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Human Metabolome Database Version 2.5

 

Showing metabocard for Sphingosine 1-phosphate (HMDB00277)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-23 12:56:36
Accession Number HMDB00277
Secondary Accession Numbers Not Available
Common Name Sphingosine 1-phosphate
Description Sphingosine 1-phosphate (S1P) is a phosphorylated sphingolipid metabolite with potent bioactive actions in the Sphingolipid metabolism, Calcium signaling pathway and Neuroactive ligand-receptor interaction. Generated by sphingosine kinases and ceramide kinase, S1P control numerous aspects of cell physiology, including cell survival and mammalian inflammatory responses. S1P is involved in cyclooxygenase-2 induction (COX-2), and regulate production of eicosanoids (important inflammatory mediators). S1P functions mainly via G-protein-coupled receptors and probably also has intracellular targets. (PMID 16219683)
Synonyms
  1. (2S,3R,4E)-1-(dihydrogen phosphate)2-amino-4-Octadecene-1,3-diol
  2. C18-Sphingosine 1-phosphate
  3. D-erythro-Sphingosine-1-phosphate
  4. Sphingosine 1-phosphate
  5. Sphingosine 1-phosphic acid
Chemical IUPAC Name (2-amino-3-hydroxy-octadec-4-enoxy)phosphonic acid
Chemical Formula C18H38NO5P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Sphingolipids
Sub Class
  • Primary amino alcohols
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-aminoalcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • phosphoric acid ester
  • alkene
Biofunction
  • Second messenger
Application
Source
  • Endogenous
Average Molecular Weight 379.472
Monoisotopic Molecular Weight 379.248749
Isomeric SMILES CCCCCCCCCCCCCC=CC(O)C(N)COP(O)(O)=O
Canonical SMILES CCCCCCCCCCCCCC=CC(O)C(N)COP(O)(O)=O
KEGG Compound ID C06124 Link Image
BioCyc ID Not Available
BiGG ID 47453 Link Image
Wikipedia Link Sphingosine 1-phosphate Link Image
NuGOwiki Link HMDB00277 Link Image
Metagene Link HMDB00277 Link Image
METLIN ID 5272 Link Image
PubChem Compound 5262 Link Image
PubChem Substance 5613381 Link Image
ChEBI ID Not Available
CAS Registry Number 26993-30-6
InChI Identifier InChI=1/C18H38NO5P/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-18(20)17(19)16-24-25(21,22)23/h14-15,17-18,20H,2-13,16,19H2,1H3,(H2,21,22,23)/b15-14+
Synthesis Reference Morigaki, Eiji; Miura, Yoshie; Takahata, Kyoya; Tada, Mikiro; Nakajima, Shuhei; Baba, Naomichi. Enzymic preparation of sphingosine 1-phosphate. Journal of Chemical Research, Synopses (1998), (12), 774-775.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 6.51e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 3.73 [Predicted by ALOGPS]; 3.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
Biofluid Location
  • Blood
Tissue Location
Tissue References
Fibroblasts
Platelet
Concentrations (Normal)
Biofluid Blood
Value 0.044 +/- 0.001 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Schmidt H, Schmidt R, Geisslinger G: LC-MS/MS-analysis of sphingosine-1-phosphate and related compounds in plasma samples. Prostaglandins Other Lipid Mediat. 2006 Dec;81(3-4):162-70. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Blood
Value 0.41 +/- 0.052 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Ohkawa R, Nakamura K, Okubo S, Hosogaya S, Ozaki Y, Tozuka M, Osima N, Yokota H, Ikeda H, Yatomi Y: Plasma sphingosine-1-phosphate measurement in healthy subjects: close correlation with red blood cell parameters. Ann Clin Biochem. 2008 Jul;45(Pt 4):356-63. [PubMed Link Image]
Biofluid Blood
Value 0.35 +/- 0.039 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Ohkawa R, Nakamura K, Okubo S, Hosogaya S, Ozaki Y, Tozuka M, Osima N, Yokota H, Ikeda H, Yatomi Y: Plasma sphingosine-1-phosphate measurement in healthy subjects: close correlation with red blood cell parameters. Ann Clin Biochem. 2008 Jul;45(Pt 4):356-63. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Sphingolipid Metabolism SMP00034 Link Image map00500 Link Image
General References
  1. Vogler R, Sauer B, Kim DS, Schafer-Korting M, Kleuser B: Sphingosine-1-phosphate and its potentially paradoxical effects on critical parameters of cutaneous wound healing. J Invest Dermatol. 2003 Apr;120(4):693-700. [PubMed Link Image]
  2. Kimura T, Sato K, Kuwabara A, Tomura H, Ishiwara M, Kobayashi I, Ui M, Okajima F: Sphingosine 1-phosphate may be a major component of plasma lipoproteins responsible for the cytoprotective actions in human umbilical vein endothelial cells. J Biol Chem. 2001 Aug 24;276(34):31780-5. Epub 2001 Jun 26. [PubMed Link Image]
  3. Kim JI, Jo EJ, Lee HY, Cha MS, Min JK, Choi CH, Lee YM, Choi YA, Baek SH, Ryu SH, Lee KS, Kwak JY, Bae YS: Sphingosine 1-phosphate in amniotic fluid modulates cyclooxygenase-2 expression in human amnion-derived WISH cells. J Biol Chem. 2003 Aug 22;278(34):31731-6. Epub 2003 Jun 9. [PubMed Link Image]
  4. Okajima F: Plasma lipoproteins behave as carriers of extracellular sphingosine 1-phosphate: is this an atherogenic mediator or an anti-atherogenic mediator? Biochim Biophys Acta. 2002 May 23;1582(1-3):132-7. [PubMed Link Image]
  5. Dorsam G, Graeler MH, Seroogy C, Kong Y, Voice JK, Goetzl EJ: Transduction of multiple effects of sphingosine 1-phosphate (S1P) on T cell functions by the S1P1 G protein-coupled receptor. J Immunol. 2003 Oct 1;171(7):3500-7. [PubMed Link Image]
  6. Hammer S, Sauer B, Spika I, Schraut C, Kleuser B, Schafer-Korting M: Glucocorticoids mediate differential anti-apoptotic effects in human fibroblasts and keratinocytes via sphingosine-1-phosphate formation. J Cell Biochem. 2004 Mar 1;91(4):840-51. [PubMed Link Image]
  7. Pyne S, Pyne NJ: Sphingosine 1-phosphate signalling and termination at lipid phosphate receptors. Biochim Biophys Acta. 2002 May 23;1582(1-3):121-31. [PubMed Link Image]
  8. Fieger CB, Huang MC, Van Brocklyn JR, Goetzl EJ: Type 1 sphingosine 1-phosphate G protein-coupled receptor signaling of lymphocyte functions requires sulfation of its extracellular amino-terminal tyrosines. FASEB J. 2005 Nov;19(13):1926-8. Epub 2005 Sep 7. [PubMed Link Image]
  9. Lee OH, Kim YM, Lee YM, Moon EJ, Lee DJ, Kim JH, Kim KW, Kwon YG: Sphingosine 1-phosphate induces angiogenesis: its angiogenic action and signaling mechanism in human umbilical vein endothelial cells. Biochem Biophys Res Commun. 1999 Nov 2;264(3):743-50. [PubMed Link Image]
  10. Barthomeuf C, Lamy S, Blanchette M, Boivin D, Gingras D, Beliveau R: Inhibition of sphingosine-1-phosphate- and vascular endothelial growth factor-induced endothelial cell chemotaxis by red grape skin polyphenols correlates with a decrease in early platelet-activating factor synthesis. Free Radic Biol Med. 2006 Feb 15;40(4):581-90. Epub 2005 Oct 14. [PubMed Link Image]
  11. Spiegel S, Cuvillier O, Edsall LC, Kohama T, Menzeleev R, Olah Z, Olivera A, Pirianov G, Thomas DM, Tu Z, Van Brocklyn JR, Wang F: Sphingosine-1-phosphate in cell growth and cell death. Ann N Y Acad Sci. 1998 Jun 19;845:11-8. [PubMed Link Image]
  12. Spiegel S, Cuvillier O, Edsall L, Kohama T, Menzeleev R, Olivera A, Thomas D, Tu Z, Van Brocklyn J, Wang F: Roles of sphingosine-1-phosphate in cell growth, differentiation, and death. Biochemistry (Mosc). 1998 Jan;63(1):69-73. [PubMed Link Image]
  13. Payne SG, Milstien S, Spiegel S: Sphingosine-1-phosphate: dual messenger functions. FEBS Lett. 2002 Oct 30;531(1):54-7. [PubMed Link Image]
  14. Esmon CT: Inflammation and the activated protein C anticoagulant pathway. Semin Thromb Hemost. 2006 Apr;32 Suppl 1:49-60. [PubMed Link Image]
  15. Cuvillier O, Pirianov G, Kleuser B, Vanek PG, Coso OA, Gutkind S, Spiegel S: Suppression of ceramide-mediated programmed cell death by sphingosine-1-phosphate. Nature. 1996 Jun 27;381(6585):800-3. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Lipid phosphate phosphohydrolase 2
  2. Lipid phosphate phosphohydrolase 1
  3. Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
  4. N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
  5. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
  6. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  7. Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
  8. Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
  9. Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
  10. Sphingosine kinase 1
  11. Sphingosine kinase 2
  12. Ganglioside GM2 activator precursor
  13. T-cell surface glycoprotein CD1e precursor
  14. Epididymal secretory protein E1 precursor
  15. T-cell surface glycoprotein CD1d precursor
  16. GPI mannosyltransferase 1
  17. Phosphatidylinositol-glycan biosynthesis class W protein
  18. Phosphatidylinositol-glycan biosynthesis class X protein precursor
  19. GPI mannosyltransferase 4
  20. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
  21. Beta-1,3-galactosyltransferase 5
  22. GPI mannosyltransferase 3
  23. Phosphatidylinositol-glycan biosynthesis class F protein
  24. GPI ethanolamine phosphate transferase 2
  25. GPI ethanolamine phosphate transferase 1
  26. GPI ethanolamine phosphate transferase 3
  27. GPI transamidase component PIG-S
  28. GPI transamidase component PIG-T precursor
  29. Phosphatidylinositol glycan anchor biosynthesis class U protein
  30. GPI mannosyltransferase 2
  31. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
  32. Pleckstrin homology domain-containing family A member 8
  33. Sphingosine-1-phosphate phosphotase 2
  34. Non-lysosomal glucosylceramidase
  35. Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
  36. cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
  37. GPI-anchor transamidase
  38. Glycosylphosphatidylinositol anchor attachment 1 protein
  39. Protein PLEKHA9
  40. Glycolipid transfer protein domain-containing protein 2
  41. Putative uncharacterized protein PLEKHA8
  42. cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
  43. T-cell surface glycoprotein CD1a
  44. Glycolipid transfer protein domain-containing protein 1
  45. T-cell surface glycoprotein CD1c
  46. Lipopolysaccharide-binding protein
  47. Putative uncharacterized protein DKFZp434L0435
  48. T-cell surface glycoprotein CD1b
  49. Glycolipid transfer protein
Enzyme 1 [top]
Enzyme 1 ID 5463
Enzyme 1 Name Lipid phosphate phosphohydrolase 2
Enzyme 1 Synonyms
  1. Phosphatidic acid phosphatase 2c
  2. Phosphatidate phosphohydrolase type 2c
  3. PAP2c
  4. PAP- 2c
  5. PAP2-gamma
  6. PAP2-G
Enzyme 1 Gene Name PPAP2C
Enzyme 1 Protein Sequence >Lipid phosphate phosphohydrolase 2
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
Enzyme 1 Number of Residues 288
Enzyme 1 Molecular Weight 32574
Enzyme 1 Theoretical pI 8.44
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-30
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 3123896 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O43688 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LPP2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >867 bp
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
Enzyme 1 GenBank Gene ID AF035959 Link Image
Enzyme 1 GeneCard ID PPAP2C Link Image
Enzyme 1 GenAtlas ID PPAP2C Link Image
Enzyme 1 HGNC ID HGNC:9230 Link Image
Enzyme 1 Chromosome Location 19
Enzyme 1 Locus 19p13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  2. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5469
Enzyme 2 Name Lipid phosphate phosphohydrolase 1
Enzyme 2 Synonyms
  1. Phosphatidic acid phosphatase 2a
  2. Phosphatidate phosphohydrolase type 2a
  3. PAP2a
  4. PAP- 2a
  5. PAP2-alpha
Enzyme 2 Gene Name PPAP2A
Enzyme 2 Protein Sequence >Lipid phosphate phosphohydrolase 1
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
Enzyme 2 Number of Residues 284
Enzyme 2 Molecular Weight 32156
Enzyme 2 Theoretical pI 8.06
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-27
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2467298 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14494 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LPP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >855 bp
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
Enzyme 2 GenBank Gene ID AB000888 Link Image
Enzyme 2 GeneCard ID PPAP2A Link Image
Enzyme 2 GenAtlas ID PPAP2A Link Image
Enzyme 2 HGNC ID HGNC:9228 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q11
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed Link Image]
  2. Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed Link Image]
  3. Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed Link Image]
  4. Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5671
Enzyme 3 Name Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
Enzyme 3 Synonyms
  1. Forssman glycolipid synthetase-like protein
Enzyme 3 Gene Name GBGT1
Enzyme 3 Protein Sequence >Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQP
VVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGK
YTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETS
MRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFP
YERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESH
LNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
Enzyme 3 Number of Residues 347
Enzyme 3 Molecular Weight 40128
Enzyme 3 Theoretical pI 8.63
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Catalyzes the formation of some glycolipid via the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to some substrate. Glycolipids probably serve for adherence of some pathogens
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-21
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 6272650 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8N5D6 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GBGT1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1044 bp
ATGCATCGCCGGAGACTGGCCCTGGGTCTGGGGTTCTGCCTGTTGGCGGGCACAAGCCTC
AGTGTCCTGTGGGTGTATCTTGAGAACTGGCTGCCAGTCTCCTATGTCCCCTATTATCTC
CCCTGCCCAGAGATCTTCAACATGAAGCTGCACTACAAGAGGGAGAAGCCACTCCAGCCC
GTGGTATGGTCACAGTACCCTCAGCCCAAGCTGCTGGAGCACAGGCCCACACAGCTGCTG
ACACTCACACCCTGGTTGGCGCCCATCGTCTCCGAGGGAACCTTCAACCCAGAGCTTCTG
CAGCACATCTACCAGCCACTGAACCTGACCATTGGGGTCACGGTGTTTGCCGTGGGGAAG
TACACTCATTTCATCCAGTCCTTCCTGGAGTCAGCCGAGGAGTTCTTCATGCGTGGGTAC
CGGGTGCACTACTACATCTTCACTGACAACCCTGCAGCCGTTCCCGGGGTCCCGCTGGGT
CCCCACCAGCTTCTCAGCTCCATCCCCATCCAGGGTCACTCCCACTGGGAGGAGACATCC
ATGCGCCGGATGGAGACCATCAGCCAGCACATTGCTAAGAGGGCTCACCGGGAGGTGGAC
TACTTTTTCTGCCTTGATGTGGACATGGTGTTTCGGAACCCGTGGGGCCCTGAGACCTTG
GGAGACCTGGTGGCTGCCATTCACCCAAGCTACTACGCCGTTCCCCGCCAGCAGTTCCCC
TATGAGCGCAGGCGTGTTTCCACTGCCTTTGTGGCAGACAGGGAAGGGGACTTCTATTAT
GGTGGGGCAGTCTTCGGGGGGCAGGTGGCCAGGGTATATGAGTTTACTAGGGGCTGCCAC
ATGGCCATCCTGGCGGACAAGGCCAATGGCATCATGGCTGCCTGGCGGGAGGAAAGCCAC
CTGAACCGTCACTTCATCTCAAACAAGCCGTCCAAGGTGCTGTCCCCCGAGTACCTCTGG
GACGACAGGAAGCCCCAGCCACCCAGCCTGAAGCTGATCCGCTTTTCTACACTGGACAAG
GATATCAGCTGCCTGAGGAGCTGA
Enzyme 3 GenBank Gene ID AF163572 Link Image
Enzyme 3 GeneCard ID GBGT1 Link Image
Enzyme 3 GenAtlas ID GBGT1 Link Image
Enzyme 3 HGNC ID HGNC:20460 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Xu H, Storch T, Yu M, Elliott SP, Haslam DB: Characterization of the human Forssman synthetase gene. An evolving association between glycolipid synthesis and host-microbial interactions. J Biol Chem. 1999 Oct 8;274(41):29390-8. [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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5829
Enzyme 4 Name N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Enzyme 4 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class L protein
  2. PIG-L
Enzyme 4 Gene Name PIGL
Enzyme 4 Protein Sequence >N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
Enzyme 4 Number of Residues 252
Enzyme 4 Molecular Weight 28532
Enzyme 4 Theoretical pI 8.23
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • 6-(N-acetyl-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-17
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 4239986 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9Y2B2 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PIGL_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
Enzyme 4 GenBank Gene ID AB017165 Link Image
Enzyme 4 GeneCard ID PIGL Link Image
Enzyme 4 GenAtlas ID PIGL Link Image
Enzyme 4 HGNC ID HGNC:8966 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17p12-p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem J. 1999 Apr 1;339 ( Pt 1):185-92. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6228
Enzyme 5 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
Enzyme 5 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class Q protein
  2. PIG-Q
  3. N-acetylglucosamyl transferase component GPI1
Enzyme 5 Gene Name PIGQ
Enzyme 5 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL
Enzyme 5 Number of Residues 760
Enzyme 5 Molecular Weight 84083
Enzyme 5 Theoretical pI 8.08
Enzyme 5 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 278-298 349-371 378-400 446-468 475-497
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 2623158 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9BRB3 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PIGQ_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1746 bp
ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGGCGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGTCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTGGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGCTGGCGTGAAGTTCCGTGTCCTCCGGCAC
GAGGCCAGCAGGCCCCTCCGCCTCCTGATGCAGATAAACCCACTGCCCTACAGCCGCGTG
GTGCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTG
TGCCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAG
GACTGA
Enzyme 5 GenBank Gene ID AF030177 Link Image
Enzyme 5 GeneCard ID PIGQ Link Image
Enzyme 5 GenAtlas ID PIGQ Link Image
Enzyme 5 HGNC ID HGNC:14135 Link Image
Enzyme 5 Chromosome Location 16
Enzyme 5 Locus 16p13.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE: Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants. Biochem J. 1998 Sep 15;334 ( Pt 3):609-16. [PubMed Link Image]
  2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6229
Enzyme 6 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 6 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol- glycan biosynthesis class A protein
  3. PIG-A
Enzyme 6 Gene Name PIGA
Enzyme 6 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 6 Number of Residues 484
Enzyme 6 Molecular Weight 54127
Enzyme 6 Theoretical pI 8.41
Enzyme 6 GO Classification
Function
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Cell wall/membrane/envelope biogenesis
Enzyme 6 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 422-442
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 219994 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1455 bp
ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG
Enzyme 6 GenBank Gene ID D11466 Link Image
Enzyme 6 GeneCard ID PIGA Link Image
Enzyme 6 GenAtlas ID PIGA Link Image
Enzyme 6 HGNC ID HGNC:8957 Link Image
Enzyme 6 Chromosome Location X
Enzyme 6 Locus Xp22.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed Link Image]
  2. Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed Link Image]
  3. Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed Link Image]
  4. Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed Link Image]
  5. Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed Link Image]
  6. Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed Link Image]
  7. Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed Link Image]
  8. Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed Link Image]
  9. Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6230
Enzyme 7 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
Enzyme 7 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class H protein
  2. PIG-H
Enzyme 7 Gene Name PIGH
Enzyme 7 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP
Enzyme 7 Number of Residues 188
Enzyme 7 Molecular Weight 21081
Enzyme 7 Theoretical pI 6.72
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 36-58
  • 63-83
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 404726 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q14442 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PIGH_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >567 bp
ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA
Enzyme 7 GenBank Gene ID L19783 Link Image
Enzyme 7 GeneCard ID PIGH Link Image
Enzyme 7 GenAtlas ID PIGH Link Image
Enzyme 7 HGNC ID HGNC:8964 Link Image
Enzyme 7 Chromosome Location 14
Enzyme 7 Locus 14q11-q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Kamitani T, Chang HM, Rollins C, Waneck GL, Yeh ET: Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone. J Biol Chem. 1993 Oct 5;268(28):20733-6. [PubMed Link Image]
  2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6231
Enzyme 8 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
Enzyme 8 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class P protein
  2. PIG-P
  3. Down syndrome critical region protein 5
  4. Down syndrome critical region protein C
Enzyme 8 Gene Name PIGP
Enzyme 8 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
MVPRSTSLTLIVFLFHRLSKAPGKMVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFI
PESWLNSLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNYAK
NQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN
Enzyme 8 Number of Residues 158
Enzyme 8 Molecular Weight 18089
Enzyme 8 Theoretical pI 9.20
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-23
Enzyme 8 Transmembrane Regions
  • 40-60 80-100
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 8698815 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P57054 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PIGP_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >405 bp
ATGGTGGAAAATTCACCGTCGCCATTGCCAGAAAGAGCGATTTATGGCTTTGTTCTTTTC
TTAAGCTCCCAATTTGGCTTCATACTTTACCTCGTGTGGGCCTTTATTCCTGAATCTTGG
CTAAACTCTTTAGGTTTAACCTATTGGCCTCAAAAATATTGGGCAGTTGCATTACCTGTC
TACCTCCTTATTGCTATAGTAATTGGCTACGTGCTCTTGTTTGGGATTAACATGATGAGT
ACCTCTCCACTCGACTCCATCCATACAATCACAGATAACTATGCAAAAAATCAACAGCAG
AAGAAATACCAAGAGGAGGCCATTCCAGCCTTAAGAGATATTTCTATTAGTGAAGTAAAC
CAAATGTTCTTTCTTGCAGCCAAAGAACTTTACACCAAAAACTGA
Enzyme 8 GenBank Gene ID AB037162 Link Image
Enzyme 8 GeneCard ID PIGP Link Image
Enzyme 8 GenAtlas ID PIGP Link Image
Enzyme 8 HGNC ID HGNC:3046 Link Image
Enzyme 8 Chromosome Location 21
Enzyme 8 Locus 21q22.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Shibuya K, Kudoh J, Minoshima S, Kawasaki K, Asakawa S, Shimizu N: Isolation of two novel genes, DSCR5 and DSCR6, from Down syndrome critical region on human chromosome 21q22.2. Biochem Biophys Res Commun. 2000 May 19;271(3):693-8. [PubMed Link Image]
  2. Togashi T, Choi DK, Taylor TD, Suzuki Y, Sugano S, Hattori M, Sakaki Y: A novel gene, DSCR5, from the distal Down syndrome critical region on chromosome 21q22.2. DNA Res. 2000 Jun 30;7(3):207-12. [PubMed Link Image]
  3. Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed Link Image]
  4. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6232
Enzyme 9 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
Enzyme 9 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class C protein
  2. PIG-C
Enzyme 9 Gene Name PIGC
Enzyme 9 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
Enzyme 9 Number of Residues 297
Enzyme 9 Molecular Weight 33583
Enzyme 9 Theoretical pI 8.55
Enzyme 9 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • 51-71 80-100 154-174 239-259
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1620890 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q92535 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PIGC_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >894 bp
ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTCCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA
Enzyme 9 GenBank Gene ID D85418 Link Image
Enzyme 9 GeneCard ID PIGC Link Image
Enzyme 9 GenAtlas ID PIGC Link Image
Enzyme 9 HGNC ID HGNC:8960 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1q23-q25
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Inoue N, Watanabe R, Takeda J, Kinoshita T: PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2. Biochem Biophys Res Commun. 1996 Sep 4;226(1):193-9. [PubMed Link Image]
  2. Hong Y, Ohishi K, Inoue N, Endo Y, Fujita T, Takeda J, Kinoshita T: Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1. Genomics. 1997 Sep 15;44(3):347-9. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6371
Enzyme 10 Name Sphingosine kinase 1
Enzyme 10 Synonyms
  1. SK 1
  2. SPK 1
Enzyme 10 Gene Name SPHK1
Enzyme 10 Protein Sequence >Sphingosine kinase 1
MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHA
RELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASL
NHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLE
SEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVP
LEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLL
RLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFW
MVSGCVEPPPSWKPQQMPPPEEPL
Enzyme 10 Number of Residues 384
Enzyme 10 Molecular Weight 42518
Enzyme 10 Theoretical pI 7.13
Enzyme 10 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • protein kinase C activation
  • signal transduction
Component
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol
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 8133100 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9NYA1 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name SPHK1_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1155 bp
ATGGATCCAGCGGGCGGCCCCCGGGGCGTGCTCCCGCGGCCCTGCCGCGTGCTGGTGCTG
CTGAACCCGCGCGGCGGCAAGGGCAAGGCCTTGCAGCTCTTCCGGAGTCACGTGCAGCCC
CTTTTGGCTGAGGCTGAAATCTCCTTCACGCTGATGCTCACTGAGCGGCGGAACCACGCG
CGGGAGCTGGTGCGGTCGGAGGAGCTGGGCCGCTGGGACGCTCTGGTGGTCATGTCTGGA
GACGGGCTGATGCACGAGGTGGTGAACGGGCTCATGGAGCGGCCTGACTGGGAGACCGCC
ATCCAGAAGCCCCTGTGTAGCCTCCCAGCAGGCTCTGGCAACGCGCTGGCAGCTTCCTTG
AACCATTATGCTGGCTATGAGCAGGTCACCAATGAAGACCTCCTGACCAACTGCACGCTA
TTGCTGTGCCGCCGGCTGCTGTCACCCATGAACCTGCTGTCTCTGCACACGGCTTCGGGG
CTGCGCCTCTTCTCTGTGCTCAGCCTGGCCTGGGGCTTCATTGCTGATGTGGACCTAGAG
AGTGAGAAGTATCGGCGTCTGGGGGAGATGCGCTTCACTCTGGGCACCTTCCTGCGTCTG
GCAGCCCTGCGCACCTACCGCGGCCGACTGGCCTACCTCCCTGTAGGAAGAGTGGGTTCC
AAGACACCTGCCTCCCCCGTTGTGGTCCAGCAGGGCCCGGTAGATGCACACCTTGTGCCA
CTGGAGGAGCCAGTGCCCTCTCACTGGACAGTGGTGCCCGACGAGGACTTTGTGCTAGTC
CTGGCACTGCTGCACTCGCACCTGGGCAGTGAGATGTTTGCTGCACCCATGGGCCGCTGT
GCAGCTGGCGTCATGCATCTGTTCTACGTGCGGGCGGGAGTGTCTCGTGCCATGCTGCTG
CGCCTCTTCCTGGCCATGGAGAAGGGCAGGCATATGGAGTATGAATGCCCCTACTTGGTA
TATGTGCCCGTGGTCGCCTTCCGCTTGGAGCCCAAGGATGGGAAAGGTGTGTTTGCAGTG
GATGGGGAATTGATGGTTAGCGAGGCCGTGCAGGGCCAGGTGCACCCAAACTACTTCTGG
ATGGTCAGCGGTTGCGTGGAGCCCCCGCCCAGCTGGAAGCCCCAGCAGATGCCACCGCCA
GAAGAGCCCTTATGA
Enzyme 10 GenBank Gene ID AF266756 Link Image
Enzyme 10 GeneCard ID SPHK1 Link Image
Enzyme 10 GenAtlas ID SPHK1 Link Image
Enzyme 10 HGNC ID HGNC:11240 Link Image
Enzyme 10 Chromosome Location 17
Enzyme 10 Locus 17q25.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Melendez AJ, Carlos-Dias E, Gosink M, Allen JM, Takacs L: Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution. Gene. 2000 Jun 13;251(1):19-26. [PubMed Link Image]
  2. Nava VE, Lacana E, Poulton S, Liu H, Sugiura M, Kono K, Milstien S, Kohama T, Spiegel S: Functional characterization of human sphingosine kinase-1. FEBS Lett. 2000 May 4;473(1):81-4. [PubMed Link Image]
  3. Pitson SM, D'andrea RJ, Vandeleur L, Moretti PA, Xia P, Gamble JR, Vadas MA, Wattenberg BW: Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes. Biochem J. 2000 Sep 1;350 Pt 2:429-41. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6372
Enzyme 11 Name Sphingosine kinase 2
Enzyme 11 Synonyms
  1. SK 2
  2. SPK 2
Enzyme 11 Gene Name SPHK2
Enzyme 11 Protein Sequence >Sphingosine kinase 2
MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPA
RGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTY
PRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRP
PRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDG
IVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDL
LLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTL
GTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSV
SDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKA
ALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVL
MLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQL
GYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIGTLLTGPPGCPGREP
Enzyme 11 Number of Residues 654
Enzyme 11 Molecular Weight 69218
Enzyme 11 Theoretical pI 6.94
Enzyme 11 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • protein kinase C activation
  • signal transduction
Component
Enzyme 11 General Function Lipid transport and metabolism
Enzyme 11 Specific Function Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro- dihydrosphingosine, D-erythro-sphingosine and L-threo- dihydrosphingosine
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 8248285 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9NRA0 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name SPHK2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1857 bp
ATGGCCCCGCCCCCACCGCCACTGGCTGCCAGCACCCCGCTCCTCCATGGCGAGTTTGGC
TCCTACCCAGCCCGAGGCCCACGCTTTGCCCTCACCCTTACATCGCAGGCCCTGCACATA
CAGCGGCTGCGCCCCAAACCTGAAGCCAGGCCCCGGGGTGGCCTGGTCCCGTTGGCCGAG
GTCTCAGGCTGCTGCACCCTGCGAAGCCGCAGCCCCTCAGACTCAGCGGCCTACTTCTGC
ATCTACACCTACCCTCGGGGCCGGCGCGGGGCCCGGCGCAGAGCCACTCGCACCTTCCGG
GCAGATGGGGCCGCCACCTACGAAGAGAACCGTGCCGAGGCCCAGCGCTGGGCCACTGCC
CTCACCTGTCTGCTCCGAGGACTGCCACTGCCCGGGGATGGGGAGATCACCCCTGACCTG
CTACCTCGGCCGCCCCGGTTGCTTCTATTGGTCAATCCCTTTGGGGGTCGGGGCCTGGCC
TGGCAGTGGTGTAAGAACCACGTGCTTCCCATGATCTCTGAAGCTGGGCTGTCCTTCAAC
CTCATCCAGACAGAACGACAGAACCACGCCCGGGAGCTGGTCCAGGGGCTGAGCCTGAGT
GAGTGGGATGGCATCGTCACGGTCTCGGGAGACGGGCTGCTCCATGAGGTGCTGAACGGG
CTCCTAGATCGCCCTGACTGGGAGGAAGCTGTGAAGATGCCTGTGGGCATCCTCCCCTGC
GGCTCGGGCAACGCGCTGGCCGGAGCAGTGAACCAGCACGGGGGATTTGAGCCAGCCCTG
GGCCTCGACCTGTTGCTCAACTGCTCACTGTTGCTGTGCCGGGGTGGTGGCCACCCACTG
GACCTGCTCTCCGTGACGCTGGCCTCGGGCTCCCGCTGTTTCTCCTTCCTGTCTGTGGCC
TGGGGCTTCGTGTCAGATGTGGATATCCAGAGCGAGCGCTTCAGGGCCTTGGGCAGTGCC
CGCTTCACACTGGGCACGGTGCTGGGCCTCGCCACACTGCACACCTACCGCGGACGCCTC
TCCTACCTCCCCGCCACTGTGGAACCTGCCTCGCCCACCCCTGCCCATAGCCTGCCTCGT
GCCAAGTCGGAGCTGACCCTAACCCCAGACCCAGCCCCGCCCATGGCCCACTCACCCCTG
CATCGTTCTGTGTCTGACCTGCCTCTTCCCCTGCCCCAGCCTGCCCTGGCCTCTCCTGGC
TCGCCAGAACCCCTGCCCATCCTGTCCCTCAACGGTGGGGGCCCAGAGCTGGCTGGGGAC
TGGGGTGGGGCTGGGGATGCTCCGCTGTCCCCGGACCCACTGCTGTCTTCACCTCCTGGC
TCTCCCAAGGCAGCTCTACACTCACCCGTCTCCGAAGGGGCCCCCGTAATTCCCCCATCC
TCTGGGCTCCCACTTCCCACCCCTGATGCCCGGGTAGGGGCCTCCACCTGCGGCCCGCCC
GACCACCTGCTGCCTCCGCTGGGCACCCCGCTGCCCCCAGACTGGGTGACGCTGGAGGGG
GACTTTGTGCTCATGTTGGCCATCTCGCCCAGCCACCTAGGCGCTGACCTGGTGGCAGCT
CCGCATGCGCGCTTCGACGACGGCCTGGTGCACCTGTGCTGGGTGCGTAGCGGCATCTCG
CGGGCTGCGCTGCTGCGCCTTTTCTTGGCCATGGAGCGTGGTAGCCACTTCAGCCTGGGC
TGTCCGCAGCTGGGCTACGCCGCGGCCCGTGCCTTCCGCCTAGAGCCGCTCACACCACGC
GGCGTGCTCACAGTGGACGGGGAGCAGGTGGAGTATGGGCCGCTACAGGCACAGATGCAC
CCTGGCATCGGTACACTGCTCACTGGGCCTCCTGGCTGCCCGGGGCGGGAGCCCTGA
Enzyme 11 GenBank Gene ID AF245447 Link Image
Enzyme 11 GeneCard ID SPHK2 Link Image
Enzyme 11 GenAtlas ID SPHK2 Link Image
Enzyme 11 HGNC ID HGNC:18859 Link Image
Enzyme 11 Chromosome Location 19
Enzyme 11 Locus 19q13.2
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Liu H, Sugiura M, Nava VE, Edsall LC, Kono K, Poulton S, Milstien S, Kohama T, Spiegel S: Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. J Biol Chem. 2000 Jun 30;275(26):19513-20. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 7061
Enzyme 12 Name Ganglioside GM2 activator precursor
Enzyme 12 Synonyms
  1. GM2-AP
  2. Cerebroside sulfate activator protein
  3. Shingolipid activator protein 3
  4. SAP-3[Contains: Ganglioside GM2 activator isoform short]
Enzyme 12 Gene Name GM2A
Enzyme 12 Protein Sequence >Ganglioside GM2 activator precursor
MQSLMQAPLLIALGLLLATPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIVV
PGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIP
TGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKR
LGCIKIAASLKGI
Enzyme 12 Number of Residues 193
Enzyme 12 Molecular Weight 20822
Enzyme 12 Theoretical pI 4.96
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function Not Available
Enzyme 12 Signals
  • 1-23
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 183357 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P17900 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name SAP3_HUMAN Link Image
Enzyme 12 PDB ID 1PU5 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >582 bp
ATGCAGTCCCTGATGCAGGCTCCCCTCCTGATCGCCCTGGGCTTGCTTCTCGCGGCCCCT
GCGCAAGCCCACCTGAAAAAGCCATCCCAGCTCAGTAGCTTTTCCTGGGATAACTGTGAT
GAAGGGAAGGACCCTGCGGTGATCAGAAGCCTGACTCTGGAGCCTGACCCCATCGTCGTT
CCTGGAAATGTGACCCTCAGTGTCGTGGGCAGCACCAGTGTCCCCCTGAGTTCTCCTCTG
AAGGTGGATTTAGTTTTGGAGAAGGAGGTGGCTGGCCTCTGGATCAAGATCCCATGCACA
GACTACATTGGCAGCTGTACCTTTGAACACTTCTGTGATGTGCTTGACATGTTAATTCCT
ACTGGGGAGCCCTGCCCAGAGCCCCTGCGTACCTATGGGCTTCCTTGCCACTGTCCCTTC
AAAGAAGGAACCTACTCACTGCCCAAGAGCGAATTCGTTGTGCCTGACCTGGAGCTGCCC
AGTTGGCTCACCACCGGGAACTACCGCATAGAGAGCGTCCTGAGCAGCAGTGGGAAGCGT
CTGGGCTGCATCAAGATCGCTGCCTCTCTAAAGGGCATATAA
Enzyme 12 GenBank Gene ID M76477 Link Image
Enzyme 12 GeneCard ID GM2A Link Image
Enzyme 12 GenAtlas ID GM2A Link Image
Enzyme 12 HGNC ID HGNC:4367 Link Image
Enzyme 12 Chromosome Location 5
Enzyme 12 Locus 5q31.3-q33.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Xie B, McInnes B, Neote K, Lamhonwah AM, Mahuran D: Isolation and expression of a full-length cDNA encoding the human GM2 activator protein. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1217-23. [PubMed Link Image]
  2. Klima H, Tanaka A, Schnabel D, Nakano T, Schroder M, Suzuki K, Sandhoff K: Characterization of full-length cDNAs and the gene coding for the human GM2 activator protein. FEBS Lett. 1991 Sep 9;289(2):260-4. [PubMed Link Image]
  3. Nagarajan S, Chen HC, Li SC, Li YT, Lockyer JM: Evidence for two cDNA clones encoding human GM2-activator protein. Biochem J. 1992 Mar 15;282 ( Pt 3):807-13. [PubMed Link Image]
  4. Xie B, Kennedy JL, McInnes B, Auger D, Mahuran D: Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5. Genomics. 1992 Nov;14(3):796-8. [PubMed Link Image]
  5. Chen B, Rigat B, Curry C, Mahuran DJ: Structure of the GM2A gene: identification of an exon 2 nonsense mutation and a naturally occurring transcript with an in-frame deletion of exon 2. Am J Hum Genet. 1999 Jul;65(1):77-87. [PubMed Link Image]
  6. Schroder M, Klima H, Nakano T, Kwon H, Quintern LE, Gartner S, Suzuki K, Sandhoff K: Isolation of a cDNA encoding the human GM2 activator protein. FEBS Lett. 1989 Jul 17;251(1-2):197-200. [PubMed Link Image]
  7. Furst W, Schubert J, Machleidt W, Meyer HE, Sandhoff K: The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein. Eur J Biochem. 1990 Sep 24;192(3):709-14. [PubMed Link Image]
  8. Wright CS, Li SC, Rastinejad F: Crystal structure of human GM2-activator protein with a novel beta-cup topology. J Mol Biol. 2000 Dec 1;304(3):411-22. [PubMed Link Image]
  9. Schroder M, Schnabel D, Suzuki K, Sandhoff K: A mutation in the gene of a glycolipid-binding protein (GM2 activator) that causes GM2-gangliosidosis variant AB. FEBS Lett. 1991 Sep 23;290(1-2):1-3. [PubMed Link Image]
  10. Schroder M, Schnabel D, Hurwitz R, Young E, Suzuki K, Sandhoff K: Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation and expression in BHK cells. Hum Genet. 1993 Nov;92(5):437-40. [PubMed Link Image]
  11. Schepers U, Glombitza G, Lemm T, Hoffmann A, Chabas A, Ozand P, Sandhoff K: Molecular analysis of a GM2-activator deficiency in two patients with GM2-gangliosidosis AB variant. Am J Hum Genet. 1996 Nov;59(5):1048-56. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 7905
Enzyme 13 Name T-cell surface glycoprotein CD1e precursor
Enzyme 13 Synonyms
  1. CD1e antigen
  2. R2G1
Enzyme 13 Gene Name CD1E
Enzyme 13 Protein Sequence >T-cell surface glycoprotein CD1e precursor
MLLLFLLFEGLCCPGENTAAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTV
LGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYPFEIQILAGCR
MNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTC
PRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQE
QRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIHWGGYSIFLIL
ICLTVIVTLVILVVVDSRLKKQ
Enzyme 13 Number of Residues 322
Enzyme 13 Molecular Weight 35986
Enzyme 13 Theoretical pI 7.25
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-19
Enzyme 13 Transmembrane Regions
  • 295-315
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 296640 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P15812 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name CD1E_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >972 bp
ATGCTGCTCCTGTTCCTCCTCTTCGAGGGTCTCTGCTGTCCTGGGGAAAATACAGCAGCA
GCAGAGGAGCAGCTGTCCTTCCGCATGCTCCAAACTTCCTCCTTTGCCAACCACAGCTGG
GCACACAGTGAGGGCTCAGGATGGCTGGGTGACCTGCAGACTCATGGCTGGGACACTGTC
TTGGGCACCATCCGCTTTCTGAAGCCCTGGTCCCATGGAAACTTCAGCAAGCAGGAGCTG
AAAAACTTACAGTCACTGTTCCAGTTATACTTCCATAGTTTTATCCAGATAGTGCAAGCT
TCTGCTGGTCAATTTCAGCTTGAATACCCCTTCGAGATCCAGATATTAGCTGGCTGTAGA
ATGAATGCCCCACAAATCTTCTTAAATATGGCATATCAAGGGTCAGATTTCCTGAGTTTC
CAAGGAATTTCCTGGGAGCCATCTCCAGGAGCAGGGATCCGGGCCCAGAACATCTGTAAA
GTGCTCAATCGCTACCTAGATATTAAGGAAATACTGCAAAGCCTTCTTGGTCACACCTGC
CCTCGATTTCTAGCGGGGCTCATGGAAGCAGGGGAGTCAGAACTGAAACGGAAAGTGAAG
CCAGAGGCCTGGCTGTCCTGTGGCCCCAGTCCTGGCCCTGGCCGTCTGCAGCTTGTGTGC
CATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGTGAGCAGGAG
CAGCGGGGCACTCAGCGAGGGGACGTCCTGCCTAATGCTGACGAGACATGGTATCTCCGA
GCAACCCTGGATGTGGCGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGGGTGAAACACAGC
AGTCTAGGGGGCCATGATCTAATCATCCATTGGGGTGGATATTCCATCTTTCTCATCCTG
ATCTGTTTGACTGTGATAGTTACCCTGGTCATATTGGTTGTAGTTGACTCACGGTTAAAA
AAACAGAGGTGA
Enzyme 13 GenBank Gene ID X14975 Link Image
Enzyme 13 GeneCard ID CD1E Link Image
Enzyme 13 GenAtlas ID CD1E Link Image
Enzyme 13 HGNC ID HGNC:1638 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1q22-q23
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Calabi F, Jarvis JM, Martin L, Milstein C: Two classes of CD1 genes. Eur J Immunol. 1989 Feb;19(2):285-92. [PubMed Link Image]
  2. Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed Link Image]
  3. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed Link Image]
  4. Mirones I, Oteo M, Parra-Cuadrado JF, Martinez-Naves E: Identification of two novel human CD1E alleles. Tissue Antigens. 2000 Aug;56(2):159-61. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 8178
Enzyme 14 Name Epididymal secretory protein E1 precursor
Enzyme 14 Synonyms
  1. Niemann-Pick disease type C2 protein
  2. hE1
Enzyme 14 Gene Name NPC2
Enzyme 14 Protein Sequence >Epididymal secretory protein E1 precursor
MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVT
FTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYP
SIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL
Enzyme 14 Number of Residues 151
Enzyme 14 Molecular Weight 16570
Enzyme 14 Theoretical pI 7.77
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function May be involved in the regulation of the lipid composition of sperm membranes during the maturation in the epididymis
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-19
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 37477 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P61916 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name NPC2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >456 bp
ATGCGTTTCCTGGCAGCTACATTCCTGCTCCTGGCGCTCAGCACCGCTGCCCAGGCCGAA
CCGGTGCAGTTCAAGGACTGCGGTTCTGTGGATGGAGTTATAAAGGAAGTGAATGTGAGC
CCATGCCCCACCCAACCCTGCCAGCTGAGCAAAGGACAGTCTTACAGCGTCAATGTCACC
TTCACCAGCAATATTCAGTCTAAAAGCAGCAAGGCCGTGGTGCATGGCATCCTGATGGGC
GTCCCAGTTCCCTTTCCCATTCCTGAGCCTGATGGTTGTAAGAGTGGAATTAACTGCCCT
ATCCAAAAAGACAAGACCTATAGCTACCTGAATAAACTACCAGTGAAAAGCGAATATCCC
TCTATAAAACTGGTGGTGGAGTGGCAACTTCAGGATGACAAAAACCAAAGTCTCTTCTGC
TGGGAAATCCCAGTACAGATCGTTTCTCATCTCTAA
Enzyme 14 GenBank Gene ID X67698 Link Image
Enzyme 14 GeneCard ID NPC2 Link Image
Enzyme 14 GenAtlas ID NPC2 Link Image
Enzyme 14 HGNC ID HGNC:14537 Link Image
Enzyme 14 Chromosome Location 14
Enzyme 14 Locus 14q24.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Krull N, Ivell R, Osterhoff C, Kirchhoff C: Region-specific variation of gene expression in the human epididymis as revealed by in situ hybridization with tissue-specific cDNAs. Mol Reprod Dev. 1993 Jan;34(1):16-24. [PubMed Link Image]
  2. Naureckiene S, Sleat DE, Lackland H, Fensom A, Vanier MT, Wattiaux R, Jadot M, Lobel P: Identification of HE1 as the second gene of Niemann-Pick C disease. Science. 2000 Dec 22;290(5500):2298-301. [PubMed Link Image]
  3. Millat G, Chikh K, Naureckiene S, Sleat DE, Fensom AH, Higaki K, Elleder M, Lobel P, Vanier MT: Niemann-Pick disease type C: spectrum of HE1 mutations and genotype/phenotype correlations in the NPC2 group. Am J Hum Genet. 2001 Nov;69(5):1013-21. Epub 2001 Sep 20. [PubMed Link Image]
  4. Klunemann HH, Elleder M, Kaminski WE, Snow K, Peyser JM, O'Brien JF, Munoz D, Schmitz G, Klein HE, Pendlebury WW: Frontal lobe atrophy due to a mutation in the cholesterol binding protein HE1/NPC2. Ann Neurol. 2002 Dec;52(6):743-9. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8289
Enzyme 15 Name T-cell surface glycoprotein CD1d precursor
Enzyme 15 Synonyms
  1. CD1d antigen
  2. R3G1
Enzyme 15 Gene Name CD1D
Enzyme 15 Protein Sequence >T-cell surface glycoprotein CD1d precursor
MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSN
DSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGC
EVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLL
NGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMR
GEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYT
SMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL
Enzyme 15 Number of Residues 335
Enzyme 15 Molecular Weight 37718
Enzyme 15 Theoretical pI 8.28
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Not known
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-19
Enzyme 15 Transmembrane Regions
  • 302-322
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 619798 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P15813 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name CD1D_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1008 bp
ATGGGGTGCCTGCTGTTTCTGCTGCTCTGGGCGCTCCTCCAGGCTTGGGGAAGCGCTGAA
GTCCCGCAAAGGCTTTTCCCCCTCCGCTGCCTCCAGATCTCGTCCTTCGCCAATAGCAGC
TGGACGCGCACCGACGGCTTGGCGTGGCTGGGGGAGCTGCAGACGCACAGCTGGAGCAAC
GACTCGGACACCGTCCGCTCTCTGAAGCCTTGGTCCCAGGGCACGTTCAGCGACCAGCAG
TGGGAGACGCTGCAGCATATATTTCGGGTTTATCGAAGCAGCTTCACCAGGGACGTGAAG
GAATTCGCCAAAATGCTACGCTTATCCTATCCCTTGGAGCTCCAGGTGTCCGCTGGCTGT
GAGGTGCACCCTGGGAACGCCTCAAATAACTTCTTCCATGTAGCATTTCAAGGAAAAGAT
ATCCTGAGTTTCCAAGGAACTTCTTGGGAGCCAACCCAAGAGGCCCCACTTTGGGTAAAC
TTGGCCATTCAAGTGCTCAACCAGGACAAGTGGACGAGGGAAACAGTGCAGTGGCTCCTT
AATGGCACCTGCCCCCAATTTGTCAGTGGCCTCCTTGAGTCAGGGAAGTCGGAACTGAAG
AAGCAAGTGAAGCCCAAGGCCTGGCTGTCCCGTGGCCCCAGTCCTGGCCCTGGCCGTCTG
CTGCTGGTGTGCCATGTCTCAGGATTCTACCCAAAGCCTGTATGGGTGAAGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCCAGGGGACATCCTGCCCAATGCTGACGAGACA
TGGTATCTCCGAGCAACCCTGGATGTGGTGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGGTGGGAGCTACACC
TCCATGGGCTTGATTGCCTTGGCAGTCCTGGCGTGCTTGCTGTTCCTCCTCATTGTGGGC
TTTACCTCCCGGTTTAAGAGGCAAACTTCCTATCAGGGCGTCCTGTGA
Enzyme 15 GenBank Gene ID L38820 Link Image
Enzyme 15 GeneCard ID CD1D Link Image
Enzyme 15 GenAtlas ID CD1D Link Image
Enzyme 15 HGNC ID HGNC:1637 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1q22-q23
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Calabi F, Jarvis JM, Martin L, Milstein C: Two classes of CD1 genes. Eur J Immunol. 1989 Feb;19(2):285-92. [PubMed Link Image]
  2. Balk SP, Bleicher PA, Terhorst C: Isolation and characterization of a cDNA and gene coding for a fourth CD1 molecule. Proc Natl Acad Sci U S A. 1989 Jan;86(1):252-6. [PubMed Link Image]
  3. Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed Link Image]
  4. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8469
Enzyme 16 Name GPI mannosyltransferase 1
Enzyme 16 Synonyms
  1. GPI mannosyltransferase I
  2. GPI-MT-I
  3. Phosphatidylinositol-glycan biosynthesis class M protein
  4. PIG-M
Enzyme 16 Gene Name PIGM
Enzyme 16 Protein Sequence >GPI mannosyltransferase 1
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
Enzyme 16 Number of Residues 423
Enzyme 16 Molecular Weight 49460
Enzyme 16 Theoretical pI 9.31
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-369
Enzyme 16 Transmembrane Regions
  • 18-38 80-100 139-161 170-190 226-246 288-308 315-337 339-350 358-378 385-405
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 11414879 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9H3S5 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PIGM_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1272 bp
ATGGGCTCCACCAAGCACTGGGGCGAATGGCTCCTGAACTTGAAGGTGGCTCCAGCCGGC
GTCTTTGGTGTGGCCTTTCTAGCCAGAGTCGCCCTGGTTTTCTATGGCGTCTTCCAGGAC
CGGACCCTGCACGTGAGGTATACGGACATCGACTACCAGGTCTTCACCGACGCCGCGCGC
TTCGTCACGGAGGGGCGCTCGCCTTACCTGAGAGCCACGTACCGTTACACCCCGCTGCTG
GGTTGGCTCCTCACTCCCAACATCTACCTCAGCGAGCTCTTTGGAAAGTTTCTCTTCATC
AGCTGCGACCTCCTCACCGCTTTCCTCTTATACCGCCTGCTGCTGCTGAAGGGGCTGGGG
CGCCGCCAGGCTTGTGGCTACTGTGTCTTTTGGCTTCTTAACCCCCTGCCTATGGCAGTA
TCCAGCCGCGGTAATGCGGACTCTATTGTCGCCTCCCTGGTCCTGATGGTCCTCTACTTG
ATAAAGAAAAGACTCGTCGCGTGTGCAGCTGTATTCTATGGTTTCGCGGTGCATATGAAG
ATATATCCAGTGACTTACATCCTTCCCATAACCCTCCACCTGCTTCCAGATCGCGACAAT
GACAAAAGCCTCCGTCAATTCCGGTACACTTTCCAGGCTTGTTTGTACGAGCTCCTGAAA
AGGCTGTGTAATCGGGCTGTGCTGCTGTTTGTAGCAGTTGCTGGACTCACGTTTTTTGCC
CTGAGCTTTGGTTTTTACTATGAGTACGGCTGGGAATTTTTGGAACACACCTACTTTTAT
CACCTGACTAGGCGGGATATCCGTCACAACTTTTCTCCGTACTTCTACATGCTGTATTTG
ACTGCAGAGAGCAAGTGGAGTTTTTCCCTGGGAATTGCTGCATTCCTGCCACAGCTCATC
TTGCTTTCAGCTGTGTCTTTCGCCTATTACAGAGACCTCGTTTTTTGTTGTTTTCTTCAT
ACGTCCATTTTTGTGACTTTTAACAAAGTCTGCACCTCCCAGTACTTTCTTTGGTACCTC
TGCTTACTGCCTCTTGTGATGCCACTAGTCAGAATGCCTTGGAAAAGAGCTGTAGTTCTC
CTAATGTTATGGTTTATAGGGCAGGCCATGTGGCTGGCTCCTGCCTATGTTCTAGAGTTT
CAAGGAAAGAACACCTTTCTGTTTATTTGGTTAGCTGGTTTGTTCTTTCTTCTTATCAAT
TGTTCCATCCTGATTCAAATTATTTCCCATTACAAAGAAGAACCCCTGACAGAGAGAATC
AAATATGACTAG
Enzyme 16 GenBank Gene ID AB028127 Link Image
Enzyme 16 GeneCard ID PIGM Link Image
Enzyme 16 GenAtlas ID PIGM Link Image
Enzyme 16 HGNC ID HGNC:18858 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 1q23.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Maeda Y, Watanabe R, Harris CL, Hong Y, Ohishi K, Kinoshita K, Kinoshita T: PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J. 2001 Jan 15;20(1-2):250-61. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8495
Enzyme 17 Name Phosphatidylinositol-glycan biosynthesis class W protein
Enzyme 17 Synonyms
  1. PIG-W
Enzyme 17 Gene Name PIGW
Enzyme 17 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class W protein
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
Enzyme 17 Number of Residues 504
Enzyme 17 Molecular Weight 56883
Enzyme 17 Theoretical pI 9.44
Enzyme 17 GO Classification
Function
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI- anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-43
Enzyme 17 Transmembrane Regions
  • 22-42 74-94 132-152 163-183 203-223 238-258 261-281 306-326 339-359 371-391 449-469 474-494
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID Q7Z7B1 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PIGW_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID AB097818 Link Image
Enzyme 17 GeneCard ID PIGW Link Image
Enzyme 17 GenAtlas ID PIGW Link Image
Enzyme 17 HGNC ID HGNC:23213 Link Image
Enzyme 17 Chromosome Location 17
Enzyme 17 Locus 17q12
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8621
Enzyme 18 Name Phosphatidylinositol-glycan biosynthesis class X protein precursor
Enzyme 18 Synonyms
  1. PIG-X
Enzyme 18 Gene Name PIGX
Enzyme 18 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class X protein precursor
MAARVAAVRAAAWLLLGAATGLTRGPATAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALDNEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
Enzyme 18 Number of Residues 258
Enzyme 18 Molecular Weight 28805
Enzyme 18 Theoretical pI 6.30
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Essential component of glycosylphosphatidylinositol- mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-21
Enzyme 18 Transmembrane Regions
  • 231-251
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 18490317 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q8TBF5 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PIGX_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >654 bp
ATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGACCTT
TTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACGTGCCGTCTCTTAATT
AAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGAGAG
AGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAACTAT
TTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGACTGT
TTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGAGAA
GCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCGATT
TTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGATAATGAGGATATA
TGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTTCCA
GTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATCCTG
TGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
Enzyme 18 GenBank Gene ID BC022542 Link Image
Enzyme 18 GeneCard ID PIGX Link Image
Enzyme 18 GenAtlas ID PIGX Link Image
Enzyme 18 HGNC ID HGNC:26046 Link Image
Enzyme 18 Chromosome Location 3
Enzyme 18 Locus 3q29
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 8625
Enzyme 19 Name GPI mannosyltransferase 4
Enzyme 19 Synonyms
  1. GPI mannosyltransferase IV
  2. GPI-MT-IV
  3. Phosphatidylinositol-glycan biosynthesis class Z protein
  4. PIG-Z
  5. hSMP3
Enzyme 19 Gene Name PIGZ
Enzyme 19 Protein Sequence >GPI mannosyltransferase 4
MAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCR
SVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPM
GADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRW
RSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGATLTAAV
FVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHA
QALQAAWQQLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARF
LIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVL
PSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDIGGTEDWALCQTLKSFTRQPACQVA
GGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLH
IVELGEET
Enzyme 19 Number of Residues 548
Enzyme 19 Molecular Weight 60249
Enzyme 19 Theoretical pI 8.40
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-28
Enzyme 19 Transmembrane Regions
  • 100-120 125-142 149-169 185-205 227-247 338-358
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID Q86VD9 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PIGZ_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AK022830 Link Image
Enzyme 19 GeneCard ID PIGZ Link Image
Enzyme 19 GenAtlas ID PIGZ Link Image
Enzyme 19 HGNC ID HGNC:30596 Link Image
Enzyme 19 Chromosome Location 3
Enzyme 19 Locus 3q29
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 11996
Enzyme 20 Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
Enzyme 20 Synonyms
  1. Beta3Gn-T5
  2. BGnT-5
  3. Beta-1,3-N- acetylglucosaminyltransferase-5
  4. Lactotriaosylceramide synthase
  5. Lc(3Cer synthase
  6. Lc3 synthase
Enzyme 20 Gene Name B3GNT5
Enzyme 20 Protein Sequence >UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
Enzyme 20 Number of Residues 378
Enzyme 20 Molecular Weight 44053
Enzyme 20 Theoretical pI Not Available
Enzyme 20 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • galactosyl glucosyl ceramide + UDP-N-acetyl-D-glucosamine --> (Gal)1 (Glc)1 (GlcNAc)1 (Cer)1 + H+ + UDP
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 15-35
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 13568434 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9BYG0 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name B3GN5_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AB045278 Link Image
Enzyme 20 GeneCard ID Not Available
Enzyme 20 GenAtlas ID B3GNT5 Link Image
Enzyme 20 HGNC ID HGNC:15684 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Togayachi A, Akashima T, Ookubo R, Kudo T, Nishihara S, Iwasaki H, Natsume A, Mio H, Inokuchi J, Irimura T, Sasaki K, Narimatsu H: Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids. J Biol Chem. 2001 Jun 22;276(25):22032-40. Epub 2001 Mar 30. [PubMed Link Image]
  2. Henion TR, Zhou D, Wolfer DP, Jungalwala FB, Hennet T: Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis. J Biol Chem. 2001 Aug 10;276(32):30261-9. Epub 2001 May 30. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 12558
Enzyme 21 Name Beta-1,3-galactosyltransferase 5
Enzyme 21 Synonyms
  1. Beta-1,3-GalTase 5
  2. Beta3Gal-T5
  3. b3Gal-T5
  4. UDP-galactose:beta-N-acetylglucosamine beta- 1,3-galactosyltransferase 5
  5. UDP-Gal:beta-GlcNAc beta-1,3- galactosyltransferase 5
  6. Beta-3-Gx-T5
Enzyme 21 Gene Name B3GALT5
Enzyme 21 Protein Sequence >Beta-1,3-galactosyltransferase 5
MAFPKMRLMYICLLVLGALCLYFSMYSLNPFKEQSFVYKKDGNFLKLPDTDCRQTPPFLV
LLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVDQESQRHGDII
QKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFF
TGFLKLNEFPIRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIK
LEDVFVGLCLERLNIRLEELHSQPTFFPGGLRFSVCLFRRIVACHFIKPRTLLDYWQALE
NSRGEDCPPV
Enzyme 21 Number of Residues 310
Enzyme 21 Molecular Weight 36190
Enzyme 21 Theoretical pI Not Available
Enzyme 21 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • globoside (homo sapiens) + UDPgalactose --> galactosylgloboside (homo sapiens) + H+ + UDP
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 8-28
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 4835503 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9Y2C3 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name B3GT5_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AB020337 Link Image
Enzyme 21 GeneCard ID Not Available
Enzyme 21 GenAtlas ID B3GALT5 Link Image
Enzyme 21 HGNC ID HGNC:920 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Isshiki S, Togayachi A, Kudo T, Nishihara S, Watanabe M, Kubota T, Kitajima M, Shiraishi N, Sasaki K, Andoh T, Narimatsu H: Cloning, expression, and characterization of a novel UDP-galactose:beta-N-acetylglucosamine beta1,3-galactosyltransferase (beta3Gal-T5) responsible for synthesis of type 1 chain in colorectal and pancreatic epithelia and tumor cells derived therefrom. J Biol Chem. 1999 Apr 30;274(18):12499-507. [PubMed Link Image]
  2. Zhou D, Berger EG, Hennet T: Molecular cloning of a human UDP-galactose:GlcNAcbeta1,3GalNAc beta1, 3 galactosyltransferase gene encoding an O-linked core3-elongation enzyme. Eur J Biochem. 1999 Jul;263(2):571-6. [PubMed Link Image]
  3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  4. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 12947
Enzyme 22 Name GPI mannosyltransferase 3
Enzyme 22 Synonyms
  1. GPI mannosyltransferase III
  2. GPI-MT-III
  3. Phosphatidylinositol-glycan biosynthesis class B protein
  4. PIG-B
Enzyme 22 Gene Name PIGB
Enzyme 22 Protein Sequence >GPI mannosyltransferase 3
MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGEN
IYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLI
FASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLC
SWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWT
PLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWG
TFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEF
RFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQK
VCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNP
LNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVY
ERKLKGKFNMKMKF
Enzyme 22 Number of Residues 554
Enzyme 22 Molecular Weight 65057
Enzyme 22 Theoretical pI 9.57
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 63-83 136-156 192-212 224-244 255-275 315-335 340-360 362-382 387-407
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 1552169 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q92521 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PIGB_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID D42138 Link Image
Enzyme 22 GeneCard ID Q92521 Link Image
Enzyme 22 GenAtlas ID PIGB Link Image
Enzyme 22 HGNC ID HGNC:8959 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T: PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J. 1996 Aug 15;15(16):4254-61. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 12948
Enzyme 23 Name Phosphatidylinositol-glycan biosynthesis class F protein
Enzyme 23 Synonyms
  1. PIG-F
  2. GPI11 homolog
Enzyme 23 Gene Name PIGF
Enzyme 23 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class F protein
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYL
VVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILS
TFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERP
WQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
Enzyme 23 Number of Residues 219
Enzyme 23 Molecular Weight 24890
Enzyme 23 Theoretical pI 8.64
Enzyme 23 GO Classification
Function
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 11-31 42-62 86-106 113-133 155-175 189-209
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 303616 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q07326 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PIGF_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence Not Available
Enzyme 23 GenBank Gene ID D13435 Link Image
Enzyme 23 GeneCard ID Q07326 Link Image
Enzyme 23 GenAtlas ID PIGF Link Image
Enzyme 23 HGNC ID HGNC:8962 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Inoue N, Kinoshita T, Orii T, Takeda J: Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy. J Biol Chem. 1993 Apr 5;268(10):6882-5. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 12949
Enzyme 24 Name GPI ethanolamine phosphate transferase 2
Enzyme 24 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class G protein
  2. PIG-G
  3. GPI7 homolog
  4. hGPI7
Enzyme 24 Gene Name PIGG
Enzyme 24 Protein Sequence >GPI ethanolamine phosphate transferase 2
MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTL
PPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIK
ALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGT
TSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMD
SVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP
GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSK
LLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLS
LSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVI
LVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNP
MHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLG
DDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWL
ILACCRLLRSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVS
KAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKS
QVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAA
EITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWAS
HLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGM
HLLITAAVCVFFTAMDQTRLTQS
Enzyme 24 Number of Residues 983
Enzyme 24 Molecular Weight 108174
Enzyme 24 Theoretical pI 7.15
Enzyme 24 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 432-452 471-491 506-526 552-572 699-719 721-741 752-772 789-809 812-832 879-899 919-939 955-975
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 58430451 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q5H8A4 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PIGG_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AB162713 Link Image
Enzyme 24 GeneCard ID Q5H8A4 Link Image
Enzyme 24 GenAtlas ID PIGG Link Image
Enzyme 24 HGNC ID HGNC:25985 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. 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]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 12950
Enzyme 25 Name GPI ethanolamine phosphate transferase 1
Enzyme 25 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class N protein
  2. PIG-N
  3. MCD4 homolog
Enzyme 25 Gene Name PIGN
Enzyme 25 Protein Sequence >GPI ethanolamine phosphate transferase 1
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALY
ELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENP
VEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFD
NVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKE
IVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ
FDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESM
FTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSL
CKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKP
SHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP
LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSL
LLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLST
VLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMST
YLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLY
LDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFV
LVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMS
MTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Enzyme 25 Number of Residues 931
Enzyme 25 Molecular Weight 105811
Enzyme 25 Theoretical pI 8.87
Enzyme 25 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 2-24 443-463 483-503 509-529 544-564 566-586 592-612 619-639 650-670 686-706 724-744 787-807 825-845 859-879 895-915
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 4206155 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O95427 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PIGN_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AF109219 Link Image
Enzyme 25 GeneCard ID O95427 Link Image
Enzyme 25 GenAtlas ID PIGN Link Image
Enzyme 25 HGNC ID HGNC:8967 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Gaynor EC, Mondesert G, Grimme SJ, Reed SI, Orlean P, Emr SD: MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol Biol Cell. 1999 Mar;10(3):627-48. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 12951
Enzyme 26 Name GPI ethanolamine phosphate transferase 3
Enzyme 26 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class O protein
  2. PIG-O
Enzyme 26 Gene Name PIGO
Enzyme 26 Protein Sequence >GPI ethanolamine phosphate transferase 3
MQKASVLLFLAWVCFLFYAGIALFTSGFLLTRLELTNHSSCQEPPGPGSLPWGSQGKPGA
CWMASRFSRVVLVLIDALRFDFAQPQHSHVPREPPVSLPFLGKLSSLQRILEIQPHHARL
YRSQVDPPTTTMQRLKALTTGSLPTFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDD
TWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGEWDVLIAHFLGVDHCGHK
HGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFL
YSPTAVFPSTPPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVMAELFSGGEDSQPHSSA
LAQASALHLNAQQVSRFLHTYSAATQDLQAKELHQLQNLFSKASADYQWLLQSPKGAEAT
LPTVIAELQQFLRGARAMCIESWARFSLVRMAGGTALLAASCFICLLASQWAISPGFPFC
PLLLTPVAWGLVGAIAYAGLLGTIELKLDLVLLGAVAAVSSFLPFLWKAWAGWGSKRPLA
TLFPIPGPVLLLLLFRLAVFFSDSFVVAEARATPFLLGSFILLLVVQLHWEGQLLPPKLL
TMPRLGTSATTNPPRHNGAYALRLGIGLLLCTRLAGLFHRCPEETPVCHSSPWLSPLASM
VGGRAKNLWYGACVAALVALLAAVRLWLRRYGNLKSPEPPMLFVRWGLPLMALGTAAYWA
LASGADEAPPRLRVLVSGASMVLPRAVAGLAASGLALLLWKPVTVLVKAGAGAPRTRTVL
TPFSGPPTSQADLDYVVPQIYRHMQEEFRGRLERTKSQGPLTVAAYQLGSVYSAAMVTAL
TLLAFPLLLLHAERISLVFLLLFLQSFLLLHLLAAGIPVTTPGPFTVPWQAVSAWALMAT
QTFYSTGHQPVFPAIHWHAAFVGFPEGHGSCTWLPALLVGANTFASHLLFAVGCPLLLLW
PFLCESQGLRKRQQPPGNEADARVRPEEEEEPLMEMRLRDAPQHFYAALLQLGLKYLFIL
GIQILACALAASILRRHLMVWKVFAPKFIFEAVGFIVSSVGLLLGIALVMRVDGAVSSWF
RQLFLAQQR
Enzyme 26 Number of Residues 1089
Enzyme 26 Molecular Weight 118700
Enzyme 26 Theoretical pI 8.18
Enzyme 26 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 4-24 457-477 482-502 510-530 541-561 575-595 668-688 701-721 747-767 830-850 857-877 944-964 1014-1034 1048-1068
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 21739535 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q8TEQ8 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PIGO_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AL833956 Link Image
Enzyme 26 GeneCard ID Q8TEQ8 Link Image
Enzyme 26 GenAtlas ID PIGO Link Image
Enzyme 26 HGNC ID HGNC:23215 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 12952
Enzyme 27 Name GPI transamidase component PIG-S
Enzyme 27 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class S protein
Enzyme 27 Gene Name PIGS
Enzyme 27 Protein Sequence >GPI transamidase component PIG-S
MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLR
LMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALS
SGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFN
IIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKS
HDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSL
PHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIM
VYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMT
WELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELA
SGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKI
FLETRKSWRKPEKTD
Enzyme 27 Number of Residues 555
Enzyme 27 Molecular Weight 61657
Enzyme 27 Theoretical pI 6.46
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates
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
  • 19-39 521-541
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 14456613 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q96S52 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PIGS_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AB057723 Link Image
Enzyme 27 GeneCard ID Q96S52 Link Image
Enzyme 27 GenAtlas ID PIGS Link Image
Enzyme 27 HGNC ID HGNC:14937 Link Image
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [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]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 12953
Enzyme 28 Name GPI transamidase component PIG-T precursor
Enzyme 28 Synonyms
  1. Phosphatidylinositol- glycan biosynthesis class T protein
Enzyme 28 Gene Name PIGT
Enzyme 28 Protein Sequence >GPI transamidase component PIG-T precursor
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQR
EGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTV
TDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREV
VCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQ
TLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPP
TTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSG
YGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQ
DRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVA
AKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCY
GSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
Enzyme 28 Number of Residues 578
Enzyme 28 Molecular Weight 65700
Enzyme 28 Theoretical pI 8.49
Enzyme 28 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • protein complex
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-21
Enzyme 28 Transmembrane Regions
  • 528-548
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 14456615 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q969N2 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PIGT_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 AB057724 Link Image
Enzyme 28 GeneCard ID Q969N2 Link Image
Enzyme 28 GenAtlas ID PIGT Link Image
Enzyme 28 HGNC ID HGNC:14938 Link Image
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 12954
Enzyme 29 Name Phosphatidylinositol glycan anchor biosynthesis class U protein
Enzyme 29 Synonyms
  1. GPI transamidase component PIG-U
  2. Cell division cycle protein 91-like 1
  3. Protein CDC91-like 1
Enzyme 29 Gene Name PIGU
Enzyme 29 Protein Sequence >Phosphatidylinositol glycan anchor biosynthesis class U protein
MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSG
AVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYA
PDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAF
LSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVI
ICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFY
TIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTC
IIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGL
YLTAKDGTEAMLVLK
Enzyme 29 Number of Residues 435
Enzyme 29 Molecular Weight 50052
Enzyme 29 Theoretical pI 7.82
Enzyme 29 GO Classification
Function
Process
  • GPI anchor biosynthesis
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein modification
Component
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • 66-86 166-186 188-208 237-257 259-279 286-306 313-333 355-375 386-406
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 27372217 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9H490 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PIGU_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 AB086842 Link Image
Enzyme 29 GeneCard ID Q9H490 Link Image
Enzyme 29 GenAtlas ID PIGU Link Image
Enzyme 29 HGNC ID HGNC:15791 Link Image
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 12955
Enzyme 30 Name GPI mannosyltransferase 2
Enzyme 30 Synonyms
  1. GPI mannosyltransferase II
  2. GPI-MT-II
  3. Phosphatidylinositol-glycan biosynthesis class V protein
  4. PIG-V
Enzyme 30 Gene Name PIGV
Enzyme 30 Protein Sequence >GPI mannosyltransferase 2
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLL
GGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVA
SLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSA
MGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMAS
LFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDV
PLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQR
SKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSSTPIMYWFPAHL
LQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWL
LGLLLHCNFLPWT
Enzyme 30 Number of Residues 493
Enzyme 30 Molecular Weight 55713
Enzyme 30 Theoretical pI 8.03
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 14-34 78-98 114-134 137-157 162-182 193-213 235-255 328-348 379-399 470-490
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 7020604 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9NUD9 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PIGV_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID AK000484 Link Image
Enzyme 30 GeneCard ID Q9NUD9 Link Image
Enzyme 30 GenAtlas ID PIGV Link Image
Enzyme 30 HGNC ID HGNC:26031 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 12956
Enzyme 31 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
Enzyme 31 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class Y protein
  2. PIG-Y
Enzyme 31 Gene Name PIGY
Enzyme 31 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLW
TWMGIKLFRHN
Enzyme 31 Number of Residues 71
Enzyme 31 Molecular Weight 8058
Enzyme 31 Theoretical pI 7.41
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI- anchors for cell surface proteins. May act by regulating the catalytic subunit PIGA
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function Not Available
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • 4-26 45-65
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 75674192 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q3MUY2 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PIGY_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence Not Available
Enzyme 31 GenBank Gene ID AB206972 Link Image
Enzyme 31 GeneCard ID Q3MUY2 Link Image
Enzyme 31 GenAtlas ID PIGY Link Image
Enzyme 31 HGNC ID HGNC:28213 Link Image
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 12961
Enzyme 32 Name Pleckstrin homology domain-containing family A member 8
Enzyme 32 Synonyms
  1. Phosphoinositol 4-phosphate adapter protein 2
  2. Phosphatidylinositol- four-phosphate adapter protein 2
  3. hFAPP2
  4. Serologically defined breast cancer antigen NY-BR-86
Enzyme 32 Gene Name PLEKHA8
Enzyme 32 Protein Sequence >Pleckstrin homology domain-containing family A member 8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGDHRKE
AFSIGMQRDLSLYLPAMKKQMAILDALYEVHGLESDEVV
Enzyme 32 Number of Residues 519
Enzyme 32 Molecular Weight 58307
Enzyme 32 Theoretical pI 4.89
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Involved in TGN-to-plasma membrane transport and in the formation of post-Golgi constitutive carriers. May play a role in ensuring the coordination of the budding and the fission reactions
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 14165198 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q96JA3 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PKHA8_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AF380162 Link Image
Enzyme 32 GeneCard ID Q96JA3 Link Image
Enzyme 32 GenAtlas ID PLEKHA8 Link Image
Enzyme 32 HGNC ID HGNC:30037 Link Image
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR: Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J. 2000 Oct 1;351(Pt 1):19-31. [PubMed Link Image]
  2. Scanlan MJ, Gout I, Gordon CM, Williamson B, Stockert E, Gure AO, Jager D, Chen YT, Mackay A, O'Hare MJ, Old LJ: Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression. Cancer Immun. 2001 Mar 30;1:4. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 13104
Enzyme 33 Name Sphingosine-1-phosphate phosphotase 2
Enzyme 33 Synonyms Not Available
Enzyme 33 Gene Name SGPP2
Enzyme 33 Protein Sequence >Sphingosine-1-phosphate phosphotase 2
MAELLRSLQDSQLVARFQRRCGLFPAPDEGPRENGADPTERAARVPGVEHLPAANGKGGE
APANGLRRAAAPEAYVQKYVVKNYFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRR
LIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLIS
TMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAWTFID
CLDSASPLFPVCVIVVPFFLCYNYPVSDYYSPTRADTTTILAAGAGVTIGFWINHFFQLV
SKPAESLPVIQNIPPLTTYMLVLGLTKFAVGIVLILLVRQLVQNLSLQVLYSWFKVVTRN
KEARRRLEIEVPYKFVTYTSVGICATTFVPMLHRFLGLP
Enzyme 33 Number of Residues 399
Enzyme 33 Molecular Weight 44741
Enzyme 33 Theoretical pI 9.25
Enzyme 33 GO Classification Not Available
Enzyme 33 General Function Lipid transport and metabolism
Enzyme 33 Specific Function Not Available
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 126632031 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID A3KPB4 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name A3KPB4_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence Not Available
Enzyme 33 GenBank Gene ID BC134342 Link Image
Enzyme 33 GeneCard ID A3KPB4 Link Image
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID Not Available
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 14925
Enzyme 34 Name Non-lysosomal glucosylceramidase
Enzyme 34 Synonyms
  1. NLGase
  2. Glucosylceramidase 2
  3. Beta-glucocerebrosidase 2
  4. Beta-glucosidase 2
Enzyme 34 Gene Name GBA2
Enzyme 34 Protein Sequence >Non-lysosomal glucosylceramidase
MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCC
NPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLR
YLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMY
QHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQ
LPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDD
APGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQ
QVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFG
AKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSAL
FNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVH
FYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDD
EPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDK
DHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILS
RGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVR
ALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWE
GFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASW
PKVKQGTGLRTGPMFGPKEAMANLSPE
Enzyme 34 Number of Residues 927
Enzyme 34 Molecular Weight 104650
Enzyme 34 Theoretical pI 5.74
Enzyme 34 GO Classification Not Available
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O- glucosides, however, the relevance of such activity is unclear in vivo
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 688-708
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 16215453 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9HCG7 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name GBA2_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >2784 bp
ATGGGGACCCAGGATCCAGGGAACATGGGAACCGGCGTCCCAGCCTCGGAGCAGATAAGC
TGTGCCAAAGAGGATCCACAAGTTTATTGCCCTGAAGAGACTGGCGGCACCAAGGATGTG
CAGGTTACAGACTGTAAGAGTCCCGAAGACAGCCGACCCCCAAAAGAGACGGACTGCTGC
AATCCGGAGGACTCTGGGCAGCTGATGGTTTCCTATGAGGGTAAAGCTATGGGCTACCAG
GTGCCTCCCTTTGGCTGGCGCATCTGTCTGGCTCATGAGTTTACAGAGAAGAGGAAACCC
TTTCAAGCTAACAACGTCTCCCTAAGCAACATGATAAAGCATATAGGCATGGGCTTGAGG
TACCTGCAGTGGTGGTACCGGAAGACCCATGTGGAAAAGAAGACACCTTTCATCGACATG
ATCAATTCTGTACCCCTAAGACAGATTTATGGTTGTCCCTTGGGTGGCATCGGGGGAGGC
ACTATTACCCGTGGCTGGAGAGGCCAGTTCTGTCGTTGGCAGCTTAACCCTGGAATGTAT
CAGCACCGGACAGTCATCGCTGACCAATTCACAGTGTGCCTGCGTCGGGAAGGGCAGACT
GTGTACCAGCAAGTCCTGTCCCTGGAGCGCCCAAGTGTCCTCCGCAGCTGGAACTGGGGC
CTGTGTGGGTACTTTGCTTTCTACCATGCCCTCTATCCCCGAGCCTGGACTGTCTATCAG
CTTCCTGGCCAGAATGTCACCCTCACCTGCCGTCAGATCACACCCATCTTGCCCCATGAC
TACCAGGACAGCAGCCTGCCTGTAGGAGTCTTTGTGTGGGATGTGGAAAATGAAGGGGAC
GAAGCTCTAGATGTGTCCATCATGTTCTCCATGCGGAATGGACTGGGTGGTGGAGACGAT
GCCCCAGGGGGTTTGTGGAATGAGCCCTTCTGTCTGGAGCGTAGCGGGGAAACTGTCCGG
GGGCTGCTCCTGCATCATCCAACCCTTCCAAACCCCTACACGATGGCTGTGGCTGCACGA
GTCACGGCAGCTACCACGGTAACCCACATCACAGCCTTTGACCCTGACAGCACGGGGCAG
CAGGTGTGGCAGGATCTACTTCAGGATGGACAGCTGGACTCTCCCACTGGCCAAAGCACC
CCTACGCAGAAAGGAGTAGGCATTGCTGGAGCTGTGTGTGTTTCCAGCAAGTTGCGACCT
CGAGGCCAGTGCCGCCTGGAGTTTTCACTGGCTTGGGACATGCCCAGGATCATGTTTGGA
GCTAAAGGCCAAGTCCACTACAGGCGGTATACAAGGTTCTTTGGCCAGGATGGAGATGCA
GCACCTGCCCTCAGCCACTATGCACTGTGCCGATACGCAGAGTGGGAAGAGAGGATCTCA
GCTTGGCAGAGCCCGGTATTGGATGACAGATCACTGCCTGCCTGGTACAAATCTGCGCTG
TTCAATGAACTATACTTCCTGGCTGATGGAGGCACAGTGTGGCTGGAAGTTCTTGAGGAC
TCCCTACCAGAGGAGCTGGGCAGAAACATGTGTCACCTCCGCCCCACCCTACGGGACTAC
GGTCGATTTGGCTACCTTGAGGGCCAGGAGTACCGCATGTACAACACATATGATGTCCAC
TTTTATGCTTCCTTTGCCCTCATCATGCTCTGGCCCAAACTTGAGCTCAGCCTACAGTAT
GACATGGCTCTGGCCACTCTCAGGGAGGACCTGACACGGCGACGGTACCTGATGAGTGGG
GTGATGGCACCTGTGAAAAGGAGGAACGTCATCCCCCATGATATTGGGGACCCAGATGAT
GAACCATGGCTCCGCGTCAATGCATATTTAATCCATGATACTGCTGATTGGAAGGACCTG
AACCTGAAGTTTGTGCTGCAGGTTTATCGGGACTATTACCTCACGGGTGATCAAAACTTC
CTGAAGGACATGTGGCCTGTGTGTCTAGCTGTGATGGAATCTGAAATGAAGTTTGACAAG
GACCATGATGGACTCATTGAAAATGGAGGCTATGCAGACCAGACCTATGATGGATGGGTG
ACCACAGGCCCCAGTGCTTACTGTGGAGGGCTGTGGCTGGCAGCTGTGGCTGTGATGGTC
CAGATGGCTGCTCTGTGTGGGGCACAGGACATCCAGGATAAGTTTTCTTCTATCCTCAGC
CGGGGCCAAGAAGCCTATGAGAGACTGCTGTGGAATGGCCGCTATTACAACTATGACAGC
AGCTCTCGGCCTCAGTCTCGTAGTGTTATGTCTGACCAGTGTGCTGGACAGTGGTTCCTG
AAGGCCTGTGGCCTAGGAGAAGGAGACACTGAGGTGTTTCCTACCCAACATGTGGTCCGT
GCTCTCCAAACTATCTTTGAGCTGAACGTCCAGGCCTTTGCAGGAGGGGCCATGGGGGCT
GTGAATGGGATGCAGCCCCATGGTGTCCCTGATAAATCCAGTGTGCAGTCTGATGAAGTC
TGGGTGGGTGTGGTCTACGGGCTGGCAGCTACCATGATCCAAGAGGGCCTGACTTGGGAG
GGCTTCCAGACAGCTGAAGGCTGCTACCGTACCGTGTGGGAGCGCCTGGGTCTGGCCTTC
CAGACCCCAGAGGCATACTGCCAGCAGCGAGTGTTCCGCTCACTGGCCTACATGCGGCCA
CTGAGCATATGGGCCATGCAGCTAGCCCTGCAACAGCAGCAGCACAAAAAGGCCTCCTGG
CCAAAAGTCAAACAGGGCACAGGACTAAGGACAGGGCCTATGTTTGGACCAAAGGAAGCC
ATGGCAAACCTGAGCCCAGAGTGA
Enzyme 34 GenBank Gene ID AJ309567 Link Image
Enzyme 34 GeneCard ID Q9HCG7 Link Image
Enzyme 34 GenAtlas ID GBA2 Link Image
Enzyme 34 HGNC ID HGNC:18986 Link Image
Enzyme 34 Chromosome Location Not Available
Enzyme 34 Locus Not Available
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Matern H, Boermans H, Lottspeich F, Matern S: Molecular cloning and expression of human bile acid beta-glucosidase. J Biol Chem. 2001 Oct 12;276(41):37929-33. Epub 2001 Aug 6. [PubMed Link Image]
  2. Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 15257
Enzyme 35 Name Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
Enzyme 35 Synonyms Not Available
Enzyme 35 Gene Name SPHK1
Enzyme 35 Protein Sequence >Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
MDPVVGCGRGLFGFVFSAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAE
ISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLC
SLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSV
LSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASP
VVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMH
LFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMV
SEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL
Enzyme 35 Number of Residues 398
Enzyme 35 Molecular Weight 43945
Enzyme 35 Theoretical pI 7.33
Enzyme 35 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • protein kinase C activation
  • signal transduction
Component
Enzyme 35 General Function Lipid transport and metabolism
Enzyme 35 Specific Function Not Available
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 14495625 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q96GK1 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name Q96GK1_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1197 bp
ATGGATCCAGTGGTCGGTTGCGGACGTGGCCTCTTTGGTTTTGTTTTCTCAGCGGGCGGC
CCCCGGGGCGTGCTCCCGCGGCCCTGCCGCGTGCTGGTGCTGCTGAACCCGCGCGGCGGC
AAGGGCAAGGCCTTGCAGCTCTTCCGGAGTCACGTGCAGCCCCTTTTGGCTGAGGCTGAA
ATCTCCTTCACGCTGATGCTCACTGAGCGGCGGAACCACGCGCGGGAGCTGGTGCGGTCG
GAGGAGCTGGGCCGCTGGGACGCTCTGGTGGTCATGTCTGGAGACGGGCTGATGCACGAG
GTGGTGAACGGGCTCATGGAGCGGCCTGACTGGGAGACCGCCATCCAGAAGCCCCTGTGT
AGCCTCCCAGCAGGCTCTGGCAACGCGCTGGCAGCTTCCTTGAACCATTATGCTGGCTAT
GAGCAGGTCACCAATGAAGACCTCCTGACCAACTGCACGCTATTGCTGTGCCGCCGGCTG
CTGTCACCCATGAACCTGCTGTCTCTGCACACGGCTTCGGGGCTGCGCCTCTTCTCTGTG
CTCAGCCTGGCCTGGGGCTTCATTGCTGATGTGGACCTAGAGAGTGAGAAGTATCGGCGT
CTGGGGGAGATGCGCTTCACTCTGGGCACCTTCCTGCGTCTGGCAGCCCTGCGCACCTAC
CGCGGCCGACTGGCCTACCTCCCTGTAGGAAGAGTGGGTTCCAAGACACCTGCCTCCCCC
GTTGTGGTCCAGCAGGGCCCGGTAGATGCACACCTTGTGCCACTGGAGGAGCCAGTGCCC
TCTCACTGGACAGTGGTGCCCGACGAGGACTTTGTGCTAGTCCTGGCACTGCTGCACTCG
CACCTGGGCAGTGAGATGTTTGCTGCACCCATGGGCCGCTGTGCAGCTGGCGTCATGCAT
CTGTTCTACGTGCGGGCGGGAGTGTCTCGTGCCATGCTGCTGCGCCTCTTCCTGGCCATG
GAGAAGGGCAGGCATATGGAGTATGAATGCCCCTACTTGGTATATGTGCCCGTGGTCGCC
TTCCGCTTGGAGCCCAAGGATGGGAAAGGTGTGTTTGCAGTGGATGGGGAATTGATGGTT
AGCGAGGCCGTGCAGGGCCAGGTGCACCCAAACTACTTCTGGATGGTCAGCGGTTGCGTG
GAGCCCCCGCCCAGCTGGAAGCCCCAGCAGATGCCACCGCCAGAAGAGCCCTTATGA
Enzyme 35 GenBank Gene ID BC009419 Link Image
Enzyme 35 GeneCard ID Q96GK1 Link Image
Enzyme 35 GenAtlas ID SPHK1 Link Image
Enzyme 35 HGNC ID HGNC:11240 Link Image
Enzyme 35 Chromosome Location 17
Enzyme 35 Locus 17q25.2
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 16543
Enzyme 36 Name cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name PPAP2B
Enzyme 36 Protein Sequence >cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
Enzyme 36 Number of Residues 311
Enzyme 36 Molecular Weight 35116
Enzyme 36 Theoretical pI 9.40
Enzyme 36 GO Classification Not Available
Enzyme 36 General Function Lipid transport and metabolism
Enzyme 36 Specific Function Not Available
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein Not Available
Enzyme 36 UniProtKB/Swiss-Prot ID B2R651 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name B2R651_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence Not Available
Enzyme 36 GenBank Gene ID AK312439 Link Image
Enzyme 36 GeneCard ID B2R651 Link Image
Enzyme 36 GenAtlas ID Not Available
Enzyme 36 HGNC ID Not Available
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References Not Available
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 17337
Enzyme 37 Name GPI-anchor transamidase
Enzyme 37 Synonyms
  1. GPI transamidase
  2. Phosphatidylinositol-glycan biosynthesis class K protein
  3. PIG-K
  4. hGPI8
Enzyme 37 Gene Name PIGK
Enzyme 37 Protein Sequence >GPI-anchor transamidase
MAVTDSLSRAATVLATVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYR
HVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVD
YRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITN
IELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPA
IGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLI
TDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEKLMEPLKYAEQLPVAQIIHQKPK
LKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
Enzyme 37 Number of Residues 395
Enzyme 37 Molecular Weight 45251.4
Enzyme 37 Theoretical pI 6.09
Enzyme 37 GO Classification
Function
  • catalytic activity
  • cysteine-type endopeptidase activity
  • endopeptidase activity
  • hydrolase activity
  • legumain activity
  • peptidase activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
Enzyme 37 General Function Involved in cysteine-type endopeptidase activity
Enzyme 37 Specific Function Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-27
Enzyme 37 Transmembrane Regions
  • 368-388
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 1518259 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q92643 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name GPI8_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence Not Available
Enzyme 37 GenBank Gene ID Y07596 Link Image
Enzyme 37 GeneCard ID PIGK Link Image
Enzyme 37 GenAtlas ID Not Available
Enzyme 37 HGNC ID HGNC:8965 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 1p31.1
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Benghezal M, Benachour A, Rusconi S, Aebi M, Conzelmann A: Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J. 1996 Dec 2;15(23):6575-83. [PubMed Link Image]
  2. Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME: The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase. Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12580-5. [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. Ohishi K, Inoue N, Maeda Y, Takeda J, Riezman H, Kinoshita T: Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. Mol Biol Cell. 2000 May;11(5):1523-33. [PubMed Link Image]
  6. Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [PubMed Link Image]
  7. Ohishi K, Nagamune K, Maeda Y, Kinoshita T: Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. J Biol Chem. 2003 Apr 18;278(16):13959-67. Epub 2003 Feb 11. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 17782
Enzyme 38 Name Glycosylphosphatidylinositol anchor attachment 1 protein
Enzyme 38 Synonyms
  1. GPI anchor attachment protein 1
  2. GAA1 protein homolog
  3. hGAA1
Enzyme 38 Gene Name GPAA1
Enzyme 38 Protein Sequence >Glycosylphosphatidylinositol anchor attachment 1 protein
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMV
EEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHE
RYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDI
VFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVE
GLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASG
RPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLY
LLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQ
GVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPH
NTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGP
RTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLF
PLLSLGLYPCWLLFWNVLFWK
Enzyme 38 Number of Residues 621
Enzyme 38 Molecular Weight 67622.5
Enzyme 38 Theoretical pI 8.16
Enzyme 38 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • protein complex
Enzyme 38 General Function Involved in tubulin binding
Enzyme 38 Specific Function Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 25-45 369-389 428-448 459-479 496-516 544-564 600-620
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 2706632 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID O43292 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name GPAA1_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1866 bp
ATGGGCCTCCTGTCGGACCCGGTTCGCCGGCGCGCGCTCGCCCGCCTAGTGCTGCGCCTC
AACGCGCCGTTGTGCGTGCTGAGCTACGTGGCGGGCATCGCCTGGTTCTTGGCGCTGGTT
TTCCCGCCGCTGACCCAGCGCACTTACATGTCGGAGAACGCCATGGGCTCCACCATGGTG
GAGGAGCAGTTTGCGGGCGGAGACCGTGCCCGGGCTTTTGCCCGGGACTTCGCCGCCCAC
CGCAAGAAGTCGGGGGCTCTGCCAGTGGCCTGGCTTGAACGGACGATGCGGTCAGTAGGG
CTGGAGGTCTACACGCAGAGTTTCTCCCGGAAACTGCCCTTCCCAGATGAGACCCACGAG
CGCTATATGGTGTCGGGCACCAACGTGTACGGCATCCTGCGGGCCCCGCGTGCTGCCAGC
ACCGAGTCGCTTGTGCTCACCGTGCCCTGTGGCTCTGACTCTACCAACAGCCAGGCTGTG
GGGCTGCTGCTGGCACTGGCTGCCCACTTCCGGGGGCAGATTTATTGGGCCAAAGATATC
GTCTTCCTGGTAACAGAACATGACCTTCTGGGCACTGAGGCTTGGCTTGAAGCCTACCAC
GATGTCAATGTCACTGGCATGCAGTCGTCTCCCCTGCAGGGCCGAGCTGGGGCCATTCAG
GCAGCCGTGGCCCTGGAGCTGAGCAGTGATGTGGTCACCAGCCTCGATGTGGCCGTGGAG
GGGCTTAACGGGCAGCTGCCCAACCTTGACCTGCTCAATCTCTTCCAGACCTTCTGCCAG
AAAGGGGGCCTGTTGTGCACGCTTCAGGGCAAGCTGCAGCCCGAGGACTGGACATCATTG
GATGGACCGCTGCAGGGCCTGCAGACACTGCTGCTCATGGTTCTGCGGCAGGCCTCCGGC
CGCCCCCACGGCTCCCATGGCCTCTTCCTGCGCTACCGTGTGGAGGCCCTAACCCTGCGT
GGCATCAATAGCTTCCGCCAGTACAAGTATGACCTGGTGGCAGTGGGCAAGGCTTTGGAG
GGCATGTTCCGCAAGCTCAACCACCTCCTGGAGCGCCTGCACCAGTCCTTCTTCCTCTAC
TTGCTCCCCGGCCTCTCCCGCTTCGTCTCCATCGGCCTCTACATGCCCGCTGTCGGCTTC
TTGCTCCTGGTCCTTGGTCTCAAGGCTCTGGAACTGTGGATGCAGCTGCATGAGGCTGGA
ATGGGCCTTGAGGAGCCCGGGGGTGCCCCTGGCCCCAGTGTACCCCTTCCCCCATCACAG
GGTGTGGGGCTGGCCTCGCTCGTGGCACCTCTGCTGATCTCACAGGCCATGGGACTGGCC
CTCTATGTCCTGCCAGTGCTGGGCCAACACGTTGCCACCCAGCACTTCCCAGTGGCAGAG
GCTGAGGCTGTGGTGCTGACACTGCTGGCGATTTATGCAGCTGGCCTGGCCCTGCCCCAC
AATACCCACCGGGTGGTAAGCACACAGGCCCCAGACAGGGGCTGGATGGCACTGAAGCTG
GTAGCCCTGATCTACCTAGCACTGCAGCTGGGCTGCATCGCCCTCACCAACTTCTCACTG
GGCTTCCTGCTGGCCACCACCATGGTGCCCACTGCTGCGCTTGCCAAGCCTCATGGGCCC
CGGACCCTTTATGCTGCCCTGCTGGTGCTGACCAGCCCGGCAGCCACGCTCCTTGGCAGC
CTGTTCCTGTGGCGGGAGCTGCAGGAGGCGCCACTGTCACTGGCCGAGGGCTGGCAGCTC
TTCCTGGCAGCGCTAGCCCAGGGTGTGCTGGAGCACCACACCTACGGCGCCCTGCTCTTC
CCACTGCTGTCCCTGGGCCTCTACCCCTGCTGGCTGCTTTTCTGGAATGTGCTCTTCTGG
AAGTGA
Enzyme 38 GenBank Gene ID AB006969 Link Image
Enzyme 38 GeneCard ID GPAA1 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID HGNC:4446 Link Image
Enzyme 38 Chromosome Location 8
Enzyme 38 Locus 8q24.3
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Hiroi Y, Komuro I, Chen R, Hosoda T, Mizuno T, Kudoh S, Georgescu SP, Medof ME, Yazaki Y: Molecular cloning of human homolog of yeast GAA1 which is required for attachment of glycosylphosphatidylinositols to proteins. FEBS Lett. 1998 Jan 16;421(3):252-8. [PubMed Link Image]
  2. Inoue N, Ohishi K, Endo Y, Fujita T, Takeda J, Kinoshita T: Human and mouse GPAA1 (Glycosylphosphatidylinositol anchor attachment 1) genes: genomic structures, chromosome loci and the presence of a minor class intron. Cytogenet Cell Genet. 1999;84(3-4):199-205. [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]
  5. Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 17783
Enzyme 39 Name Protein PLEKHA9
Enzyme 39 Synonyms Not Available
Enzyme 39 Gene Name PLEKHA9
Enzyme 39 Protein Sequence >Protein PLEKHA9
MSELRLCCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAA
FTSELLYHTPPGSPQLAMLKSSKMKHPIIPIHNSLERQTELSTCENGSLNMEINGEEEIL
MKNKNSLYLKSAEIDCSISSEENTDDNITVQGEIMKEDRMENLKNHDNNLSQSGSDSSCS
PECLWEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCCAVVPVLDKLGPTVFAP
VKMDLVENIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLK
GFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGD
HRKEAFSIGMQRDLSLYLPAMKKQMAILDAL
Enzyme 39 Number of Residues 391
Enzyme 39 Molecular Weight 43538.3
Enzyme 39 Theoretical pI 4.76
Enzyme 39 GO Classification Not Available
Enzyme 39 General Function Involved in glycolipid binding
Enzyme 39 Specific Function Not Available
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 4050073 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID O95397 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name PKHA9_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1176 bp
ATGTCAGAACTAAGACTCTGCTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAA
GTGACCACAACTGGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAA
TCAACCTGTAATACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATTGCAAATGCAGCC
TTCACCTCTGAGCTGCTCTACCACACTCCACCAGGATCACCACAGCTGGCCATGCTCAAG
TCCAGCAAGATGAAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAACGGAG
TTGAGCACTTGTGAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTA
ATGAAAAATAAGAATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGT
GAGGAAAATACAGATGATAATATAACCGTCCAAGGTGAAATAATGAAGGAAGATAGAATG
GAAAACCTGAAAAATCATGACAATAACTTGTCTCAGTCTGGATCAGACTCAAGTTGCTCT
CCAGAATGCCTCTGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAAC
ACAAGCTTTAGTGACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTG
GCATCATGTTGTGCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCT
GTTAAGATGGATCTTGTTGAAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAA
GAAGAGTTTACCACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAG
GTTAGGAACTCAGCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAG
GGATTTTTGACAGAAGTGAAAAATGGGGAAAAGGATATCCAGACAGCCCTGAATAACGCA
TATGGTAAAACATTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCT
TTAAGGGCAACTCCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGAC
CACCGGAAAGAAGCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCC
ATGAAGAAGCAGATGGCCATACTGGACGCTTTATAA
Enzyme 39 GenBank Gene ID AF103731 Link Image
Enzyme 39 GeneCard ID PLEKHA9 Link Image
Enzyme 39 GenAtlas ID Not Available
Enzyme 39 HGNC ID HGNC:30222 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 12q
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 17784
Enzyme 40 Name Glycolipid transfer protein domain-containing protein 2
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name GLTPD2
Enzyme 40 Protein Sequence >Glycolipid transfer protein domain-containing protein 2
MGVAARPPALRHWFSHSIPLAIFALLLLYLSVRSLGARSGCGPRAQPCVPGETAPFQVRQ
ESGTLEAPERKQPPCLGPRGMLGRMMRRFHASLKPEGDVGLSPYLAGWRALVEFLTPLGS
VFAFATREAFTKVTDLEARVHGPDAEHYWSLAAMAAWERRAGLLEQPGAAPRDPTRSSGS
RTLLLLHRALRWSQLCLHRVATGALGGPEAGVQCSDAYRAALGPHHPWLVRQTARLAFLA
FPGRRRLLELACPGATEAEARAALLRAAGTLEDVYNRTQSLLAERGLLQLA
Enzyme 40 Number of Residues 291
Enzyme 40 Molecular Weight 31641.2
Enzyme 40 Theoretical pI 10.54
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Involved in glycolipid binding
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 152061018 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID A6NH11 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name GLTD2_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence Not Available
Enzyme 40 GenBank Gene ID BC150536 Link Image
Enzyme 40 GeneCard ID GLTPD2 Link Image
Enzyme 40 GenAtlas ID Not Available
Enzyme 40 HGNC ID HGNC:33756 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 17p13.2
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed 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. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 17785
Enzyme 41 Name Putative uncharacterized protein PLEKHA8
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name PLEKHA8
Enzyme 41 Protein Sequence >Putative uncharacterized protein PLEKHA8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALSVGMWV
Enzyme 41 Number of Residues 439
Enzyme 41 Molecular Weight 49308.8
Enzyme 41 Theoretical pI 4.67
Enzyme 41 GO Classification Not Available
Enzyme 41 General Function Involved in glycolipid binding
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein Not Available
Enzyme 41 UniProtKB/Swiss-Prot ID B5MDU3 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name B5MDU3_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence Not Available
Enzyme 41 GenBank Gene ID AC007285 Link Image
Enzyme 41 GeneCard ID PLEKHA8 Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID HGNC:30037 Link Image
Enzyme 41 Chromosome Location 7
Enzyme 41 Locus 7p21-p11.2
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References Not Available
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 17786
Enzyme 42 Name cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
Enzyme 42 Synonyms
  1. SubName: Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
Enzyme 42 Gene Name PLEKHA8
Enzyme 42 Protein Sequence >cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTVKEGDHQKE
AFSIGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV
Enzyme 42 Number of Residues 519
Enzyme 42 Molecular Weight 58260.9
Enzyme 42 Theoretical pI 4.76
Enzyme 42 GO Classification Not Available
Enzyme 42 General Function Involved in glycolipid binding
Enzyme 42 Specific Function Not Available
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 194378422 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID B4DH00 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name B4DH00_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1560 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAATAATGCATATGGTAAAACG
TTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCTTTAAGGGCAGCT
CCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGACCACCAGAAAGAA
GCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCCATGGAGAAGCAG
CTGGCCATACTGGACACTTTATATGAGGTCCACGGGCTGGAATCTGATGAGGTGGTATGA
Enzyme 42 GenBank Gene ID AK294857 Link Image
Enzyme 42 GeneCard ID PLEKHA8 Link Image
Enzyme 42 GenAtlas ID Not Available
Enzyme 42 HGNC ID HGNC:30037 Link Image
Enzyme 42 Chromosome Location 7
Enzyme 42 Locus 7p21-p11.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References Not Available
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 17787
Enzyme 43 Name T-cell surface glycoprotein CD1a
Enzyme 43 Synonyms
  1. T-cell surface antigen T6/Leu-6
  2. hTa1 thymocyte antigen
  3. CD1a antigen
Enzyme 43 Gene Name CD1A
Enzyme 43 Protein Sequence >T-cell surface glycoprotein CD1a
MLFLLLPLLAVLPGDGNADGLKEPLSFHVIWIASFYNHSWKQNLVSGWLSDLQTHTWDSN
SSTIVFLWPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCE
LHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLS
DTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRG
EQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSV
GFIILAVIVPLLLLIGLALWFRKRCFC
Enzyme 43 Number of Residues 327
Enzyme 43 Molecular Weight 37172.2
Enzyme 43 Theoretical pI 6.79
Enzyme 43 GO Classification
Function
  • MHC class I receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • antigen presentation
  • defense response
  • immune response
  • response to biotic stimulus
  • response to stimulus
Component
  • MHC class I protein complex
  • MHC protein complex
  • protein complex
Enzyme 43 General Function Involved in antigen processing and presentation
Enzyme 43 Specific Function Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • 1-16
Enzyme 43 Transmembrane Regions
  • 301-321
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 180036 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P06126 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name CD1A_HUMAN Link Image
Enzyme 43 PDB ID 1ONQ Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >984 bp
ATGCTGTTTTTGCTACTTCCATTGTTAGCTGTTCTCCCAGGTGATGGCAATGCAGACGGG
CTCAAGGAGCCTCTCTCCTTCCATGTCATCTGGATCGCATCCTTTTACAACCATTCCTGG
AAACAAAATCTGGTCTCAGGTTGGCTGAGTGATTTGCAGACTCATACCTGGGACAGCAAT
TCCAGCACCATCGTTTTCCTGTGGCCCTGGTCCAGGGGAAACTTCAGCAATGAGGAGTGG
AAGGAACTGGAAACATTATTCCGTATACGCACCATTCGGTCATTTGAGGGAATTCGTAGA
TACGCCCATGAATTGCAGTTTGAATATCCTTTTGAGATACAGGTGACAGGAGGCTGTGAG
CTGCACTCTGGAAAGGTCTCAGGAAGCTTCTTGCAGTTAGCTTATCAAGGATCAGACTTT
GTGAGCTTCCAGAACAATTCATGGTTGCCATATCCAGTGGCTGGGAATATGGCCAAGCAT
TTCTGCAAAGTGCTCAATCAGAATCAGCATGAAAATGACATAACACACAATCTTCTCAGT
GACACCTGCCCACGTTTCATCTTGGGTCTTCTTGATGCAGGAAAGGCACATCTCCAGCGG
CAAGTGAAGCCCGAGGCCTGGCTGTCCCATGGCCCCAGTCCTGGCCCTGGCCATCTGCAG
CTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGT
GAGCAGGAGCAGCAGGGCACTCAGCGAGGGGACATCTTGCCCAGTGCTGATGGGACATGG
TATCTCCGCGCAACCCTGGAGGTGGCCGCTGGGGAGGCAGCTGACCTGTCCTGTCGGGTG
AAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGAGCATCACAGTTCCGTG
GGCTTCATCATCTTGGCGGTGATAGTGCCTTTACTTCTTCTGATAGGTCTTGCGCTTTGG
TTCAGGAAACGCTGTTTCTGTTAA
Enzyme 43 GenBank Gene ID M28825 Link Image
Enzyme 43 GeneCard ID CD1A Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID HGNC:1634 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 1q22-q23
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Aruffo A, Seed B: Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. J Immunol. 1989 Sep 1;143(5):1723-30. [PubMed Link Image]
  2. Martin LH, Calabi F, Lefebvre FA, Bilsland CA, Milstein C: Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9189-93. [PubMed Link Image]
  3. Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed Link Image]
  4. Longley J, Kraus J, Alonso M, Edelson R: Molecular cloning of CD1a (T6), a human epidermal dendritic cell marker related to class I MHC molecules. J Invest Dermatol. 1989 Apr;92(4):628-31. [PubMed Link Image]
  5. Calabi F, Milstein C: A novel family of human major histocompatibility complex-related genes not mapping to chromosome 6. Nature. 1986 Oct 9-15;323(6088):540-3. [PubMed Link Image]
  6. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed Link Image]
  7. Salamero J, Bausinger H, Mommaas AM, Lipsker D, Proamer F, Cazenave JP, Goud B, de la Salle H, Hanau D: CD1a molecules traffic through the early recycling endosomal pathway in human Langerhans cells. J Invest Dermatol. 2001 Mar;116(3):401-8. [PubMed Link Image]
  8. Vincent MS, Xiong X, Grant EP, Peng W, Brenner MB: CD1a-, b-, and c-restricted TCRs recognize both self and foreign antigens. J Immunol. 2005 Nov 15;175(10):6344-51. [PubMed Link Image]
  9. Sloma I, Zilber MT, Vasselon T, Setterblad N, Cavallari M, Mori L, De Libero G, Charron D, Mooney N, Gelin C: Regulation of CD1a surface expression and antigen presentation by invariant chain and lipid rafts. J Immunol. 2008 Jan 15;180(2):980-7. [PubMed Link Image]
  10. Zajonc DM, Elsliger MA, Teyton L, Wilson IA: Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. Nat Immunol. 2003 Aug;4(8):808-15. Epub 2003 Jun 29. [PubMed Link Image]
  11. Zajonc DM, Crispin MD, Bowden TA, Young DC, Cheng TY, Hu J, Costello CE, Rudd PM, Dwek RA, Miller MJ, Brenner MB, Moody DB, Wilson IA: Molecular mechanism of lipopeptide presentation by CD1a. Immunity. 2005 Feb;22(2):209-19. [PubMed Link Image]
  12. Oteo M, Arribas P, Setien F, Parra JF, Mirones I, Gomez del Moral M, Martinez-Naves E: Structural characterization of two CD1A allelic variants. Hum Immunol. 2001 Oct;62(10):1137-41. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 17788
Enzyme 44 Name Glycolipid transfer protein domain-containing protein 1
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name GLTPD1
Enzyme 44 Protein Sequence >Glycolipid transfer protein domain-containing protein 1
MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSK
LRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQL
FLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPP
EQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Enzyme 44 Number of Residues 214
Enzyme 44 Molecular Weight 24364.8
Enzyme 44 Theoretical pI 7.23
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Involved in glycolipid binding
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID Q5TA50 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name GLTD1_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence Not Available
Enzyme 44 GenBank Gene ID CR599582 Link Image
Enzyme 44 GeneCard ID GLTPD1 Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID HGNC:28116 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 1p36.33
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 17789
Enzyme 45 Name T-cell surface glycoprotein CD1c
Enzyme 45 Synonyms
  1. CD1c antigen
Enzyme 45 Gene Name CD1C
Enzyme 45 Protein Sequence >T-cell surface glycoprotein CD1c
MLFLQFLLLALLLPGGDNADASQEHVSFHVIQIFSFVNQSWARGQGSGWLDELQTHGWDS
ESGTIIFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGC
ELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNL
IRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWM
RNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWGHHF
SMNWIALVVIVPLVILIVLVLWFKKHCSYQDIL
Enzyme 45 Number of Residues 333
Enzyme 45 Molecular Weight 37653.7
Enzyme 45 Theoretical pI 6.09
Enzyme 45 GO Classification
Function
  • MHC class I receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • antigen presentation
  • defense response
  • immune response
  • response to biotic stimulus
  • response to stimulus
Component
  • MHC class I protein complex
  • MHC protein complex
  • protein complex
Enzyme 45 General Function Involved in antigen processing and presentation
Enzyme 45 Specific Function Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • 1-17
Enzyme 45 Transmembrane Regions
  • 303-323
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 180066 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P29017 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name CD1C_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1002 bp
ATGCTGTTTCTGCAGTTTCTGCTGCTAGCTCTTCTTCTCCCAGGTGGTGACAATGCAGAC
GCATCCCAGGAACACGTCTCCTTCCATGTCATCCAGATCTTCTCATTTGTCAACCAATCC
TGGGCACGAGGTCAGGGCTCAGGATGGCTGGACGAGTTGCAGACTCATGGCTGGGACAGT
GAATCAGGCACAATAATTTTCCTGCATAACTGGTCCAAGGGCAACTTCAGCAATGAAGAG
TTGTCAGACCTAGAGTTGTTATTTCGTTTCTACCTCTTTGGATTAACTCGGGAGATTCAA
GACCATGCAAGTCAAGATTACTCGAAATATCCCTTTGAAGTACAGGTGAAAGCGGGCTGT
GAGCTGCATTCTGGAAAGAGCCCAGAAGGCTTCTTTCAGGTAGCTTTCAACGGATTAGAT
TTACTGAGTTTCCAGAATACAACATGGGTGCCATCTCCAGGCTGTGGAAGTTTGGCCCAA
AGTGTCTGTCATCTACTCAATCATCAGTATGAAGGCGTCACAGAAACAGTGTATAATCTC
ATAAGAAGCACTTGCCCCCGATTTCTCTTGGGTCTCCTGGATGCAGGGAAGATGTATGTA
CACAGGCAAGTGAGGCCAGAAGCCTGGCTGTCCAGTCGCCCCAGCCTTGGGTCTGGCCAG
CTGTTGCTGGTTTGTCATGCCTCCGGCTTCTACCCAAAGCCTGTTTGGGTGACATGGATG
CGGAATGAACAGGAGCAACTGGGCACTAAACATGGTGATATTCTTCCTAATGCTGATGGG
ACATGGTATCTTCAGGTGATCCTGGAGGTGGCATCTGAGGAGCCTGCTGGCCTGTCTTGT
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTCT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
Enzyme 45 GenBank Gene ID M28827 Link Image
Enzyme 45 GeneCard ID CD1C Link Image
Enzyme 45 GenAtlas ID Not Available
Enzyme 45 HGNC ID HGNC:1636 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 1q22-q23
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Martin LH, Calabi F, Lefebvre FA, Bilsland CA, Milstein C: Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9189-93. [PubMed Link Image]
  2. Aruffo A, Seed B: Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. J Immunol. 1989 Sep 1;143(5):1723-30. [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. Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed Link Image]
  6. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed Link Image]
  7. Briken V, Jackman RM, Watts GF, Rogers RA, Porcelli SA: Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens. J Exp Med. 2000 Jul 17;192(2):281-8. [PubMed Link Image]
  8. Moody DB, Ulrichs T, Muhlecker W, Young DC, Gurcha SS, Grant E, Rosat JP, Brenner MB, Costello CE, Besra GS, Porcelli SA: CD1c-mediated T-cell recognition of isoprenoid glycolipids in Mycobacterium tuberculosis infection. Nature. 2000 Apr 20;404(6780):884-8. [PubMed Link Image]
  9. Sugita M, van Der Wel N, Rogers RA, Peters PJ, Brenner MB: CD1c molecules broadly survey the endocytic system. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8445-50. [PubMed Link Image]
  10. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 17790
Enzyme 46 Name Lipopolysaccharide-binding protein
Enzyme 46 Synonyms
  1. LBP
Enzyme 46 Gene Name LBP
Enzyme 46 Protein Sequence >Lipopolysaccharide-binding protein
MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLP
DFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRK
SFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNL
FHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATA
QMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLN
FSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDP
YMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFN
AELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMR
V
Enzyme 46 Number of Residues 481
Enzyme 46 Molecular Weight 53383.0
Enzyme 46 Theoretical pI 6.68
Enzyme 46 GO Classification
Function
  • binding
  • lipid binding
Process
Component
Enzyme 46 General Function Involved in Gram-negative bacterial cell surface binding
Enzyme 46 Specific Function Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. The LBP/LPS complex seems to interact with the CD14 receptor
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • 1-25
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 186966 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P18428 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name LBP_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID M35533 Link Image
Enzyme 46 GeneCard ID LBP Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID HGNC:6517 Link Image
Enzyme 46 Chromosome Location 2
Enzyme 46 Locus 20q11.23-q12
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Schumann RR, Leong SR, Flaggs GW, Gray PW, Wright SD, Mathison JC, Tobias PS, Ulevitch RJ: Structure and function of lipopolysaccharide binding protein. Science. 1990 Sep 21;249(4975):1429-31. [PubMed Link Image]
  2. Wilde CG, Seilhamer JJ, McGrogan M, Ashton N, Snable JL, Lane JC, Leong SR, Thornton MB, Miller KL, Scott RW, et al.: Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation. J Biol Chem. 1994 Jul 1;269(26):17411-6. [PubMed Link Image]
  3. Hubacek JA, Buchler C, Aslanidis C, Schmitz G: The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved. Biochem Biophys Res Commun. 1997 Jul 18;236(2):427-30. [PubMed Link Image]
  4. Kirschning CJ, Au-Young J, Lamping N, Reuter D, Pfeil D, Seilhamer JJ, Schumann RR: Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins. Genomics. 1997 Dec 15;46(3):416-25. [PubMed Link Image]
  5. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Beamer LJ, Carroll SF, Eisenberg D: The BPI/LBP family of proteins: a structural analysis of conserved regions. Protein Sci. 1998 Apr;7(4):906-14. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 17791
Enzyme 47 Name Putative uncharacterized protein DKFZp434L0435
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name DKFZp434L0435
Enzyme 47 Protein Sequence >Putative uncharacterized protein DKFZp434L0435
VAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Enzyme 47 Number of Residues 55
Enzyme 47 Molecular Weight 6175.1
Enzyme 47 Theoretical pI 4.41
Enzyme 47 GO Classification Not Available
Enzyme 47 General Function Involved in glycolipid binding
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function Not Available
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 50978454 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q9UFH6 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name Q9UFH6_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AL122073 Link Image
Enzyme 47 GeneCard ID DKFZp434L0435 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID HGNC:28116 Link Image
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 17792
Enzyme 48 Name T-cell surface glycoprotein CD1b
Enzyme 48 Synonyms
  1. CD1b antigen
Enzyme 48 Gene Name CD1B
Enzyme 48 Protein Sequence >T-cell surface glycoprotein CD1b
MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDS
DSGTAIFLKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDFQMKYPFEIQGIAGC
ELHSGGAIVSFLRGALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQGIMETVRILL
YETCPRYLLGVLNAGKADLQRQVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVWVMWMR
GEQEQQGTQLGDILPNANWTWYLRATLDVADGEAAGLSCRVKHSSLEGQDIILYWRNPTS
IGSIVLAIIVPSLLLLLCLALWYMRRRSYQNIP
Enzyme 48 Number of Residues 333
Enzyme 48 Molecular Weight 36939.1
Enzyme 48 Theoretical pI 6.24
Enzyme 48 GO Classification
Function
  • MHC class I receptor activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • antigen presentation
  • defense response
  • immune response
  • response to biotic stimulus
  • response to stimulus
Component
  • MHC class I protein complex
  • MHC protein complex
  • protein complex
Enzyme 48 General Function Involved in protein binding
Enzyme 48 Specific Function Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • 1-17
Enzyme 48 Transmembrane Regions
  • 304-324
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 180056 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P29016 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name CD1B_HUMAN Link Image
Enzyme 48 PDB ID 1UQS Link Image
Enzyme 48 PDB File Show
Enzyme 48 3D Structure
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >1002 bp
ATGCTGCTGCTGCCATTTCAACTGTTAGCTGTTCTCTTTCCTGGTGGTAACAGTGAACAT
GCCTTCCAGGGGCCGACCTCCTTTCATGTTATCCAGACCTCGTCCTTTACCAATAGTACC
TGGGCACAAACTCAAGGCTCAGGCTGGTTGGATGATTTGCAGATTCATGGCTGGGATAGC
GACTCAGGCACTGCCATATTCCTGAAGCCTTGGTCTAAAGGTAACTTTAGTGATAAGGAG
GTTGCTGAGTTAGAGGAGATATTCCGAGTCTACATCTTTGGATTCGCTCGAGAAGTACAA
GACTTTGCCGGTGATTTCCAGATGAAATACCCCTTTGAGATCCAGGGCATAGCAGGCTGT
GAGCTACATTCTGGAGGTGCCATAGTAAGCTTCCTGAGGGGAGCTCTAGGAGGATTGGAT
TTCCTGAGTGTCAAGAATGCTTCATGTGTGCCTTCCCCAGAAGGTGGCAGCAGGGCACAG
AAATTCTGTGCACTAATCATACAATATCAAGGTATCATGGAAACTGTGAGAATTCTCCTC
TATGAAACCTGCCCCCGATATCTCTTGGGCGTCCTCAATGCAGGAAAAGCAGATCTGCAA
AGACAAGTGAAGCCTGAGGCCTGGCTGTCCAGTGGCCCCAGTCCTGGACCTGGCCGTCTG
CAGCTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCTAGGGGACATCCTGCCCAATGCTAACTGGACA
TGGTATCTCCGAGCAACCCTGGATGTGGCAGATGGGGAGGCGGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTTTAGAGGGCCAGGACATCATCCTCTACTGGAGAAACCCCACCTCC
ATTGGCTCAATTGTTTTGGCAATAATAGTGCCTTCCTTGCTCCTTTTGCTATGCCTTGCA
TTATGGTATATGAGGCGCCGGTCATATCAGAATATCCCATGA
Enzyme 48 GenBank Gene ID M28826 Link Image
Enzyme 48 GeneCard ID CD1B Link Image
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID HGNC:1635 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 1q22-q23
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Martin LH, Calabi F, Lefebvre FA, Bilsland CA, Milstein C: Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9189-93. [PubMed Link Image]
  2. Aruffo A, Seed B: Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. J Immunol. 1989 Sep 1;143(5):1723-30. [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. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed Link Image]
  6. Shamshiev A, Donda A, Prigozy TI, Mori L, Chigorno V, Benedict CA, Kappos L, Sonnino S, Kronenberg M, De Libero G: The alphabeta T cell response to self-glycolipids shows a novel mechanism of CD1b loading and a requirement for complex oligosaccharides. Immunity. 2000 Aug;13(2):255-64. [PubMed Link Image]
  7. Briken V, Jackman RM, Watts GF, Rogers RA, Porcelli SA: Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens. J Exp Med. 2000 Jul 17;192(2):281-8. [PubMed Link Image]
  8. Winau F, Schwierzeck V, Hurwitz R, Remmel N, Sieling PA, Modlin RL, Porcelli SA, Brinkmann V, Sugita M, Sandhoff K, Kaufmann SH, Schaible UE: Saposin C is required for lipid presentation by human CD1b. Nat Immunol. 2004 Feb;5(2):169-74. Epub 2004 Jan 11. [PubMed Link Image]
  9. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  10. Gadola SD, Zaccai NR, Harlos K, Shepherd D, Castro-Palomino JC, Ritter G, Schmidt RR, Jones EY, Cerundolo V: Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl chains. Nat Immunol. 2002 Aug;3(8):721-6. Epub 2002 Jul 15. [PubMed Link Image]
  11. Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY: The crystal structure of human CD1b with a bound bacterial glycolipid. J Immunol. 2004 Feb 15;172(4):2382-8. [PubMed Link Image]
  12. Garcia-Alles LF, Versluis K, Maveyraud L, Vallina AT, Sansano S, Bello NF, Gober HJ, Guillet V, de la Salle H, Puzo G, Mori L, Heck AJ, De Libero G, Mourey L: Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b. EMBO J. 2006 Aug 9;25(15):3684-92. Epub 2006 Jul 27. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 17793
Enzyme 49 Name Glycolipid transfer protein
Enzyme 49 Synonyms
  1. GLTP
Enzyme 49 Gene Name GLTP
Enzyme 49 Protein Sequence >Glycolipid transfer protein
MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVY
DTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENH
PNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKI
RLFLVNYTATIDVIYEMYTQMNAELNYKV
Enzyme 49 Number of Residues 209
Enzyme 49 Molecular Weight 23849.6
Enzyme 49 Theoretical pI 7.49
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Involved in glycolipid binding
Enzyme 49 Specific Function Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 6959686 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9NZD2 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name GLTP_HUMAN Link Image
Enzyme 49 PDB ID 1SX6 Link Image
Enzyme 49 PDB File Show
Enzyme 49 3D Structure
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >630 bp
ATGGCGCTGCTGGCGGAGCACTTGCTGAAGCCGCTGCCCGCGGACAAGCAGATCGAGACC
GGGCCCTTCCTCGAGGCGGTGTCCCACCTGCCGCCCTTCTTCGATTGCCTTGGGTCCCCA
GTGTTTACTCCCATCAAGGCAGACATAAGCGGCAACATCACGAAAATCAAAGCTGTGTAC
GACACCAACCCAGCCAAGTTCCGGACCCTGCAGAACATCCTGGAGGTGGAGAAAGAAATG
TATGGAGCAGAGTGGCCCAAAGTAGGGGCCACACTGGCGCTGATGTGGCTGAAAAGAGGC
CTCCGCTTCATCCAGGTCTTCCTCCAGAGCATCTGCGACGGGGAGCGGGACGAGAACCAC
CCCAACCTCATCCGTGTCAACGCCACCAAGGCCTACGAGATGGCCCTCAAGAAGTACCAT
GGCTGGATCGTGCAGAAGATCTTCCAGGCAGCACTGTACGCAGCACCCTATAAGTCTGAC
TTCCTGAAAGCGCTCTCCAAGGGGCAGAATGTTACGGAGGAGGAGTGCCTGGAGAAGATC
CGCCTCTTCCTAGTCAACTACACGGCGACCATCGATGTCATCTACGAGATGTACACCCAG
ATGAACGCTGAGCTCAACTACAAGGTGTAG
Enzyme 49 GenBank Gene ID AF209704 Link Image
Enzyme 49 GeneCard ID GLTP Link Image
Enzyme 49 GenAtlas ID Not Available
Enzyme 49 HGNC ID HGNC:24867 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 12q24.11
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Li XM, Malakhova ML, Lin X, Pike HM, Chung T, Molotkovsky JG, Brown RE: Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy. Biochemistry. 2004 Aug 10;43(31):10285-94. [PubMed Link Image]
  2. Zou X, Chung T, Lin X, Malakhova ML, Pike HM, Brown RE: Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution. BMC Genomics. 2008 Feb 8;9:72. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rao CS, Lin X, Pike HM, Molotkovsky JG, Brown RE: Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses. Biochemistry. 2004 Nov 2;43(43):13805-15. [PubMed Link Image]
  6. Tuuf J, Mattjus P: Human glycolipid transfer protein--intracellular localization and effects on the sphingolipid synthesis. Biochim Biophys Acta. 2007 Nov;1771(11):1353-63. Epub 2007 Sep 21. [PubMed Link Image]
  7. Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ: Structural basis for glycosphingolipid transfer specificity. Nature. 2004 Aug 26;430(7003):1048-53. [PubMed Link Image]
  8. Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ: The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure. PLoS Biol. 2006 Nov;4(11):e362. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available