAAGAATGGCAAAAAGTGGGAAATT
CTGAATTTCAACCAGTACTATGAGGCTTGTCGGAAGGCTGCAAAATCCTTGATCAAGCTG
GGTTTGGAGCGTTTCCACGGAGTTGGTATCCTGGGGTTTAACTCTGCAGAGTGGTTTATC
ACTGCTGTTGGTGCCATCCTAGCCGGGGGTCTTTGTGTTGGTATTTATGCCACCAACTCT
GCCGAGGCTTGTCAATATGTCATCACTCATGCCAAAGTGAACATCTTGCTGGTTGAGAAT
GATCAACAGTTACAGAAAATCCTTTCGATTCCACAGAGCAGCCTAGAGCCCCTAAAAGCG
ATCATCCAGTACAGACTGCCAATGAAGAAGAACAACAACTTGTACTCTTGGGATGATTTC
ATGGAACTTGGCAGAAGTATCCCTGACACCCAACTGGAGCAGGTCATCGAGAGCCAGAAG
GCGAATCAATGCGCAGTGCTCATCTACACTTCAGGGACCACAGGCATACCCAAGGGAGTG
ATGCTCAGTCATGACAACATCACGTGGATTGCAGGAGCAGTGACAAAGGACTTTAAACTG
ACAGACAAGCATGAGACGGTGGTTAGCTACCTCCCACTCAGCCATATTGCAGCACAGATG
ATGGACATCTGGGTACCCATAAAGATTGGGGCGCTCACATACTTTGCTCAAGCAGATGCT
CTCAAGGGCACCTTGGTAAGTACTCTAAAGGAGGTAAAACCTACTGTCTTCATTGGAGTG
CCTCAAATTTGGGAGAAGATACATGAGATGGTGAAGAAAAATAGTGCCAAGTCCATGGGC
TTGAAGAAGAAGGCATTCGTGTGGGCAAGAAACATTGGCTTCAAGGTCAACTCAAAAAAG
ATGTTGGGGAAATATAATACTCCCGTGAGCTACCGCATGGCTAAGACTCTCGTGTTCAGC
AAAGTCAAGACATCCCTTGGCTTGGATCACTGTCACTCTTTTATCAGTGGGACTGCGCCC
CTCAACCAAGAGACTGCCGAGTTCTTTCTAAGCTTGGACATACCTATAGGCGAGTTGTAT
GGGTTGAGTGAGAGCTCGGGACCCCACACGATATCCAACCAGAATAACTACAGGCTTCTA
AGCTGTGGCAAGATCTTGACTGGGTGTAAGAATATGCTGTTCCAGCAGAACAAGGATGGC
ATTGGGGAGATCTGCCTCTGGGGTAGGCACATCTTCATGGGCTATCTGGAAAGTGAGACT
GAAACTACAGAGGCCATCGATGATGAAGGCTGGCTACACTCTGGGGATCTGGGCCAGCTG
GACGGTCTGGGTTTCCTCTATGTCACCGGCCACATCAAAGAAATCCTTATCACTGCTGGT
GGTGAAAATGTGCCCCCCATTCCTGTTGAGACCTTGGTTAAGAAGAAGATCCCCATCATC
AGTAACGCCATGTTAGTAGGAGATAAACTGAAGTTTCTGAGCATGTTGCTGACGCTGAAG
TGTGAGATGAATCAGATGAGCGGAGAACCTCTGGACAAGCTGAACTTCGAGGCCATCAAC
TTCTGTCGGGGTCTGGGCAGCCAGGCATCCACCGTGACTGAGATGGTGAAGCAGCAAGAC
CCCCTGGTCTACAAGGCCATCCAGCAAGGCATCAATGCTGTGAACCAGGAAGCCATGAAC
AATGCACAGAGGATTGAAAAGTGGGTCATCTTGGAGAAGGACTTTTCCATCTATGGTGGA
GAGCTAGGTCCAATGATGAAACTTAAGAGACATTTTGTAGCCCAGAAATACAAAAAACAA
ATTGATCACATGTACCACTGA
Enzyme 103 GenBank Gene ID AJ577571 Link Image
Enzyme 103 GeneCard ID ACSBG2 Link Image
Enzyme 103 GenAtlas ID ACSBG2 Link Image
Enzyme 103 HGNC ID HGNC:24174 Link Image
Enzyme 103 Chromosome Location 1
Enzyme 103 Locus 19p13.3
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. Zheng Y, Zhou ZM, Min X, Li JM, Sha JH: Identification and characterization of the BGR-like gene with a potential role in human testicular development/spermatogenesis. Asian J Androl. 2005 Mar;7(1):21-32. [PubMed Link Image]
  2. Fraisl P, Tanaka H, Forss-Petter S, Lassmann H, Nishimune Y, Berger J: A novel mammalian bubblegum-related acyl-CoA synthetase restricted to testes and possibly involved in spermatogenesis. Arch Biochem Biophys. 2006 Jul 1;451(1):23-33. Epub 2006 May 8. [PubMed Link Image]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  4. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Pei Z, Jia Z, Watkins PA: The second member of the human and murine bubblegum family is a testis- and brainstem-specific acyl-CoA synthetase. J Biol Chem. 2006 Mar 10;281(10):6632-41. Epub 2005 Dec 21. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 17329
Enzyme 104 Name Long-chain-fatty-acid--CoA ligase ACSBG1
Enzyme 104 Synonyms
  1. Acyl-CoA synthetase bubblegum family member 1
  2. hBG1
  3. hsBG
  4. hsBGM
  5. Lipodisin
Enzyme 104 Gene Name ACSBG1
Enzyme 104 Protein Sequence >Long-chain-fatty-acid--CoA ligase ACSBG1
MPRNSGAGYGCPHGDPSMLDSRETPQESRQDMIVRTTQEKLKTSSLTDRQPLSKESLNHA
LELSVPEKVNNAQWDAPEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLI
ALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFA
GGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPP
NKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNIT
WTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSL
VNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDL
KPFTTRLADYLVLAKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETS
GPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAI
DEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLI
GDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQA
IEEGIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQ
EQKM
Enzyme 104 Number of Residues 724
Enzyme 104 Molecular Weight 81289.6
Enzyme 104 Theoretical pI 5.86
Enzyme 104 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 104 General Function Involved in catalytic activity
Enzyme 104 Specific Function Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00390]
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein Not Available
Enzyme 104 UniProtKB/Swiss-Prot ID Q96GR2 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name ACBG1_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >2175 bp
ATGCCACGCAATTCTGGAGCTGGATACGGCTGCCCACACGGGGACCCCAGCATGCTGGAC
AGCAGAGAGACCCCACAGGAGAGCCGGCAGGACATGATTGTGAGGACCACCCAAGAAAAA
TTGAAAACCAGCTCACTGACTGACAGGCAGCCACTCTCCAAAGAGTCCCTGAACCATGCT
CTCGAGCTCTCAGTGCCAGAGAAGGTGAATAATGCCCAGTGGGATGCTCCAGAGGAGGCG
CTGTGGACGACTCGGGCCGATGGGCGGGTGCGCCTGCGCATAGACCCCAGCTGCCCACAG
CTTCCCTACACTGTGCATCGGATGTTCTACGAGGCCCTGGATAAGTATGGGGACCTCATC
GCTTTGGGCTTCAAGCGCCAGGACAAGTGGGAACACATCTCCTACTCCCAATACTACCTG
CTCGCCCGCAGAGCCGCCAAGGGCTTCCTGAAGCTCGGCCTGAAGCAGGCCCACAGTGTG
GCCATCCTCGGCTTCAACTCCCCGGAGTGGTTCTTCTCGGCAGTGGGCACAGTATTTGCA
GGTGGCATCGTCACTGGCATCTACACCACCAGCTCCCCAGAGGCCTGCCAGTACATCGCT
TATGACTGCTGCGCCAATGTCATCATGGTCGACACGCAGAAGCAGCTGGAAAAGATCCTG
AAGATCTGGAAACAGTTGCCACATCTAAAGGCAGTCGTGATATATAAAGAACCTCCTCCA
AACAAGATGGCCAATGTGTACACGATGGAGGAATTCATGGAGCTGGGGAATGAAGTGCCT
GAGGAAGCCCTGGACGCCATCATTGACACCCAGCAGCCCAACCAGTGCTGTGTGCTAGTC
TACACTTCCGGCACCACTGGGAACCCCAAGGGCGTGATGCTGAGTCAAGACAATATCACG
TGGACGGCACGGTACGGCAGCCAGGCCGGTGACATCCGGCCGGCAGAAGTCCAGCAGGAG
GTGGTAGTCAGCTACCTGCCCCTCAGCCATATTGCCGCCCAGATCTACGACCTGTGGACA
GGCATCCAGTGGGGGGCCCAGGTTTGCTTTGCCGAACCCGACGCCCTGAAGGGGAGCCTG
GTGAACACGCTGCGGGAGGTGGAGCCCACATCACACATGGGGGTGCCCCGGGTATGGGAG
AAGATCATGGAGCGCATCCAGGAGGTGGCGGCTCAGTCTGGCTTCATCCGGCGAAAGATG
CTGCTGTGGGCCATGTCGGTGACCTTGGAGCAGAACCTCACCTGCCCCGGCAGCGACCTG
AAGCCCTTCACAACCAGACTGGCAGATTACCTGGTGCTAGCCAAGGTTCGCCAGGCACTG
GGATTTGCCAAGTGTCAAAAGAACTTCTATGGAGCGGCCCCCATGATGGCAGAGACACAG
CACTTCTTCCTGGGTCTCAACATCCGCTTGTATGCGGGCTACGGCCTCAGTGAGACCTCA
GGCCCCCACTTCATGTCCAGTCCCTACAACTACCGGCTGTACAGCTCAGGCAAGTTGGTG
CCCGGCTGTCGGGTGAAGCTGGTGAACCAGGACGCAGAGGGCATTGGCGAGATCTGCCTG
TGGGGCCGCACCATATTCATGGGCTACCTGAACATGGAGGACAAGACTTGTGAGGCCATC
GACGAGGAAGGCTGGCTGCACACGGGTGATGCTGGCCGCCTGGACGCCGATGGCTTCCTC
TACATCACTGGGCGCCTCAAAGAATTAATCATCACAGCTGGTGGGGAGAATGTGCCCCCT
GTGCCCATCGAGGAGGCCGTGAAGATGGAGCTGCCCATCATCAGCAACGCCATGCTCATT
GGGGACCAGAGGAAGTTCCTGTCCATGCTGCTCACCTTGAAGTGCACTCTGGACCCAGAC
ACCTCTGACCAGACTGATAATCTGACTGAACAAGCTATGGAGTTCTGCCAGAGGGTGGGC
AGCAGAGCCACCACAGTGTCCGAGATCATAGAGAAGAAGGATGAGGCCGTGTACCAGGCC
ATCGAAGAGGGGATCCGGAGGGTCAACATGAACGCGGCGGCCCGGCCCTACCACATCCAG
AAGTGGGCCATTCTCGAGAGAGACTTCTCCATTTCGGGTGGAGAGTTGGGTCCCACGATG
AAACTGAAACGGCTCACAGTTTTGGAGAAGTACAAAGGTATCATTGACTCCTTTTACCAA
GAGCAAAAAATGTAA
Enzyme 104 GenBank Gene ID AF179481 Link Image
Enzyme 104 GeneCard ID ACSBG1 Link Image
Enzyme 104 GenAtlas ID ACSBG1 Link Image
Enzyme 104 HGNC ID HGNC:29567 Link Image
Enzyme 104 Chromosome Location 1
Enzyme 104 Locus 15q23-q24
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Steinberg SJ, Morgenthaler J, Heinzer AK, Smith KD, Watkins PA: Very long-chain acyl-CoA synthetases. Human "bubblegum" represents a new family of proteins capable of activating very long-chain fatty acids. J Biol Chem. 2000 Nov 10;275(45):35162-9. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Pei Z, Oey NA, Zuidervaart MM, Jia Z, Li Y, Steinberg SJ, Smith KD, Watkins PA: The acyl-CoA synthetase "bubblegum" (lipidosin): further characterization and role in neuronal fatty acid beta-oxidation.. J Biol Chem. 2003 Nov 21;278(47):47070-8. Epub 2003 Sep 15. [PubMed Link Image]
  8. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 17698
Enzyme 105 Name Golgi resident protein GCP60
Enzyme 105 Synonyms
  1. Acyl-CoA-binding domain-containing protein 3
  2. Golgi complex-associated protein 1
  3. GOCAP1
  4. Golgi phosphoprotein 1
  5. GOLPH1
  6. PBR- and PKA-associated protein 7
  7. Peripheral benzodiazepine receptor-associated protein PAP7
Enzyme 105 Gene Name ACBD3
Enzyme 105 Protein Sequence >Golgi resident protein GCP60
MAAVLNAERLEVSVDGLTLSPDPEERPGAEGAPLLPPPLPPPSPPGSGRGPGASGEQPEP
GEAAAGGAAEEARRLEQRWGFGLEELYGLALRFFKEKDGKAFHPTYEEKLKLVALHKQVL
MGPYNPDTCPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVKLLNRCCHLFSTYVASHK
IEKEEQEKKRKEEEERRRREEEERERLQKEEEKRRREEEERLRREEEERRRIEEERLRLE
QQKQQIMAALNSQTAVQFQQYAAQQYPGNYEQQQILIRQLQEQHYQQYMQQLYQVQLAQQ
QAALQKQQEVVVAGSSLPTSSKVNATVPSNMMSVNGQAKTHTDSSEKELEPEAAEEALEN
GPKESLPVIAAPSMWTRPQIKDFKEKIQQDADSVITVGRGEVVTVRVPTHEEGSYLFWEF
ATDNYDIGFGVYFEWTDSPNTAVSVHVSESSDDDEEEEENIGCEEKAKKNANKPLLDEIV
PVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYTR
Enzyme 105 Number of Residues 528
Enzyme 105 Molecular Weight 60593.0
Enzyme 105 Theoretical pI 4.73
Enzyme 105 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 105 General Function Involved in acyl-CoA binding
Enzyme 105 Specific Function Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells
Enzyme 105 Pathways Not Available
Enzyme 105 Reactions Not Available
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 15799259 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID Q9H3P7 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name GCP60_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >1587 bp
ATGGCGGCGGTGCTGAACGCAGAGCGACTCGAGGTGTCCGTCGACGGCCTCACGCTCAGC
CCGGACCCGGAGGAGCGGCCTGGGGCGGAGGGCGCCCCGCTGCTGCCGCCACCGCTGCCA
CCGCCCTCGCCACCTGGATCCGGTCGCGGCCCGGGCGCCTCAGGGGAGCAGCCCGAGCCC
GGGGAGGCGGCGGCTGGGGGCGCGGCGGAGGAGGCGCGGCGGCTGGAGCAGCGCTGGGGT
TTCGGCCTGGAGGAGTTGTACGGCCTGGCACTGCGCTTCTTCAAAGAAAAAGATGGCAAA
GCATTTCATCCAACTTATGAAGAAAAATTGAAGCTTGTGGCACTGCATAAGCAAGTTCTT
ATGGGCCCATATAATCCAGACACTTGTCCTGAGGTTGGATTCTTTGATGTGTTGGGGAAT
GACAGGAGGAGAGAATGGGCAGCCCTGGGAAACATGTCTAAAGAGGATGCCATGGTGGAG
TTTGTCAAGCTCTTAAATAGGTGTTGCCATCTCTTTTCAACATATGTTGCGTCCCACAAA
ATAGAGAAGGAAGAGCAAGAAAAAAAAAGGAAGGAGGAAGAGGAGCGAAGGCGGCGTGAA
GAGGAAGAAAGAGAACGTCTGCAAAAGGAGGAAGAGAAACGTAGGAGAGAAGAAGAGGAA
AGGCTTCGACGGGAGGAAGAGGAAAGGAGACGGATAGAAGAAGAAAGGCTTCGGTTGGAG
CAGCAAAAGCAGCAGATAATGGCAGCTTTAAACTCCCAGACTGCCGTGCAGTTCCAGCAG
TATGCAGCCCAACAGTATCCAGGGAACTACGAACAGCAGCAAATTCTCATCCGCCAGTTG
CAGGAGCAACACTATCAGCAGTACATGCAGCAGTTGTATCAAGTCCAGCTTGCACAGCAA
CAGGCAGCATTACAGAAACAACAGGAAGTAGTAGTGGCTGGGTCTTCCTTGCCTACATCA
TCAAAAGTGAATGCAACTGTACCAAGTAATATGATGTCAGTTAATGGACAGGCCAAAACA
CACACTGACAGCTCCGAAAAAGAACTGGAACCAGAAGCTGCAGAAGAAGCCCTGGAGAAT
GGACCAAAAGAATCTCTTCCAGTAATAGCAGCTCCATCCATGTGGACACGACCTCAGATC
AAAGACTTCAAAGAGAAGATTCAGCAGGATGCAGATTCCGTGATTACAGTGGGCCGAGGA
GAAGTGGTCACTGTTCGAGTACCCACCCATGAAGAAGGATCATATCTCTTTTGGGAATTT
GCCACAGACAATTATGACATTGGGTTTGGGGTGTATTTTGAATGGACAGACTCTCCAAAC
ACTGCTGTCAGCGTGCATGTCAGTGAGTCCAGCGATGACGACGAGGAGGAAGAAGAAAAC
ATCGGTTGTGAAGAGAAAGCCAAAAAGAATGCCAACAAGCCTTTGCTGGATGAGATTGTG
CCTGTGTACCGACGGGACTGTCATGAGGAGGTGTATGCTGGCAGCCATCAATATCCAGGG
AGAGGAGTCTATCTCCTCAAGTTTGACAACTCCTACTCTTTGTGGCGGTCAAAATCAGTC
TACTACAGAGTCTATTATACTAGATAA
Enzyme 105 GenBank Gene ID AB043587 Link Image
Enzyme 105 GeneCard ID ACBD3 Link Image
Enzyme 105 GenAtlas ID ACBD3 Link Image
Enzyme 105 HGNC ID HGNC:15453 Link Image
Enzyme 105 Chromosome Location 1
Enzyme 105 Locus 1q42.12
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y: Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J Biol Chem. 2001 Nov 30;276(48):45298-306. Epub 2001 Oct 5. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 17699
Enzyme 106 Name Acyl-CoA-binding domain-containing protein 4
Enzyme 106 Synonyms Not Available
Enzyme 106 Gene Name ACBD4
Enzyme 106 Protein Sequence >Acyl-CoA-binding domain-containing protein 4
MGTEKESPEPDCQKQFQAAVSVIQNLPKNGSYRPSYEEMLRFYSYYKQATMGPCLVPRPG
FWDPIGRYKWDAWNSLGKMSREEAMSAYITEMKLVAQKVIDTVPLGEVAEDMFGYFEPLY
QVIPDMPRPPETFLRRVTGWKEQVVNGDVGAVSEPPCLPKEPAPPSPESHSPRDLDSEVF
CDSLEQLEPELSSGQHLEESVIPGTAPCPPQRKRGCGAARRGPRSWTCGCWGQFEHYRRA
CRRCRRGCRAWRACPGPLSSLTLSVRLE
Enzyme 106 Number of Residues 268
Enzyme 106 Molecular Weight 30307.3
Enzyme 106 Theoretical pI 7.16
Enzyme 106 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 106 General Function Involved in acyl-CoA binding
Enzyme 106 Specific Function Not Available
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein 209364600 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID Q8NC06 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name ACBD4_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >807 bp
ATGGGCACCGAGAAAGAAAGCCCAGAGCCCGACTGCCAGAAACAGTTCCAGGCTGCAGTG
AGCGTCATCCAGAACCTGCCCAAGAACGGTTCTTACCGCCCCTCCTATGAAGAGATGCTG
CGATTCTACAGTTACTACAAGCAGGCCACCATGGGGCCCTGCCTGGTCCCCCGGCCCGGG
TTCTGGGACCCCATTGGACGATATAAGTGGGACGCCTGGAACAGTCTGGGCAAGATGAGC
AGGGAGGAGGCCATGTCTGCCTACATCACTGAAATGAAACTGGTGGCACAGAAGGTGATC
GACACAGTGCCCCTGGGTGAGGTGGCAGAGGACATGTTTGGTTACTTCGAGCCCCTGTAC
CAGGTGATCCCTGACATGCCGAGGCCCCCAGAGACCTTCCTGAGAAGGGTCACAGGTTGG
AAAGAGCAGGTTGTGAATGGAGATGTTGGGGCTGTTTCAGAGCCTCCCTGCCTCCCCAAG
GAACCGGCACCCCCAAGCCCAGAGTCCCATTCACCCAGGGACCTGGACTCCGAGGTTTTC
TGTGATTCCCTGGAGCAGCTGGAGCCTGAGCTGAGCAGCGGGCAGCATCTGGAGGAAAGC
GTGATCCCAGGAACAGCCCCGTGCCCCCCACAAAGAAAGAGGGGTTGCGGGGCAGCCCGC
CGGGGCCCCAGGAGTTGGACGTGTGGCTGCTGGGGACAGTTCGAGCACTACAGGAGAGCA
TGCAGGAGGTGCAGGCGAGGGTGCAGAGCCTGGAGAGCATGCCCCGGCCCCCTGAGCAGT
CTCACTCTGTCGGTCAGACTGGAGTGA
Enzyme 106 GenBank Gene ID NM_001135707.1 Link Image
Enzyme 106 GeneCard ID ACBD4 Link Image
Enzyme 106 GenAtlas ID ACBD4 Link Image
Enzyme 106 HGNC ID HGNC:23337 Link Image
Enzyme 106 Chromosome Location 1
Enzyme 106 Locus 17q21.31
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A: Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. Oncogene. 2004 Aug 5;23(35):5901-11. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 17700
Enzyme 107 Name Not Available
Enzyme 107 Synonyms Not Available
Enzyme 107 Gene Name Not Available
Enzyme 107 Protein Sequence Not Available
Enzyme 107 Number of Residues Not Available
Enzyme 107 Molecular Weight Not Available
Enzyme 107 Theoretical pI Not Available
Enzyme 107 GO Classification Not Available
Enzyme 107 General Function Not Available
Enzyme 107 Specific Function Not Available
Enzyme 107 Pathways Not Available
Enzyme 107 Reactions Not Available
Enzyme 107 Pfam Domain Function Not Available
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein Not Available
Enzyme 107 UniProtKB/Swiss-Prot ID Not Available
Enzyme 107 UniProtKB/Swiss-Prot Entry Name Not Available
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence Not Available
Enzyme 107 GenBank Gene ID Not Available
Enzyme 107 GeneCard ID Not Available
Enzyme 107 GenAtlas ID Not Available
Enzyme 107 HGNC ID Not Available
Enzyme 107 Chromosome Location Not Available
Enzyme 107 Locus Not Available
Enzyme 107 SNPs Not Available
Enzyme 107 General References Not Available
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 17701
Enzyme 108 Name cDNA, FLJ94802
Enzyme 108 Synonyms Not Available
Enzyme 108 Gene Name Not Available
Enzyme 108 Protein Sequence >cDNA, FLJ94802
MASSFLPAGAITGDSGGELSSGDDSGEVEFPHSPEIEETSCLAELFEKAAAHLQGLIQVA
SREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKK
LDPGWNPQIPEKKGKEANTGFGGPVISSLYHEETIREEDKNIFDYCRENNIDHITKAIKS
KNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADVNCQDNEGQTALHYASACEFLDI
VELLLQSGADPTLRDQDGCLPEEVTGCKTVSLVLQRHTTGKA
Enzyme 108 Number of Residues 282
Enzyme 108 Molecular Weight 31136.6
Enzyme 108 Theoretical pI 4.76
Enzyme 108 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 108 General Function Involved in acyl-CoA binding
Enzyme 108 Specific Function Not Available
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 189054285 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID B2RAA8 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name B2RAA8_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >849 bp
ATGGCTTCATCATTCCTGCCCGCGGGGGCCATCACCGGCGACAGCGGTGGAGAGCTGAGC
TCAGGGGACGACTCCGGGGAGGTGGAGTTCCCCCATAGCCCTGAGATCGAGGAGACCAGT
TGCCTGGCCGAGCTGTTTGAGAAGGCTGCCGCGCACCTGCAAGGCCTGATTCAGGTGGCC
AGCAGGGAGCAGCTCTTGTACCTGTATGCCAGGTACAAACAGGTCAAAGTTGGAAATTGT
AATACTCCTAAACCAAGCTTCTTTGATTTTGAAGGAAAGCAAAAATGGGAAGCTTGGAAA
GCACTTGGTGATTCAAGCCCCAGCCAAGCAATGCAGGAATATATCGCAGTAGTTAAAAAA
CTAGATCCAGGTTGGAATCCTCAGATACCAGAGAAGAAAGGAAAAGAAGCAAATACAGGT
TTTGGTGGGCCAGTTATTAGTTCTCTATATCATGAAGAAACCATCAGGGAAGAAGACAAA
AATATATTTGATTACTGCAGGGAAAACAACATTGACCATATAACCAAAGCCATCAAATCG
AAAAATGTGGATGTGAATGTGAAAGATGAAGAGGGTAGGGCTCTACTTCACTGGGCCTGT
GATCGAGGACATAAGGAACTAGTCACAGTGTTGCTGCAACATAGAGCTGACGTTAACTGT
CAGGACAATGAAGGCCAAACAGCTCTACATTATGCCTCTGCCTGTGAGTTTCTGGATATT
GTAGAGCTGCTGCTCCAGTCTGGTGCTGACCCCACTCTCCGAGACCAGGATGGCTGCCTG
CCAGAGGAGGTGACAGGCTGCAAAACAGTTTCTTTGGTGCTGCAGCGGCACACAACTGGC
AAGGCTTAA
Enzyme 108 GenBank Gene ID AK314112 Link Image
Enzyme 108 GeneCard ID Not Available
Enzyme 108 GenAtlas ID Not Available
Enzyme 108 HGNC ID HGNC:23339 Link Image
Enzyme 108 Chromosome Location Not Available
Enzyme 108 Locus Not Available
Enzyme 108 SNPs Not Available
Enzyme 108 General References Not Available
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 17702
Enzyme 109 Name Acyl-CoA-binding domain-containing protein 5
Enzyme 109 Synonyms Not Available
Enzyme 109 Gene Name ACBD5
Enzyme 109 Protein Sequence >Acyl-CoA-binding domain-containing protein 5
MFQFHAGSWESWCCCCLIPADRPWDRGQHWQLEMADTRSVHETRFEAAVKVIQSLPKNGS
FQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEE
MKKIIETMPMTEKVEELLRVIGPFYEIVEDKKSGRSSDITSVRLEKISKCLEDLGNVLTS
TPNAKTVNGKAESSDSGAESEEEEAQEEVKGAEQSDNDKKMMKKSADHKNLEVIVTNGYD
KDGFVQDIQNDIHASSSLNGRSTEEVKPIDENLGQTGKSAVCIHQDINDDHVEDVTGIQH
LTSDSDSEVYCDSMEQFGQEESLDSFTSNNGPFQYYLGGHSSQPMENSGFREDIQVPPGN
GNIGNMQVVAVEGKGEVKHGGEDGRNNSGAPHREKRGGETDEFSNVRRGRGHRMQHLSEG
TKGRQVGSGGDGERWGSDRGSRGSLNEQIALVLMRLQEDMQNVLQRLQKLETLTALQAKS
STSTLQTAPQPTSQRPSWWPFEMSPGVLTFAIIWPFIAQWLVYLYYQRRRRKLN
Enzyme 109 Number of Residues 534
Enzyme 109 Molecular Weight 60091.5
Enzyme 109 Theoretical pI 4.98
Enzyme 109 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 109 General Function Involved in acyl-CoA binding
Enzyme 109 Specific Function Not Available
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • 506-526
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 55958295 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID Q5T8D3 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name ACBD5_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >3216 bp
ATGTTCCAGTTTCATGCAGGCTCTTGGGAAAGCTGGTGCTGCTGCTGCCTGATTCCCGCC
GACAGACCTTGGGACCGGGGCCAACACTGGCAGCTGGAGATGGCGGACACGAGATCCGTG
CACGAGACTAGGTTTGAGGCGGCCGTGAAGGTGATCCAGAGTTTGCCGAAGAATGGTTCA
TTCCAGCCAACAAATGAAATGATGCTTAAATTTTATAGCTTCTATAAGCAGGCAACTGAA
GGACCCTGTAAACTTTCAAGGCCTGGATTTTGGGATCCTATTGGAAGATATAAATGGGAT
GCTTGGAGTTCACTGGGTGATATGACCAAAGAGGAAGCCATGATTGCATATGTTGAAGAA
ATGAAAAAGATTATTGAAACTATGCCAATGACTGAGAAAGTTGAAGAATTGCTGCGTGTC
ATAGGTCCATTTTATGAAATTGTCGAGGACAAAAAGAGTGGCAGGAGTTCTGATATAACC
TCAGTCCGACTGGAGAAAATCTCTAAATGTTTAGAAGATCTTGGTAATGTTCTCACTTCT
ACTCCAAACGCCAAAACCGTTAATGGTAAAGCTGAAAGCAGTGACAGTGGAGCCGAGTCT
GAGGAAGAAGAGGCCCAAGAAGAAGTGAAAGGAGCAGAACAAAGTGATAATGATAAGAAA
ATGATGAAGAAGTCAGCAGACCATAAGAATTTGGAAGTCATTGTCACTAATGGCTATGAT
AAAGATGGCTTTGTTCAGGATATACAGAATGACATTCATGCCAGTTCTTCCCTGAATGGC
AGAAGCACTGAAGAAGTAAAGCCCATTGATGAAAACTTGGGGCAAACTGGAAAATCTGCT
GTTTGCATTCACCAAGATATAAATGATGATCATGTTGAAGATGTTACAGGAATTCAGCAT
TTGACAAGCGATTCAGACAGTGAAGTTTACTGTGATTCTATGGAACAATTTGGACAAGAA
GAGTCTTTAGACAGCTTTACGTCCAACAATGGACCATTTCAGTATTACTTGGGTGGTCAT
TCCAGTCAACCCATGGAAAATTCTGGATTTCGTGAAGATATTCAAGTACCTCCTGGAAAT
GGCAACATTGGGAATATGCAGGTGGTTGCAGTTGAAGGAAAAGGTGAAGTCAAGCATGGA
GGAGAAGATGGCAGGAATAACAGCGGAGCACCACACCGGGAGAAGCGAGGCGGAGAAACT
GACGAATTCTCTAATGTTAGAAGAGGAAGAGGACATAGGATGCAACACTTGAGCGAAGGA
ACCAAGGGCCGGCAGGTGGGAAGTGGAGGTGATGGGGAGCGCTGGGGCTCCGACAGAGGG
TCCCGAGGCAGCCTCAATGAGCAGATCGCCCTCGTGCTGATGAGACTGCAGGAGGACATG
CAGAATGTCCTTCAGAGACTGCAGAAACTGGAAACGCTGACTGCTTTGCAGGCAAAATCA
TCAACATCAACATTGCAGACTGCTCCTCAGCCCACCTCACAGAGACCATCTTGGTGGCCC
TTCGAGATGTCTCCTGGTGTGCTAACGTTTGCCATCATATGGCCTTTTATTGCACAGTGG
TTGGTGTATTTATACTATCAAAGAAGGAGAAGAAAACTGAACTGA
Enzyme 109 GenBank Gene ID AL160291 Link Image
Enzyme 109 GeneCard ID ACBD5 Link Image
Enzyme 109 GenAtlas ID ACBD5 Link Image
Enzyme 109 HGNC ID HGNC:23338 Link Image
Enzyme 109 Chromosome Location 1
Enzyme 109 Locus 10p12.1
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  7. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 17703
Enzyme 110 Name Not Available
Enzyme 110 Synonyms Not Available
Enzyme 110 Gene Name Not Available
Enzyme 110 Protein Sequence Not Available
Enzyme 110 Number of Residues Not Available
Enzyme 110 Molecular Weight Not Available
Enzyme 110 Theoretical pI Not Available
Enzyme 110 GO Classification Not Available
Enzyme 110 General Function Not Available
Enzyme 110 Specific Function Not Available
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function Not Available
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein Not Available
Enzyme 110 UniProtKB/Swiss-Prot ID Not Available
Enzyme 110 UniProtKB/Swiss-Prot Entry Name Not Available
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence Not Available
Enzyme 110 GenBank Gene ID Not Available
Enzyme 110 GeneCard ID Not Available
Enzyme 110 GenAtlas ID Not Available
Enzyme 110 HGNC ID Not Available
Enzyme 110 Chromosome Location Not Available
Enzyme 110 Locus Not Available
Enzyme 110 SNPs Not Available
Enzyme 110 General References Not Available
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 17704
Enzyme 111 Name ACAD11 protein
Enzyme 111 Synonyms Not Available
Enzyme 111 Gene Name ACAD11
Enzyme 111 Protein Sequence >ACAD11 protein
MEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDVASSDATNIECSIQRDEDSYVINGK
KWWSSGAGNPKCKIAIVLGRTQNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNFH
GGHFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERAT
QRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAMIKVAAP
RAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELRDQAKR
LTAKI
Enzyme 111 Number of Residues 305
Enzyme 111 Molecular Weight 33775.9
Enzyme 111 Theoretical pI 9.43
Enzyme 111 GO Classification
Function
  • acyl-CoA dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 111 General Function Involved in oxidoreductase activity, acting on the CH-CH group of donors
Enzyme 111 Specific Function Not Available
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 115528754 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID Q08AE9 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name Q08AE9_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >918 bp
ATGGAGGTTCTGCACCTGTATGGAAGTGAGGAACAGAAGAAACAGTGGCTTGAGCCTCTT
CTTCAAGGGAACATTACCTCTTGCTTCTGTATGACAGAACCTGATGTAGCTTCAAGTGAT
GCCACGAATATTGAATGCAGCATCCAACGAGATGAAGATAGCTATGTAATTAACGGCAAA
AAATGGTGGAGCAGTGGAGCTGGGAATCCCAAGTGCAAAATTGCAATTGTTTTGGGAAGA
ACTCAAAATACTTCTCTCTCCAGACACAAACAGCACAGCATGATTCTTGTTCCCATGAAC
ACACCTGGAGTAAAAATAATAAGGCCTTTGTCAGTTTTTGGCTACACAGATAATTTTCAT
GGAGGACATTTTGAGATCCATTTTAATCAAGTGCGAGTTCCTGCCACAAATCTAATACTA
GGTGAAGGTAGGGGATTTGAAATTTCCCAAGGCCGCCTTGGACCTGGCAGAATCCACCAC
TGTATGAGAACAGTAGGTTTGGCGGAACGCGCTTTGCAGATCATGTGTGAGCGGGCAACA
CAAAGGATAGCTTTCAAGAAGAAGTTGTATGCACATGAGGTTGTGGCTCACTGGATTGCT
GAAAGCCGCATTGCCATTGAGAAGATCCGCTTGTTGACTCTGAAAGCTGCTCACAGCATG
GACACTCTGGGCAGTGCTGGCGCTAAGAAAGAGATTGCAATGATCAAAGTGGCTGCCCCA
CGGGCTGTCAGCAAAATCGTTGACTGGGCCATCCAGGTGTGCGGAGGTGCTGGTGTTTCC
CAGGATTACCCTCTGGCTAACATGTATGCTATAACCCGAGTTTTGCGTTTAGCAGATGGA
CCTGACGAAGTTCATCTTTCAGCAATCGCAACAATGGAGCTGCGGGACCAAGCCAAAAGA
CTGACAGCCAAGATATAA
Enzyme 111 GenBank Gene ID BC125205 Link Image
Enzyme 111 GeneCard ID ACAD11 Link Image
Enzyme 111 GenAtlas ID ACAD11 Link Image
Enzyme 111 HGNC ID HGNC:30211 Link Image
Enzyme 111 Chromosome Location 3
Enzyme 111 Locus 3q22.1
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 17705
Enzyme 112 Name Putative uncharacterized protein HADHA
Enzyme 112 Synonyms Not Available
Enzyme 112 Gene Name HADHA
Enzyme 112 Protein Sequence >Putative uncharacterized protein HADHA
PGLKPPEERTIEYLEEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKV
EEKVRKQTKGLYPAPLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQ
VLCKKNKFGAPQKDVKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFK
GLNDKVKKKALTSFERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVI
PDHCIFASNTSALPISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAV
AVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAAT
LVDEVGVDVAKHVAEDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRK
DLNSDMDSILASLKLPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVF
GLGFPPCLGGPFRFVDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 112 Number of Residues 537
Enzyme 112 Molecular Weight 58786.9
Enzyme 112 Theoretical pI 9.12
Enzyme 112 GO Classification
Function
  • 3-hydroxyacyl-CoA dehydrogenase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • enoyl-CoA hydratase activity
  • hydro-lyase activity
  • lyase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • fatty acid beta-oxidation multienzyme complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • mitochondrion
  • organelle
  • protein complex
Enzyme 112 General Function Involved in oxidoreductase activity
Enzyme 112 Specific Function Not Available
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 62702215 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID Q53T69 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name Q53T69_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >1616 bp
GACCAGGACTAAAACCTCCAGAGGAACGGACAATAGAATACCTAGAAGAAGTTGCAATTA
CTTTTGCCAAAGGACTAGCTGATAAGAAGATCTCTCCAAAGAGAGACAAGGGATTGGTGG
AAAAATTGACAGCGTATGCCATGACTATTCCATTTGTCAGGCAACAGGTTTACAAAAAAG
TGGAAGAAAAAGTGCGAAAGCAGACTAAAGGCCTTTATCCTGCACCTCTGAAAATAATTG
ATGTGGTAAAGACTGGAATTGAGCAAGGGAGTGATGCCGGTTATCTCTGTGAATCTCAGA
AATTTGGAGAGCTTGTAATGACCAAAGAATCAAAGGCCTTGATGGGACTCTACCATGGTC
AGGTCCTGTGCAAGAAGAATAAATTTGGAGCTCCACAGAAGGATGTTAAGCATCTGGCTA
TTCTTGGTGCAGGGCTGATGGGAGCAGGCATCGCCCAAGTCTCCGTGGATAAGGGGCTAA
AGACTATACTTAAAGATGCCACCCTCACTGCGCTAGACCGAGGACAGCAACAAGTGTTCA
AAGGATTGAATGACAAAGTGAAGAAGAAAGCTCTAACATCATTTGAAAGGGATTCCATCT
TCAGCAACTTGACTGGGCAGCTTGATTACCAAGGTTTTGAAAAGGCCGACATGGTGATTG
AAGCTGTGTTTGAGGACCTTAGTCTTAAGCACAGAGTGCTAAAGGAAGTAGAAGCGGTGA
TTCCAGATCACTGTATCTTTGCCAGTAACACATCTGCTCTCCCAATCAGTGAAATCGCTG
CTGTCAGCAAAAGACCTGAGAAGGTGATTGGCATGCACTACTTCTCTCCCGTGGACAAGA
TGCAGCTGCTGGAGATTATCACGACCGAGAAAACTTCCAAAGACACCAGTGCTTCAGCTG
TAGCAGTTGGTCTCAAGCAGGGGAAGGTCATCATTGTGGTTAAGGATGGACCTGGCTTCT
ATACTACCAGGTGTCTTGCGCCCATGATGTCTGAAGTCATCCGAATCCTCCAGGAAGGAG
TTGACCCGAAGAAGCTGGATTCCCTGACCACAAGCTTTGGCTTTCCTGTGGGTGCCGCCA
CACTGGTGGATGAAGTTGGTGTGGATGTAGCGAAACATGTGGCGGAAGATCTGGGCAAAG
TCTTTGGGGAGCGGTTTGGAGGTGGAAACCCAGAACTGCTGACACAGATGGTGTCCAAGG
GCTTCCTAGGTCGTAAATCTGGGAAGGGCTTTTACATCTATCAGGAGGGTGTGAAGAGGA
AGGATTTGAATTCTGACATGGATAGTATTTTAGCGAGTCTGAAGCTGCCTCCTAAGTCTG
AAGTCTCATCAGACGAAGACATCCAGTTCCGCCTGGTGACAAGATTTGTGAATGAGGCAG
TCATGTGCCTGCAAGAGGGGATCTTGGCCACACCTGCAGAGGGAGACATCGGAGCCGTCT
TTGGGCTTGGCTTCCCGCCTTGTCTGGGAGGGCCTTTCCGCTTTGTGGATCTGTATGGCG
CCCAGAAGATAGTGGACCGGCTCAAGAAATATGAAGCTGCCTATGGAAAACAGTTCACCC
CATGCCAGCTGCTAGCTGACCATGCTAACAGCCCTAACAAGAAGTTCTACCAGTGA
Enzyme 112 GenBank Gene ID AC011742 Link Image
Enzyme 112 GeneCard ID HADHA Link Image
Enzyme 112 GenAtlas ID HADHA Link Image
Enzyme 112 HGNC ID HGNC:4801 Link Image
Enzyme 112 Chromosome Location 2
Enzyme 112 Locus 2p23
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References Not Available
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 17706
Enzyme 113 Name KIAA1996 protein
Enzyme 113 Synonyms Not Available
Enzyme 113 Gene Name KIAA1996
Enzyme 113 Protein Sequence >KIAA1996 protein
GGREGDPEFAEEWDAWSSLGDMTKEEAMIAYVEEMKKIIETMPMTEKVEELLRVIGPFYE
IVEDKKSGRSSDITSDLGNVLTSTPNAKTVNGKAESSDSGAESEEEEAQEEVKGAEQSDN
DKKMMKKSADHKNLEVIVTNGYDKDGFVQDIQNDIHASSSLNGRSTEEVKPIDENLGQTG
KSAVCIHQDINDDHVEDVTGIQHLTSDSDSEVYCDSMEQFGQEESLDSFTSNNGPFQYYL
GGHSSQPMENSGFREDIQVPPGNGNIGNMQVVAVEGKGEVKHGGEDGRNNSGAPHREKRG
GETDEFSNVRRGRGHRMQHLSEGTKGRQVGSGGDGERWGSDRGSRGSLNEQIALVLMRLQ
EDMQNVLQRLQKLETLTALQAKSSTSTLQTAPQPTSQRPSWWPFEMSPGVLTFAIIWPFI
AQWLVYLYYQRRRRKLN
Enzyme 113 Number of Residues 437
Enzyme 113 Molecular Weight 48560.1
Enzyme 113 Theoretical pI 4.53
Enzyme 113 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 113 General Function Involved in acyl-CoA binding
Enzyme 113 Specific Function Not Available
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 21693138 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q8NCM9 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name Q8NCM9_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >1314 bp
GGCGGCCGTGAAGGTGATCCAGAGTTTGCCGAAGAATGGGATGCTTGGAGTTCACTGGGT
GATATGACCAAAGAGGAAGCCATGATTGCATATGTTGAAGAAATGAAAAAGATTATTGAA
ACTATGCCAATGACTGAGAAAGTTGAAGAATTGCTGCGTGTCATAGGTCCATTTTATGAA
ATTGTCGAGGACAAAAAGAGTGGCAGGAGTTCTGATATAACCTCAGATCTTGGTAATGTT
CTCACTTCTACTCCAAACGCCAAAACCGTTAATGGTAAAGCTGAAAGCAGTGACAGTGGA
GCCGAGTCTGAGGAAGAAGAGGCCCAAGAAGAAGTGAAAGGAGCAGAACAAAGTGATAAT
GATAAGAAAATGATGAAGAAGTCAGCAGACCATAAGAATTTGGAAGTCATTGTCACTAAT
GGCTATGATAAAGATGGCTTTGTTCAGGATATACAGAATGACATTCATGCCAGTTCTTCC
CTGAATGGCAGAAGCACTGAAGAAGTAAAGCCTATTGATGAAAACTTGGGGCAAACTGGA
AAATCTGCTGTTTGCATTCACCAAGATATAAATGATGATCATGTTGAAGATGTTACAGGA
ATTCAGCATTTGACAAGCGATTCAGACAGTGAAGTTTACTGTGATTCTATGGAACAATTT
GGACAAGAAGAGTCTTTAGACAGCTTTACGTCCAACAATGGACCATTTCAGTATTACTTG
GGTGGTCATTCCAGTCAACCCATGGAAAATTCTGGATTTCGTGAAGATATTCAAGTACCT
CCTGGAAATGGCAACATTGGGAATATGCAGGTGGTTGCAGTTGAAGGAAAAGGTGAAGTC
AAGCATGGAGGAGAAGATGGCAGGAATAACAGCGGAGCGCCACACCGGGAGAAGCGAGGC
GGAGAAACTGATGAATTCTCTAATGTTAGAAGAGGAAGAGGACATAGGATGCAACACTTG
AGCGAAGGAACCAAGGGCCGGCAGGTGGGAAGTGGAGGTGATGGGGAGCGCTGGGGCTCC
GACAGAGGGTCCCGAGGCAGCCTCAATGAGCAGATCGCCCTCGTGCTGATGAGACTGCAG
GAGGACATGCAGAATGTCCTTCAGAGACTGCAGAAACTGGAAACGCTGACTGCTTTGCAG
GCAAAATCATCAACATCAACATTGCAGACTGCTCCTCAGCCCACCTCACAGAGACCATCT
TGGTGGCCCTTCGAGATGTCTCCTGGTGTGCTAACGTTTGCCATCATATGGCCTTTTATT
GCACAGTGGTTGGTGTATTTATACTATCAAAGAAGGAGAAGAAAACTGAACTGA
Enzyme 113 GenBank Gene ID AB082527 Link Image
Enzyme 113 GeneCard ID KIAA1996 Link Image
Enzyme 113 GenAtlas ID KIAA1996 Link Image
Enzyme 113 HGNC ID HGNC:23338 Link Image
Enzyme 113 Chromosome Location Not Available
Enzyme 113 Locus Not Available
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Ohara O, Nagase T, Mitsui G, Kohga H, Kikuno R, Hiraoka S, Takahashi Y, Kitajima S, Saga Y, Koseki H: Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method. DNA Res. 2002 Apr 30;9(2):47-57. [PubMed Link Image]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 17707
Enzyme 114 Name Benzodiazepine receptor ligand
Enzyme 114 Synonyms Not Available
Enzyme 114 Gene Name BRL
Enzyme 114 Protein Sequence >Benzodiazepine receptor ligand
MSQAEFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWN
KLKGTSKESAMKTYVEKVDELKKKYGI
Enzyme 114 Number of Residues 87
Enzyme 114 Molecular Weight 10000.4
Enzyme 114 Theoretical pI 9.43
Enzyme 114 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 114 General Function Involved in acyl-CoA binding
Enzyme 114 Specific Function Not Available
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 33150786 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID Q71U42 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name Q71U42_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >264 bp
ATGTCTCAGGCTGAATTTGACAAAGCCGCTGAGGAGGTGAAGCGCCTCAAGACTCAGCCA
ACTGATGAAGAGATGCTGTTCATCTACAGTCACTTCAAACAAGCTACTGTGGGCGATGTA
AATACAGATCGGCCGGGGCTCTTGGACCTCAAGGGCAAAGCCAAGTGGGACTCGTGGAAC
AAGCTGAAAGGGACTTCCAAGGAAAGTGCCATGAAGACCTATGTGGAAAAGGTAGACGAG
CTAAAGAAGAAATACGGAATATAA
Enzyme 114 GenBank Gene ID AF139542 Link Image
Enzyme 114 GeneCard ID BRL Link Image
Enzyme 114 GenAtlas ID Not Available
Enzyme 114 HGNC ID Not Available
Enzyme 114 Chromosome Location Not Available
Enzyme 114 Locus Not Available
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References Not Available
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 17708
Enzyme 115 Name Not Available
Enzyme 115 Synonyms Not Available
Enzyme 115 Gene Name Not Available
Enzyme 115 Protein Sequence Not Available
Enzyme 115 Number of Residues Not Available
Enzyme 115 Molecular Weight Not Available
Enzyme 115 Theoretical pI Not Available
Enzyme 115 GO Classification Not Available
Enzyme 115 General Function Not Available
Enzyme 115 Specific Function Not Available
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function Not Available
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein Not Available
Enzyme 115 UniProtKB/Swiss-Prot ID Not Available
Enzyme 115 UniProtKB/Swiss-Prot Entry Name Not Available
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence Not Available
Enzyme 115 GenBank Gene ID Not Available
Enzyme 115 GeneCard ID Not Available
Enzyme 115 GenAtlas ID Not Available
Enzyme 115 HGNC ID Not Available
Enzyme 115 Chromosome Location Not Available
Enzyme 115 Locus Not Available
Enzyme 115 SNPs Not Available
Enzyme 115 General References Not Available
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 17709
Enzyme 116 Name Putative uncharacterized protein HADHA
Enzyme 116 Synonyms Not Available
Enzyme 116 Gene Name HADHA
Enzyme 116 Protein Sequence >Putative uncharacterized protein HADHA
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPL
Enzyme 116 Number of Residues 225
Enzyme 116 Molecular Weight 24173.0
Enzyme 116 Theoretical pI 10.17
Enzyme 116 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 116 General Function Involved in catalytic activity
Enzyme 116 Specific Function Not Available
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 62822074 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q53TA2 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name Q53TA2_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >676 bp
ATGGTGGCCTGCCGGGCGATTGGCATCCTCAGCCGCTTTTCTGCCTTCAGGATCCTCCGC
TCCCGAGGTTATATATGCCGCAATTTTACAGGGTCTTCTGCTTTGCTGACCAGAACCCAT
ATTAACTATGGAGTCAAAGGGGATGTGGCAGTTGTTCGAATTAACTCTCCCAATTCAAAG
GTAAATACACTGAGTAAAGAGCTACATTCAGAGTTCTCAGAAGTTATGAATGAAATCTGG
GCTAGTGATCAAATCAGAAGTGCCGTCCTTATCTCATCAAAGCCAGGCTGCTTTATTGCA
GGTGCTGATATCAACATGTTAGCCGCTTGCAAGACCCTTCAAGAAGTAACACAGCTATCA
CAAGAAGCACAGAGAATAGTTGAGAAACTTGAAAAGTCCACAAAGCCTATTGTGGCTGCC
ATCAATGGATCCTGCCTGGGAGGAGGACTTGAGGTTGCCATTTCATGCCAATACAGAATA
GCAACAAAAGACAGAAAAACAGTATTAGGTACCCCTGAAGTTTTGCTGGGGGCCTTACCA
GGAGCAGGAGGCACACAAAGGCTGCCCAAAATGGTGGGTGTGCCTGCTGCTTTGGACATG
ATGCTGACTGGTAGAAGCATTCGTGCAGACAGGGCAAAGAAAATGGGACTGGTTGACCAA
CTGGTGGAACCCCTGG
Enzyme 116 GenBank Gene ID AC010896 Link Image
Enzyme 116 GeneCard ID HADHA Link Image
Enzyme 116 GenAtlas ID HADHA Link Image
Enzyme 116 HGNC ID HGNC:4801 Link Image
Enzyme 116 Chromosome Location 2
Enzyme 116 Locus 2p23
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References Not Available
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 17710
Enzyme 117 Name Acyl-CoA-binding domain-containing protein 6
Enzyme 117 Synonyms Not Available
Enzyme 117 Gene Name ACBD6
Enzyme 117 Protein Sequence >Acyl-CoA-binding domain-containing protein 6
MASSFLPAGAITGDSGGELSSGDDSGEVEFPHSPEIEETSCLAELFEKAAAHLQGLIQVA
SREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKK
LDPGWNPQIPEKKGKEANTGFGGPVISSLYHEETIREEDKNIFDYCRENNIDHITKAIKS
KNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDI
VELLLQSGADPTLRDQDGCLPEEVTGCKTVSLVLQRHTTGKA
Enzyme 117 Number of Residues 282
Enzyme 117 Molecular Weight 31150.6
Enzyme 117 Theoretical pI 4.76
Enzyme 117 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 117 General Function Involved in acyl-CoA binding
Enzyme 117 Specific Function Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0- CoA. Does not bind fatty acids
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein 56204928 Link Image
Enzyme 117 UniProtKB/Swiss-Prot ID Q9BR61 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name ACBD6_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >849 bp
ATGGCTTCATCATTCCTGCCCGCGGGGGCCATCACCGGCGACAGCGGTGGAGAGCTGAGC
TCAGGGGACGACTCCGGGGAGGTGGAGTTCCCCCATAGCCCTGAGATCGAGGAGACCAGT
TGCCTGGCCGAGCTGTTTGAGAAGGCTGCCGCGCACCTGCAAGGCCTGATTCAGGTGGCC
AGCAGGGAGCAGCTCTTGTACCTGTATGCCAGGTACAAACAGGTCAAAGTTGGAAATTGT
AATACTCCTAAACCAAGCTTCTTTGATTTTGAAGGAAAGCAAAAATGGGAAGCTTGGAAA
GCACTTGGTGATTCAAGCCCCAGCCAAGCAATGCAGGAATATATCGCAGTAGTTAAAAAA
CTAGATCCAGGTTGGAATCCTCAGATACCAGAGAAGAAAGGAAAAGAAGCAAATACAGGT
TTTGGTGGGCCAGTTATTAGTTCTCTATATCATGAAGAAACCATCAGGGAAGAAGACAAA
AATATATTTGATTACTGCAGGGAAAACAACATTGACCATATAACCAAAGCCATCAAATCG
AAAAATGTGGATGTGAATGTGAAAGATGAAGAGGGTAGGGCTCTACTTCACTGGGCCTGT
GATCGAGGACATAAGGAACTAGTCACAGTGTTGCTGCAACATAGAGCTGACATTAACTGT
CAGGACAATGAAGGCCAAACAGCTCTACATTATGCCTCTGCCTGTGAGTTTCTGGATATT
GTAGAGCTGCTGCTCCAGTCTGGTGCTGACCCCACTCTCCGAGACCAGGATGGCTGCCTG
CCAGAGGAGGTGACAGGCTGCAAAACAGTTTCTTTGGTGCTGCAGCGGCACACAACTGGC
AAGGCTTAA
Enzyme 117 GenBank Gene ID AL139141 Link Image
Enzyme 117 GeneCard ID ACBD6 Link Image
Enzyme 117 GenAtlas ID ACBD6 Link Image
Enzyme 117 HGNC ID HGNC:23339 Link Image
Enzyme 117 Chromosome Location 1
Enzyme 117 Locus 1q25.1
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Soupene E, Serikov V, Kuypers FA: Characterization of an acyl-coenzyme A binding protein predominantly expressed in human primitive progenitor cells. J Lipid Res. 2008 May;49(5):1103-12. Epub 2008 Feb 11. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 17711
Enzyme 118 Name Not Available
Enzyme 118 Synonyms Not Available
Enzyme 118 Gene Name Not Available
Enzyme 118 Protein Sequence Not Available
Enzyme 118 Number of Residues Not Available
Enzyme 118 Molecular Weight Not Available
Enzyme 118 Theoretical pI Not Available
Enzyme 118 GO Classification Not Available
Enzyme 118 General Function Not Available
Enzyme 118 Specific Function Not Available
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function Not Available
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein Not Available
Enzyme 118 UniProtKB/Swiss-Prot ID Not Available
Enzyme 118 UniProtKB/Swiss-Prot Entry Name Not Available
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence Not Available
Enzyme 118 GenBank Gene ID Not Available
Enzyme 118 GeneCard ID Not Available
Enzyme 118 GenAtlas ID Not Available
Enzyme 118 HGNC ID Not Available
Enzyme 118 Chromosome Location Not Available
Enzyme 118 Locus Not Available
Enzyme 118 SNPs Not Available
Enzyme 118 General References Not Available
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 17712
Enzyme 119 Name PECI protein
Enzyme 119 Synonyms Not Available
Enzyme 119 Gene Name PECI
Enzyme 119 Protein Sequence >PECI protein
MNRTAMRASQKDFENSINQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINK
AKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGI
TKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPP
GGVEEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHT
PFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEV
WTRLKAFAKLPPNVLRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSR
KSKL
Enzyme 119 Number of Residues 364
Enzyme 119 Molecular Weight 40192.8
Enzyme 119 Theoretical pI 9.11
Enzyme 119 GO Classification
Function
  • acyl-CoA binding
  • binding
  • catalytic activity
  • fatty acid binding
  • lipid binding
Process
  • metabolic process
Component
Enzyme 119 General Function Involved in acyl-CoA binding
Enzyme 119 Specific Function Not Available
Enzyme 119 Pathways Not Available
Enzyme 119 Reactions Not Available
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 48145653 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID Q6IBN4 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name Q6IBN4_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >1095 bp
ATGAATAGAACAGCAATGAGAGCCAGTCAGAAGGACTTTGAAAATTCAATAAATCAAGTG
AAACTCTTGAAAAAGGATCCAGGAAACGAAGTGAAGCTAAAACTCTACGCGCTATATAAG
CAGGCCACTGAAGGACCTTGTAACATGCCCAAACCAGGTGTATTTGACTTGATCAACAAG
GCCAAATGGGACGCATGGAATGCCCTTGGCAGCCTGCCCAAGGAAGCTGCCAGGCAGAAC
TATGTGGATTTGGTGTCCAGTTTGAGTCCTTCATTGGAATCCTCTAGTCAGGTGGAGCCT
GGAACAGACAGGAAATCAACTGGGTTTGAAACTCTGGTGGTGACCTCCGAAGATGGCATC
ACAAAGATCATGTTCAACCGGCCCAAAAAGAAAAATGCCATAAACACTGAGATGTATCAT
GAAATTATGCGTGCACTTAAAGCTGCCAGCAAGGATGACTCAATCATCACTGTTTTAACA
GGAAATGGTGACTATTACAGTAGTGGGAATGATCTGACTAACTTCACTGATATTCCCCCT
GGTGGAGTAGAGGAGAAAGCTAAAAATAATGCCGTTTTACTGAGGGAATTTGTGGGCTGT
TTTATAGATTTTCCTAAGCCTCTGATTGCAGTGGTCAATGGTCCAGCTGTGGGCATCTCC
GTCACCCTCCTTGGGCTATTCGATGCCGTGTATGCATCTGACAGGGCAACATTTCATACA
CCATTTAGTCACCTAGGCCAAAGTCCGGAAGGATGCTCCTCTTACACTTTTCCGAAGATA
ATGAGCCCAGCCAAGGCAACAGAGATGCTTATTTTTGGAAAGAAGTTAACAGCGGGAGAG
GCATGTGCTCAAGGACTTGTTACTGAAGTTTTCCCTGATAGCACTTTTCAGAAAGAAGTC
TGGACCAGGCTGAAGGCATTTGCAAAGCTTCCCCCAAATGTCTTGAGAATTTCAAAAGAG
GTAATCAGGAAAAGAGAGAGAGAAAAACTACACGCTGTTAATGCTGAAGAATGCAATGTC
CTTCAGGGAAGATGGCTATCAGATGAATGCACAAATGCTGTGGTGAACTTCTTATCCAGA
AAATCAAAACTTTAA
Enzyme 119 GenBank Gene ID CR456768 Link Image
Enzyme 119 GeneCard ID PECI Link Image
Enzyme 119 GenAtlas ID PECI Link Image
Enzyme 119 HGNC ID HGNC:14601 Link Image
Enzyme 119 Chromosome Location 6
Enzyme 119 Locus 6p24.3
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References Not Available
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 17713
Enzyme 120 Name cDNA FLJ53969, highly similar to Trifunctional enzyme subunit alpha, mitochondrial
Enzyme 120 Synonyms Not Available
Enzyme 120 Gene Name Not Available
Enzyme 120 Protein Sequence >cDNA FLJ53969, highly similar to Trifunctional enzyme subunit alpha, mitochondrial
MVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYLEEVAITFAKG
LADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPAPLKIIDVVKT
GIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKDVKHLAILGAG
LMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSFERDSIFSNLT
GQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALPISEIAAVSKR
PEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVKDGPGFYTTRC
LAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVAEDLGKVFGER
FGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLKLPPKSEVSSD
EDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKIV
DRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 120 Number of Residues 573
Enzyme 120 Molecular Weight 62609.5
Enzyme 120 Theoretical pI 9.22
Enzyme 120 GO Classification
Function
  • 3-hydroxyacyl-CoA dehydrogenase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • enoyl-CoA hydratase activity
  • hydro-lyase activity
  • lyase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid beta-oxidation
  • fatty acid catabolic process
  • fatty acid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
Component
  • fatty acid beta-oxidation multienzyme complex
  • intracellular membrane-bounded organelle
  • macromolecular complex
  • membrane-bounded organelle
  • mitochondrion
  • organelle
  • protein complex
Enzyme 120 General Function Involved in oxidoreductase activity
Enzyme 120 Specific Function Not Available
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions Not Available
Enzyme 120 Pfam Domain Function
Enzyme 120 Signals
  • None
Enzyme 120 Transmembrane Regions
  • None
Enzyme 120 Essentiality Not Available
Enzyme 120 GenBank ID Protein 194373621 Link Image
Enzyme 120 UniProtKB/Swiss-Prot ID B4DDZ5 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name B4DDZ5_HUMAN Link Image
Enzyme 120 PDB ID Not Available
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence >1722 bp
ATGGTGGGTGTGCCTGCTGCTTTGGACATGATGCTGACTGGTAGAAGCATTCGTGCAGAC
AGGGCAAAGAAAATGGGACTGGTTGACCAACTGGTGGAACCCCTGGGACCAGGACTAAAA
CCTCCAGAGGAACGGACAATAGAATACCTAGAAGAAGTTGCAATTACTTTTGCCAAAGGA
CTAGCTGATAAGAAGATCTCTCCAAAGAGAGACAAGGGATTGGTGGAAAAATTGACAGCG
TATGCCATGACTATTCCATTTGTCAGGCAACAGGTTTACAAAAAAGTGGAAGAAAAAGTG
CGAAAGCAGACTAAAGGCCTTTATCCTGCACCTCTGAAAATAATTGATGTGGTAAAGACT
GGAATTGAGCAAGGGAGTGATGCCGGTTATCTCTGTGAATCTCAGAAATTTGGAGAGCTT
GTAATGACCAAAGAATCAAAGGCCTTGATGGGACTCTACCATGGTCAGGTCCTGTGCAAG
AAGAATAAATTTGGAGCTCCACAGAAGGATGTTAAGCATCTGGCTATTCTTGGTGCAGGG
CTGATGGGAGCAGGCATCGCCCAAGTCTCCGTGGATAAGGGGCTAAAGACTATACTTAAA
GATGCCACCCTCACTGCGCTAGACCGAGGACAGCAACAAGTGTTCAAAGGATTGAATGAC
AAAGTGAAGAAGAAAGCTCTAACATCATTTGAAAGGGATTCCATCTTCAGCAACTTGACT
GGGCAGCTTGATTACCAAGGTTTTGAAAAGGCCGACATGGTGATTGAAGCTGTGTTTGAG
GACCTTAGTCTTAAGCACAGAGTGCTAAAGGAAGTAGAAGCGGTGATTCCAGATCACTGT
ATCTTTGCCAGTAACACATCTGCTCTCCCAATCAGTGAAATCGCTGCTGTCAGCAAAAGA
CCTGAGAAGGTGATTGGCATGCACTACTTCTCTCCCGTGGACAAGATGCAGCTGCTGGAG
ATTATCACGACCGAGAAAACTTCCAAAGACACCAGTGCTTCAGCTGTAGCAGTTGGTCTC
AAGCAGGGGAAGGTCATCATTGTGGTTAAGGATGGACCTGGCTTCTATACTACCAGGTGT
CTTGCGCCCATGATGTCTGAAGTCATCCGAATCCTCCAGGAAGGAGTTGACCCGAAGAAG
CTGGATTCCCTGACCACAAGCTTTGGCTTTCCTGTGGGTGCCGCCACACTGGTGGATGAA
GTTGGTGTGGATGTAGCGAAACATGTGGCGGAAGATCTGGGCAAAGTCTTTGGGGAGCGG
TTTGGAGGTGGAAACCCAGAACTGCTGACACAGATGGTGTCCAAGGGCTTCCTAGGTCGT
AAATCTGGGAAGGGCTTTTACATCTATCAGGAGGGTGTGAAGAGGAAGGATTTGAATTCT
GACATGGATAGTATTTTAGCGAGTCTGAAGCTGCCTCCTAAGTCTGAAGTCTCATCAGAC
GAAGACATCCAGTTCCGCCTGGTGACAAGATTTGTGAATGAGGCAGTCATGTGCCTGCAA
GAGGGGATCTTGGCCACACCTGCAGAGGGAGACATCGGAGCCGTCTTTGGGCTTGGCTTC
CCGCCTTGTCTGGGAGGGCCTTTCCGCTTTGTGGATCTGTATGGCGCCCAGAAGATAGTG
GACCGGCTCAAGAAATATGAAGCTGCCTATGGAAAACAGTTCACCCCATGCCAGCTGCTA
GCTGACCATGCTAACAGCCCTAACAAGAAGTTCTACCAGTGA
Enzyme 120 GenBank Gene ID AK293398 Link Image
Enzyme 120 GeneCard ID Not Available
Enzyme 120 GenAtlas ID Not Available
Enzyme 120 HGNC ID HGNC:4801 Link Image
Enzyme 120 Chromosome Location Not Available
Enzyme 120 Locus Not Available
Enzyme 120 SNPs Not Available
Enzyme 120 General References Not Available
Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 17714
Enzyme 121 Name Acyl-Coenzyme A binding domain containing 5
Enzyme 121 Synonyms Not Available
Enzyme 121 Gene Name ACBD5
Enzyme 121 Protein Sequence >Acyl-Coenzyme A binding domain containing 5
MPGPPLSSARHALPLGSWESWCCCCLIPADRPWDRGQHWQLEMADTRSVHETRFEAAVKV
IQSLPKNGSFQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKE
EAMIAYVEEMKKIIETMPMTEKVEELLRVIGPFYEIVEDKKSGRSSDITSVRLEKISKCL
EDLGNVLTSTPNAKTVNGKAESSDSGAESEEEEAQEEVKGAEQSDNDKKMMKKSADHKNL
EVIVTNGYDKDGFVQDIQNDIHASSSLNGRSTEEVKPIDENLGQTGKSAVCIHQ
Enzyme 121 Number of Residues 294
Enzyme 121 Molecular Weight 32973.9
Enzyme 121 Theoretical pI 4.81
Enzyme 121 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 121 General Function Involved in acyl-CoA binding
Enzyme 121 Specific Function Not Available
Enzyme 121 Pathways Not Available
Enzyme 121 Reactions Not Available
Enzyme 121 Pfam Domain Function
Enzyme 121 Signals
  • None
Enzyme 121 Transmembrane Regions
  • None
Enzyme 121 Essentiality Not Available
Enzyme 121 GenBank ID Protein 55958299 Link Image
Enzyme 121 UniProtKB/Swiss-Prot ID Q5T8E0 Link Image
Enzyme 121 UniProtKB/Swiss-Prot Entry Name Q5T8E0_HUMAN Link Image
Enzyme 121 PDB ID Not Available
Enzyme 121 Cellular Location Not Available
Enzyme 121 Gene Sequence >883 bp
ATGCCCGGACCCCCTCTGTCTTCTGCTAGACATGCTCTTCCTCTCGGCTCTTGGGAAAGC
TGGTGCTGCTGCTGCCTGATTCCCGCCGACAGACCTTGGGACCGGGGCCAACACTGGCAG
CTGGAGATGGCGGACACGAGATCCGTGCACGAGACTAGGTTTGAGGCGGCCGTGAAGGTG
ATCCAGAGTTTGCCGAAGAATGGTTCATTCCAGCCAACAAATGAAATGATGCTTAAATTT
TATAGCTTCTATAAGCAGGCAACTGAAGGACCCTGTAAACTTTCAAGGCCTGGATTTTGG
GATCCTATTGGAAGATATAAATGGGATGCTTGGAGTTCACTGGGTGATATGACCAAAGAG
GAAGCCATGATTGCATATGTTGAAGAAATGAAAAAGATTATTGAAACTATGCCAATGACT
GAGAAAGTTGAAGAATTGCTGCGTGTCATAGGTCCATTTTATGAAATTGTCGAGGACAAA
AAGAGTGGCAGGAGTTCTGATATAACCTCAGTCCGACTGGAGAAAATCTCTAAATGTTTA
GAAGATCTTGGTAATGTTCTCACTTCTACTCCAAACGCCAAAACCGTTAATGGTAAAGCT
GAAAGCAGTGACAGTGGAGCCGAGTCTGAGGAAGAAGAGGCCCAAGAAGAAGTGAAAGGA
GCAGAACAAAGTGATAATGATAAGAAAATGATGAAGAAGTCAGCAGACCATAAGAATTTG
GAAGTCATTGTCACTAATGGCTATGATAAAGATGGCTTTGTTCAGGATATACAGAATGAC
ATTCATGCCAGTTCTTCCCTGAATGGCAGAAGCACTGAAGAAGTAAAGCCCATTGATGAA
AACTTGGGGCAAACTGGAAAATCTGCTGTTTGCATTCACCAAG
Enzyme 121 GenBank Gene ID AL160291 Link Image
Enzyme 121 GeneCard ID ACBD5 Link Image
Enzyme 121 GenAtlas ID ACBD5 Link Image
Enzyme 121 HGNC ID HGNC:23338 Link Image
Enzyme 121 Chromosome Location 1
Enzyme 121 Locus 10p12.1
Enzyme 121 SNPs SNPJam Report Link Image
Enzyme 121 General References Not Available
Enzyme 121 Metabolite References Not Available
Enzyme 122 [top]
Enzyme 122 ID 17715
Enzyme 122 Name Acyl-Coenzyme A binding domain containing 5, isoform CRA_a
Enzyme 122 Synonyms
  1. SubName: Putative uncharacterized protein ACBD5
Enzyme 122 Gene Name ACBD5
Enzyme 122 Protein Sequence >Acyl-Coenzyme A binding domain containing 5, isoform CRA_a
MADTRSVHETRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDP
IGRYKWDAWSSLGDMTKEEAMIAYVEEMKKIIETMPMTEKVEELLRVIGPFYEIVEDKKS
GRSSDITSVRLEKISKCLEDLGNVLTSTPNAKTVNGKAESSDSGAESEEEEAQEEVKGAE
QSDNDKKMMKKSADHKNLEVIVTNGYDKDGFVQDIQNDIHASSSLNGRSTEEVKPIDENL
GQTGKSAVCIHQDINDDHVEDVTGIQHLTSDSDSEVYCDSMEQFGQEESLDSFTSNNGPF
QYYLGGHSSQPMENSGFREDIQVPPGNGNIGNMQVVAVEGKGEVKHGGEDGRNNSGAPHR
EKRGGETDEFSNVRRGRGHRMQHLSEGTKGRQVGSGGDGERWGSDRGSRGSLNEQIALVL
MRLQEDMQNVLQRLQKLETLTALQAKSSTSTLQTAPQPTSQRPSWWPFEMSPGVLTFAII
WPFIAQWLVYLYYQRRRRKLN
Enzyme 122 Number of Residues 501
Enzyme 122 Molecular Weight 56085.0
Enzyme 122 Theoretical pI 4.96
Enzyme 122 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 122 General Function Involved in acyl-CoA binding
Enzyme 122 Specific Function Not Available
Enzyme 122 Pathways Not Available
Enzyme 122 Reactions Not Available
Enzyme 122 Pfam Domain Function
Enzyme 122 Signals
  • None
Enzyme 122 Transmembrane Regions
  • None
Enzyme 122 Essentiality Not Available
Enzyme 122 GenBank ID Protein 55958288 Link Image
Enzyme 122 UniProtKB/Swiss-Prot ID A8MSV1 Link Image
Enzyme 122 UniProtKB/Swiss-Prot Entry Name A8MSV1_HUMAN Link Image
Enzyme 122 PDB ID Not Available
Enzyme 122 Cellular Location Not Available
Enzyme 122 Gene Sequence Not Available
Enzyme 122 GenBank Gene ID AL160291 Link Image
Enzyme 122 GeneCard ID ACBD5 Link Image
Enzyme 122 GenAtlas ID Not Available
Enzyme 122 HGNC ID HGNC:23338 Link Image
Enzyme 122 Chromosome Location 1
Enzyme 122 Locus 10p12.1
Enzyme 122 SNPs SNPJam Report Link Image
Enzyme 122 General References Not Available
Enzyme 122 Metabolite References Not Available
Enzyme 123 [top]
Enzyme 123 ID 17716
Enzyme 123 Name cDNA FLJ50016, highly similar to Acyl-CoA-binding domain-containing protein 4
Enzyme 123 Synonyms Not Available
Enzyme 123 Gene Name Not Available
Enzyme 123 Protein Sequence >cDNA FLJ50016, highly similar to Acyl-CoA-binding domain-containing protein 4
MGTEKESPEPDCQKQFQAAVSVIQNLPKNGSYRPSYEEMLRFYSYYKQATMGPCLVPRPG
FWDPIGRYKWDAWNSLGKMSREEAMSAYITEMKLVAQKVIDTVPLGEVAEDMFGYFEPLY
QVIPDMPRPPETFLRRVTGWKEQVVNGDVGAVSEPPCLPKEPAPPSPASLWAVTLPTPPQ
SPIHPGTWTPRFSVIPWSSWSLSWFGQSSGQHLEESVIPGTAPCPPQRKRGCGAARRGPR
SWTCGCWGQFEHYRRACRRCRRGCRAWRACPGPLSRGRSPGPVLGHGPLGSRGPRCSSSS
CGPSSSSGSSECFGPKRGDCQWRGLCSQLRLSRCALSLPRV
Enzyme 123 Number of Residues 341
Enzyme 123 Molecular Weight 37838.9
Enzyme 123 Theoretical pI 9.16
Enzyme 123 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 123 General Function Involved in acyl-CoA binding
Enzyme 123 Specific Function Not Available
Enzyme 123 Pathways Not Available
Enzyme 123 Reactions Not Available
Enzyme 123 Pfam Domain Function
Enzyme 123 Signals
  • None
Enzyme 123 Transmembrane Regions
  • None
Enzyme 123 Essentiality Not Available
Enzyme 123 GenBank ID Protein 194382300 Link Image
Enzyme 123 UniProtKB/Swiss-Prot ID B4DJP3 Link Image
Enzyme 123 UniProtKB/Swiss-Prot Entry Name B4DJP3_HUMAN Link Image
Enzyme 123 PDB ID Not Available
Enzyme 123 Cellular Location Not Available
Enzyme 123 Gene Sequence >1026 bp
ATGGGCACCGAGAAAGAAAGCCCAGAGCCCGACTGCCAGAAACAGTTCCAGGCTGCAGTG
AGCGTCATCCAGAACCTGCCCAAGAACGGTTCTTACCGCCCCTCCTATGAAGAGATGCTG
CGATTCTACAGTTACTACAAGCAGGCCACCATGGGGCCCTGCCTGGTCCCCCGGCCCGGG
TTCTGGGACCCCATTGGACGATATAAGTGGGACGCCTGGAACAGTCTGGGCAAGATGAGC
AGGGAGGAGGCCATGTCTGCCTACATCACTGAAATGAAACTGGTGGCACAGAAGGTGATC
GACACAGTGCCCCTGGGTGAGGTGGCAGAGGACATGTTTGGTTACTTCGAGCCCCTGTAC
CAGGTGATCCCTGACATGCCGAGGCCCCCAGAGACCTTCCTGAGAAGGGTCACAGGTTGG
AAAGAGCAGGTTGTGAATGGAGATGTTGGGGCTGTTTCAGAGCCTCCCTGCCTCCCCAAG
GAACCGGCACCCCCAAGCCCAGCTTCCCTCTGGGCAGTAACTCTACCAACCCCTCCACAG
AGTCCCATTCACCCAGGGACCTGGACTCCGAGGTTTTCTGTGATTCCCTGGAGCAGCTGG
AGCCTGAGCTGGTTTGGACAGAGCAGCGGGCAGCATCTGGAGGAAAGCGTGATCCCAGGA
ACAGCCCCGTGCCCCCCACAAAGAAAGAGGGGTTGCGGGGCAGCCCGCCGGGGCCCCAGG
AGTTGGACGTGTGGCTGCTGGGGACAGTTCGAGCACTACAGGAGAGCATGCAGGAGGTGC
AGGCGAGGGTGCAGAGCCTGGAGAGCATGCCCCGGCCCCCTGAGCAGAGGCCGCAGCCCA
GGCCCAGTGCTCGGCCATGGCCCCTTGGGCTCCCGGGGCCCGCGCTGCTCTTCTTCCTCC
TGTGGCCCTTCGTCGTCCAGTGGCTCTTCCGAATGTTTCGGACCCAAAAGAGGTGACTGT
CAGTGGAGGGGTCTCTGCAGCCAACTGAGACTATCTCGCTGTGCCCTGAGCCTTCCTAGG
GTTTAG
Enzyme 123 GenBank Gene ID AK296167 Link Image
Enzyme 123 GeneCard ID Not Available
Enzyme 123 GenAtlas ID Not Available
Enzyme 123 HGNC ID HGNC:23337 Link Image
Enzyme 123 Chromosome Location Not Available
Enzyme 123 Locus Not Available
Enzyme 123 SNPs Not Available
Enzyme 123 General References Not Available
Enzyme 123 Metabolite References Not Available
Enzyme 124 [top]
Enzyme 124 ID 17717
Enzyme 124 Name Acyl-CoA-binding domain-containing protein 7
Enzyme 124 Synonyms Not Available
Enzyme 124 Gene Name ACBD7
Enzyme 124 Protein Sequence >Acyl-CoA-binding domain-containing protein 7
MALQADFDRAAEDVRKLKARPDDGELKELYGLYKQAIVGDINIACPGMLDLKGKAKWEAW
NLKKGLSTEDATSAYISKAKELIEKYGI
Enzyme 124 Number of Residues 88
Enzyme 124 Molecular Weight 9790.2
Enzyme 124 Theoretical pI 6.73
Enzyme 124 GO Classification
Function
  • acyl-CoA binding
  • binding
  • fatty acid binding
  • lipid binding
Process
Component
Enzyme 124 General Function Involved in acyl-CoA binding
Enzyme 124 Specific Function Not Available
Enzyme 124 Pathways Not Available
Enzyme 124 Reactions Not Available
Enzyme 124 Pfam Domain Function
Enzyme 124 Signals
  • None
Enzyme 124 Transmembrane Regions
  • None
Enzyme 124 Essentiality Not Available
Enzyme 124 GenBank ID Protein 193787877 Link Image
Enzyme 124 UniProtKB/Swiss-Prot ID Q8N6N7 Link Image
Enzyme 124 UniProtKB/Swiss-Prot Entry Name ACBD7_HUMAN Link Image
Enzyme 124 PDB ID Not Available
Enzyme 124 Cellular Location Not Available
Enzyme 124 Gene Sequence >267 bp
ATGGCCCTGCAGGCTGATTTTGACAGGGCTGCAGAAGATGTGAGGAAGCTGAAAGCAAGA
CCAGATGATGGAGAACTGAAAGAACTCTATGGGCTTTACAAACAAGCAATAGTTGGAGAC
ATTAATATTGCGTGTCCAGGAATGCTAGATTTAAAAGGCAAAGCCAAATGGGAAGCATGG
AACCTCAAAAAAGGGTTGTCGACGGAAGATGCGACGAGTGCCTATATTTCTAAAGCAAAG
GAGCTGATAGAAAAATACGGAATTTAG
Enzyme 124 GenBank Gene ID AK095538 Link Image
Enzyme 124 GeneCard ID ACBD7 Link Image
Enzyme 124 GenAtlas ID ACBD7 Link Image
Enzyme 124 HGNC ID HGNC:17715 Link Image
Enzyme 124 Chromosome Location 1
Enzyme 124 Locus 10p13
Enzyme 124 SNPs SNPJam Report Link Image
Enzyme 124 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 124 Metabolite References Not Available
Enzyme 125 [top]
Enzyme 125 ID 17718
Enzyme 125 Name Fatty acid-binding protein, intestinal
Enzyme 125 Synonyms
  1. Fatty acid-binding protein 2
  2. Intestinal-type fatty acid-binding protein
  3. I-FABP
Enzyme 125 Gene Name FABP2
Enzyme 125 Protein Sequence >Fatty acid-binding protein, intestinal
MAFDSTWKVDRSENYDKFMEKMGVNIVKRKLAAHDNLKLTITQEGNKFTVKESSAFRNIE
VVFELGVTFNYNLADGTELRGTWSLEGNKLIGKFKRTDNGNELNTVREIIGDELVQTYVY
EGVEAKRIFKKD
Enzyme 125 Number of Residues 132
Enzyme 125 Molecular Weight 15207.2
Enzyme 125 Theoretical pI 7.52
Enzyme 125 GO Classification
Function
  • binding
  • lipid binding
  • transporter activity
Process
  • establishment of localization
  • transport
Component
Enzyme 125 General Function Involved in binding
Enzyme 125 Specific Function FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long- chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor
Enzyme 125 Pathways Not Available
Enzyme 125 Reactions Not Available
Enzyme 125 Pfam Domain Function
Enzyme 125 Signals
  • None
Enzyme 125 Transmembrane Regions
  • None
Enzyme 125 Essentiality Not Available
Enzyme 125 GenBank ID Protein 46854681 Link Image
Enzyme 125 UniProtKB/Swiss-Prot ID P12104 Link Image
Enzyme 125 UniProtKB/Swiss-Prot Entry Name FABPI_HUMAN Link Image
Enzyme 125 PDB ID 3IFB Link Image
Enzyme 125 PDB File Show
Enzyme 125 3D Structure
Enzyme 125 Cellular Location Not Available
Enzyme 125 Gene Sequence >399 bp
ATGGCGTTTGACAGCACTTGGAAGGTAGACCGGAGTGAAAACTATGACAAGTTCATGGAA
AAAATGGGTGTTAATATAGTGAAAAGGAAGCTTGCAGCTCATGACAATTTGAAGCTGACA
ATTACACAAGAAGGAAATAAATTCACAGTCAAAGAATCAAGCGCTTTTCGAAACATTGAA
GTTGTTTTTGAACTTGGTGTCACCTTTAATTACAATCTAGCAGACGGAACTGAACTCAGG
GGGACCTGGAGCCTTGAGGGAAATAAACTTATTGGAAAATTCAAACGGACAGACAATGGA
AACGAACTGAATACTGTCCGAGAAATTATAGGTGATGAACTAGTCCAGACTTATGTATAT
GAAGGAGTAGAAGCCAAAAGGATCTTTAAAAAGGATTGA
Enzyme 125 GenBank Gene ID BC069466 Link Image
Enzyme 125 GeneCard ID FABP2 Link Image
Enzyme 125 GenAtlas ID FABP2 Link Image
Enzyme 125 HGNC ID HGNC:3556 Link Image
Enzyme 125 Chromosome Location 4
Enzyme 125 Locus 4q28-q31
Enzyme 125 SNPs SNPJam Report Link Image
Enzyme 125 General References
  1. Sweetser DA, Birkenmeier EH, Klisak IJ, Zollman S, Sparkes RS, Mohandas T, Lusis AJ, Gordon JI: The human and rodent intestinal fatty acid binding protein genes. A comparative analysis of their structure, expression, and linkage relationships. J Biol Chem. 1987 Nov 25;262(33):16060-71. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Pelsers MM, Namiot Z, Kisielewski W, Namiot A, Januszkiewicz M, Hermens WT, Glatz JF: Intestinal-type and liver-type fatty acid-binding protein in the intestine. Tissue distribution and clinical utility. Clin Biochem. 2003 Oct;36(7):529-35. [PubMed Link Image]
  4. Darimont C, Gradoux N, de Pover A: Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells. Am J Physiol. 1999 Mar;276(3 Pt 1):G606-12. [PubMed Link Image]
  5. Rajabzadeh M, Kao J, Frieden C: Consequences of single-site mutations in the intestinal fatty acid binding protein. Biochemistry. 2003 Oct 28;42(42):12192-9. [PubMed Link Image]
  6. Zhang F, Lucke C, Baier LJ, Sacchettini JC, Hamilton JA: Solution structure of human intestinal fatty acid binding protein: implications for ligand entry and exit. J Biomol NMR. 1997 Apr;9(3):213-28. [PubMed Link Image]
  7. Zhang F, Lucke C, Baier LJ, Sacchettini JC, Hamilton JA: Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism. Biochemistry. 2003 Jun 24;42(24):7339-47. [PubMed Link Image]
  8. Baier LJ, Sacchettini JC, Knowler WC, Eads J, Paolisso G, Tataranni PA, Mochizuki H, Bennett PH, Bogardus C, Prochazka M: An amino acid substitution in the human intestinal fatty acid binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance. J Clin Invest. 1995 Mar;95(3):1281-7. [PubMed Link Image]
  9. Kunsan X, Taisan Z, Weiping J, Duoqi S, Wei D, Jie L, Junxi L, Rong Z: The association of Ala54Thr variant of intestinal fatty acid binding protein gene with general and regional adipose tissue depots. Chin Med Sci J. 1999 Mar;14(1):46-51. [PubMed Link Image]
Enzyme 125 Metabolite References Not Available