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Human Metabolome Database Version 2.5

 

Showing metabocard for LysoPC(16:0) (HMDB10382)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-09-16 14:19:56
Update Date 2009-10-22 15:35:39
Accession Number HMDB10382
Secondary Accession Numbers Not Available
Common Name LysoPC(16:0)
Description LysoPC(16:0) is a lysophospholipid (LyP). It is a monoglycerophospholipid in which a phosphorylcholine moiety occupies a glycerol substitution site. Lysophosphatidylcholines can have different combinations of fatty acids of varying lengths and saturation attached at the C-1 (sn-1) position. Fatty acids containing 16, 18 and 20 carbons are the most common. LysoPC(16:0), in particular, consists of one chain of palmitic acid at the C-1 position. The palmitic acid moiety is derived from fish oils, milk fats, vegetable oils and animal fats. Lysophosphatidylcholine is found in small amounts in most tissues. It is formed by hydrolysis of phosphatidylcholine by the enzyme phospholipase A2, as part of the de-acylation/re-acylation cycle that controls its overall molecular species composition. It can also be formed inadvertently during extraction of lipids from tissues if the phospholipase is activated by careless handling. In blood plasma significant amounts of lysophosphatidylcholine are formed by a specific enzyme system, lecithin:cholesterol acyltransferase (LCAT), which is secreted from the liver. The enzyme catalyzes the transfer of the fatty acids of position sn-2 of phosphatidylcholine to the free cholesterol in plasma, with formation of cholesterol esters and lysophosphatidylcholine. Lysophospholipids have a role in lipid signaling by acting on lysophospholipid receptors (LPL-R). LPL-R's are members of the G protein-coupled receptor family of integral membrane proteins.
Synonyms
  1. LysoPC(16:0/0:0)
  2. Lysophosphatidylcholine(16:0/0:0)
  3. LPC(16:0)
  4. LPC(16:0/0:0)
  5. LyPC(16:0)
  6. LyPC(16:0/0:0)
  7. Lysophosphatidylcholine(16:0)
  8. LysoPC(16:0)
  9. 1-palmitoyl-glycero-3-phosphocholine
  10. 1-palmitoyl-lysophosphatidylcholine
Chemical IUPAC Name 1-hexadecanoyl-glycero-3-phosphocholine
Chemical Formula C24H50NO7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Phospholipids
Sub Class
  • Lysophosphatidylcholines
Family
  • Mammalian Metabolite
Species
  • cation
  • anion
  • secondary alcohol
  • quaternary ammonium salt
  • carboxylic acid ester
  • phosphoric acid ester
Biofunction
  • Membrane component
  • Energy source
  • Cell signaling
Application
Source
  • Endogenous
Average Molecular Weight 495.630
Monoisotopic Molecular Weight 495.332489
Isomeric SMILES CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP([O-])(=O)OCC[N+](C)(C)C
Canonical SMILES CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C
KEGG Compound ID C04230 Link Image
BioCyc ID PHOSPHATIDYLCHOLINE Link Image
BiGG ID Not Available
Wikipedia Link Lecithin Link Image
NuGOwiki Link HMDB10382 Link Image
Metagene Link HMDB10382 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C24H50NO7P/c1-5-6-7-8-9-10-11-12-13-14-15-16-17-18-24(27)30-21-23(26)22-32-33(28,29)31-20-19-25(2,3)4/h23,26H,5-22H2,1-4H3/t23-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.68e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.83 [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 Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
Biofluid Location
  • Blood
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 106.598 +/- 16.732 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments quantified by Lipomics Technologies, Inc.
References
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Phospholipid Biosynthesis SMP00025 Link Image map00564 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Acyl-protein thioesterase 1
  2. Group XV phospholipase A2
  3. Calcium-dependent phospholipase A2
  4. Group IIF secretory phospholipase A2
  5. Cytosolic phospholipase A2
  6. Phospholipase A2
  7. Group XIIB secretory phospholipase A2-like protein
  8. Group 10 secretory phospholipase A2
  9. Group IIE secretory phospholipase A2
  10. Acyl-protein thioesterase 2
  11. 85 kDa calcium-independent phospholipase A2
  12. Phosphatidylcholine-sterol acyltransferase
  13. Eosinophil lysophospholipase
  14. Group IID secretory phospholipase A2
  15. Platelet-activating factor acetylhydrolase
  16. Platelet-activating factor acetylhydrolase IB subunit gamma
  17. Platelet-activating factor acetylhydrolase IB subunit beta
  18. Group 3 secretory phospholipase A2
  19. Platelet-activating factor acetylhydrolase 2, cytoplasmic
  20. Phospholipase A2, group XIIA, isoform CRA_b
  21. Lysophospholipid acyltransferase 5
  22. Lysophosphatidylcholine acyltransferase 1
  23. Lysophosphatidylcholine acyltransferase 2
  24. 60 kDa lysophospholipase
  25. Phospholipase B1, membrane-associated
  26. Cytosolic phospholipase A2 beta
  27. cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
  28. cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
  29. Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5285
Enzyme 1 Name Acyl-protein thioesterase 1
Enzyme 1 Synonyms
  1. APT-1
  2. hAPT1
  3. Lysophospholipase 1
  4. Lysophospholipase I
  5. LPL-I
  6. LysoPLA I
Enzyme 1 Gene Name LYPLA1
Enzyme 1 Protein Sequence >Acyl-protein thioesterase 1
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRP
VTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQ
GGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLM
FGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
Enzyme 1 Number of Residues 230
Enzyme 1 Molecular Weight 24669.4
Enzyme 1 Theoretical pI 6.77
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Involved in hydrolase activity
Enzyme 1 Specific Function Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity and also low lysophospholipase activity
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 5453722 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O75608 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LYPA1_HUMAN Link Image
Enzyme 1 PDB ID 1FJ2 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >693 bp
ATGTGCGGCAATAACATGTCAACCCCGCTGCCCGCCATCGTGCCCGCCGCCCGGAAGGCC
ACCGCTGCGGTGATTTTCCTGCATGGATTGGGAGATACTGGGCACGGATGGGCAGAAGCC
TTTGCAGGTATCAGAAGTTCACATATCAAATATATCTGCCCGCATGCGCCTGTTAGGCCT
GTTACATTAAATATGAACGTGGCTATGCCTTCATGGTTTGATATTATTGGGCTTTCACCA
GATTCACAGGAGGATGAATCTGGGATTAAACAGGCAGCAGAAAATATAAAAGCTTTGATT
GATCAAGAAGTGAAGAATGGCATTCCTTCTAACAGAATTATTTTGGGAGGGTTTTCTCAG
GGAGGAGCTTTATCTTTATATACTGCCCTTACCACACAGCAGAAACTGGCAGGTGTCACT
GCACTCAGTTGCTGGCTTCCACTTCGGGCTTCCTTTCCACAGGGTCCTATCGGTGGTGCT
AATAGAGATATTTCTATTCTCCAGTGCCACGGGGATTGTGACCCTTTGGTTCCCCTGATG
TTTGGTTCTCTTACGGTGGAAAAACTAAAAACATTGGTGAATCCAGCCAATGTGACCTTT
AAAACCTATGAAGGTATGATGCACAGTTCGTGTCAACAGGAAATGATGGATGTCAAGCAA
TTCATTGATAAACTCCTACCTCCAATTGATTGA
Enzyme 1 GenBank Gene ID NM_006330.2 Link Image
Enzyme 1 GeneCard ID LYPLA1 Link Image
Enzyme 1 GenAtlas ID LYPLA1 Link Image
Enzyme 1 HGNC ID HGNC:6737 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8q11.23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS: Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A. Structure. 2000 Nov 15;8(11):1137-46. [PubMed Link Image]
  2. 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]
  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. Dekker FJ, Rocks O, Vartak N, Menninger S, Hedberg C, Balamurugan R, Wetzel S, Renner S, Gerauer M, Scholermann B, Rusch M, Kramer JW, Rauh D, Coates GW, Brunsveld L, Bastiaens PI, Waldmann H: Small-molecule inhibition of APT1 affects Ras localization and signaling. Nat Chem Biol. 2010 Jun;6(6):449-56. Epub 2010 Apr 25. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5286
Enzyme 2 Name Group XV phospholipase A2
Enzyme 2 Synonyms
  1. 1-O-acylceramide synthase
  2. ACS
  3. LCAT-like lysophospholipase
  4. LLPL
  5. Lysophospholipase 3
  6. Lysosomal phospholipase A2
  7. LPLA2
Enzyme 2 Gene Name PLA2G15
Enzyme 2 Protein Sequence >Group XV phospholipase A2
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Enzyme 2 Number of Residues 412
Enzyme 2 Molecular Weight 46657.4
Enzyme 2 Theoretical pI 6.72
Enzyme 2 GO Classification
Function
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • phosphatidylcholine-sterol O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 2 General Function Involved in phosphatidylcholine-sterol O-acyltransferase activity
Enzyme 2 Specific Function Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N- acetylsphingosine and the concomitant release of a lyso- phospholipid. May have weak lysophospholipase activity
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-33
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q8NCC3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PAG15_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1239 bp
ATGGGCCTCCACCTCCGCCCCTACCGTGTGGGGCTGCTCCCGGATGGCCTCCTGTTCCTC
TTGCTGCTGCTAATGCTGCTCGCGGACCCAGCGCTCCCGGCCGGACGTCACCCCCCAGTG
GTGCTGGTCCCTGGTGATTTGGGTAACCAACTGGAAGCCAAGCTGGACAAGCCGACAGTG
GTGCACTACCTCTGCTCCAAGAAGACCGAAAGCTACTTCACAATCTGGCTGAACCTGGAA
CTGCTGCTGCCTGTCATCATTGACTGCTGGATTGACAATATCAGGCTGGTTTACAACAAA
ACATCCAGGGCCACCCAGTTTCCTGATGGTGTGGATGTACGTGTCCCTGGCTTTGGGAAG
ACCTTCTCACTGGAGTTCCTGGACCCCAGCAAAAGCAGCGTGGGTTCCTATTTCCACACC
ATGGTGGAGAGCCTTGTGGGCTGGGGCTACACACGGGGTGAGGATGTCCGAGGGGCTCCC
TATGACTGGCGCCGAGCCCCAAATGAAAACGGGCCCTACTTCCTGGCCCTCCGCGAGATG
ATCGAGGAGATGTACCAGCTGTATGGGGGCCCCGTGGTGCTGGTTGCCCACAGTATGGGC
AACATGTACACGCTCTACTTTCTGCAGCGGCAGCCGCAGGCCTGGAAGGACAAGTATATC
CGGGCCTTCGTGTCACTGGGTGCGCCCTGGGGGGGCGTGGCCAAGACCCTGCGCGTCCTG
GCTTCAGGAGACAACAACCGGATCCCAGTCATCGGGCCCCTGAAGATCCGGGAGCAGCAG
CGGTCAGCTGTCTCCACCAGCTGGCTGCTGCCCTACAACTACACATGGTCACCTGAGAAG
GTGTTCGTGCAGACACCCACAATCAACTACACACTGCGGGACTACCGCAAGTTCTTCCAG
GACATCGGCTTTGAAGATGGCTGGCTCATGCGGCAGGACACAGAAGGGCTGGTGGAAGCC
ACGATGCCACCTGGCGTGCAGCTGCACTGCCTCTATGGCACTGGCGTCCCCACACCAGAC
TCCTTCTACTATGAGAGCTTCCCTGACCGTGACCCTAAAATCTGCTTTGGTGACGGCGAT
GGTACTGTGAACTTGAAGAGTGCCCTGCAGTGCCAGGCCTGGCAGAGCCGCCAGGAGCAC
CAAGTGTTGCTGCAGGAGCTGCCAGGCAGCGAGCACATCGAGATGCTGGCCAACGCCACC
ACCCTGGCCTATCTGAAACGTGTGCTCCTTGGGCCCTGA
Enzyme 2 GenBank Gene ID AB017494 Link Image
Enzyme 2 GeneCard ID PLA2G15 Link Image
Enzyme 2 GenAtlas ID PLA2G15 Link Image
Enzyme 2 HGNC ID HGNC:17163 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 16q22.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Taniyama Y, Shibata S, Kita S, Horikoshi K, Fuse H, Shirafuji H, Sumino Y, Fujino M: Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase. Biochem Biophys Res Commun. 1999 Apr 2;257(1):50-6. [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. 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
  7. Hiraoka M, Abe A, Shayman JA: Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase. J Biol Chem. 2002 Mar 22;277(12):10090-9. Epub 2002 Jan 14. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5287
Enzyme 3 Name Calcium-dependent phospholipase A2
Enzyme 3 Synonyms
  1. Group V phospholipase A2
  2. PLA2-10
  3. Phosphatidylcholine 2-acylhydrolase 5
Enzyme 3 Gene Name PLA2G5
Enzyme 3 Protein Sequence >Calcium-dependent phospholipase A2
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 3 Number of Residues 138
Enzyme 3 Molecular Weight 15674.1
Enzyme 3 Theoretical pI 8.48
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 3 General Function Involved in phospholipase A2 activity
Enzyme 3 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle
Enzyme 3 Pathways
Enzyme 3 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-20
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 10862735 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P39877 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PA2G5_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
Enzyme 3 GenBank Gene ID AL158172 Link Image
Enzyme 3 GeneCard ID PLA2G5 Link Image
Enzyme 3 GenAtlas ID PLA2G5 Link Image
Enzyme 3 HGNC ID HGNC:9038 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p36-p34
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5288
Enzyme 4 Name Group IIF secretory phospholipase A2
Enzyme 4 Synonyms
  1. GIIF sPLA2
  2. sPLA2-IIF
  3. Phosphatidylcholine 2-acylhydrolase 2F
Enzyme 4 Gene Name PLA2G2F
Enzyme 4 Protein Sequence >Group IIF secretory phospholipase A2
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 4 Number of Residues 168
Enzyme 4 Molecular Weight 18658.0
Enzyme 4 Theoretical pI 4.94
Enzyme 4 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 4 General Function Involved in phospholipase A2 activity
Enzyme 4 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference
Enzyme 4 Pathways
Enzyme 4 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-20
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 12276060 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9BZM2 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PA2GF_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
Enzyme 4 GenBank Gene ID AF306566 Link Image
Enzyme 4 GeneCard ID PLA2G2F Link Image
Enzyme 4 GenAtlas ID PLA2G2F Link Image
Enzyme 4 HGNC ID HGNC:30040 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p35
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5289
Enzyme 5 Name Cytosolic phospholipase A2
Enzyme 5 Synonyms
  1. cPLA2
  2. Phospholipase A2 group IVA
  3. Phospholipase A2
  4. Phosphatidylcholine 2-acylhydrolase
  5. Lysophospholipase
Enzyme 5 Gene Name PLA2G4A
Enzyme 5 Protein Sequence >Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
Enzyme 5 Number of Residues 749
Enzyme 5 Molecular Weight 85210.2
Enzyme 5 Theoretical pI 5.03
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
Component
Enzyme 5 General Function Involved in metabolic process
Enzyme 5 Specific Function Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID P47712 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN Link Image
Enzyme 5 PDB ID 1CJY Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2250 bp
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
Enzyme 5 GenBank Gene ID M72393 Link Image
Enzyme 5 GeneCard ID PLA2G4A Link Image
Enzyme 5 GenAtlas ID PLA2G4A Link Image
Enzyme 5 HGNC ID HGNC:9035 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1q25
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed Link Image]
  2. Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [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. Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed Link Image]
  6. Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Varshavsky AD, Roberts EF, Strifler BA, Brems DN, et al.: Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1994 Sep 16;269(37):23250-4. [PubMed Link Image]
  7. Borsch-Haubold AG, Bartoli F, Asselin J, Dudler T, Kramer RM, Apitz-Castro R, Watson SP, Gelb MH: Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. J Biol Chem. 1998 Feb 20;273(8):4449-58. [PubMed Link Image]
  8. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed Link Image]
  9. 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]
  10. 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]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed Link Image]
  17. Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed Link Image]
  18. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5290
Enzyme 6 Name Phospholipase A2
Enzyme 6 Synonyms
  1. Group IB phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase 1B
Enzyme 6 Gene Name PLA2G1B
Enzyme 6 Protein Sequence >Phospholipase A2
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 6 Number of Residues 148
Enzyme 6 Molecular Weight 16359.5
Enzyme 6 Theoretical pI 7.91
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 6 General Function Involved in phospholipase A2 activity
Enzyme 6 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 6 Pathways
Enzyme 6 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-15
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID P04054 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PA21B_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTATGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 6 GenBank Gene ID M21054 Link Image
Enzyme 6 GeneCard ID PLA2G1B Link Image
Enzyme 6 GenAtlas ID PLA2G1B Link Image
Enzyme 6 HGNC ID HGNC:9030 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 12q23-q24.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [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. 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]
  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. Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed Link Image]
  6. Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5291
Enzyme 7 Name Group XIIB secretory phospholipase A2-like protein
Enzyme 7 Synonyms
  1. Group XIII secretory phospholipase A2-like protein
  2. GXIII sPLA2-like
  3. sPLA2-GXIIB
  4. GXIIB
Enzyme 7 Gene Name PLA2G12B
Enzyme 7 Protein Sequence >Group XIIB secretory phospholipase A2-like protein
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
Enzyme 7 Number of Residues 195
Enzyme 7 Molecular Weight 21658.5
Enzyme 7 Theoretical pI 5.81
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 7 General Function Involved in phospholipase A2 activity
Enzyme 7 Specific Function Not known; does not seem to have catalytic activity
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-19
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 15824793 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9BX93 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PG12B_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >588 bp
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCAGCCTGTGATTCC
CTGGTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGT
CAGCGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
Enzyme 7 GenBank Gene ID AF339053 Link Image
Enzyme 7 GeneCard ID PLA2G12B Link Image
Enzyme 7 GenAtlas ID PLA2G12B Link Image
Enzyme 7 HGNC ID HGNC:18555 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 10q22.1
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [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. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5292
Enzyme 8 Name Group 10 secretory phospholipase A2
Enzyme 8 Synonyms
  1. Group X secretory phospholipase A2
  2. GX sPLA2
  3. sPLA2-X
  4. Phosphatidylcholine 2-acylhydrolase 10
Enzyme 8 Gene Name PLA2G10
Enzyme 8 Protein Sequence >Group 10 secretory phospholipase A2
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPI
AYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGP
AENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 8 Number of Residues 165
Enzyme 8 Molecular Weight 18153.0
Enzyme 8 Theoretical pI 6.46
Enzyme 8 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 8 General Function Involved in phospholipase A2 activity
Enzyme 8 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine
Enzyme 8 Pathways
Enzyme 8 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-31
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 8 PDB ID 1LE7 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 8 GenBank Gene ID U95301 Link Image
Enzyme 8 GeneCard ID PLA2G10 Link Image
Enzyme 8 GenAtlas ID PLA2G10 Link Image
Enzyme 8 HGNC ID HGNC:9029 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 16p13.1-p12
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [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]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5294
Enzyme 9 Name Group IIE secretory phospholipase A2
Enzyme 9 Synonyms
  1. GIIE sPLA2
  2. sPLA2-IIE
  3. Phosphatidylcholine 2-acylhydrolase 2E
Enzyme 9 Gene Name PLA2G2E
Enzyme 9 Protein Sequence >Group IIE secretory phospholipase A2
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 9 Number of Residues 142
Enzyme 9 Molecular Weight 15988.5
Enzyme 9 Theoretical pI 8.28
Enzyme 9 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 9 General Function Involved in phospholipase A2 activity
Enzyme 9 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids
Enzyme 9 Pathways
Enzyme 9 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID Q9NZK7 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PA2GE_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
Enzyme 9 GenBank Gene ID AF189279 Link Image
Enzyme 9 GeneCard ID PLA2G2E Link Image
Enzyme 9 GenAtlas ID PLA2G2E Link Image
Enzyme 9 HGNC ID HGNC:13414 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p36.13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5295
Enzyme 10 Name Acyl-protein thioesterase 2
Enzyme 10 Synonyms
  1. APT-2
  2. Lysophospholipase II
  3. LPL-II
  4. LysoPLA II
Enzyme 10 Gene Name LYPLA2
Enzyme 10 Protein Sequence >Acyl-protein thioesterase 2
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAP
RIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGG
FSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP
VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
Enzyme 10 Number of Residues 231
Enzyme 10 Molecular Weight 24736.7
Enzyme 10 Theoretical pI 7.25
Enzyme 10 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 10 General Function Involved in hydrolase activity
Enzyme 10 Specific Function May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 9966764 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O95372 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name LYPA2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >696 bp
ATGTGTGGTAACACCATGTCTGTGCCCCTGCTCACCGATGCTGCCACCGTGTCTGGAGCT
GAGCGGGAAACGGCCGCGGTTATTTTTTTACATGGACTTGGAGACACAGGGCACAGCTGG
GCTGACGCCCTCTCCACCATCCGGCTCCCTCACGTCAAGTACATCTGTCCCCATGCGCCT
AGGATCCCTGTGACCCTCAACATGAAGATGGTGATGCCCTCCTGGTTTGACCTGATGGGG
CTGAGTCCAGATGCCCCAGAGGACGAGGCTGGCATCAAGAAGGCAGCAGAGAACATCAAG
GCCTTGATTGAGCATGAAATGAAGAACGGGATCCCTGCCAATCGAATCGTCCTGGGAGGC
TTTTCACAGGGCGGGGCCCTGTCCCTCTACACGGCCCTCACCTGCCCCCACCCTCTGGCT
GGCATCGTGGCGTTGAGCTGCTGGCTGCCTCTGCACCGGGCCTTCCCCCAGGCAGCTAAT
GGCAGTGCCAAGGACCTGGCCATACTCCAGTGCCATGGGGAGCTGGACCCCATGGTGCCC
GTACGGTTTGGGGCCCTGACGGCTGAGAAGCTCCGGTCTGTTGTCACACCTGCCAGGGTC
CAGTTCAAGACATACCCGGGTGTCATGCACAGCTCCTGTCCTCAGGAGATGGCAGCTGTG
AAGGAATTTCTTGAGAAGCTGCTGCCTCCTGTCTAA
Enzyme 10 GenBank Gene ID NM_007260.2 Link Image
Enzyme 10 GeneCard ID LYPLA2 Link Image
Enzyme 10 GenAtlas ID LYPLA2 Link Image
Enzyme 10 HGNC ID HGNC:6738 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p36.11
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5297
Enzyme 11 Name 85 kDa calcium-independent phospholipase A2
Enzyme 11 Synonyms
  1. CaI-PLA2
  2. iPLA2
  3. Group VI phospholipase A2
  4. GVI PLA2
Enzyme 11 Gene Name PLA2G6
Enzyme 11 Protein Sequence >85 kDa calcium-independent phospholipase A2
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
Enzyme 11 Number of Residues 806
Enzyme 11 Molecular Weight 89902.3
Enzyme 11 Theoretical pI 7.28
Enzyme 11 GO Classification
Function
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 11 General Function Involved in metabolic process
Enzyme 11 Specific Function Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity
Enzyme 11 Pathways
Enzyme 11 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3142700 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O60733 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PA2G6_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2421 bp
ATGCAGTTCTTTGGCCGCCTGGTCAATACCTTCAGTGGCGTCACCAACTTGTTCTCTAAC
CCATTCCGGGTGAAGGAGGTGGCTGTGGCCGACTACACCTCGAGTGACCGAGTTCGGGAG
GAAGGGCAGCTGATTCTGTTCCAGAACACTCCCAACCGCACCTGGGACTGCGTCCTGGTC
AACCCCAGGAACTCACAGAGTGGATTCCGACTCTTCCAGCTGGAGTTGGAGGCTGACGCC
CTAGTGAATTTCCATCAGTATTCTTCCCAGCTGCTACCCTTCTATGAGAGCTCCCCTCAG
GTCCTGCACACTGAGGTCCTGCAGCACCTGACCGACCTCATCCGTAACCACCCCAGCTGG
TCAGTGGCCCACCTGGCTGTGGAGCTAGGGATCCGCGAGTGCTTCCATCACAGCCGTATC
ATCAGCTGTGCCAATTGCGCGGAGAACGAGGAGGGCTGCACACCCCTGCACCTGGCCTGC
CGCAAGGGTGATGGGGAGATCCTGGTGGAGCTGGTGCAGTACTGCCACACTCAGATGGAT
GTCACCGACTACAAGGGAGAGACCGTCTTCCATTATGCTGTCCAGGGTGACAATTCTCAG
GTGCTGCAGCTCCTTGGAAGGAACGCAGTGGCTGGCCTGAACCAGGTGAATAACCAAGGG
CTGACCCCGCTGCACCTGGCCTGCCAGCTGGGGAAGCAGGAGATGGTCCGCGTGCTGCTG
CTGTGCAATGCTCGGTGCAACATCATGGGCCCCAACGGCTACCCCATCCACTCGGCCATG
AAGTTCTCTCAGAAGGGGTGTGCGGAGATGATCATCAGCATGGACAGCAGCCAGATCCAC
AGCAAAGACCCCCGTTACGGAGCCAGCCCCCTCCACTGGGCCAAGAACGCAGAGATGGCC
CGCATGCTGCTGAAACGGGGCTGCAACGTGAACAGCACCAGCTCCGCGGGGAACACGGCC
CTGCACGTGGCGGTGATGCGCAACCGCTTCGACTGTGCCATAGTGCTGCTGACCCACGGG
GCCAACGCGGATGCCCGCGGAGAGCACGGCAACACCCCGCTGCACCTGGCCATGTCGAAA
GACAACGTGGAGATGATCAAGGCCCTCATCGTGTTCGGAGCAGAAGTGGACACCCCGAAT
GACTTTGGGGAGACTCCTACATTCCTAGCCTCCAAAATCGGCAGACTTGTCACCAGGAAG
GCGATCTTGACTCTGCTGAGAACCGTGGGGGCCGAATACTGCTTCCCACCCATCCACGGG
GTCCCCGCGGAGCAGGGCTCTGCAGCGCCACATCATCCCTTCTCCCTGGAAAGAGCTCAG
CCCCCACCGATCAGCCTAAACAACCTAGAACTACAGGATCTCATGCACATCTCACGGGCC
CGGAAGCCAGCGTTCATCCTGGGCTCCATGAGGGACGAGAAGCGGACCCACGACCACCTG
CTGTGCCTGGATGGAGGAGGAGTGAAAGGCCTCATCATCATCCAGCTCCTCATCGCCATC
GAGAAGGCCTCGGGTGTGGCCACCAAGGACCTGTTTGACTGGGTGGCGGGCACCAGCACT
GGAGGCATCCTGGCCCTGGCCATTCTGCACAGTAAGTCCATGGCCTACATGCGCGGCATG
TACTTTCGCATGAAGGATGAGGTGTTCCGGGGCTCCAGGCCCTACGAGTCGGGGCCCCTG
GAGGAGTTCCTGAAGCGGGAGTTTGGGGAGCACACCAAGATGACGGACGTCAGGAAACCC
AAGGTGATGCTGACAGGGACACTGTCTGACCGGCAGCCGGCTGAACTCCACCTCTTCCGG
AACTACGATGCTCCAGAAACTGTCCGGGAGCCTCGTTTCAACCAGAACGTTAACCTCAGG
CCTCCAGCTCAGCCCTCAGACCAGCTGGTGTGGCGGGCGGCCCGAAGCAGCGGGGCAGCT
CCTACTTACTTCCGACCCAATGGGCGCTTCCTGGACGGTGGGCTGCTGGCCAACAACCCC
ACGCTGGATGCCATGACCGAGATCCATGAGTACAATCAGGACCTGATCCGCAAGGGTCAG
GCCAACAAGGTGAAGAAACTCTCCATCGTTGTCTCCCTGGGGACAGGGAGGTCCCCACAA
GTGCCTGTGACCTGTGTGGATGTCTTCCGTCCCAGCAACCCCTGGGAGCTGGCCAAGACT
GTTTTTGGGGCCAAGGAACTGGGCAAGATGGTGGTGGACTGTTGCACGGATCCAGACGGG
CGGGCTGTGGACCGGGCACGGGCCTGGTGCGAGATGGTCGGCATCCAGTACTTCAGATTG
AACCCCCAGCTGGGGACGGACATCATGCTGGATGAGGTCAGTGACACAGTGCTGGTCAAC
GCCCTCTGGGAGACCGAGGTCTACATCTATGAGCACCGCGAGGAGTTCCAGAAGCTCATC
CACCTGCTGCTCTCACCCTGA
Enzyme 11 GenBank Gene ID AF064594 Link Image
Enzyme 11 GeneCard ID PLA2G6 Link Image
Enzyme 11 GenAtlas ID PLA2G6 Link Image
Enzyme 11 HGNC ID HGNC:9039 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 22q13.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Larsson PK, Claesson HE, Kennedy BP: Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity. J Biol Chem. 1998 Jan 2;273(1):207-14. [PubMed Link Image]
  2. Ma Z, Wang X, Nowatzke W, Ramanadham S, Turk J: Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1. J Biol Chem. 1999 Apr 2;274(14):9607-16. [PubMed Link Image]
  3. Larsson Forsell PK, Kennedy BP, Claesson HE: The human calcium-independent phospholipase A2 gene multiple enzymes with distinct properties from a single gene. Eur J Biochem. 1999 Jun;262(2):575-85. [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. 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]
  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. 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]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, 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]
  9. Malhotra A, Edelman-Novemsky I, Xu Y, Plesken H, Ma J, Schlame M, Ren M: Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome. Proc Natl Acad Sci U S A. 2009 Feb 17;106(7):2337-41. Epub 2009 Jan 21. [PubMed Link Image]
  10. Khateeb S, Flusser H, Ofir R, Shelef I, Narkis G, Vardi G, Shorer Z, Levy R, Galil A, Elbedour K, Birk OS: PLA2G6 mutation underlies infantile neuroaxonal dystrophy. Am J Hum Genet. 2006 Nov;79(5):942-8. Epub 2006 Sep 19. [PubMed Link Image]
  11. Morgan NV, Westaway SK, Morton JE, Gregory A, Gissen P, Sonek S, Cangul H, Coryell J, Canham N, Nardocci N, Zorzi G, Pasha S, Rodriguez D, Desguerre I, Mubaidin A, Bertini E, Trembath RC, Simonati A, Schanen C, Johnson CA, Levinson B, Woods CG, Wilmot B, Kramer P, Gitschier J, Maher ER, Hayflick SJ: PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron. Nat Genet. 2006 Jul;38(7):752-4. Epub 2006 Jun 18. [PubMed Link Image]
  12. Paisan-Ruiz C, Bhatia KP, Li A, Hernandez D, Davis M, Wood NW, Hardy J, Houlden H, Singleton A, Schneider SA: Characterization of PLA2G6 as a locus for dystonia-parkinsonism. Ann Neurol. 2009 Jan;65(1):19-23. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5298
Enzyme 12 Name Phosphatidylcholine-sterol acyltransferase
Enzyme 12 Synonyms
  1. Lecithin-cholesterol acyltransferase
  2. Phospholipid-cholesterol acyltransferase
Enzyme 12 Gene Name LCAT
Enzyme 12 Protein Sequence >Phosphatidylcholine-sterol acyltransferase
MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQL
EAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGV
QIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEY
YRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGS
IKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGR
DFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDP
VGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLG
AYRQGPPASPTASPEPPPPE
Enzyme 12 Number of Residues 440
Enzyme 12 Molecular Weight 49577.5
Enzyme 12 Theoretical pI 6.04
Enzyme 12 GO Classification
Function
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • phosphatidylcholine-sterol O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 12 General Function Involved in phosphatidylcholine-sterol O-acyltransferase activity
Enzyme 12 Specific Function Central enzyme in the extracellular metabolism of plasma lipoproteins. Among other substrates it esterifies the free cholesterol transported in plasma lipoproteins
Enzyme 12 Pathways
Enzyme 12 Reactions
  • phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester [RN:R02114]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-24
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 15928623 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P04180 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name LCAT_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1323 bp
ATGGGGCCGCCCGGCTCCCCATGGCAGTGGGTGACGCTGCTGCTGGGGCTGCTGCTCCCT
CCTGCCGCCCCCTTCTGGCTCCTCAATGTGCTCTTCCCCCCGCACACCACGCCCAAGGCT
GAGCTCAGTAACCACACACGGCCCGTCATCCTCGTGCCCGGCTGCCTGGGGAATCAGCTA
GAAGCCAAGCTGGACAAACCAGATGTGGTGAACTGGATGTGCTACCGCAAGACAGAGGAC
TTCTTCACCATCTGGCTGGATCTCAACATGTTCCTACCCCTTGGGGTAGACTGCTGGATC
GATAACACCAGGGTTGTCTACAACCGGAGCTCTGGGCTCGTGTCCAACGCCCCTGGTGTC
CAGATCCGCGTCCCTGGCTTTGGCAAGACCTACTCTGTGGAGTACCTGGACAGCAGCAAG
CTGGCAGGGTACCTGCACACACTGGTGCAGAACCTGGTCAACAATGGCTACGTGCGGGAC
GAGACTGTGCGCGCCGCCCCCTATGACTGGCGGCTGGAGCCCGGCCAGCAGGAGGAGTAC
TACCGCAAGCTCGCAGGGCTGGTGGAGGAGATGCACGCTGCCTATGGGAAGCCTGTCTTC
CTCATTGGCCACAGCCTCGGCTGTCTACACTTGCTCTATTTCCTGCTGCGCCAGCCCCAG
GCCTGGAAGGACCGCTTTATTGATGGCTTCATCTCTCTTGGGGCTCCCTGGGGTGGCTCC
ATCAAGCCCATGCTGGTCTTGGCCTCAGGTGACAACCAGGGCATCCCCATCATGTCCAGC
ATCAAGCTGAAAGAGGAGCAGCGCATAACCACCACCTCCCCCTGGATGTTTCCCTCTCGC
ATGGCGTGGCCTGAGGACCACGTGTTCATTTCCACACCCAGCTTCAACTACACAGGCCGT
GACTTCCAACGCTTCTTTGCAGACCTGCACTTTGAGGAAGGCTGGTACATGTGGCTGCAG
TCACGTGACCTCCTGGCAGGACTCCCAGCACCTGGTGTGGAAGTATACTGTCTTTACGGC
GTGGGCCTGCCCACGCCCCGCACCTACATCTACGACCACGGCTTCCCCTACACGGACCCT
GTGGGTGTGCTCTATGAGGATGGTGATGACACGGTGGCGACCCGCAGCACCGAGCTCTGT
GGCCTGTGGCAGGGCCGCCAGCCACAGCCTGTGCACCTGCTGCCCCTGCACGGGATACAG
CATCTCAACATGGTCTTCAGCAACCTGACCCTGGAGCACATCAATGCCATCCTGCTGGGT
GCCTACCGCCAGGGTCCCCCTGCATCCCCGACTGCCAGCCCAGAGCCCCCGCCTCCTGAA
TAA
Enzyme 12 GenBank Gene ID BC014781 Link Image
Enzyme 12 GeneCard ID LCAT Link Image
Enzyme 12 GenAtlas ID LCAT Link Image
Enzyme 12 HGNC ID HGNC:6522 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 16q22.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R: Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2335-9. [PubMed Link Image]
  2. McLean J, Wion K, Drayna D, Fielding C, Lawn R: Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression. Nucleic Acids Res. 1986 Dec 9;14(23):9397-406. [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. Tata F, Chaves ME, Markham AF, Scrace GD, Waterfield MD, McIntyre N, Williamson R, Humphries SE: The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase. Biochim Biophys Acta. 1987 Nov 20;910(2):142-8. [PubMed Link Image]
  5. Rogne S, Skretting G, Larsen F, Myklebost O, Mevag B, Carlson LA, Holmquist L, Gjone E, Prydz H: The isolation and characterisation of a cDNA clone for human lecithin:cholesterol acyl transferase and its use to analyse the genes in patients with LCAT deficiency and fish eye disease. Biochem Biophys Res Commun. 1987 Oct 14;148(1):161-9. [PubMed Link Image]
  6. Yang CY, Manoogian D, Pao Q, Lee FS, Knapp RD, Gotto AM Jr, Pownall HJ: Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme. J Biol Chem. 1987 Mar 5;262(7):3086-91. [PubMed Link Image]
  7. Schindler PA, Settineri CA, Collet X, Fielding CJ, Burlingame AL: Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. Protein Sci. 1995 Apr;4(4):791-803. [PubMed Link Image]
  8. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  9. Skretting G, Prydz H: An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease. Biochem Biophys Res Commun. 1992 Jan 31;182(2):583-7. [PubMed Link Image]
  10. Klein HG, Lohse P, Pritchard PH, Bojanovski D, Schmidt H, Brewer HB Jr: Two different allelic mutations in the lecithin-cholesterol acyltransferase gene associated with the fish eye syndrome. Lecithin-cholesterol acyltransferase (Thr123----Ile) and lecithin-cholesterol acyltransferase (Thr347----Met). J Clin Invest. 1992 Feb;89(2):499-506. [PubMed Link Image]
  11. Taramelli R, Pontoglio M, Candiani G, Ottolenghi S, Dieplinger H, Catapano A, Albers J, Vergani C, McLean J: Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele. Hum Genet. 1990 Jul;85(2):195-9. [PubMed Link Image]
  12. Gotoda T, Yamada N, Murase T, Sakuma M, Murayama N, Shimano H, Kozaki K, Albers JJ, Yazaki Y, Akanuma Y: Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency. Lancet. 1991 Sep 28;338(8770):778-81. [PubMed Link Image]
  13. Skretting G, Blomhoff JP, Solheim J, Prydz H: The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families. FEBS Lett. 1992 Sep 14;309(3):307-10. [PubMed Link Image]
  14. Maeda E, Naka Y, Matozaki T, Sakuma M, Akanuma Y, Yoshino G, Kasuga M: Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene. Biochem Biophys Res Commun. 1991 Jul 31;178(2):460-6. [PubMed Link Image]
  15. Funke H, von Eckardstein A, Pritchard PH, Hornby AE, Wiebusch H, Motti C, Hayden MR, Dachet C, Jacotot B, Gerdes U, et al.: Genetic and phenotypic heterogeneity in familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Six newly identified defective alleles further contribute to the structural heterogeneity in this disease. J Clin Invest. 1993 Feb;91(2):677-83. [PubMed Link Image]
  16. Hill JS, O K, Wang X, Pritchard PH: Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism. Biochim Biophys Acta. 1993 Jun 19;1181(3):321-3. [PubMed Link Image]
  17. Steyrer E, Haubenwallner S, Horl G, Giessauf W, Kostner GM, Zechner R: A single G to A nucleotide transition in exon IV of the lecithin: cholesterol acyltransferase (LCAT) gene results in an Arg140 to His substitution and causes LCAT-deficiency. Hum Genet. 1995 Jul;96(1):105-9. [PubMed Link Image]
  18. Wiebusch H, Cullen P, Owen JS, Collins D, Sharp PS, Funke H, Assmann G: Deficiency of lecithin:cholesterol acyltransferase due to compound heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the LCAT gene. Hum Mol Genet. 1995 Jan;4(1):143-5. [PubMed Link Image]
  19. Kuivenhoven JA, Stalenhoef AF, Hill JS, Demacker PN, Errami A, Kastelein JJ, Pritchard PH: Two novel molecular defects in the LCAT gene are associated with fish eye disease. Arterioscler Thromb Vasc Biol. 1996 Feb;16(2):294-303. [PubMed Link Image]
  20. Owen JS, Wiebusch H, Cullen P, Watts GF, Lima VL, Funke H, Assmann G: Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT gene. Hum Mutat. 1996;8(1):79-82. [PubMed Link Image]
  21. Okubo M, Aoyama Y, Shio H, Albers JJ, Murase T: A novel missense mutation (Asn5-->Ile) in lecithin: cholesterol acyltransferase (LCAT) gene in a Japanese patient with LCAT deficiency. Int J Clin Lab Res. 1996;26(4):250-4. [PubMed Link Image]
  22. Blanco-Vaca F, Qu SJ, Fiol C, Fan HZ, Pao Q, Marzal-Casacuberta A, Albers JJ, Hurtado I, Gracia V, Pinto X, Marti T, Pownall HJ: Molecular basis of fish-eye disease in a patient from Spain. Characterization of a novel mutation in the LCAT gene and lipid analysis of the cornea. Arterioscler Thromb Vasc Biol. 1997 Jul;17(7):1382-91. [PubMed Link Image]
  23. Argyropoulos G, Jenkins A, Klein RL, Lyons T, Wagenhorst B, St Armand J, Marcovina SM, Albers JJ, Pritchard PH, Garvey WT: Transmission of two novel mutations in a pedigree with familial lecithin:cholesterol acyltransferase deficiency: structure-function relationships and studies in a compound heterozygous proband. J Lipid Res. 1998 Sep;39(9):1870-6. [PubMed Link Image]
  24. Sessa A, Battini G, Meroni M, Daidone G, Carnera I, Brambilla PL, Vigano G, Giordano F, Pallotti F, Torri Tarelli L, Calabresi L, Rolleri M, Bertolini S: Hypocomplementemic type II membranoproliferative glomerulonephritis in a male patient with familial lecithin-cholesterol acyltransferase deficiency due to two different allelic mutations. Nephron. 2001 Jul;88(3):268-72. [PubMed Link Image]
  25. Nanjee MN, Stocks J, Cooke CJ, Molhuizen HO, Marcovina S, Crook D, Kastelein JP, Miller NE: A novel LCAT mutation (Phe382-->Val) in a kindred with familial LCAT deficiency and defective apolipoprotein B-100. Atherosclerosis. 2003 Sep;170(1):105-13. [PubMed Link Image]
  26. 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]
  27. Calabresi L, Pisciotta L, Costantin A, Frigerio I, Eberini I, Alessandrini P, Arca M, Bon GB, Boscutti G, Busnach G, Frasca G, Gesualdo L, Gigante M, Lupattelli G, Montali A, Pizzolitto S, Rabbone I, Rolleri M, Ruotolo G, Sampietro T, Sessa A, Vaudo G, Cantafora A, Veglia F, Calandra S, Bertolini S, Franceschini G: The molecular basis of lecithin:cholesterol acyltransferase deficiency syndromes: a comprehensive study of molecular and biochemical findings in 13 unrelated Italian families. Arterioscler Thromb Vasc Biol. 2005 Sep;25(9):1972-8. Epub 2005 Jun 30. [PubMed Link Image]
  28. Idzior-Walus B, Sieradzki J, Kostner G, Malecki MT, Klupa T, Wesolowska T, Rostworowski W, Hartwich J, Walus M, Kiec AD, Naruszewicz M: Familial lecithin-cholesterol acyltransferase deficiency: biochemical characteristics and molecular analysis of a new LCAT mutation in a Polish family. Atherosclerosis. 2006 Apr;185(2):413-20. Epub 2005 Jul 26. [PubMed Link Image]
  29. Horl G, Kroisel PM, Wagner E, Tiran B, Petek E, Steyrer E: Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol acyltransferase (LCAT) gene results in an intermediate phenotype between LCAT-deficiency and fish-eye disease. Atherosclerosis. 2006 Jul;187(1):101-9. Epub 2005 Oct 10. [PubMed Link Image]
  30. Gigante M, Ranieri E, Cerullo G, Calabresi L, Iolascon A, Assmann G, Morrone L, Pisciotta L, Schena FP, Gesualdo L: LCAT deficiency: molecular and phenotypic characterization of an Italian family. J Nephrol. 2006 May-Jun;19(3):375-81. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5299
Enzyme 13 Name Eosinophil lysophospholipase
Enzyme 13 Synonyms
  1. Charcot-Leyden crystal protein
  2. CLC
  3. Galectin-10
  4. Gal-10
  5. Lysolecithin acylhydrolase
Enzyme 13 Gene Name CLC
Enzyme 13 Protein Sequence >Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
Enzyme 13 Number of Residues 142
Enzyme 13 Molecular Weight 16480.8
Enzyme 13 Theoretical pI 7.50
Enzyme 13 GO Classification
Function
  • binding
  • carbohydrate binding
  • sugar binding
Process
Component
Enzyme 13 General Function Involved in sugar binding
Enzyme 13 Specific Function May have both lysophospholipase and carbohydrate-binding activities
Enzyme 13 Pathways
Enzyme 13 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3399666 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q05315 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name LPPL_HUMAN Link Image
Enzyme 13 PDB ID 1QKQ Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
Enzyme 13 GenBank Gene ID AC005393 Link Image
Enzyme 13 GeneCard ID CLC Link Image
Enzyme 13 GenAtlas ID CLC Link Image
Enzyme 13 HGNC ID HGNC:2014 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 19q13.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Ackerman SJ, Corrette SE, Rosenberg HF, Bennett JC, Mastrianni DM, Nicholson-Weller A, Weller PF, Chin DT, Tenen DG: Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. J Immunol. 1993 Jan 15;150(2):456-68. [PubMed Link Image]
  2. Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ: Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. Genomics. 1992 May;13(1):240-2. [PubMed Link Image]
  3. Dyer KD, Handen JS, Rosenberg HF: The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. Genomics. 1997 Mar 1;40(2):217-21. [PubMed Link Image]
  4. 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]
  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. Ghafouri B, Irander K, Lindbom J, Tagesson C, Lindahl M: Comparative proteomics of nasal fluid in seasonal allergic rhinitis. J Proteome Res. 2006 Feb;5(2):330-8. [PubMed Link Image]
  7. Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 1995 Dec 15;3(12):1379-93. [PubMed Link Image]
  8. Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR: Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 1999 Oct 19;38(42):13837-43. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5302
Enzyme 14 Name Group IID secretory phospholipase A2
Enzyme 14 Synonyms
  1. GIID sPLA2
  2. sPLA2-IID
  3. PLA2IID
  4. Phosphatidylcholine 2-acylhydrolase 2D
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 14 Gene Name PLA2G2D
Enzyme 14 Protein Sequence >Group IID secretory phospholipase A2
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 14 Number of Residues 145
Enzyme 14 Molecular Weight 16546.1
Enzyme 14 Theoretical pI 8.28
Enzyme 14 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 14 General Function Involved in phospholipase A2 activity
Enzyme 14 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined
Enzyme 14 Pathways
Enzyme 14 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-20
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 5771420 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 14 GenBank Gene ID AF112982 Link Image
Enzyme 14 GeneCard ID PLA2G2D Link Image
Enzyme 14 GenAtlas ID PLA2G2D Link Image
Enzyme 14 HGNC ID HGNC:9033 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1p36.12
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed Link Image]
  2. Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [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]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5771
Enzyme 15 Name Platelet-activating factor acetylhydrolase
Enzyme 15 Synonyms
  1. PAF acetylhydrolase
  2. 1-alkyl-2-acetylglycerophosphocholine esterase
  3. 2-acetyl-1-alkylglycerophosphocholine esterase
  4. Group-VIIA phospholipase A2
  5. gVIIA-PLA2
  6. LDL-associated phospholipase A2
  7. LDL-PLA(2)
  8. PAF 2-acylhydrolase
Enzyme 15 Gene Name PLA2G7
Enzyme 15 Protein Sequence >Platelet-activating factor acetylhydrolase
MVPPKLHVLFCLCGCLAVVYPFDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGN
GPYSVGCTDLMFDHTNKGTFLRLYYPSQDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNI
LRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR
DRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRNEQVRQRAKECSQALSLILDID
HGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAWMF
PLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFA
TGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLIPGT
NINTTNQHIMLQNSSGIEKYN
Enzyme 15 Number of Residues 441
Enzyme 15 Molecular Weight 50077.0
Enzyme 15 Theoretical pI 7.61
Enzyme 15 GO Classification
Function
  • 1-alkyl-2-acetylglycerophosphocholine esterase activity
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 15 General Function Involved in 1-alkyl-2-acetylglycerophosphocholine esterase activity
Enzyme 15 Specific Function Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids
Enzyme 15 Pathways
Enzyme 15 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate [RN:R04452]
Enzyme 15 Pfam Domain Function Not Available
Enzyme 15 Signals
  • 1-21
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q13093 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PAFA_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1326 bp
ATGGTGCCACCCAAATTGCATGTGCTTTTCTGCCTCTGCGGCTGCCTGGCTGTGGTTTAT
CCTTTTGACTGGCAATACATAAATCCTGTTGCCCATATGAAATCATCAGCATGGGTCAAC
AAAATACAAGTACTGATGGCTGCTGCAAGCTTTGGCCAAACTAAAATCCCCCGGGGAAAT
GGGCCTTATTCCGTTGGTTGTACAGACTTAATGTTTGATCACACTAATAAGGGCACCTTC
TTGCGTTTATATTATCCATCCCAAGATAATGATCGCCTTGACACCCTTTGGATCCCAAAT
AAAGAATATTTTTGGGGTCTTAGCAAATTTCTTGGAACACACTGGCTTATGGGCAACATT
TTGAGGTTACTCTTTGGTTCAATGACAACTCCTGCAAACTGGAATTCCCCTCTGAGGCCT
GGTGAAAAATATCCACTTGTTGTTTTTTCTCATGGTCTTGGGGCATTCAGGACACTTTAT
TCTGCTATTGGCATTGACCTGGCATCTCATGGGTTTATAGTTGCTGCTGTAGAACACAGA
GATAGATCTGCATCTGCAACTTACTATTTCAAGGACCAATCTGCTGCAGAAATAGGGGAC
AAGTCTTGGCTCTACCTTAGAACCCTGAAACAAGAGGAGGAGACACATATACGAAATGAG
CAGGTACGGCAAAGAGCAAAAGAATGTTCCCAAGCTCTCAGTCTGATTCTTGACATTGAT
CATGGAAAGCCAGTGAAGAATGCATTAGATTTAAAGTTTGATATGGAACAACTGAAGGAC
TCTATTGATAGGGAAAAAATAGCAGTAATTGGACATTCTTTTGGTGGAGCAACGGTTATT
CAGACTCTTAGTGAAGATCAGAGATTCAGATGTGGTATTGCCCTGGATGCATGGATGTTT
CCACTGGGTGATGAAGTATATTCCAGAATTCCTCAGCCCCTCTTTTTTATCAACTCTGAA
TATTTCCAATATCCTGCTAATATCATAAAAATGAAAAAATGCTACTCACCTGATAAAGAA
AGAAAGATGATTACAATCAGGGGTTCAGTCCACCAGAATTTTGCTGACTTCACTTTTGCA
ACTGGCAAAATAATTGGACACATGCTCAAATTAAAGGGAGACATAGATTCAAATGTAGCT
ATTGATCTTAGCAACAAAGCTTCATTAGCATTCTTACAAAAGCATTTAGGACTTCATAAA
GATTTTGATCAGTGGGACTGCTTGATTGAAGGAGATGATGAGAATCTTATTCCAGGGACC
AACATTAACACAACCAATCAACACATCATGTTACAGAACTCTTCAGGAATAGAGAAATAC
AATTAG
Enzyme 15 GenBank Gene ID U20157 Link Image
Enzyme 15 GeneCard ID PLA2G7 Link Image
Enzyme 15 GenAtlas ID PLA2G7 Link Image
Enzyme 15 HGNC ID HGNC:9040 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6p21.2-p12
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Tjoelker LW, Wilder C, Eberhardt C, Stafforini DM, Dietsch G, Schimpf B, Hooper S, Le Trong H, Cousens LS, Zimmerman GA, et al.: Anti-inflammatory properties of a platelet-activating factor acetylhydrolase. Nature. 1995 Apr 6;374(6522):549-53. [PubMed Link Image]
  2. Tew DG, Southan C, Rice SQ, Lawrence MP, Li H, Boyd HF, Moores K, Gloger IS, Macphee CH: Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins. Arterioscler Thromb Vasc Biol. 1996 Apr;16(4):591-9. [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]
  5. Tjoelker LW, Eberhardt C, Unger J, Trong HL, Zimmerman GA, McIntyre TM, Stafforini DM, Prescott SM, Gray PW: Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad. J Biol Chem. 1995 Oct 27;270(43):25481-7. [PubMed Link Image]
  6. Samanta U, Bahnson BJ: Crystal structure of human plasma platelet-activating factor acetylhydrolase: structural implication to lipoprotein binding and catalysis. J Biol Chem. 2008 Nov 14;283(46):31617-24. Epub 2008 Sep 10. [PubMed Link Image]
  7. Samanta U, Kirby SD, Srinivasan P, Cerasoli DM, Bahnson BJ: Crystal structures of human group-VIIA phospholipase A2 inhibited by organophosphorus nerve agents exhibit non-aged complexes. Biochem Pharmacol. 2009 Aug 15;78(4):420-9. Epub 2009 Apr 24. [PubMed Link Image]
  8. Stafforini DM, Satoh K, Atkinson DL, Tjoelker LW, Eberhardt C, Yoshida H, Imaizumi T, Takamatsu S, Zimmerman GA, McIntyre TM, Gray PW, Prescott SM: Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase. J Clin Invest. 1996 Jun 15;97(12):2784-91. [PubMed Link Image]
  9. Yamada Y, Yokota M: Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation. Biochem Biophys Res Commun. 1997 Jul 30;236(3):772-5. [PubMed Link Image]
  10. Hiramoto M, Yoshida H, Imaizumi T, Yoshimizu N, Satoh K: A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke. Stroke. 1997 Dec;28(12):2417-20. [PubMed Link Image]
  11. Yamada Y, Ichihara S, Fujimura T, Yokota M: Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men. Metabolism. 1998 Feb;47(2):177-81. [PubMed Link Image]
  12. Yoshida H, Imaizumi T, Fujimoto K, Itaya H, Hiramoto M, Yoshimizu N, Fukushi K, Satoh K: A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension. Thromb Haemost. 1998 Sep;80(3):372-5. [PubMed Link Image]
  13. Kruse S, Mao XQ, Heinzmann A, Blattmann S, Roberts MH, Braun S, Gao PS, Forster J, Kuehr J, Hopkin JM, Shirakawa T, Deichmann KA: The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma. Am J Hum Genet. 2000 May;66(5):1522-30. Epub 2000 Mar 24. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5777
Enzyme 16 Name Platelet-activating factor acetylhydrolase IB subunit gamma
Enzyme 16 Synonyms
  1. PAF acetylhydrolase 29 kDa subunit
  2. PAF-AH 29 kDa subunit
  3. PAF-AH subunit gamma
  4. PAFAH subunit gamma
Enzyme 16 Gene Name PAFAH1B3
Enzyme 16 Protein Sequence >Platelet-activating factor acetylhydrolase IB subunit gamma
MSGEENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRE
LFSPLHALNFGIGGDGTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAI
VQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPRAHFLDADPGFVH
SDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGAPLLEPAP
Enzyme 16 Number of Residues 231
Enzyme 16 Molecular Weight 25734.1
Enzyme 16 Theoretical pI 6.84
Enzyme 16 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 16 General Function Involved in hydrolase activity
Enzyme 16 Specific Function Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain
Enzyme 16 Pathways
Enzyme 16 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate [RN:R04452]
Enzyme 16 Pfam Domain Function Not Available
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID Q15102 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PA1B3_HUMAN Link Image
Enzyme 16 PDB ID 1FXW Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >696 bp
ATGAGTGGAGAGGAGAACCCAGCCAGCAAGCCCACGCCGGTGCAGGACGTACAGGGCGAC
GGGCGCTGGATGTCCCTGCACCATCGGTTCGTGGCTGACAGCAAAGATAAGGAACCCGAA
GTCGTCTTCATCGGGGACTCCTTGGTCCAGCTCATGCACCAGTGCGAGATCTGGCGCGAG
CTCTTCTCTCCTCTGCATGCACTTAACTTTGGCATTGGTGGTGACGGCACACAGCATGTA
CTGTGGCGGCTGGAGAATGGGGAGCTGGAACACATCCGGCCCAAGATTGTGGTGGTCTGG
GTGGGCACCAACAACCACGGACACACAGCAGAGCAGGTGACTGGTGGCATCAAGGCCATT
GTGCAACTGGTGAATGAGCGACAGCCCCAGGCCCGGGTTGTGGTGCTGGGCCTGCTTCCG
CGAGGCCAACATCCCAACCCACTTCGGGAGAAGAACCGACAGGTGAACGAGCTGGTACGG
GCGGCACTGGCTGGCCACCCTCGGGCCCACTTCCTAGATGCCGACCCTGGCTTTGTGCAC
TCAGATGGCACCATCAGCCATCATGACATGTATGATTACCTGCATCTGAGCCGCCTGGGC
TACACACCTGTTTGCCGGGCTCTGCACTCCCTGCTTCTGCGTCTGCTGGCCCAAGACCAG
GGCCAAGGTGCTCCCCTGCTGGAGCCCGCACCCTAA
Enzyme 16 GenBank Gene ID D63391 Link Image
Enzyme 16 GeneCard ID PAFAH1B3 Link Image
Enzyme 16 GenAtlas ID PAFAH1B3 Link Image
Enzyme 16 HGNC ID HGNC:8576 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 19q13.1
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Adachi H, Tsujimoto M, Hattori M, Arai H, Inoue K: cDNA cloning of human cytosolic platelet-activating factor acetylhydrolase gamma-subunit and its mRNA expression in human tissues. Biochem Biophys Res Commun. 1995 Sep 5;214(1):180-7. [PubMed Link Image]
  2. 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]
  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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5780
Enzyme 17 Name Platelet-activating factor acetylhydrolase IB subunit beta
Enzyme 17 Synonyms
  1. PAF acetylhydrolase 30 kDa subunit
  2. PAF-AH 30 kDa subunit
  3. PAF-AH subunit beta
  4. PAFAH subunit beta
Enzyme 17 Gene Name PAFAH1B2
Enzyme 17 Protein Sequence >Platelet-activating factor acetylhydrolase IB subunit beta
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWR
ELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEA
IVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFV
HSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
Enzyme 17 Number of Residues 229
Enzyme 17 Molecular Weight 25569.1
Enzyme 17 Theoretical pI 5.80
Enzyme 17 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 17 General Function Involved in hydrolase activity
Enzyme 17 Specific Function Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit
Enzyme 17 Pathways
Enzyme 17 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate [RN:R04452]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 12653259 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P68402 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PA1B2_HUMAN Link Image
Enzyme 17 PDB ID 1FXW Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >690 bp
ATGAGCCAAGGAGACTCAAACCCAGCAGCTATTCCGCATGCAGCAGAAGATATTCAAGGA
GATGACCGATGGATGTCTCAGCACAACAGATTTGTTTTGGACTGTAAAGACAAAGAGCCT
GATGTACTGTTCGTGGGAGACTCCATGGTGCAGTTAATGCAGCAATATGAGATATGGCGA
GAGCTTTTTTCCCCACTTCATGCACTGAATTTTGGAATTGGGGGAGATACAACAAGACAT
GTTTTGTGGAGACTAAAGAATGGAGAACTGGAGAATATTAAGCCTAAGGTCATTGTTGTC
TGGGTAGGAACAAATAACCACGAAAATACAGCAGAAGAAGTAGCAGGTGGGATCGAGGCC
ATTGTACAACTTATCAACACAAGGCAGCCACAGGCCAAAATCATTGTATTGGGTTTGTTA
CCTCGAGGTGAGAAACCCAATCCTTTGAGGCAAAAGAACGCCAAGGTGAACCAACTCCTC
AAGGTTTCGCTGCCGAAGCTTGCCAACGTGCAGCTCCTGGATACCGACGGGGGTTTTGTG
CACTCGGACGGTGCCATCTCCTGCCACGACATGTTTGATTTTCTGCATCTGACAGGAGGG
GGCTATGCAAAGATCTGCAAACCCCTGCATGAACTGATCATGCAGTTGTTGGAGGAAACA
CCTGAGGAGAAACAAACCACCATTGCCTGA
Enzyme 17 GenBank Gene ID BC000398 Link Image
Enzyme 17 GeneCard ID PAFAH1B2 Link Image
Enzyme 17 GenAtlas ID PAFAH1B2 Link Image
Enzyme 17 HGNC ID HGNC:8575 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 11q23
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Adachi H, Tsujimoto M, Hattori M, Arai H, Inoue K: Differential tissue distribution of the beta- and gamma-subunits of human cytosolic platelet-activating factor acetylhydrolase (isoform I). Biochem Biophys Res Commun. 1997 Apr 7;233(1):10-3. [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. 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5783
Enzyme 18 Name Group 3 secretory phospholipase A2
Enzyme 18 Synonyms
  1. Group III secretory phospholipase A2
  2. GIII sPLA2
  3. sPLA2-III
  4. Phosphatidylcholine 2-acylhydrolase 3
Enzyme 18 Gene Name PLA2G3
Enzyme 18 Protein Sequence >Group 3 secretory phospholipase A2
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
Enzyme 18 Number of Residues 509
Enzyme 18 Molecular Weight 57150.5
Enzyme 18 Theoretical pI 9.23
Enzyme 18 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
Enzyme 18 General Function Involved in phospholipase A2 activity
Enzyme 18 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage:1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE
Enzyme 18 Pathways
Enzyme 18 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-19
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 142976884 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NZ20 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PA2G3_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1530 bp
ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGTCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA
Enzyme 18 GenBank Gene ID NM_015715.3 Link Image
Enzyme 18 GeneCard ID PLA2G3 Link Image
Enzyme 18 GenAtlas ID PLA2G3 Link Image
Enzyme 18 HGNC ID HGNC:17934 Link Image
Enzyme 18 Chromosome Location 2
Enzyme 18 Locus 22q12.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed Link Image]
  2. 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]
  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. Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed Link Image]
  5. Murakami M, Masuda S, Shimbara S, Ishikawa Y, Ishii T, Kudo I: Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholipase A(2). J Biol Chem. 2005 Jul 1;280(26):24987-98. Epub 2005 Apr 29. [PubMed Link Image]
  6. 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5785
Enzyme 19 Name Platelet-activating factor acetylhydrolase 2, cytoplasmic
Enzyme 19 Synonyms
  1. Serine-dependent phospholipase A2
  2. SD-PLA2
  3. hSD-PLA2
Enzyme 19 Gene Name PAFAH2
Enzyme 19 Protein Sequence >Platelet-activating factor acetylhydrolase 2, cytoplasmic
MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCT
GLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAF
CMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHV
RNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGA
TAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQ
HEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKH
LDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL
Enzyme 19 Number of Residues 392
Enzyme 19 Molecular Weight 44035.3
Enzyme 19 Theoretical pI 6.89
Enzyme 19 GO Classification
Function
  • 1-alkyl-2-acetylglycerophosphocholine esterase activity
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 19 General Function Involved in 1-alkyl-2-acetylglycerophosphocholine esterase activity
Enzyme 19 Specific Function Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme
Enzyme 19 Pathways
Enzyme 19 Reactions
  • 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate [RN:R04452]
Enzyme 19 Pfam Domain Function Not Available
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 55859645 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q99487 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PAFA2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1179 bp
ATGGGGGTCAACCAGTCTGTGGGCTTTCCACCTGTCACAGGACCCCACCTCGTAGGCTGT
GGGGATGTGATGGAGGGTCAGAATCTCCAGGGGAGCTTCTTTCGACTCTTCTACCCCTGC
CAAAAGGCAGAGGAGACCATGGAGCAGCCCCTGTGGATTCCCCGCTATGAGTACTGCACT
GGCCTGGCCGAGTACCTGCAGTTTAATAAGCGCTGCGGGGGCTTGCTGTTCAACCTGGCG
GTGGGATCTTGTCGCCTGCCTGTTAGCTGGAATGGCCCCTTTAAGACAAAGGACTCTGGA
TACCCCTTGATCATCTTCTCCCATGGCCTAGGAGCCTTCAGGACTTTGTATTCAGCCTTC
TGCATGGAGCTGGCCTCACGTGGCTTTGTGGTTGCTGTGCCAGAGCACAGGGACCGGTCA
GCGGCAACCACCTATTTCTGCAAGCAGGCCCCAGAAGAGAACCAGCCCACCAATGAATCG
CTGCAGGAGGAATGGATCCCTTTCCGTCGAGTTGAGGAAGGGGAGAAGGAATTTCATGTT
CGGAATCCCCAGGTGCATCAGCGGGTAAGCGAGTGTTTACGGGTGTTGAAGATCCTGCAA
GAGGTCACTGCTGGGCAGACTGTCTTCAACATCTTGCCTGGTGGCTTGGATCTGATGACT
TTGAAGGGCAACATTGACATGAGCCGTGTGGCTGTGATGGGACATTCATTTGGAGGGGCC
ACAGCTATTCTGGCTTTGGCCAAGGAGACCCAATTTCGGTGTGCGGTGGCTCTGGATGCT
TGGATGTTTCCTCTGGAACGTGACTTTTACCCCAAGGCCCGAGGACCTGTGTTCTTTATC
AATACTGAGAAATTCCAGACAATGGAGAGTGTCAATTTGATGAAGAAGATATGTGCCCAG
CATGAACAGTCTAGGATCATAACCGTTCTTGGTTCTGTTCATCGGAGTCAAACTGACTTT
GCTTTTGTGACTGGCAACTTGATTGGTAAATTCTTCTCCACTGAAACCCGTGGGAGCCTG
GACCCCTATGAAGGGCAGGAGGTTATGGTACGGGCCATGTTGGCCTTCCTGCAGAAGCAC
CTCGACCTGAAAGAAGACTATAATCAATGGAACAACCTTATTGAAGGCATTGGACCGTCG
CTCACCCCAGGGGCCCCCCACCATCTGTCCAGCCTGTAG
Enzyme 19 GenBank Gene ID AL592064 Link Image
Enzyme 19 GeneCard ID PAFAH2 Link Image
Enzyme 19 GenAtlas ID PAFAH2 Link Image
Enzyme 19 HGNC ID HGNC:8579 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 1p36
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Hattori K, Adachi H, Matsuzawa A, Yamamoto K, Tsujimoto M, Aoki J, Hattori M, Arai H, Inoue K: cDNA cloning and expression of intracellular platelet-activating factor (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase. J Biol Chem. 1996 Dec 20;271(51):33032-8. [PubMed Link Image]
  2. Rice SQ, Southan C, Boyd HF, Terrett JA, MacPhee CH, Moores K, Gloger IS, Tew DG: Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor. Biochem J. 1998 Mar 15;330 ( Pt 3):1309-15. [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. Stafforini DM, McIntyre TM, Zimmerman GA, Prescott SM: Platelet-activating factor acetylhydrolases. J Biol Chem. 1997 Jul 18;272(29):17895-8. [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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8755
Enzyme 20 Name Phospholipase A2, group XIIA, isoform CRA_b
Enzyme 20 Synonyms
  1. SubName: cDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2 (EC 3.1.1.4)
  2. SubName: cDNA, FLJ93563, Homo sapiens phospholipase A2, group XII (PLA2G12), mRNA
Enzyme 20 Gene Name PLA2G12A
Enzyme 20 Protein Sequence >Phospholipase A2, group XIIA, isoform CRA_b
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
Enzyme 20 Number of Residues 189
Enzyme 20 Molecular Weight 21067.0
Enzyme 20 Theoretical pI 7.27
Enzyme 20 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 20 General Function Involved in phospholipase A2 activity
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 22761446 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q542Y6 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name Q542Y6_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTAGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
Enzyme 20 GenBank Gene ID AK075389 Link Image
Enzyme 20 GeneCard ID PLA2G12A Link Image
Enzyme 20 GenAtlas ID PLA2G12A Link Image
Enzyme 20 HGNC ID HGNC:18554 Link Image
Enzyme 20 Chromosome Location 4
Enzyme 20 Locus 4q25
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. 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]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 12907
Enzyme 21 Name Lysophospholipid acyltransferase 5
Enzyme 21 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 21 Gene Name LPCAT3
Enzyme 21 Protein Sequence >Lysophospholipid acyltransferase 5
MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRH
YLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCF
QMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRG
VPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFY
LVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGL
GFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKE
LSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFY
YLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRK
EKLKKME
Enzyme 21 Number of Residues 487
Enzyme 21 Molecular Weight 56034.5
Enzyme 21 Theoretical pI 8.87
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Involved in 1-acylglycerophosphocholine O-acyltransfera
Enzyme 21 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 21 Pathways Not Available
Enzyme 21 Reactions
  • acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 44-64 84-104 111-131 180-200 227-247 285-305 364-384 422-442 453-473
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 42542394 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q6P1A2 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name MBOA5_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID NM_005768.5 Link Image
Enzyme 21 GeneCard ID LPCAT3 Link Image
Enzyme 21 GenAtlas ID LPCAT3 Link Image
Enzyme 21 HGNC ID HGNC:30244 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 12p13
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 12909
Enzyme 22 Name Lysophosphatidylcholine acyltransferase 1
Enzyme 22 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 22 Gene Name LPCAT1
Enzyme 22 Protein Sequence >Lysophosphatidylcholine acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
Enzyme 22 Number of Residues 534
Enzyme 22 Molecular Weight 59150.7
Enzyme 22 Theoretical pI 5.82
Enzyme 22 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 22 General Function Involved in acyltransferase activity
Enzyme 22 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 22 Pathways
Enzyme 22 Reactions
  • acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 58-78
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 100811832 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q8NF37 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PCAT1_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID AB244719 Link Image
Enzyme 22 GeneCard ID LPCAT1 Link Image
Enzyme 22 GenAtlas ID LPCAT1 Link Image
Enzyme 22 HGNC ID HGNC:25718 Link Image
Enzyme 22 Chromosome Location 5
Enzyme 22 Locus 5p15.33
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 12910
Enzyme 23 Name Lysophosphatidylcholine acyltransferase 2
Enzyme 23 Synonyms
  1. LPC acyltransferase 2
  2. LPCAT-2
  3. LysoPC acyltransferase 2
  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 1
Enzyme 23 Gene Name LPCAT2
Enzyme 23 Protein Sequence >Lysophosphatidylcholine acyltransferase 2
MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVL
LGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFF
SMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLR
AVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPG
VPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPV
LFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGV
RKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGL
AVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDS
ISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSD
KKDD
Enzyme 23 Number of Residues 544
Enzyme 23 Molecular Weight 60207.3
Enzyme 23 Theoretical pI 6.51
Enzyme 23 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 23 General Function Involved in acyltransferase activity
Enzyme 23 Specific Function Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet- activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso- PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-alkyl-phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 58-78
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 126364244 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q7L5N7 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PCAT2_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1635 bp
ATGAGCCGGTGCGCCCAGGCGGCGGAAGTGGCGGCCACAGTGCCAGGTGCCGGCGTCGGG
AACGTGGGGCTGCGGCCGCCCATGGTGCCCCGTCAGGCGTCCTTCTTCCCGCCGCCGGTG
CCGAACCCCTTCGTGCAGCAGACGCAGATCGGCTCCGCGAGGCGGGTCCAGATTGTCCTT
CTTGGGATTATCTTGCTTCCAATTCGTGTCTTATTGGTTGCGTTAATTTTATTACTTGCA
TGGCCATTTGCTGCAATTTCAACAGTATGCTGTCCTGAAAAGCTGACCCACCCAATAACT
GGTTGGAGGAGGAAAATTACTCAAACAGCTTTGAAATTTCTGGGTCGTGCTATGTTCTTT
TCAATGGGATTTATAGTTGCTGTAAAAGGAAAGATTGCAAGTCCTTTGGAAGCACCAGTT
TTTGTTGCTGCCCCTCATTCAACATTCTTTGATGGAATTGCCTGTGTTGTAGCTGGGTTA
CCTTCTATGGTATCTCGAAATGAGAATGCACAAGTCCCTCTGATTGGCAGACTGTTACGG
GCTGTGCAACCAGTTTTGGTGTCCCGTGTAGATCCGGATTCCCGAAAAAACACAATAAAT
GAAATAATAAAGCGAACAACATCAGGAGGAGAATGGCCCCAGATACTAGTTTTCCCAGAA
GGTACTTGTACTAATCGTTCCTGTTTGATTACTTTTAAACCAGGAGCCTTCATTCCAGGA
GTTCCAGTGCAGCCAGTCCTCCTCAGATACCCAAACAAGCTGGATACTGTGACCTGGACA
TGGCAAGGATATACATTCATTCAGCTTTGTATGCTTACTTTCTGCCAGCTCTTCACAAAG
GTAGAAGTTGAGTTTATGCCAGTTCAAGTACCAAATGATGAAGAAAAAAATGATCCTGTC
CTTTTTGCCAATAAAGTCCGGAATTTAATGGCAGAAGCTCTGGGAATACCAGTAACAGAT
CATACCTATGAAGACTGCAGATTGATGATTTCAGCAGGACAGCTAACATTGCCTATGGAA
GCTGGGCTGGTGGAATTTACTAAAATTAGCCGAAAATTGAAATTAGATTGGGATGGTGTT
CGTAAGCATTTGGATGAATATGCATCTATTGCGAGTTCCTCAAAAGGAGGAAGAATTGGA
ATTGAAGAATTCGCCAAGTATTTAAAGTTGCCTGTTTCAGATGTCTTGAGACAACTTTTT
GCACTCTTTGACAGGAACCATGATGGCAGCATTGACTTCCGAGAGTATGTGATTGGCCTG
GCTGTCTTGTGCAACCCTTCCAACACAGAGGAGATCATCCAGGTGGCATTTAAGCTGTTT
GACGTTGATGAGGATGGCTACATAACGGAGGAAGAGTTCTCCACCATTCTACAGGCTTCC
CTTGGAGTGCCTGACCTTGATGTTTCTGGTCTCTTCAAGGAAATAGCCCAAGGGGACTCA
ATTTCCTATGAGGAATTTAAAAGTTTTGCCTTAAAGCATCCAGAATATGCTAAGATATTT
ACAACATACCTAGACCTCCAGACGTGCCATGTGTTTTCATTACCAAAAGAAGTCCAGACA
ACCCCCTCCACCGCCAGTAATAAAGTCAGCCCTGAAAAGCATGAAGAGAGTACCTCAGAC
AAAAAAGATGACTGA
Enzyme 23 GenBank Gene ID AB244718 Link Image
Enzyme 23 GeneCard ID LPCAT2 Link Image
Enzyme 23 GenAtlas ID LPCAT2 Link Image
Enzyme 23 HGNC ID HGNC:26032 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 16q12.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Shindou H, Hishikawa D, Nakanishi H, Harayama T, Ishii S, Taguchi R, Shimizu T: A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase. J Biol Chem. 2007 Mar 2;282(9):6532-9. Epub 2006 Dec 20. [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. 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 12921
Enzyme 24 Name 60 kDa lysophospholipase
Enzyme 24 Synonyms
  1. L-asparaginase
  2. L-asparagine amidohydrolase
  3. Platelet-activating factor acetylhydrolase
  4. PAF acetylhydrolase
Enzyme 24 Gene Name ASPG
Enzyme 24 Protein Sequence >60 kDa lysophospholipase
MARAVGPERRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPMFHDEEHARARGLSEDT
LVLPPASRNQRILYTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMA
FAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQL
FRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGL
LRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCL
QGAVTTDYAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGLSLDVRKELLTKDLRGEM
TPPSVEERRPSLQGNTLGGGVSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQAL
VELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHP
GVIGLLREAGASLSTQELEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHV
AEAAGNLAVVAFLQSLEGAVGAQAPCP
Enzyme 24 Number of Residues 567
Enzyme 24 Molecular Weight 60287.7
Enzyme 24 Theoretical pI 5.59
Enzyme 24 GO Classification
Function
  • asparaginase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 24 General Function Involved in asparaginase activity
Enzyme 24 Specific Function Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 122937331 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q86U10 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name LPP60_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1740 bp
ATGGCGCGCGCGGTGGGGCCCGAGCGGAGGCTGCTGGCCGTCTACACCGGCGGCACCATT
GGCATGCGGAGTGAGCTCGGCGTGCTTGTGCCCGGGACGGGCCTGGCTGCCATCCTGAGG
ACACTGCCCATGTTCCATGACGAGGAGCACGCCCGAGCCCGCGGCCTCTCTGAGGACACC
CTGGTGCTACCCCCGGCCAGCCGCAACCAGAGGATTCTCTACACCGTGCTGGAGTGCCAG
CCCCTCTTCGACTCCAGTGACATGACCATCGCTGAGTGGGTTTGCCTTGCCCAGACCATC
AAGAGGCACTACGAGCAGTACCACGGCTTTGTGGTCATCCACGGCACCGACACCATGGCC
TTTGCTGCCTCGATGCTGTCCTTCATGCTGGAGAACCTGCAGAAGACTGTCATCCTCACT
GGGGCCCAGGTGCCCATCCATGCCCTGTGGAGCGACGGCCGTGAGAACCTGCTGGGGGCA
CTGCTCATGGCTGGCCAGTATGTGATCCCAGAGGTCTGCCTTTTCTTCCAGAATCAGCTG
TTTCGGGGCAACCGGGCAACCAAGGTAGACGCTCGGAGGTTCGCAGCTTTCTGCTCCCCG
AACCTGCTGCCTCTGGCCACAGTGGGTGCTGACATCACAATCAACAGGGAGCTGGTGCGG
AAGGTGGACGGGAAGGCTGGGCTGGTGGTGCACAGCAGCATGGAGCAGGACGTGGGCCTG
CTGCGCCTCTACCCTGGGATCCCTGCCGCCCTGGTTCGGGCCTTCTTGCAGCCTCCCCTG
AAGGGCGTGGTCATGGAGACCTTCGGTTCAGGGAACGGACCCACCAAGCCCGACCTGCTG
CAGGAGCTGCGGGTGGCCACCGAGCGCGGCCTGGTCATCGTCAACTGTACCCACTGCCTC
CAGGGGGCTGTGACCACAGACTATGCAGCTGGCATGGCCATGGCGGGAGCCGGCGTCATC
TCAGGCTTCGACATGACATCGGAGGCCGCCCTGGCCAAGCTATCGTATGTGCTGGGCCAG
CCAGGGCTGAGCCTGGATGTCAGGAAGGAGCTGCTGACCAAGGACCTTCGGGGGGAGATG
ACGCCACCCTCGGTGGAAGAGCGCCGGCCCTCACTGCAGGGCAACACGCTGGGCGGTGGG
GTCTCCTGGCTCCTCAGTCTGAGCGGCAGCCAGGAGGCAGATGCCCTGCGGAATGCCCTG
GTGCCCAGCCTGGCCTGTGCTGCTGCCCACGCCGGTGACGTGGAGGCGCTGCAGGCGCTT
GTGGAGCTGGGCAGTGACCTGGGCCTGGTGGACTTTAACGGCCAAACCCCACTGCACGCG
GCCGCCCGGGGAGGCCACACAGAGGCAGTCACCATGCTGCTGCAGAGAGGTGTGGACGTG
AACACCCGGGACACGGATGGCTTCAGCCCGCTGCTGCTGGCCGTGCGGGGCAGGCATCCG
GGTGTCATTGGGTTGCTGCGGGAAGCCGGGGCCTCCCTGTCCACCCAGGAGCTGGAGGAA
GCAGGGACGGAGCTGTGCAGGCTGGCATACAGGGCCGACCTCGAAGGCCTGCAGGTGTGG
TGGCAGGCAGGGGCTGACCTGGGGCAGCCGGGCTATGACGGGCACAGCGCCCTGCACGTC
GCAGAGGCAGCCGGGAACCTGGCAGTGGTGGCCTTTCTACAGAGCCTGGAGGGTGCGGTT
GGTGCCCAGGCCCCATGCCCAGAGCCCTCATGTTTTCAGGAAGTGCTGCCTGGTGTCTAA
Enzyme 24 GenBank Gene ID NM_001080464 Link Image
Enzyme 24 GeneCard ID ASPG Link Image
Enzyme 24 GenAtlas ID ASPG Link Image
Enzyme 24 HGNC ID HGNC:20123 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 14q32.33
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 12922
Enzyme 25 Name Phospholipase B1, membrane-associated
Enzyme 25 Synonyms
  1. Phospholipase B
  2. hPLB
  3. Phospholipase B/lipase
  4. PLB/LIP
  5. Phospholipase A2
  6. Lysophospholipase
Enzyme 25 Gene Name PLB1
Enzyme 25 Protein Sequence >Phospholipase B1, membrane-associated
MGLRPGIFLLELLLLLGQGTPQIHTSPRKSTLEGQLWPETLKNSPFPCNPNKLGVNMPSK
SVHSLKPSDIKFVAAIGNLEIPPDPGTGDLEKQDWTERPQQVCMGVMTVLSDIIRYFSPS
VPMPVCHTGKRVIPHDGAEDLWIQAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLC
PSAQQNGLAAGGVDELMGVLDYLQQEVPRAFVNLVDLSEVAEVSRQYHGTWLSPAPEPCN
CSEETTRLAKVVMQWSYQEAWNSLLASSRYSEQESFTVVFQPFFYETTPSLHSEDPRLQD
STTLAWHLWNRMMEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKL
EVREGAEIRCPDKDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQ
YRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDL
PVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDI
LHAEVPRAFVNLVTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEF
NKKFQEKTHQLIESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKS
HSRAASALWNNMLEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDR
APSALHPTSVHALRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYSAGGDGS
LENVTTLPNILREFNRNLTGYAVGTGDANDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKD
DHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLV
DFLNPTIMRQVFLGNPDKCPVQQASVLCNCVLTLRENSQELARLEAFSRAYRSSMRELVG
SGRYDTQEDFSVVLQPFFQNIQLPVLADGLPDTSFFAPDCIHPNQKFHSQLARALWTNML
EPLGSKTETLDLRAEMPITCPTQNEPFLRTPRNSNYTYPIKPAIENWGSDFLCTEWKASN
SVPTSVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTT
LPNILKKFNPYLLGFSTSTWEGTAGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKD
WKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELASLY
QGQGGKCAMLAAQNNCTCLRHSQSSLEKQELKKVNWNLQHGISSFSYWHQYTQREDFAVV
VQPFFQNTLTPLNERGDTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVGRKTTSNNFT
HSRAKLKCPSPESPYLYTLRNSRLLPDQAEEAPEVLYWAVPVAAGVGLVVGIIGTVVWRC
RRGGRREDPPMSLRTVAL
Enzyme 25 Number of Residues 1458
Enzyme 25 Molecular Weight 163079.3
Enzyme 25 Theoretical pI 5.72
Enzyme 25 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 25 General Function Involved in hydrolase activity
Enzyme 25 Specific Function Membrane-associated phospholipase. Exhibits a calcium- independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-21
Enzyme 25 Transmembrane Regions
  • 1418-1438
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 283436112 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q6P1J6 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PLB1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >4377 bp
ATGGGGCTGCGGCCAGGCATTTTCCTCCTGGAGCTGCTGCTGCTTCTGGGGCAAGGGACC
CCTCAGATCCATACCTCTCCTAGAAAGAGTACATTGGAAGGGCAGCTATGGCCAGAGACC
CTGAAGAATTCTCCATTCCCATGCAACCCAAATAAATTAGGAGTGAATATGCCTTCTAAA
TCAGTTCACTCTCTGAAGCCTTCTGATATTAAATTTGTGGCAGCCATTGGCAATCTGGAA
ATTCCTCCAGACCCAGGGACGGGCGATCTGGAGAAGCAAGACTGGACTGAAAGGCCACAG
CAGGTGTGCATGGGAGTGATGACAGTCCTTTCAGACATCATCAGATATTTCAGTCCTTCT
GTTCCAATGCCTGTGTGCCACACTGGAAAGAGAGTCATACCCCACGATGGTGCTGAAGAC
TTGTGGATTCAGGCTCAAGAACTGGTGAGAAACATGAAAGAGAACCTGCAACTTGACTTT
CAATTTGACTGGAAGCTCATCAATGTGTTCTTCAGTAATGCAAGCCAGTGTTACCTGTGC
CCCTCTGCTCAACAGAATGGGCTTGCGGCGGGCGGCGTGGATGAGCTGATGGGGGTGCTG
GACTACCTGCAGCAGGAGGTCCCCAGAGCATTTGTAAACCTGGTGGACCTCTCTGAGGTT
GCAGAGGTCTCTCGTCAGTATCACGGCACTTGGCTCAGCCCTGCACCAGAGCCCTGTAAT
TGCTCAGAGGAGACCACCCGGCTGGCCAAGGTGGTGATGCAGTGGTCTTATCAGGAAGCC
TGGAACAGCCTCCTGGCCTCCAGCAGGTACAGTGAGCAGGAGTCCTTCACCGTGGTTTTC
CAGCCTTTCTTCTATGAGACCACCCCATCTCTACACTCGGAGGACCCCCGACTCCAGGAT
TCTACCACGCTGGCCTGGCATCTCTGGAATAGGATGATGGAGCCAGCAGGAGAGAAAGAT
GAGCCATTGAGTGTAAAACACGGGAGGCCAATGAAGTGTCCCTCTCAGGAGAGCCCCTAT
CTGTTCAGCTACAGAAACAGCAACTACCTGACCAGACTGCAGAAACCCCAAGACAAGCTT
GAGGTAAGAGAAGGAGCGGAAATCAGATGTCCTGACAAAGACCCCTCCGATACGGTTCCC
ACCTCAGTTCATAGGCTGAAGCCGGCTGACATCAACGTAATTGGAGCCCTGGGTGACTCT
CTCACGGCAGGCAATGGGGCCGGGTCCACACCTGGGAACGTCTTGGACGTCTTGACTCAG
TACCGAGGCCTGTCCTGGAGCGTCGGCGGAGATGAGAACATCGGCACCGTTACCACCCTG
GCGAACATCCTCCGGGAATTCAACCCTTCCCTGAAGGGCTTCTCTGTTGGCACTGGGAAA
GAAACCAGTCCTAATGCCTTCTTAAACCAGGCTGTGGCAGGAGGCCGAGCTGAGGATCTA
CCTGTCCAGGCCAGGAGGCTGGTGGACCTGATGAAGAATGACACGAGGATACACTTTCAG
GAAGACTGGAAGATAATAACCCTGTTTATAGGCGGCAATGACCTCTGTGATTTCTGCAAT
GATCTGGTCCACTATTCTCCCCAGAACTTCACAGACAACATTGGAAAGGCCCTGGACATC
CTCCATGCTGAGGTTCCTCGGGCATTTGTGAACCTGGTGACGGTGCTTGAGATCGTCAAC
CTGAGGGAGCTGTACCAGGAGAAAAAAGTCTACTGCCCAAGGATGATCCTCAGGTCTCTG
TGTCCCTGTGTCCTGAAGTTTGATGATAACTCAACAGAACTTGCTACCCTCATCGAATTC
AACAAGAAGTTTCAGGAGAAGACCCACCAACTGATTGAGAGTGGGCGATATGACACAAGG
GAAGATTTTACTGTGGTTGTGCAGCCGTTCTTTGAAAACGTGGACATGCCAAAGACCTCG
GAAGGATTGCCTGACAACTCTTTCTTCGCTCCTGACTGTTTCCACTTCAGCAGCAAGTCT
CACTCCCGAGCAGCCAGTGCTCTCTGGAACAATATGCTGGAGCCTGTTGGCCAGAAGACG
ACTCGTCATAAGTTTGAAAACAAGATCAATATCACATGTCCGAACCAGGTCCAGCCGTTT
CTGAGGACCTACAAGAACAGCATGCAGGGTCATGGGACCTGGCTGCCATGCAGGGACAGA
GCCCCTTCTGCCTTGCACCCTACCTCAGTGCATGCCCTGAGACCTGCAGACATCCAAGTT
GTGGCTGCTCTGGGGGATTCTCTGACCGCTGGCAATGGAATTGGCTCCAAACCAGACGAC
CTCCCCGATGTCACCACACAGTATCGGGGACTGTCATACAGTGCAGGAGGGGACGGCTCC
CTGGAGAATGTGACCACCTTACCTAATATCCTTCGGGAGTTTAACAGAAACCTCACAGGC
TACGCCGTGGGCACGGGTGATGCCAATGACACGAATGCATTCCTCAATCAAGCTGTTCCC
GGAGCAAAGGCTGAGGATCTTATGAGCCAAGTCCAAACTCTGATGCAGAAGATGAAAGAT
GATCATAGAGTAAATTTCCATGAAGACTGGAAGGTCATCACAGTGCTGATCGGAGGCAGC
GATTTATGTGACTACTGCACAGATTCGAATCTGTATTCTGCAGCCAACTTTGTTCACCAT
CTCCGCAATGCCTTGGACGTCCTGCATAGAGAGGTGCCCAGAGTCCTGGTCAACCTCGTG
GACTTCCTGAACCCCACTATCATGCGGCAGGTGTTCCTGGGAAACCCAGACAAGTGCCCA
GTGCAGCAGGCCAGCGTTTTGTGTAACTGCGTTCTGACCCTGCGGGAGAACTCCCAAGAG
CTAGCCAGGCTGGAGGCCTTCAGCCGAGCCTACCGGAGCAGCATGCGCGAGCTGGTGGGG
TCAGGCCGCTATGACACGCAGGAGGACTTCTCTGTGGTGCTGCAGCCCTTCTTCCAGAAC
ATCCAGCTCCCTGTCCTGGCGGATGGGCTCCCAGATACGTCCTTCTTTGCCCCAGACTGC
ATCCACCCAAATCAGAAATTCCACTCCCAGCTGGCCAGAGCCCTTTGGACCAATATGCTT
GAACCACTTGGAAGCAAAACAGAGACCCTGGACCTGAGAGCAGAGATGCCCATCACCTGT
CCCACTCAGAATGAGCCCTTCCTGAGAACCCCTCGGAATAGTAACTACACGTACCCCATC
AAGCCAGCCATTGAGAACTGGGGCAGTGACTTCCTGTGTACAGAGTGGAAGGCTTCCAAT
AGTGTTCCAACCTCTGTCCACCAGCTCCGACCAGCAGACATCAAAGTGGTGGCCGCCCTG
GGTGACTCTCTGACTACAGCAGTGGGAGCTCGACCAAACAACTCCAGTGACCTACCCACA
TCTTGGAGGGGACTCTCTTGGAGCATTGGAGGGGATGGGAACTTGGAGACTCACACCACA
CTGCCCAACATTCTGAAGAAGTTCAACCCTTACCTCCTTGGCTTCTCTACCAGCACCTGG
GAGGGGACAGCAGGACTAAATGTGGCAGCGGAAGGGGCCAGAGCTAGGGACATGCCAGCC
CAGGCCTGGGACCTGGTAGAGCGAATGAAAAACAGCCCCGACATCAACCTGGAGAAAGAC
TGGAAGCTGGTCACACTCTTCATTGGGGTCAACGACTTGTGTCATTACTGTGAGAATCCG
GAGGCCCACTTGGCCACGGAATATGTTCAGCACATCCAACAGGCCCTGGACATCCTCTCT
GAGGAGCTCCCAAGGGCTTTCGTCAACGTGGTGGAGGTCATGGAGCTGGCTAGCCTGTAC
CAGGGCCAAGGCGGGAAATGTGCCATGCTGGCAGCTCAGAACAACTGCACTTGCCTCAGA
CACTCGCAAAGCTCCCTGGAGAAGCAAGAACTGAAGAAAGTGAACTGGAACCTCCAGCAT
GGCATCTCCAGTTTCTCCTACTGGCACCAATACACACAGCGTGAGGACTTTGCGGTTGTG
GTGCAGCCTTTCTTCCAAAACACACTCACCCCACTGAACGAGAGAGGGGACACTGACCTC
ACCTTCTTCTCCGAGGACTGTTTTCACTTCTCAGACCGCGGGCATGCCGAGATGGCCATC
GCACTCTGGAACAACATGCTGGAACCAGTGGGCCGCAAGACTACCTCCAACAACTTCACC
CACAGCCGAGCCAAACTCAAGTGCCCCTCTCCTGAGAGCCCTTACCTCTACACCCTGCGG
AACAGCCGATTGCTCCCAGACCAGGCTGAAGAAGCCCCCGAGGTGCTCTACTGGGCTGTC
CCAGTGGCAGCGGGAGTCGGCCTTGTGGTGGGCATCATCGGGACAGTGGTCTGGAGGTGC
AGGAGAGGTGGCCGGAGGGAAGATCCTCCAATGAGCCTGCGCACTGTGGCCCTCTAG
Enzyme 25 GenBank Gene ID NM_153021.4 Link Image
Enzyme 25 GeneCard ID PLB1 Link Image
Enzyme 25 GenAtlas ID PLB1 Link Image
Enzyme 25 HGNC ID HGNC:30041 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p23.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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]
  4. Maury E, Prevost MC, Nauze M, Redoules D, Tarroux R, Charveron M, Salles JP, Perret B, Chap H, Gassama-Diagne A: Human epidermis is a novel site of phospholipase B expression. Biochem Biophys Res Commun. 2002 Jul 12;295(2):362-9. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 14866
Enzyme 26 Name Cytosolic phospholipase A2 beta
Enzyme 26 Synonyms
  1. cPLA2-beta
  2. Phospholipase A2 group IVB
Enzyme 26 Gene Name PLA2G4B
Enzyme 26 Protein Sequence >Cytosolic phospholipase A2 beta
MAVAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVW
NQSFHFRIHRQLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEG
RLEVEFRLQSLADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGP
QEASVGTGTFRFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMR
VELKKEAGLRELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIM
ATGGGIRAMTSLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTE
LLKTQVTKNKLGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLS
DQREALSHGQNPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEF
FMGQLMKRLPESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPL
LKIEEPPSTAGRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGL
PNQLTPSEPHLCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQE
QGIPFPPISPSPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEA
AAGEVNLSSSDSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRP
H
Enzyme 26 Number of Residues 781
Enzyme 26 Molecular Weight 87977.0
Enzyme 26 Theoretical pI 5.85
Enzyme 26 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
Component
Enzyme 26 General Function Involved in metabolic process
Enzyme 26 Specific Function Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 194387976 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P0C869 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PA24B_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >2346 bp
ATGGCTGTGGCAGAGGTGTCCAGGACCTGCCTGCTCACGGTTCGTGTCCTGCAGGCCCAT
CGCCTACCCTCTAAGGACCTAGTGACCCCCTCTGACTGCTACGTGACTCTCTGGCTGCCC
ACGGCCTGCAGCCACAGGCTCCAGACACGCACGGTCAAGAACAGCAGTAGCCCTGTCTGG
AACCAGAGCTTTCACTTCAGGATCCACAGGCAGCTCAAGAATGTCATGGAACTGAAAGTC
TTTGACCAGGACCTGGTGACCGGAGATGACCCTGTGTTGTCAGTACTGTTTGATGCGGGG
ACTCTGCGGGCTGGGGAGTTCCGGCGCGAGAGCTTCTCACTGAGCCCTCAGGGTGAGGGG
CGCCTGGAAGTTGAATTTCGCCTGCAGAGTCTGGCTGACCGTGGCGAGTGGCTCGTCAGC
AATGGCGTTCTGGTGGCCCGGGAGCTCTCCTGCTTGCACGTTCAACTGGAGGAGACAGGA
GACCAGAAGTCCTCAGAGCACAGAGTTCAGCTTGTGGTTCCTGGGTCCTGTGAGGGTCCG
CAGGAGGCCTCTGTGGGCACTGGCACCTTCTGCTTCCACTGCCCAGCCTGCTGGGAGCAG
GAGCTGAGTATTCGCCTGCAGGATGCCCCCGAGGAGCAACTAAAGGCGCCACTGAGTGCC
CTGCCCTCTGGTCAAGTGGTGAGGCTTGTCTTCCCCACGTCCCAGGAGCCCCTGATGAGA
GTGGAGCTGAAAAAAGAAGCAGGACTGAGGGAGCTGGCCGTGCGACTGGGCTTCGGGCCC
TGTGCAGAGGAGCAGGCCTTCCTGAGCAGGAGGAAGCAGGTGGTGGCCGCGGCCTTGAGG
CAGGCCCTGCAGCTGGATGGAGACCTGCAGGAGGATGAGATCCCAGTGGTAGCTATTATG
GCCACTGGTGGTGGGATCCGGGCAATGACTTCCCTGTATGGGCAGCTGGCTGGCCTGAAG
GAGCTGGGCCTCTTGGATTGCGTCTCCTACATCACCGGGGCCTCGGGCTCCACCTGGGCC
TTGGCCAACCTTTATGAGGACCCAGAGTGGTCTCAGAAGGACCTGGCAGGGCCCACTGAG
TTGCTGAAGACCCAGGTGACCAAGAACAAGCTGGGTGTGCTGGCCCCCAGCCAGCTGCAG
CGGTACCGGCAGGAGCTGGCCGAGCGTGCCCGCTTGGGCTACCCAAGCTGCTTCACCAAC
CTGTGGGCCCTCATCAACGAGGCGCTGCTGCATGATGAGCCCCATGATCACAAGCTCTCA
GATCAACGGGAGGCCCTGAGTCATGGCCAGAACCCTCTGCCCATCTACTGTGCCCTCAAC
ACCAAAGGGCAGAGCCTGACCACTTTTGAATTTGGGGAGTGGTGCGAGTTCTCTCCCTAC
GAGGTCGGCTTCCCCAAGTACGGGGCCTTCATCCCCTCTGAGCTCTTTGGCTCCGAGTTC
TTTATGGGGCAGCTGATGAAGAGGCTTCCTGAGTCCCGCATCTGCTTCTTAGAAGGTATC
TGGAGCAACCTGTATGCAGCCAACCTCCAGGACAGCTTATACTGGGCCTCAGAGCCCAGC
CAGTTCTGGGACCGCTGGGTCAGGAACCAGGCCAACCTGGACAAGGAGCAGGTCCCCCTT
CTGAAGATAGAAGAACCACCCTCAACAGCCGGCAGGATAGCTGAGTTTTTCACCGATCTT
CTGACGTGGCGTCCACTGGCCCAGGCCACACATAATTTCCTGTGTGGCCTCCATTTCCAC
AAAGACTACTTTCAGCATCCTCACTTCTCCACATGGAAAGCTACCACTCTGGATGGGCTC
CCCAACCAGCTGACACCCTCGGAGCCCCACCTGTGCCTGCTGGATGTTGGCTACCTCATC
AATACCAGCTGCCTGCCCCTCCTGCAGCCCACTCGGGACGTGGACCTCATCCTGTCATTG
GACTACAACCTCCACGGAGCCTTCCAGCAGTTGCAGCTCCTGGGCCGGTTCTGCCAGGAG
CAGGGGATCCCGTTCCCACCCATCTCGCCCAGCCCCGAAGAGCAGCTCCAGCCTCGGGAG
TGCCACACCTTCTCTGACCCCACCTGCCCCGGAGCCCCTGCGGTGCTGCACTTTCCTCTG
GTCAGCGACTCCTTCCGGGAGTACTCGGCCCCTGGGGTCCGGCGGACACCCGAGGAGGCG
GCAGCTGAGGAGGTGAACCTGTCTTCATCGGACTCTCCCTACCACTACACGAAGGTGACC
TACAGCCAGGAGGACGTGGACAAGCTGCTGCACCTGACACATTACAATGTCTGCAACAAC
CAGGAGCAGCTGCTGGAGGCTCTGCGCCAGGCAGTGCAGCGGAGGCGGCAGCGCAGGCCC
CACTGA
Enzyme 26 GenBank Gene ID AK299419 Link Image
Enzyme 26 GeneCard ID PLA2G4B Link Image
Enzyme 26 GenAtlas ID PLA2G4B Link Image
Enzyme 26 HGNC ID HGNC:9036 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 15q11.2-q21.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed Link Image]
  2. Song C, Chang XJ, Bean KM, Proia MS, Knopf JL, Kriz RW: Molecular characterization of cytosolic phospholipase A2-beta. J Biol Chem. 1999 Jun 11;274(24):17063-7. [PubMed Link Image]
  3. Ghosh M, Loper R, Gelb MH, Leslie CC: Identification of the expressed form of human cytosolic phospholipase A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria and early endosomes. J Biol Chem. 2006 Jun 16;281(24):16615-24. Epub 2006 Apr 14. [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]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15299
Enzyme 27 Name cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name PLA2G2A
Enzyme 27 Protein Sequence >cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
Enzyme 27 Number of Residues 144
Enzyme 27 Molecular Weight 16083
Enzyme 27 Theoretical pI 9.51
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function Not Available
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 158256040 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID A8K5I7 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name A8K5I7_HUMAN Link Image
Enzyme 27 PDB ID 1DB4 Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Enzyme 27 GenBank Gene ID AK291302 Link Image
Enzyme 27 GeneCard ID A8K5I7 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16479
Enzyme 28 Name cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
Enzyme 28 Synonyms
  1. SubName: Lysophospholipase 3 (Lysosomal phospholipase A2), isoform CRA_a
Enzyme 28 Gene Name LYPLA3
Enzyme 28 Protein Sequence >cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Enzyme 28 Number of Residues 412
Enzyme 28 Molecular Weight 46658
Enzyme 28 Theoretical pI 6.72
Enzyme 28 GO Classification
Function
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • phosphatidylcholine-sterol O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID B3KMF3 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B3KMF3_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AK001705 Link Image
Enzyme 28 GeneCard ID B3KMF3 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location 16
Enzyme 28 Locus 16q22.1
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16561
Enzyme 29 Name Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name PLA2G6
Enzyme 29 Protein Sequence >Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRQLQDLMHISRARKPAFILGSMRDEK
RTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSM
AYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPA
ELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGG
LLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNP
WELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVS
DTVLVNALWETEVYIYEHREEFQKLIQLLLSP
Enzyme 29 Number of Residues 752
Enzyme 29 Molecular Weight 84094
Enzyme 29 Theoretical pI 7.24
Enzyme 29 GO Classification
Function
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID B0QYE8 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name B0QYE8_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AL022322 Link Image
Enzyme 29 GeneCard ID B0QYE8 Link Image
Enzyme 29 GenAtlas ID Not Available
Enzyme 29 HGNC ID Not Available
Enzyme 29 Chromosome Location 22
Enzyme 29 Locus 22q13.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available