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Human Metabolome Database Version 2.5

 

Showing metabocard for Sphingosine (HMDB00252)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-22 11:26:17
Accession Number HMDB00252
Secondary Accession Numbers Not Available
Common Name Sphingosine
Description A 18-carbon amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed.) Sphingosine can be phosphorylated in vivo via two kinases, sphingosine kinase type 1 and sphingosine kinase type 2. This leads to the formation of sphingosine-1-phosphate, a potent signaling lipid.(Wikipedia)
Synonyms
  1. (-)-D-erythro-Sphingosine
  2. (2S,3R)-Sphingosine
  3. (2S,3R,4E)-2-Amino-4-octadecene-1,3-diol
  4. (4E)-Sphingenine
  5. 4-Sphingenine
  6. 4-trans-Sphingenine
  7. [R-[R*,S*-(E)]]-2-amino-4-Octadecene-1,3-diol
Chemical IUPAC Name (2S,3R,4E)-2-amino-4-Octadecene-1,3-diol
Chemical Formula C18H37NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Amino Alcohols
Sub Class
  • Primary amino alcohols
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-aminoalcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • alkene
Biofunction
  • Component of Glycosphingolipid metabolism
Application
Source
  • Endogenous
Average Molecular Weight 299.492
Monoisotopic Molecular Weight 299.282440
Isomeric SMILES CCCCCCCCCCCCCC=CC(O)C(N)CO
Canonical SMILES CCCCCCCCCCCCCC=CC(O)C(N)CO
KEGG Compound ID C00319 Link Image
BioCyc ID SPHINGOSINE Link Image
BiGG ID 34606 Link Image
Wikipedia Link Sphingosine Link Image
NuGOwiki Link HMDB00252 Link Image
Metagene Link HMDB00252 Link Image
METLIN ID 392 Link Image
PubChem Compound 31270 Link Image
PubChem Substance 11147278 Link Image
ChEBI ID 16393 Link Image
CAS Registry Number 123-78-4
InChI Identifier InChI=1/C18H37NO2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-18(21)17(19)16-20/h14-15,17-18,20-21H,2-13,16,19H2,1H3/b15-14+
Synthesis Reference Obayashi, Michio; Schlosser, Manfred. An efficient synthesis of (2S,3R)- and (2S,3S)-sphingosine. Chemistry Letters (1985), (11), 1715-18.
Melting Point (Experimental) 81
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.00236 mg/mL [MEYLAN,WM et al. (1996)]; 3.90e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5.15 [Predicted by ALOGPS]; 4.5 [Predicted by PubChem via XLOGP]; 5.53 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1SX6 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
  • lysosome
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Fibroblasts
Intestine
Kidney
Liver
Muscle
Neutrophil
Platelet
Skin
Spleen
Stratum Corneum
Concentrations (Normal)
Biofluid Blood
Value 0.050 +/- 0.0013 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 Urine
Value 0.000038485 (0.0000375-0.00003947) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Ribar S, Mesaric M, Bauman M: High-performance liquid chromatographic determination of sphinganine and sphingosine in serum and urine of subjects from an endemic nephropathy area in Croatia. J Chromatogr B Biomed Sci Appl. 2001 Apr 25;754(2):511-9. [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. Qiu M, Liu X: Determination of sphinganine, sphingosine and Sa/So ratio in urine of humans exposed to dietary fumonisin B1. Food Addit Contam. 2001 Mar;18(3):263-9. [PubMed Link Image]
  2. Ribar S, Mesaric M, Bauman M: High-performance liquid chromatographic determination of sphinganine and sphingosine in serum and urine of subjects from an endemic nephropathy area in Croatia. J Chromatogr B Biomed Sci Appl. 2001 Apr 25;754(2):511-9. [PubMed Link Image]
  3. Wong K, Kwan-Yeung L: Sphingosine mobilizes intracellular calcium in human neutrophils. Cell Calcium. 1993 Jun;14(6):493-505. [PubMed Link Image]
  4. Wertz PW, Downing DT: Free sphingosine in human epidermis. J Invest Dermatol. 1990 Feb;94(2):159-61. [PubMed Link Image]
  5. Rusakov SA, Filippova GN, Pushkareva MIu, Korobko VG, Alesenko AV: [The effect of tumor necrosis factor on the free sphingosine level and sphingomyelinase in murine liver cells and nuclei] Biokhimiia. 1993 May;58(5):724-32. [PubMed Link Image]
  6. Hisano N, Yatomi Y, Fujino MA, Igarashi Y, Kume S, Ozaki Y: Quantification of sphingosine derivatives in human platelets: inducible formation of free sphingosine. J Biochem (Tokyo). 1998 Feb;123(2):263-8. [PubMed Link Image]
  7. Arikawa J, Ishibashi M, Kawashima M, Takagi Y, Ichikawa Y, Imokawa G: Decreased levels of sphingosine, a natural antimicrobial agent, may be associated with vulnerability of the stratum corneum from patients with atopic dermatitis to colonization by Staphylococcus aureus. J Invest Dermatol. 2002 Aug;119(2):433-9. [PubMed Link Image]
  8. Gorska M, Dobrzyn A, Baranowski M: Concentrations of sphingosine and sphinganine in plasma of patients with type 2 diabetes. Med Sci Monit. 2005 Jan;11(1):CR35-8. [PubMed Link Image]
  9. Toxicology and carcinogenesis studies of fumonisin B1 (cas no. 116355-83-0) in F344/N rats and B6C3F1 mice (feed studies). Natl Toxicol Program Tech Rep Ser. 2001 Dec;(496):1-352. [PubMed Link Image]
  10. Alessenko AV, Korobko VG, Khrenov AV, Rozhnova UA, Soloviev AS, Shingarova LN: Relation of biological activity of mutant forms of recombinant human tumor necrosis factor alpha and accumulation of sphingosine in murine liver. Biochem Mol Biol Int. 1997 Jun;42(1):143-54. [PubMed Link Image]
  11. Sweeney EA, Sakakura C, Shirahama T, Masamune A, Ohta H, Hakomori S, Igarashi Y: Sphingosine and its methylated derivative N,N-dimethylsphingosine (DMS) induce apoptosis in a variety of human cancer cell lines. Int J Cancer. 1996 May 3;66(3):358-66. [PubMed Link Image]
  12. Shin Y, Daly JW, Choi OH: Diverse effects of sphingosine on calcium mobilization and influx in differentiated HL-60 cells. Cell Calcium. 2000 May;27(5):269-80. [PubMed Link Image]
  13. van der Westhuizen L, Shephard GS, van Schalkwyk DJ: The effect of repeated gavage doses of fumonisin B1 on the sphinganine and sphingosine levels in vervet monkeys. Toxicon. 2001 Jul;39(7):969-72. [PubMed Link Image]
  14. van der Westhuizen L, Brown NL, Marasas WF, Swanevelder S, Shephard GS: Sphinganine/sphingosine ratio in plasma and urine as a possible biomarker for fumonisin exposure in humans in rural areas of Africa. Food Chem Toxicol. 1999 Dec;37(12):1153-8. [PubMed Link Image]
  15. Khan WA, Mascarella SW, Lewin AH, Wyrick CD, Carroll FI, Hannun YA: Use of D-erythro-sphingosine as a pharmacological inhibitor of protein kinase C in human platelets. Biochem J. 1991 Sep 1;278 ( Pt 2):387-92. [PubMed Link Image]
  16. 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]
  17. 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. Acid ceramidase precursor
  13. Ganglioside GM2 activator precursor
  14. T-cell surface glycoprotein CD1e precursor
  15. Sphingosine 1-phosphate receptor Edg-6
  16. Sphingosine 1-phosphate receptor Edg-5
  17. Epididymal secretory protein E1 precursor
  18. Sphingosine 1-phosphate receptor Edg-1
  19. Sphingosine 1-phosphate receptor Edg-8
  20. T-cell surface glycoprotein CD1d precursor
  21. GPI mannosyltransferase 1
  22. Phosphatidylinositol-glycan biosynthesis class W protein
  23. Phosphatidylinositol-glycan biosynthesis class X protein precursor
  24. GPI mannosyltransferase 4
  25. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
  26. Beta-1,3-galactosyltransferase 5
  27. GPI mannosyltransferase 3
  28. Phosphatidylinositol-glycan biosynthesis class F protein
  29. GPI ethanolamine phosphate transferase 2
  30. GPI ethanolamine phosphate transferase 1
  31. GPI ethanolamine phosphate transferase 3
  32. GPI transamidase component PIG-S
  33. GPI transamidase component PIG-T precursor
  34. Phosphatidylinositol glycan anchor biosynthesis class U protein
  35. GPI mannosyltransferase 2
  36. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
  37. Pleckstrin homology domain-containing family A member 8
  38. Sphingosine-1-phosphate phosphotase 2
  39. N-acylsphingosine amidohydrolase 3-like
  40. Sphingosine 1-phosphate receptor GPR6
  41. Alkaline ceramidase 2
  42. Neutral ceramidase
  43. Non-lysosomal glucosylceramidase
  44. Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
  45. ASAH1 protein
  46. cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
  47. Alkaline ceramidase 1
  48. Sphingosine 1-phosphate receptor 3
  49. GPI-anchor transamidase
  50. Glycosylphosphatidylinositol anchor attachment 1 protein
  51. Protein PLEKHA9
  52. Glycolipid transfer protein domain-containing protein 2
  53. Putative uncharacterized protein PLEKHA8
  54. cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
  55. T-cell surface glycoprotein CD1a
  56. Glycolipid transfer protein domain-containing protein 1
  57. T-cell surface glycoprotein CD1c
  58. Lipopolysaccharide-binding protein
  59. Putative uncharacterized protein DKFZp434L0435
  60. T-cell surface glycoprotein CD1b
  61. 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 6373
Enzyme 12 Name Acid ceramidase precursor
Enzyme 12 Synonyms
  1. Acylsphingosine deacylase
  2. N-acylsphingosine amidohydrolase
  3. AC
  4. Putative 32 kDa heart protein
  5. PHP32[Contains: Acid ceramidase subunit alpha
  6. Acid ceramidase subunit beta]
Enzyme 12 Gene Name ASAH1
Enzyme 12 Protein Sequence >Acid ceramidase precursor
MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYK
RWHELMLDKAPMLKVIVNSLKNMINTFVPSGKVMQVVDEKLPGLLGNFPGPFEEEMKGIA
AVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITE
QLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWI
LGKKDAMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKE
SLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLST
KPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW
Enzyme 12 Number of Residues 395
Enzyme 12 Molecular Weight 44650
Enzyme 12 Theoretical pI 7.70
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid
Enzyme 12 Pathways
Enzyme 12 Reactions
  • N-acylsphingosine + H2O = a carboxylate + sphingosine
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-21
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 1743867 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q13510 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ASAH1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1188 bp
ATGCCGGGCCGGAGTTGCGTCGCCTTAGTCCTCCTGGCTGCCGCCGTCAGCTGTGCCGTC
GCGCAGCACGCGCCGCCGTGGACAGAGGACTGCAGAAAATCAACCTATCCTCCTTCAGGA
CCAACGTACAGAGGTGCAGTTCCATGGTACACCATAAATCTTGACTTACCACCCTACAAA
AGATGGCATGAATTGATGCTTGACAAGGCACCAATGCTAAAGGTTATAGTGAATTCTCTG
AAGAATATGATAAATACATTCGTGCCAAGTGGAAAAGTTATGCAGGTGGTGGATGAAAAA
TTGCCTGGCCTACTTGGCAACTTTCCTGGCCCTTTTGAAGAGGAAATGAAGGGTATTGCC
GCTGTTACTGATATACCTTTAGGAGAGATTATTTCATTCAATATTTTTTATGAATTATTT
ACCATTTGTACTTCAATAGTAGCAGAAGACAAAAAAGGTCATCTAATACATGGGAGAAAC
ATGGATTTTGGAGTATTTCTTGGGTGGAACATAAATAATGATACCTGGGTCATAACTGAG
CAACTAAAACCTTTAACAGTGAATTTGGATTTCCAAAGAAACAACAAAACTGTCTTCAAG
GCTTCAAGCTTTGCTGGCTATGTGGGCATGTTAACAGGATTCAAACCAGGACTGTTCAGT
CTTACACTGAATGAACGTTTCAGTATAAATGGTGGTTATCTGGGTATTCTAGAATGGATT
CTGGGAAAGAAAGATGCCATGTGGATAGGGTTCCTCACTAGAACAGTTCTGGAAAATAGC
ACAAGTTATGAAGAAGCCAAGAATTTATTGACCAAGACCAAGATATTGGCCCCAGCCTAC
TTTATCCTGGGAGGCAACCAGTCTGGGGAAGGTTGTGTGATTACACGAGACAGAAAGGAA
TCATTGGATGTATATGAACTCGATGCTAAGCAGGGTAGATGGTATGTGGTACAAACAAAT
TATGACCGTTGGAAACATCCCTTCTTCCTTGATGATCGCAGAACGCCTGCAAAGATGTGT
CTGAACCGCACCAGCCAAGAGAATATCTCATTTGAAACCATGTATGATGTCCTGTCAACA
AAACCTGTCCTCAACAAGCTGACCGTATACACAACCTTGATAGATGTTACCAAAGGTCAA
TTCGAAACTTACCTGCGGGACTGCCCTGACCCTTGTATAGGTTGGTGA
Enzyme 12 GenBank Gene ID U70063 Link Image
Enzyme 12 GeneCard ID ASAH1 Link Image
Enzyme 12 GenAtlas ID ASAH1 Link Image
Enzyme 12 HGNC ID HGNC:735 Link Image
Enzyme 12 Chromosome Location 8
Enzyme 12 Locus 8p22-p21.3
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Koch J, Gartner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K: Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease. J Biol Chem. 1996 Dec 20;271(51):33110-5. [PubMed Link Image]
  2. Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, Schuchman EH, Sandhoff K: Purification, characterization, and biosynthesis of human acid ceramidase. J Biol Chem. 1995 May 12;270(19):11098-102. [PubMed Link Image]
  3. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 7061
Enzyme 13 Name Ganglioside GM2 activator precursor
Enzyme 13 Synonyms
  1. GM2-AP
  2. Cerebroside sulfate activator protein
  3. Shingolipid activator protein 3
  4. SAP-3[Contains: Ganglioside GM2 activator isoform short]
Enzyme 13 Gene Name GM2A
Enzyme 13 Protein Sequence >Ganglioside GM2 activator precursor
MQSLMQAPLLIALGLLLATPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIVV
PGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIP
TGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKR
LGCIKIAASLKGI
Enzyme 13 Number of Residues 193
Enzyme 13 Molecular Weight 20822
Enzyme 13 Theoretical pI 4.96
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 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 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function Not Available
Enzyme 13 Signals
  • 1-23
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 183357 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P17900 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name SAP3_HUMAN Link Image
Enzyme 13 PDB ID 1PU5 Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >582 bp
ATGCAGTCCCTGATGCAGGCTCCCCTCCTGATCGCCCTGGGCTTGCTTCTCGCGGCCCCT
GCGCAAGCCCACCTGAAAAAGCCATCCCAGCTCAGTAGCTTTTCCTGGGATAACTGTGAT
GAAGGGAAGGACCCTGCGGTGATCAGAAGCCTGACTCTGGAGCCTGACCCCATCGTCGTT
CCTGGAAATGTGACCCTCAGTGTCGTGGGCAGCACCAGTGTCCCCCTGAGTTCTCCTCTG
AAGGTGGATTTAGTTTTGGAGAAGGAGGTGGCTGGCCTCTGGATCAAGATCCCATGCACA
GACTACATTGGCAGCTGTACCTTTGAACACTTCTGTGATGTGCTTGACATGTTAATTCCT
ACTGGGGAGCCCTGCCCAGAGCCCCTGCGTACCTATGGGCTTCCTTGCCACTGTCCCTTC
AAAGAAGGAACCTACTCACTGCCCAAGAGCGAATTCGTTGTGCCTGACCTGGAGCTGCCC
AGTTGGCTCACCACCGGGAACTACCGCATAGAGAGCGTCCTGAGCAGCAGTGGGAAGCGT
CTGGGCTGCATCAAGATCGCTGCCTCTCTAAAGGGCATATAA
Enzyme 13 GenBank Gene ID M76477 Link Image
Enzyme 13 GeneCard ID GM2A Link Image
Enzyme 13 GenAtlas ID GM2A Link Image
Enzyme 13 HGNC ID HGNC:4367 Link Image
Enzyme 13 Chromosome Location 5
Enzyme 13 Locus 5q31.3-q33.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 7905
Enzyme 14 Name T-cell surface glycoprotein CD1e precursor
Enzyme 14 Synonyms
  1. CD1e antigen
  2. R2G1
Enzyme 14 Gene Name CD1E
Enzyme 14 Protein Sequence >T-cell surface glycoprotein CD1e precursor
MLLLFLLFEGLCCPGENTAAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTV
LGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYPFEIQILAGCR
MNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTC
PRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQE
QRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIHWGGYSIFLIL
ICLTVIVTLVILVVVDSRLKKQ
Enzyme 14 Number of Residues 322
Enzyme 14 Molecular Weight 35986
Enzyme 14 Theoretical pI 7.25
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-19
Enzyme 14 Transmembrane Regions
  • 295-315
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 296640 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P15812 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name CD1E_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >972 bp
ATGCTGCTCCTGTTCCTCCTCTTCGAGGGTCTCTGCTGTCCTGGGGAAAATACAGCAGCA
GCAGAGGAGCAGCTGTCCTTCCGCATGCTCCAAACTTCCTCCTTTGCCAACCACAGCTGG
GCACACAGTGAGGGCTCAGGATGGCTGGGTGACCTGCAGACTCATGGCTGGGACACTGTC
TTGGGCACCATCCGCTTTCTGAAGCCCTGGTCCCATGGAAACTTCAGCAAGCAGGAGCTG
AAAAACTTACAGTCACTGTTCCAGTTATACTTCCATAGTTTTATCCAGATAGTGCAAGCT
TCTGCTGGTCAATTTCAGCTTGAATACCCCTTCGAGATCCAGATATTAGCTGGCTGTAGA
ATGAATGCCCCACAAATCTTCTTAAATATGGCATATCAAGGGTCAGATTTCCTGAGTTTC
CAAGGAATTTCCTGGGAGCCATCTCCAGGAGCAGGGATCCGGGCCCAGAACATCTGTAAA
GTGCTCAATCGCTACCTAGATATTAAGGAAATACTGCAAAGCCTTCTTGGTCACACCTGC
CCTCGATTTCTAGCGGGGCTCATGGAAGCAGGGGAGTCAGAACTGAAACGGAAAGTGAAG
CCAGAGGCCTGGCTGTCCTGTGGCCCCAGTCCTGGCCCTGGCCGTCTGCAGCTTGTGTGC
CATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGTGAGCAGGAG
CAGCGGGGCACTCAGCGAGGGGACGTCCTGCCTAATGCTGACGAGACATGGTATCTCCGA
GCAACCCTGGATGTGGCGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGGGTGAAACACAGC
AGTCTAGGGGGCCATGATCTAATCATCCATTGGGGTGGATATTCCATCTTTCTCATCCTG
ATCTGTTTGACTGTGATAGTTACCCTGGTCATATTGGTTGTAGTTGACTCACGGTTAAAA
AAACAGAGGTGA
Enzyme 14 GenBank Gene ID X14975 Link Image
Enzyme 14 GeneCard ID CD1E Link Image
Enzyme 14 GenAtlas ID CD1E Link Image
Enzyme 14 HGNC ID HGNC:1638 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1q22-q23
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8060
Enzyme 15 Name Sphingosine 1-phosphate receptor Edg-6
Enzyme 15 Synonyms
  1. S1P receptor Edg-6
  2. Endothelial differentiation G-protein coupled receptor 6
  3. Sphingosine 1-phosphate receptor 4
  4. S1P4
Enzyme 15 Gene Name EDG6
Enzyme 15 Protein Sequence >Sphingosine 1-phosphate receptor Edg-6
MNATGTPVAPESCQQLAAGGHSRLIVLHYNHSGRLAGRGGPEDGGLGALRGLSVAASCLV
VLENLLVLAAITSHMRSRRWVYYCLVNITLSDLLTGAAYLANVLLSGARTFRLAPAQWFL
REGLLFTALAASTFSLLFTAGERFATMVRPVAESGATKTSRVYGFIGLCWLLAALLGMLP
LLGWNCLCAFDRCSSLLPLYSKRYILFCLVIFAGVLATIMGLYGAIFRLVQASGQKAPRP
AARRKARRLLKTVLMILLAFLVCWGPLFGLLLADVFGSNLWAQEYLRGMDWILALAVLNS
AVNPIIYSFRSREVCRAVLSFLCCGCLRLGMRGPGDCLARAVEAHSGASTTDSSLRPRDS
FRGSRSLSFRMREPLSSISSVRSI
Enzyme 15 Number of Residues 384
Enzyme 15 Molecular Weight 41624
Enzyme 15 Theoretical pI 10.26
Enzyme 15 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • 51-71 85-105 118-138 162-182 207-227 253-273 289-309
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 3805932 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O95977 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name EDG6_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1155 bp
ATGAACGCCACGGGGACCCCGGTGGCCCCCGAGTCCTGCCAACAGCTGGCGGCCGGCGGG
CACAGCCGGCTCATTGTTCTGCACTACAACCACTCGGGCCGGCTGGCCGGGCGCGGGGGG
CCGGAGGATGGCGGCCTGGGGGCCCTGCGGGGGCTGTCGGTGGCCGCCAGCTGCCTGGTG
GTGCTGGAGAACTTGCTGGTGCTGGCGGCCATCACCAGCCACATGCGGTCGCGACGCTGG
GTCTACTATTGCCTGGTGAACATCACGCTGAGTGACCTGCTCACGGGCGCGGCCTACCTG
GCCAACGTGCTGCTGTCGGGGGCCCGCACCTTCCGTCTGGCGCCCGCCCAGTGGTTCCTA
CGGGAGGGCCTGCTCTTCACCGCCCTGGCCGCCTCCACCTTCAGCCTGCTCTTCACTGCA
GGGGAGCGCTTTGCCACCATGGTGCGGCCGGTGGCCGAGAGCGGGGCCACCAAGACCAGC
CGCGTCTACGGCTTCATCGGCCTCTGCTGGCTGCTGGCCGCGCTGCTGGGGATGCTGCCT
TTGCTGGGCTGGAACTGCCTGTGCGCCTTTGACCGCTGCTCCAGCCTTCTGCCCCTCTAC
TCCAAGCGCTACATCCTCTTCTGCCTGGTGATCTTCGCCGGCGTCCTGGCCACCATCATG
GGCCTCTATGGGGCCATCTTCCGCCTGGTGCAGGCCAGCGGGCAGAAGGCCCCACGCCCA
GCGGCCCGCCGCAAGGCCCGCCGCCTGCTGAAGACGGTGCTGATGATCCTGCTGGCCTTC
CTGGTGTGCTGGGGCCCACTCTTCGGGCTGCTGCTGGCCGACGTCTTTGGCTCCAACCTC
TGGGCCCAGGAGTACCTGCGGGGCATGGACTGGATCCTGGCCCTGGCCGTCCTCAACTCG
GCGGTCAACCCCATCATCTACTCCTTCCGCAGCAGGGAGGTGTGCAGAGCCGTGCTCAGC
TTCCTCTGCTGCGGGTGTCTCCGGCTGGGCATGCGAGGGCCCGGGGACTGCCTGGCCCGG
GCCGTCGAGGCTCACTCCGGAGCTTCCACCACCGACAGCTCTCTGAGGCCAAGGGACAGC
TTTCGCGGCTCCCGCTCGCTCAGCTTTCGGATGCGGGAGCCCCTGTCCAGCATCTCCAGC
GTGCGGAGCATCTGA
Enzyme 15 GenBank Gene ID AJ000479 Link Image
Enzyme 15 GeneCard ID EDG6 Link Image
Enzyme 15 GenAtlas ID EDG6 Link Image
Enzyme 15 HGNC ID HGNC:3170 Link Image
Enzyme 15 Chromosome Location 19
Enzyme 15 Locus 19p13.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Graler MH, Bernhardt G, Lipp M: EDG6, a novel G-protein-coupled receptor related to receptors for bioactive lysophospholipids, is specifically expressed in lymphoid tissue. Genomics. 1998 Oct 15;53(2):164-9. [PubMed Link Image]
  2. Yamazaki Y, Kon J, Sato K, Tomura H, Sato M, Yoneya T, Okazaki H, Okajima F, Ohta H: Edg-6 as a putative sphingosine 1-phosphate receptor coupling to Ca(2+) signaling pathway. Biochem Biophys Res Commun. 2000 Feb 16;268(2):583-9. [PubMed Link Image]
  3. Van Brocklyn JR, Graler MH, Bernhardt G, Hobson JP, Lipp M, Spiegel S: Sphingosine-1-phosphate is a ligand for the G protein-coupled receptor EDG-6. Blood. 2000 Apr 15;95(8):2624-9. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8103
Enzyme 16 Name Sphingosine 1-phosphate receptor Edg-5
Enzyme 16 Synonyms
  1. S1P receptor Edg-5
  2. Endothelial differentiation G-protein coupled receptor 5
  3. Sphingosine 1-phosphate receptor 2
  4. S1P2
Enzyme 16 Gene Name EDG5
Enzyme 16 Protein Sequence >Sphingosine 1-phosphate receptor Edg-5
MGSLYSEYLNPNKVQEHYNYTKETLETQETTSRQVASAFIVILCCAIVVENLLVLIAVAR
NSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGSVTLRLTPVQWFAREGSAFITLSASV
FSLLAIAIERHVAIAKVKLYGSDKSCRMLLLIGASWLISLVLGGLPILGWNCLGHLEACS
TVLPLYAKHYVLCVVTIFSIILLAIVALYVRIYCVVRSSHADMAAPQTLALLKTVTIVLG
VFIVCWLPAFSILLLDYACPVHSCPILYKAHYFFAVSTLNSLLNPVIYTWRSRDLRREVL
RPLQCWRPGVGVQGRRRGGTPGHHLLPLRSSSSLERGMHMPTSPTFLEGNTVV
Enzyme 16 Number of Residues 353
Enzyme 16 Molecular Weight 38867
Enzyme 16 Theoretical pI 9.10
Enzyme 16 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 35-59 67-95 110-128 148-173 190-210 234-255 272-292
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 4090956 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O95136 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name EDG5_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1062 bp
ATGGGCAGCTTGTACTCGGAGTACCTGAACCCCAACAAGGTCCAGGAACACTATAATTAT
ACCAAGGAGACGCTGGAAACGCAGGAGACGACCTCCCGCCAGGTGGCCTCGGCCTTCATC
GTCATCCTCTGTTGCGCCATTGTGGTGGAAAACCTTCTGGTGCTCATTGCGGTGGCCCGA
AACAGCAAGTTCCACTCGGCAATGTACCTGTTTCTGGGCAACCTGGCCGCCTCCGATCTA
CTGGCAGGCGTGGCCTTCGTAGCCAATACCTTGCTCTCTGGCTCTGTCACGCTGAGGCTG
ACGCCTGTGCAGTGGTTTGCCCGGGAGGGCTCTGCCTCCATCACGCTCTCGGCCTCTGTC
TTCAGCCTCCTGGCCATCGCCATTGAGCGCCACGTGGCCATTGCCAAGGTCAAGCTGTAT
GGCAGCGACAAGAGCTGCCGCATGCTTCTGCTCATCGGGGCCTCGTGGCTCATCTCGCTG
GTCCTCGGTGGCCTGCCCATCCTTGGCTGGAACTGCCTGGGCCACCTCGAGGCCTGCTCC
ACTGTCCTGCCTCTCTACGCCAAGCATTATGTGCTGTGCGTGGTGACCATCTTCTCCATC
ATCCTGTTGGCCATCGTGGCCCTGTACGTGCGCATCTACTGCGTGGTCCGCTCAAGCCAC
GCTGACATGGCCGCCCCGCAGACGCTAGCCCTGCTCAAGACGGTCACCATCGTGCTAGGC
GTCTTTATCGTCTGCTGGCTGCCCGCCTTCAGCATCCTCCTTCTGGACTATGCCTGTCCC
GTCCACTCCTGCCCGATCCTCTACAAAGCCCACTACTTTTTCGCCGTCTCCACCCTGAAT
TCCCTGCTCAACCCCGTCATCTACACGTGGCGCAGCCGGGACCTGCGGCGGGAGGTGCTT
CGGCCGCTGCAGTGCTGGCGGCCGGGGGTGGGGGTGCAAGGACGGAGGCGGGTCGGGACC
CCGGGCCACCACCTCCTGCCACTCCGCAGCTCCAGCTCCCTGGAGAGGGGCATGCACATG
CCCACGTCACCCACGTTTCTGGAGGGCAACACGGTGGTCTGA
Enzyme 16 GenBank Gene ID AF034780 Link Image
Enzyme 16 GeneCard ID EDG5 Link Image
Enzyme 16 GenAtlas ID EDG5 Link Image
Enzyme 16 HGNC ID HGNC:3169 Link Image
Enzyme 16 Chromosome Location 19
Enzyme 16 Locus 19p13.2
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8178
Enzyme 17 Name Epididymal secretory protein E1 precursor
Enzyme 17 Synonyms
  1. Niemann-Pick disease type C2 protein
  2. hE1
Enzyme 17 Gene Name NPC2
Enzyme 17 Protein Sequence >Epididymal secretory protein E1 precursor
MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVT
FTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYP
SIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL
Enzyme 17 Number of Residues 151
Enzyme 17 Molecular Weight 16570
Enzyme 17 Theoretical pI 7.77
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function May be involved in the regulation of the lipid composition of sperm membranes during the maturation in the epididymis
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-19
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 37477 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P61916 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name NPC2_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >456 bp
ATGCGTTTCCTGGCAGCTACATTCCTGCTCCTGGCGCTCAGCACCGCTGCCCAGGCCGAA
CCGGTGCAGTTCAAGGACTGCGGTTCTGTGGATGGAGTTATAAAGGAAGTGAATGTGAGC
CCATGCCCCACCCAACCCTGCCAGCTGAGCAAAGGACAGTCTTACAGCGTCAATGTCACC
TTCACCAGCAATATTCAGTCTAAAAGCAGCAAGGCCGTGGTGCATGGCATCCTGATGGGC
GTCCCAGTTCCCTTTCCCATTCCTGAGCCTGATGGTTGTAAGAGTGGAATTAACTGCCCT
ATCCAAAAAGACAAGACCTATAGCTACCTGAATAAACTACCAGTGAAAAGCGAATATCCC
TCTATAAAACTGGTGGTGGAGTGGCAACTTCAGGATGACAAAAACCAAAGTCTCTTCTGC
TGGGAAATCCCAGTACAGATCGTTTCTCATCTCTAA
Enzyme 17 GenBank Gene ID X67698 Link Image
Enzyme 17 GeneCard ID NPC2 Link Image
Enzyme 17 GenAtlas ID NPC2 Link Image
Enzyme 17 HGNC ID HGNC:14537 Link Image
Enzyme 17 Chromosome Location 14
Enzyme 17 Locus 14q24.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8182
Enzyme 18 Name Sphingosine 1-phosphate receptor Edg-1
Enzyme 18 Synonyms
  1. Sphingosine 1-phosphate receptor 1
  2. S1P1
Enzyme 18 Gene Name EDG1
Enzyme 18 Protein Sequence >Sphingosine 1-phosphate receptor Edg-1
MGPTSVPLVKAHRSSVSDYVNYDIIVRHYNYTGKLNISADKENSIKLTSVVFILICCFII
LENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLR
EGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNNFRLFLLISACWVISLILGGLPIM
GWNCISALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKN
ISKASRSSENVALLKTVIIVLSVFIACWAPLFILLLLDVGCKVKTCDILFRAEYFLVLAV
LNSGTNPIIYTLTNKEMRRAFIRIMSCCKCPSGDSAGKFKRPIIAGMEFSRSKSDNSSHP
QKDEGDNPETIMSSGNVNSSS
Enzyme 18 Number of Residues 381
Enzyme 18 Molecular Weight 42696
Enzyme 18 Theoretical pI 9.85
Enzyme 18 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. This inducible epithelial cell G-protein-coupled receptor may be involved in the processes that regulate the differentiation of endothelial cells. Seems to be coupled to the G(i) subclass of heteromeric G proteins
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 47-71 79-107 122-140 160-185 202-222 256-277 294-314
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 181949 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P21453 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name EDG1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1146 bp
ATGGGGCCCACCAGCGTCCCGCTGGTCAAGGCCCACCGCAGCTCGGTCTCTGACTACGTC
AACTATGATATCATCGTCCGGCATTACAACTACACGGGAAAGCTGAATATCAGCGCGGAC
AAGGAGAACAGCATTAAACTGACCTCGGTGGTGTTCATTCTCATCTGCTGCTTTATCATC
CTGGAGAACATCTTTGTCTTGCTGACCATTTGGAAAACCAAGAAATTCCACCGACCCATG
TACTATTTTATTGGCAATCTGGCCCTCTCAGACCTGTTGGCAGGAGTAGCCTACACAGCT
AACCTGCTCTTGTCTGGGGCCACCACCTACAAGCTCACTCCCGCCCAGTGGTTTCTGCGG
GAAGGGAGTATGTTTGTGGCCCTGTCAGCCTCCGTGTTCAGTCTCCTCGCCATCGCCATT
GAGCGCTATATCACAATGCTGAAAATGAAACTCCACAACGGGAGCAATAACTTCCGCCTC
TTCCTGCTAATCAGCGCCTGCTGGGTCATCTCCCTCATCCTGGGTGGCCTGCCTATCATG
GGCTGGAACTGCATCAGTGCGCTGTCCAGCTGCTCCACCGTGCTGCCGCTCTACCACAAG
CACTATATCCTCTTCTGCACCACGGTCTTCACTCTGCTTCTGCTCTCCATCGTCATTCTG
TACTGCAGAATCTACTCCTTGGTCAGGACTCGGAGCCGCCGCCTGACGTTCCGCAAGAAC
ATTTCCAAGGCCAGCCGCAGCTCTGAGAATGTGGCGCTGCTCAAGACCGTAATTATCGTC
CTGAGCGTCTTCATCGCCTGCTGGGCACCGCTCTTCATCCTGCTCCTGCTGGATGTGGGC
TGCAAGGTGAAGACCTGTGACATCCTCTTCAGAGCGGAGTACTTCCTGGTGTTAGCTGTG
CTCAACTCCGGCACCAACCCCATCATTTACACTCTGACCAACAAGGAGATGCGTCGGGCC
TTCATCCGGATCATGTCCTGCTGCAAGTGCCCGAGCGGAGACTCTGCTGGCAAATTCAAG
CGACCCATCATCGCCGGCATGGAATTCAGCCGCAGCAAATCGGACAATTCCTCCCACCCC
CAGAAAGACGAAGGGGACAACCCAGAGACCATTATGTCTTCTGGAAACGTCAACTCTTCT
TCCTAG
Enzyme 18 GenBank Gene ID M31210 Link Image
Enzyme 18 GeneCard ID EDG1 Link Image
Enzyme 18 GenAtlas ID EDG1 Link Image
Enzyme 18 HGNC ID HGNC:3165 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p21
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Hla T, Maciag T: An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors. J Biol Chem. 1990 Jun 5;265(16):9308-13. [PubMed Link Image]
  2. An S, Bleu T, Huang W, Hallmark OG, Coughlin SR, Goetzl EJ: Identification of cDNAs encoding two G protein-coupled receptors for lysosphingolipids. FEBS Lett. 1997 Nov 17;417(3):279-82. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 8276
Enzyme 19 Name Sphingosine 1-phosphate receptor Edg-8
Enzyme 19 Synonyms
  1. Endothelial differentiation sphingolipid G-protein-coupled receptor 8
  2. Sphingosine 1-phosphate receptor 5
  3. S1P5
Enzyme 19 Gene Name EDG8
Enzyme 19 Protein Sequence >Sphingosine 1-phosphate receptor Edg-8
MESGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAVVCLAVCAFIVLENLAVLLV
LGRHPRFHAPMFLLLGSLTLSDLLAGAAYAANILLSGPLTLKLSPALWFAREGGVFVALT
ASVLSLLAIALERSLTMARRGPAPVSSRGRTLAMAAAAWGVSLLLGLLPALGWNCLGRLD
ACSTVLPLYAKAYVLFCVLAFVGILAAICALYARIYCQVRANARRLPARPGTAGTTSTRA
RRKPRSLALLRTLSVVLLAFVACWGPLFLLLLLDVACPARTCPVLLQADPFLGLAMANSL
LNPIIYTLTNRDLRHALLRLVCCGRHSCGRDPSGSQQSASAAEASGGLRRCLPPGLDGSF
SGSERSSPQRDGLDTSGSTGSPGAPTAARTLVSEPAAD
Enzyme 19 Number of Residues 398
Enzyme 19 Molecular Weight 41776
Enzyme 19 Theoretical pI 9.98
Enzyme 19 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/0)alpha and G(12) subclass of heteromeric G-proteins. May play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 41-61 71-91 112-132 152-172 193-213 253-273 288-308
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 18033257 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9H228 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name EDG8_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1197 bp
ATGGAGTCGGGGCTGCTGCGGCCGGCGCCGGTGAGCGAGGTCATCGTCCTGCATTACAAC
TACACCGGCAAGCTCCGCGGTGCGCGCTACCAGCCGGGTGCCGGCCTGCGCGCCGACGCC
GTGGTGTGCCTGGCGGTGTGCGCCTTCATCGTGCTAGAGAATCTAGCCGTGTTGTTGGTG
CTCGGACGCCACCCGCGCTTCCACGCTCCCATGTTCCTGCTCCTGGGCAGCCTCACGTTG
TCGGATCTGCTGGCAGGCGCCGCCTACGCCGCCAACATCCTACTGTCGGGGCCGCTCACG
CTGAAACTGTCCCCCGCGCTCTGGTTCGCACGGGAGGGAGGCGTCTTCGTGGCACTCACT
GCGTCCGTGCTGAGCCTCCTGGCCATCGCGCTGGAGCGCAGCCTCACCATGGCGCGCAGG
GGGCCCGCGCCCGTCTCCAGTCGGGGGCGCACGCTGGCGATGGCAGCCGCGGCCTGGGGC
GTGTCGCTGCTCCTCGGGCTCCTGCCAGCGCTGGGCTGGAATTGCCTGGGTCGCCTGGAC
GCTTGCTCCACTGTCTTGCCGCTCTACGCCAAGGCCTACGTGCTCTTCTGCGTGCTCGCC
TTCGTGGGCATCCTGGCCGCGATCTGTGCACTCTACGCGCGCATCTACTGCCAGGTACGC
GCCAACGCGCGGCGCCTGCCGGCACGGCCCGGGACTGCGGGGACCACCTCGACCCGGGCG
CGTCGCAAGCCGCGCTCGCTGGCCTTGCTGCGCACGCTCAGCGTGGTGCTCCTGGCCTTT
GTGGCATGTTGGGGCCCCCTCTTCCTGCTGCTGTTGCTCGACGTGGCGTGCCCGGCGCGC
ACCTGTCCTGTACTCCTGCAGGCCGATCCCTTCCTGGGACTGGCCATGGCCAACTCACTT
CTGAACCCCATCATCTACACGCTCACCAACCGCGACCTGCGCCACGCGCTCCTGCGCCTG
GTCTGCTGCGGACGCCACTCCTGCGGCAGAGACCCGAGTGGCTCCCAGCAGTCGGCGAGC
GCGGCTGAGGCTTCCGGGGGCCTGCGCCGCTGCCTGCCCCCGGGCCTTGATGGGAGCTTC
AGCGGCTCGGAGCGCTCATCGCCCCAGCGCGACGGGCTGGACACCAGCGGCTCCACAGGC
AGCCCCGGTGCACCCACAGCCGCCCGGACTCTGGTATCAGAACCGGCTGCAGACTGA
Enzyme 19 GenBank Gene ID AF331840 Link Image
Enzyme 19 GeneCard ID EDG8 Link Image
Enzyme 19 GenAtlas ID EDG8 Link Image
Enzyme 19 HGNC ID HGNC:14299 Link Image
Enzyme 19 Chromosome Location 19
Enzyme 19 Locus 19p13.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8289
Enzyme 20 Name T-cell surface glycoprotein CD1d precursor
Enzyme 20 Synonyms
  1. CD1d antigen
  2. R3G1
Enzyme 20 Gene Name CD1D
Enzyme 20 Protein Sequence >T-cell surface glycoprotein CD1d precursor
MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSN
DSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGC
EVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLL
NGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMR
GEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYT
SMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL
Enzyme 20 Number of Residues 335
Enzyme 20 Molecular Weight 37718
Enzyme 20 Theoretical pI 8.28
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Not known
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-19
Enzyme 20 Transmembrane Regions
  • 302-322
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 619798 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P15813 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name CD1D_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1008 bp
ATGGGGTGCCTGCTGTTTCTGCTGCTCTGGGCGCTCCTCCAGGCTTGGGGAAGCGCTGAA
GTCCCGCAAAGGCTTTTCCCCCTCCGCTGCCTCCAGATCTCGTCCTTCGCCAATAGCAGC
TGGACGCGCACCGACGGCTTGGCGTGGCTGGGGGAGCTGCAGACGCACAGCTGGAGCAAC
GACTCGGACACCGTCCGCTCTCTGAAGCCTTGGTCCCAGGGCACGTTCAGCGACCAGCAG
TGGGAGACGCTGCAGCATATATTTCGGGTTTATCGAAGCAGCTTCACCAGGGACGTGAAG
GAATTCGCCAAAATGCTACGCTTATCCTATCCCTTGGAGCTCCAGGTGTCCGCTGGCTGT
GAGGTGCACCCTGGGAACGCCTCAAATAACTTCTTCCATGTAGCATTTCAAGGAAAAGAT
ATCCTGAGTTTCCAAGGAACTTCTTGGGAGCCAACCCAAGAGGCCCCACTTTGGGTAAAC
TTGGCCATTCAAGTGCTCAACCAGGACAAGTGGACGAGGGAAACAGTGCAGTGGCTCCTT
AATGGCACCTGCCCCCAATTTGTCAGTGGCCTCCTTGAGTCAGGGAAGTCGGAACTGAAG
AAGCAAGTGAAGCCCAAGGCCTGGCTGTCCCGTGGCCCCAGTCCTGGCCCTGGCCGTCTG
CTGCTGGTGTGCCATGTCTCAGGATTCTACCCAAAGCCTGTATGGGTGAAGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCCAGGGGACATCCTGCCCAATGCTGACGAGACA
TGGTATCTCCGAGCAACCCTGGATGTGGTGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGGTGGGAGCTACACC
TCCATGGGCTTGATTGCCTTGGCAGTCCTGGCGTGCTTGCTGTTCCTCCTCATTGTGGGC
TTTACCTCCCGGTTTAAGAGGCAAACTTCCTATCAGGGCGTCCTGTGA
Enzyme 20 GenBank Gene ID L38820 Link Image
Enzyme 20 GeneCard ID CD1D Link Image
Enzyme 20 GenAtlas ID CD1D Link Image
Enzyme 20 HGNC ID HGNC:1637 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 1q22-q23
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 8469
Enzyme 21 Name GPI mannosyltransferase 1
Enzyme 21 Synonyms
  1. GPI mannosyltransferase I
  2. GPI-MT-I
  3. Phosphatidylinositol-glycan biosynthesis class M protein
  4. PIG-M
Enzyme 21 Gene Name PIGM
Enzyme 21 Protein Sequence >GPI mannosyltransferase 1
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
Enzyme 21 Number of Residues 423
Enzyme 21 Molecular Weight 49460
Enzyme 21 Theoretical pI 9.31
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-369
Enzyme 21 Transmembrane Regions
  • 18-38 80-100 139-161 170-190 226-246 288-308 315-337 339-350 358-378 385-405
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 11414879 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9H3S5 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PIGM_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID AB028127 Link Image
Enzyme 21 GeneCard ID PIGM Link Image
Enzyme 21 GenAtlas ID PIGM Link Image
Enzyme 21 HGNC ID HGNC:18858 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 1q23.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 8495
Enzyme 22 Name Phosphatidylinositol-glycan biosynthesis class W protein
Enzyme 22 Synonyms
  1. PIG-W
Enzyme 22 Gene Name PIGW
Enzyme 22 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class W protein
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
Enzyme 22 Number of Residues 504
Enzyme 22 Molecular Weight 56883
Enzyme 22 Theoretical pI 9.44
Enzyme 22 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 22 General Function Not Available
Enzyme 22 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 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-43
Enzyme 22 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 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID Q7Z7B1 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PIGW_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 AB097818 Link Image
Enzyme 22 GeneCard ID PIGW Link Image
Enzyme 22 GenAtlas ID PIGW Link Image
Enzyme 22 HGNC ID HGNC:23213 Link Image
Enzyme 22 Chromosome Location 17
Enzyme 22 Locus 17q12
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8621
Enzyme 23 Name Phosphatidylinositol-glycan biosynthesis class X protein precursor
Enzyme 23 Synonyms
  1. PIG-X
Enzyme 23 Gene Name PIGX
Enzyme 23 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class X protein precursor
MAARVAAVRAAAWLLLGAATGLTRGPATAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALDNEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
Enzyme 23 Number of Residues 258
Enzyme 23 Molecular Weight 28805
Enzyme 23 Theoretical pI 6.30
Enzyme 23 GO Classification Not Available
Enzyme 23 General Function Not Available
Enzyme 23 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 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-21
Enzyme 23 Transmembrane Regions
  • 231-251
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 18490317 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q8TBF5 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PIGX_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >654 bp
ATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGACCTT
TTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACGTGCCGTCTCTTAATT
AAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGAGAG
AGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAACTAT
TTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGACTGT
TTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGAGAA
GCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCGATT
TTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGATAATGAGGATATA
TGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTTCCA
GTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATCCTG
TGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
Enzyme 23 GenBank Gene ID BC022542 Link Image
Enzyme 23 GeneCard ID PIGX Link Image
Enzyme 23 GenAtlas ID PIGX Link Image
Enzyme 23 HGNC ID HGNC:26046 Link Image
Enzyme 23 Chromosome Location 3
Enzyme 23 Locus 3q29
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References Not Available
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 8625
Enzyme 24 Name GPI mannosyltransferase 4
Enzyme 24 Synonyms
  1. GPI mannosyltransferase IV
  2. GPI-MT-IV
  3. Phosphatidylinositol-glycan biosynthesis class Z protein
  4. PIG-Z
  5. hSMP3
Enzyme 24 Gene Name PIGZ
Enzyme 24 Protein Sequence >GPI mannosyltransferase 4
MAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCR
SVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPM
GADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRW
RSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGATLTAAV
FVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHA
QALQAAWQQLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARF
LIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVL
PSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDIGGTEDWALCQTLKSFTRQPACQVA
GGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLH
IVELGEET
Enzyme 24 Number of Residues 548
Enzyme 24 Molecular Weight 60249
Enzyme 24 Theoretical pI 8.40
Enzyme 24 GO Classification Not Available
Enzyme 24 General Function Not Available
Enzyme 24 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 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-28
Enzyme 24 Transmembrane Regions
  • 100-120 125-142 149-169 185-205 227-247 338-358
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID Q86VD9 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PIGZ_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 AK022830 Link Image
Enzyme 24 GeneCard ID PIGZ Link Image
Enzyme 24 GenAtlas ID PIGZ Link Image
Enzyme 24 HGNC ID HGNC:30596 Link Image
Enzyme 24 Chromosome Location 3
Enzyme 24 Locus 3q29
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 11996
Enzyme 25 Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
Enzyme 25 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 25 Gene Name B3GNT5
Enzyme 25 Protein Sequence >UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
Enzyme 25 Number of Residues 378
Enzyme 25 Molecular Weight 44053
Enzyme 25 Theoretical pI Not Available
Enzyme 25 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 25 General Function Not Available
Enzyme 25 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 25 Pathways Not Available
Enzyme 25 Reactions
  • galactosyl glucosyl ceramide + UDP-N-acetyl-D-glucosamine --> (Gal)1 (Glc)1 (GlcNAc)1 (Cer)1 + H+ + UDP
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 15-35
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 13568434 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q9BYG0 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name B3GN5_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 AB045278 Link Image
Enzyme 25 GeneCard ID Not Available
Enzyme 25 GenAtlas ID B3GNT5 Link Image
Enzyme 25 HGNC ID HGNC:15684 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. 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 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 12558
Enzyme 26 Name Beta-1,3-galactosyltransferase 5
Enzyme 26 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 26 Gene Name B3GALT5
Enzyme 26 Protein Sequence >Beta-1,3-galactosyltransferase 5
MAFPKMRLMYICLLVLGALCLYFSMYSLNPFKEQSFVYKKDGNFLKLPDTDCRQTPPFLV
LLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVDQESQRHGDII
QKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFF
TGFLKLNEFPIRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIK
LEDVFVGLCLERLNIRLEELHSQPTFFPGGLRFSVCLFRRIVACHFIKPRTLLDYWQALE
NSRGEDCPPV
Enzyme 26 Number of Residues 310
Enzyme 26 Molecular Weight 36190
Enzyme 26 Theoretical pI Not Available
Enzyme 26 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 26 General Function Not Available
Enzyme 26 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 26 Pathways Not Available
Enzyme 26 Reactions
  • globoside (homo sapiens) + UDPgalactose --> galactosylgloboside (homo sapiens) + H+ + UDP
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 8-28
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 4835503 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9Y2C3 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name B3GT5_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 AB020337 Link Image
Enzyme 26 GeneCard ID Not Available
Enzyme 26 GenAtlas ID B3GALT5 Link Image
Enzyme 26 HGNC ID HGNC:920 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. 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 12947
Enzyme 27 Name GPI mannosyltransferase 3
Enzyme 27 Synonyms
  1. GPI mannosyltransferase III
  2. GPI-MT-III
  3. Phosphatidylinositol-glycan biosynthesis class B protein
  4. PIG-B
Enzyme 27 Gene Name PIGB
Enzyme 27 Protein Sequence >GPI mannosyltransferase 3
MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGEN
IYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLI
FASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLC
SWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWT
PLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWG
TFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEF
RFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQK
VCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNP
LNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVY
ERKLKGKFNMKMKF
Enzyme 27 Number of Residues 554
Enzyme 27 Molecular Weight 65057
Enzyme 27 Theoretical pI 9.57
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Not Available
Enzyme 27 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 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • 63-83 136-156 192-212 224-244 255-275 315-335 340-360 362-382 387-407
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 1552169 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q92521 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PIGB_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 D42138 Link Image
Enzyme 27 GeneCard ID Q92521 Link Image
Enzyme 27 GenAtlas ID PIGB Link Image
Enzyme 27 HGNC ID HGNC:8959 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. 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 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 12948
Enzyme 28 Name Phosphatidylinositol-glycan biosynthesis class F protein
Enzyme 28 Synonyms
  1. PIG-F
  2. GPI11 homolog
Enzyme 28 Gene Name PIGF
Enzyme 28 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class F protein
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYL
VVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILS
TFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERP
WQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
Enzyme 28 Number of Residues 219
Enzyme 28 Molecular Weight 24890
Enzyme 28 Theoretical pI 8.64
Enzyme 28 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 28 General Function Not Available
Enzyme 28 Specific Function Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • 11-31 42-62 86-106 113-133 155-175 189-209
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 303616 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q07326 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PIGF_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 D13435 Link Image
Enzyme 28 GeneCard ID Q07326 Link Image
Enzyme 28 GenAtlas ID PIGF Link Image
Enzyme 28 HGNC ID HGNC:8962 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. 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 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 12949
Enzyme 29 Name GPI ethanolamine phosphate transferase 2
Enzyme 29 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class G protein
  2. PIG-G
  3. GPI7 homolog
  4. hGPI7
Enzyme 29 Gene Name PIGG
Enzyme 29 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 29 Number of Residues 983
Enzyme 29 Molecular Weight 108174
Enzyme 29 Theoretical pI 7.15
Enzyme 29 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 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 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 58430451 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q5H8A4 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PIGG_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 AB162713 Link Image
Enzyme 29 GeneCard ID Q5H8A4 Link Image
Enzyme 29 GenAtlas ID PIGG Link Image
Enzyme 29 HGNC ID HGNC:25985 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]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 12950
Enzyme 30 Name GPI ethanolamine phosphate transferase 1
Enzyme 30 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class N protein
  2. PIG-N
  3. MCD4 homolog
Enzyme 30 Gene Name PIGN
Enzyme 30 Protein Sequence >GPI ethanolamine phosphate transferase 1
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALY
ELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENP
VEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFD
NVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKE
IVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ
FDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESM
FTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSL
CKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKP
SHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP
LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSL
LLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLST
VLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMST
YLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLY
LDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFV
LVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMS
MTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Enzyme 30 Number of Residues 931
Enzyme 30 Molecular Weight 105811
Enzyme 30 Theoretical pI 8.87
Enzyme 30 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 30 General Function Not Available
Enzyme 30 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 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 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 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 4206155 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID O95427 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PIGN_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 AF109219 Link Image
Enzyme 30 GeneCard ID O95427 Link Image
Enzyme 30 GenAtlas ID PIGN Link Image
Enzyme 30 HGNC ID HGNC:8967 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 12951
Enzyme 31 Name GPI ethanolamine phosphate transferase 3
Enzyme 31 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class O protein
  2. PIG-O
Enzyme 31 Gene Name PIGO
Enzyme 31 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 31 Number of Residues 1089
Enzyme 31 Molecular Weight 118700
Enzyme 31 Theoretical pI 8.18
Enzyme 31 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 31 General Function Not Available
Enzyme 31 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 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 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 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 21739535 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q8TEQ8 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PIGO_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 AL833956 Link Image
Enzyme 31 GeneCard ID Q8TEQ8 Link Image
Enzyme 31 GenAtlas ID PIGO Link Image
Enzyme 31 HGNC ID HGNC:23215 Link Image
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 12952
Enzyme 32 Name GPI transamidase component PIG-S
Enzyme 32 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class S protein
Enzyme 32 Gene Name PIGS
Enzyme 32 Protein Sequence >GPI transamidase component PIG-S
MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLR
LMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALS
SGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFN
IIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKS
HDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSL
PHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIM
VYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMT
WELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELA
SGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKI
FLETRKSWRKPEKTD
Enzyme 32 Number of Residues 555
Enzyme 32 Molecular Weight 61657
Enzyme 32 Theoretical pI 6.46
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function Not Available
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 19-39 521-541
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 14456613 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q96S52 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PIGS_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 AB057723 Link Image
Enzyme 32 GeneCard ID Q96S52 Link Image
Enzyme 32 GenAtlas ID PIGS Link Image
Enzyme 32 HGNC ID HGNC:14937 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. 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 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 12953
Enzyme 33 Name GPI transamidase component PIG-T precursor
Enzyme 33 Synonyms
  1. Phosphatidylinositol- glycan biosynthesis class T protein
Enzyme 33 Gene Name PIGT
Enzyme 33 Protein Sequence >GPI transamidase component PIG-T precursor
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQR
EGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTV
TDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREV
VCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQ
TLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPP
TTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSG
YGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQ
DRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVA
AKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCY
GSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
Enzyme 33 Number of Residues 578
Enzyme 33 Molecular Weight 65700
Enzyme 33 Theoretical pI 8.49
Enzyme 33 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • protein complex
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-21
Enzyme 33 Transmembrane Regions
  • 528-548
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 14456615 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q969N2 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PIGT_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 AB057724 Link Image
Enzyme 33 GeneCard ID Q969N2 Link Image
Enzyme 33 GenAtlas ID PIGT Link Image
Enzyme 33 HGNC ID HGNC:14938 Link Image
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 12954
Enzyme 34 Name Phosphatidylinositol glycan anchor biosynthesis class U protein
Enzyme 34 Synonyms
  1. GPI transamidase component PIG-U
  2. Cell division cycle protein 91-like 1
  3. Protein CDC91-like 1
Enzyme 34 Gene Name PIGU
Enzyme 34 Protein Sequence >Phosphatidylinositol glycan anchor biosynthesis class U protein
MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSG
AVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYA
PDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAF
LSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVI
ICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFY
TIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTC
IIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGL
YLTAKDGTEAMLVLK
Enzyme 34 Number of Residues 435
Enzyme 34 Molecular Weight 50052
Enzyme 34 Theoretical pI 7.82
Enzyme 34 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 34 General Function Not Available
Enzyme 34 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 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 66-86 166-186 188-208 237-257 259-279 286-306 313-333 355-375 386-406
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 27372217 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9H490 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name PIGU_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence Not Available
Enzyme 34 GenBank Gene ID AB086842 Link Image
Enzyme 34 GeneCard ID Q9H490 Link Image
Enzyme 34 GenAtlas ID PIGU Link Image
Enzyme 34 HGNC ID HGNC:15791 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. 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 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 12955
Enzyme 35 Name GPI mannosyltransferase 2
Enzyme 35 Synonyms
  1. GPI mannosyltransferase II
  2. GPI-MT-II
  3. Phosphatidylinositol-glycan biosynthesis class V protein
  4. PIG-V
Enzyme 35 Gene Name PIGV
Enzyme 35 Protein Sequence >GPI mannosyltransferase 2
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLL
GGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVA
SLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSA
MGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMAS
LFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDV
PLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQR
SKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSSTPIMYWFPAHL
LQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWL
LGLLLHCNFLPWT
Enzyme 35 Number of Residues 493
Enzyme 35 Molecular Weight 55713
Enzyme 35 Theoretical pI 8.03
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 14-34 78-98 114-134 137-157 162-182 193-213 235-255 328-348 379-399 470-490
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 7020604 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9NUD9 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name PIGV_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence Not Available
Enzyme 35 GenBank Gene ID AK000484 Link Image
Enzyme 35 GeneCard ID Q9NUD9 Link Image
Enzyme 35 GenAtlas ID PIGV Link Image
Enzyme 35 HGNC ID HGNC:26031 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References Not Available
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 12956
Enzyme 36 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
Enzyme 36 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class Y protein
  2. PIG-Y
Enzyme 36 Gene Name PIGY
Enzyme 36 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLW
TWMGIKLFRHN
Enzyme 36 Number of Residues 71
Enzyme 36 Molecular Weight 8058
Enzyme 36 Theoretical pI 7.41
Enzyme 36 GO Classification Not Available
Enzyme 36 General Function Not Available
Enzyme 36 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 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function Not Available
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 4-26 45-65
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 75674192 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q3MUY2 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name PIGY_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 AB206972 Link Image
Enzyme 36 GeneCard ID Q3MUY2 Link Image
Enzyme 36 GenAtlas ID PIGY Link Image
Enzyme 36 HGNC ID HGNC:28213 Link Image
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 12961
Enzyme 37 Name Pleckstrin homology domain-containing family A member 8
Enzyme 37 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 37 Gene Name PLEKHA8
Enzyme 37 Protein Sequence >Pleckstrin homology domain-containing family A member 8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGDHRKE
AFSIGMQRDLSLYLPAMKKQMAILDALYEVHGLESDEVV
Enzyme 37 Number of Residues 519
Enzyme 37 Molecular Weight 58307
Enzyme 37 Theoretical pI 4.89
Enzyme 37 GO Classification Not Available
Enzyme 37 General Function Not Available
Enzyme 37 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 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 14165198 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q96JA3 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name PKHA8_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 AF380162 Link Image
Enzyme 37 GeneCard ID Q96JA3 Link Image
Enzyme 37 GenAtlas ID PLEKHA8 Link Image
Enzyme 37 HGNC ID HGNC:30037 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 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 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 13104
Enzyme 38 Name Sphingosine-1-phosphate phosphotase 2
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name SGPP2
Enzyme 38 Protein Sequence >Sphingosine-1-phosphate phosphotase 2
MAELLRSLQDSQLVARFQRRCGLFPAPDEGPRENGADPTERAARVPGVEHLPAANGKGGE
APANGLRRAAAPEAYVQKYVVKNYFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRR
LIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLIS
TMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAWTFID
CLDSASPLFPVCVIVVPFFLCYNYPVSDYYSPTRADTTTILAAGAGVTIGFWINHFFQLV
SKPAESLPVIQNIPPLTTYMLVLGLTKFAVGIVLILLVRQLVQNLSLQVLYSWFKVVTRN
KEARRRLEIEVPYKFVTYTSVGICATTFVPMLHRFLGLP
Enzyme 38 Number of Residues 399
Enzyme 38 Molecular Weight 44741
Enzyme 38 Theoretical pI 9.25
Enzyme 38 GO Classification Not Available
Enzyme 38 General Function Lipid transport and metabolism
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 126632031 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID A3KPB4 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name A3KPB4_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence Not Available
Enzyme 38 GenBank Gene ID BC134342 Link Image
Enzyme 38 GeneCard ID A3KPB4 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID Not Available
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 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 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 13105
Enzyme 39 Name N-acylsphingosine amidohydrolase 3-like
Enzyme 39 Synonyms Not Available
Enzyme 39 Gene Name Not Available
Enzyme 39 Protein Sequence >N-acylsphingosine amidohydrolase 3-like
MGAPHWWDQLQAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCF
NSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAVLWVLMCALAMWFPRRYLPKIFRN
DRGRFKVVVSVLSAVTTCLAFVKPAINNISLMTLGVPCTALLIAELKRCDNMRVFKLGLF
SGLWWTLALFCWISDRAFCELLSSFNFPYLHCMWHILICLAAYLGCVCFAYFDAASEIPE
QGPVIKFWPNEKWAFIGVPYVSLLCANKKSSVKIT
Enzyme 39 Number of Residues 275
Enzyme 39 Molecular Weight 31309
Enzyme 39 Theoretical pI 7.71
Enzyme 39 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • cellular lipid metabolism
  • ceramide metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • sphingoid metabolism
  • sphingolipid metabolism
Component
  • Golgi membrane
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 39 General Function Not Available
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 Not Available
Enzyme 39 UniProtKB/Swiss-Prot ID A2A3R8 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name A2A3R8_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence Not Available
Enzyme 39 GenBank Gene ID AL391834 Link Image
Enzyme 39 GeneCard ID A2A3R8 Link Image
Enzyme 39 GenAtlas ID Not Available
Enzyme 39 HGNC ID Not Available
Enzyme 39 Chromosome Location Not Available
Enzyme 39 Locus Not Available
Enzyme 39 SNPs Not Available
Enzyme 39 General References Not Available
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 13425
Enzyme 40 Name Sphingosine 1-phosphate receptor GPR6
Enzyme 40 Synonyms
  1. G-protein coupled receptor 6
Enzyme 40 Gene Name GPR6
Enzyme 40 Protein Sequence >Sphingosine 1-phosphate receptor GPR6
MNASAASLNDSQVVVVAAEGAAAAATAAGGPDTGEWGPPAAAALGAGGGANGSLELSSQL
SAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLVGSLATADLL
AGCGLILHFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNALTYYSRR
TLLGVHLLLAATWTVSLGLGLLPVLGWNCLAERAACSVVRPLARSHVALLSAAFFMVFGI
MLHLYVRICQVVWRHAHQIALQQHCLAPPHLAATRKGVGTLAVVLGTFGASWLPFAIYCV
VGSHEDPAVYTYATLLPATYNSMINPIIYAFRNQEIQRALWLLLCGCFQSKVPFRSRSPS
EV
Enzyme 40 Number of Residues 362
Enzyme 40 Molecular Weight 37882
Enzyme 40 Theoretical pI 7.74
Enzyme 40 GO Classification
Function
  • G-protein coupled receptor activity
  • G-protein coupled receptor activity, unknown ligand
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • 75-94 107-130 143-164 186-205 231-249 278-304 310-331
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 598157 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P46095 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name GPR6_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1089 bp
ATGAACGCGAGCGCCGCCTCGCTCAACGACTCCCAGGTGGTGGTAGTGGCGGCCGAAGGA
GCGGCGGCGGCGGCCACAGCAGCAGGGGGGCCGGACACGGGCGAATGGGGACCCCCTGCT
GCGGCGGCTCTAGGAGCCGGCGGCGGAGCTAATGGGTCTCTGGAGCTGTCCTCGCAGCTG
TCGGCTGGGCCACCGGGACTCCTGCTGCCAGCGGTGAATCCGTGGGACGTGCTCCTGTGC
GTGTCGGGGACAGTGATCGCTGGAGAAAACGCGCTGGTGGTGGCGCTCATCGCGTCCACT
CCGGCGCTGCGCACGCCCATGTTCGTGCTGGTAGGCAGCCTGGCCACCGCTGACCTGTTG
GCGGGCTGTGGCCTCATCTTGCACTTTGTGTTCCAGTACTTGGTGCCCTCGGAGACTGTG
AGTCTGCTCACGGTGGGCTTCCTCGTGGCCTCCTTCGCCGCCTCTGTCAGCAGCCTGCTG
GCCATTACGGTGGACCGCTACCTGTCCCTGTATAACGCGCTCACCTATTACTCGCGCCGG
ACCCTGTTGGGCGTGCACCTCCTGCTTGCCGCCACTTGGACCGTGTCCCTAGGCCTGGGG
CTGCTGCCCGTGCTGGGCTGGAACTGCCTGGCAGAGCGCGCCGCCTGCAGCGTGGTGCGC
CCGCTGGCGCGCAGCCACGTGGCTCTGCTCTCCGCCGCCTTCTTCATGGTCTTCGGCATC
ATGCTGCACCTGTACGTGCGCATCTGCCAGGTGGTCTGGCGCCACGCGCACCAGATCGCG
CTGCAGCAGCACTGCCTGGCGCCACCCCATCTCGCTGCCACCAGAAAGGGTGTGGGTACA
CTGGCTGTGGTGCTGGGCACTTTCGGCGCCAGCTGGCTGCCCTTCGCCATCTATTGCGTG
GTGGGCAGCCATGAGGACCCGGCGGTCTACACTTACGCCACCCTGCTGCCCGCCACCTAC
AACTCCATGATCAATCCCATCATCTATGCCTTCCGCAACCAGGAGATCCAGCGCGCCCTG
TGGCTCCTGCTCTGTGGCTGTTTCCAGTCCAAAGTGCCCTTTCGTTCCAGGTCTCCCAGC
GAGGTCTGA
Enzyme 40 GenBank Gene ID L36150 Link Image
Enzyme 40 GeneCard ID P46095 Link Image
Enzyme 40 GenAtlas ID GPR6 Link Image
Enzyme 40 HGNC ID HGNC:4515 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Heiber M, Docherty JM, Shah G, Nguyen T, Cheng R, Heng HH, Marchese A, Tsui LC, Shi X, George SR, et al.: Isolation of three novel human genes encoding G protein-coupled receptors. DNA Cell Biol. 1995 Jan;14(1):25-35. [PubMed Link Image]
  2. Song ZH, Modi W, Bonner TI: Molecular cloning and chromosomal localization of human genes encoding three closely related G protein-coupled receptors. Genomics. 1995 Jul 20;28(2):347-9. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 14919
Enzyme 41 Name Alkaline ceramidase 2
Enzyme 41 Synonyms
  1. AlkCDase 2
  2. N-acylsphingosine amidohydrolase 3-like
  3. Acylsphingosine deacylase 3-like
Enzyme 41 Gene Name ASAH3L
Enzyme 41 Protein Sequence >Alkaline ceramidase 2
MGAPHWWDQLQAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCF
NSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAVLWVLMCALAMWFPRRYLPKIFRN
DRGRFKVVVSVLSAVTTCLAFVKPAINNISLMTLGVPCTALLIAELKRCDNMRVFKLGLF
SGLWWTLALFCWISDRAFCELLSSFNFPYLHCMWHILICLAAYLGCVCFAYFDAASEIPE
QGPVIKFWPNEKWAFIGVPYVSLLCANKKSSVKIT
Enzyme 41 Number of Residues 275
Enzyme 41 Molecular Weight 31309
Enzyme 41 Theoretical pI 7.71
Enzyme 41 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • cellular lipid metabolism
  • ceramide metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • sphingoid metabolism
  • sphingolipid metabolism
Component
  • Golgi membrane
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • 33-53 63-83 87-107 125-142 144-164 174-194 212-232
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 36304156 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q5QJU3 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name ASA3L_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >828 bp
ATGGGCGCCCCGCACTGGTGGGACCAGCTGCAGGCTGGTAGCTCGGAGGTGGACTGGTGC
GAGGACAACTACACCATCGTGCCTGCTATCGCCGAGTTCTACAACACGATCAGCAATGTC
TTATTTTTCATTTTACCGCCCATCTGCATGTGCTTGTTTCGTCAGTATGCAACATGCTTC
AACAGTGGCATCTACTTAATCTGGACTCTTTTGGTTGTAGTGGGAATTGGATCCGTCTAC
TTCCATGCAACCCTTAGTTTCTTGGGTCAGATGCTTGATGAACTTGCAGTCCTTTGGGTT
CTGATGTGTGCTTTGGCCATGTGGTTCCCCAGAAGGTATCTACCAAAGATCTTTCGGAAT
GACCGGGGTAGGTTCAAGGTGGTGGTCAGTGTCCTGTCTGCGGTTACGACGTGCCTGGCA
TTTGTCAAGCCTGCCATCAACAACATCTCTCTGATGACCCTGGGAGTTCCTTGCACTGCA
CTGCTCATCGCAGAGCTAAAGAGGTGTGACAACATGCGTGTGTTTAAGCTGGGCCTCTTC
TCGGGCCTCTGGTGGACCCTGGCCCTGTTCTGCTGGATCAGTGACCGAGCTTTCTGCGAG
CTGCTGTCATCCTTCAACTTCCCCTACCTGCACTGCATGTGGCACATCCTCATCTGCCTT
GCTGCCTACCTGGGCTGTGTATGCTTTGCCTACTTTGATGCTGCCTCAGAGATTCCTGAG
CAAGGCCCTGTCATCAAGTTCTGGCCCAATGAGAAATGGGCCTTCATTGGTGTCCCCTAT
GTGTCCCTCCTGTGTGCCAACAAGAAATCATCAGTCAAGACCACGTGA
Enzyme 41 GenBank Gene ID AY312516 Link Image
Enzyme 41 GeneCard ID Q5QJU3 Link Image
Enzyme 41 GenAtlas ID ASAH3L Link Image
Enzyme 41 HGNC ID HGNC:23675 Link Image
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
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 14921
Enzyme 42 Name Neutral ceramidase
Enzyme 42 Synonyms
  1. N-CDase
  2. NCDase
  3. Acylsphingosine deacylase 2
  4. N-acylsphingosine amidohydrolase 2
  5. Non-lysosomal ceramidase
  6. BCDase
  7. LCDase
  8. hCD
  9. Contains: RecName: Neutral ceramidase soluble form
Enzyme 42 Gene Name ASAH2
Enzyme 42 Protein Sequence >Neutral ceramidase
MAKRTFSNLETFLIFLLVMMSAITVALLSLLFITSGTIENHKDLGGHFFSTTQSPPATQG
STAAQRSTATQHSTATQSSTATQTSPVPLTPESPLFQNFSGYHIGVGRADCTGQVADINL
MGYGKSGQNAQGILTRLYSRAFIMAEPDGSNRTVFVSIDIGMVSQRLRLEVLNRLQSKYG
SLYRRDNVILSGTHTHSGPAGYFQYTVFVIASEGFSNQTFQHMVTGILKSIDIAHTNMKP
GKIFINKGNVDGVQINRSPYSYLQNPQSERARYSSNTDKEMIVLKMVDLNGDDLGLISWF
AIHPVSMNNSNHLVNSDNVGYASYLLEQEKNKGYLPGQGPFVAAFASSNLGDVSPNILGP
RCINTGESCDNANSTCPIGGPSMCIAKGPGQDMFDSTQIIGRAMYQRAKELYASASQEVT
GPLASAHQWVDMTDVTVWLNSTHASKTCKPALGYSFAAGTIDGVGGLNFTQGKTEGDPFW
DTIRDQILGKPSEEIKECHKPKPILLHTGELSKPHPWHPDIVDVQIITLGSLAITAIPGE
FTTMSGRRLREAVQAEFASHGMQNMTVVISGLCNVYTHYITTYEEYQAQRYEAASTIYGP
HTLSAYIQLFRNLAKAIATDTVANLSRGPEPPFFKQLIVPLIPSIVDRAPKGRTFGDVLQ
PAKPEYRVGEVAEVIFVGANPKNSVQNQTHQTFLTVEKYEATSTSWQIVCNDASWETRFY
WHKGLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDILKPAVILSFEGTSPAFEVVTI
Enzyme 42 Number of Residues 780
Enzyme 42 Molecular Weight 85517
Enzyme 42 Theoretical pI 7.24
Enzyme 42 GO Classification Not Available
Enzyme 42 General Function Not Available
Enzyme 42 Specific Function Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Acts as a repressor of apoptosis both by reducing C16-ceramide, thereby preventing ceramide-induced apoptosis, and generating sphingosine, a precursor of the antiapoptotic factor sphingosine 1-phosphate. Probably involved in the digestion of dietary sphingolipids in intestine by acting as a key enzyme for the catabolism of dietary sphingolipids and regulating the levels of bioactive sphingolipid metabolites in the intestinal tract
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • 13-33
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 27227443 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q9NR71 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name ASAH2_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2286 bp
ATGAGTGCCATCACAGTGGCCCTTCTCAGCCTCTTGTTTATCACCAGTGGGACCATTGAA
AACCACAAAGATTTAGGAGGCCATTTTTTTTCAACCACCCAAAGCCCTCCAGCCACCCAG
GGCTCCACAGCTGCCCAACGCTCCACAGCCACCCAGCATTCCACAGCCACCCAGAGCTCC
ACAGCCACTCAAACTTCTCCAGTGCCTTTAACCCCAGAGTCTCCTCTATTTCAGAACTTC
AGTGGCTACCATATTGGTGTTGGACGAGCTGACTGCACAGGACAAGTAGCAGATATCAAT
TTGATGGGCTATGGCAAATCCGGCCAGAATGCACAGGGCATCCTCACCAGGCTATACAGT
CGTGCCTTCATCATGGCAGAACCTGATGGGTCCAATCGAACAGTGTTTGTCAGCATCGAC
ATAGGCATGGTATCACAAAGGCTCAGGCTGGAGGTCCTGAACAGACTGCAGAGTAAATAT
GGCTCCCTGTACAGAAGAGATAATGTCATCCTGAGTGGCACTCACACTCATTCAGGTCCT
GCAGGATATTTCCAGTATACCGTGTTTGTAATTGCCAGTGAAGGATTTAGCAATCAAACT
TTTCAGCACATGGTCACTGGTATCTTGAAGAGCATTGACATAGCACACACAAATATGAAA
CCAGGCAAAATCTTCATCAATAAAGGAAATGTGGATGGTGTGCAGATCAACAGAAGTCCG
TATTCTTACCTTCAAAATCCGCAGTCAGAGAGAGCAAGGTATCCTTCAAATACAGACAAG
GAAATGATAGTTTTGAAAATGGTAGATTTGAATGGAGATGACTTGGGCCTTATCAGCTGG
TTTGCCATCCACCCGGTCAGCATGAACAACAGTAACCATCTTGTAAACAGTGACAATGTG
GGCTATGCATCTTACCTGCTTGAGCAAGAGAAGAACAAAGGATATCTACCTGGACAGGGG
CCATTTGTAGCAGCCTTTGCTTCATCAAACCTAGGAGATGTGTCCCCCAACATTCTTGGA
CCACGTTGCATCAACACAGGAGAGTCCTGTGATAACGCCAATAGCACTTGTCCCATTGGT
GGGCCTAGCATGTGCATTGCTAAGGGACCTGGACAGGATATGTTTGACAGCACACAAATT
ATAGGACGGGCCATGTATCAGAGAGCAAAGGAACTCTATGCCTCTGCCTCCCAGGAGGTA
ACAGGACCACTGGCTTCAGCACACCAGTGGGTGGATATGACAGATGTGACTGTCTGGCTC
AATTCCACACATGCATCAAAAACATGTAAACCAGCATTGGGCTACAGTTTTGCGGCTGGC
ACTATTGATGGAGTTGGAGGCCTCAATTTTACACAGGGGAAAACAGAAGGGGATCCATTT
TGGGACACCATTCGGGACCAGATCCTGGGAAAGCCATCTGAAGAAATTAAAGAATGTCAT
AAACCAAAGCCCATCCTTCTTCACACCGGAGAACTATCAAAACCTCACCCCTGGCATCCA
GACATTGTTGATGTTCAGATTATTACCCTTGGGTCCTTGGCCATAACTGCCATCCCCGGG
GAGTTTACGACCATGTCTGGACGAAGACTTCGAGAGGCAGTTCAAGCAGAATTTGCATCT
CATGGGATGCAGAACATGACTGTTGTTATTTCAGGTCTATGCAACGTCTATACACATTAC
ATTACCACTTATGAAGAATACCAGGCTCAGCGATATGAGGCAGCATCGACAATTTATGGA
CCGCACGCATTATCTGCTTACATTCAGCTCTTCAGAAACCTTGCTAAGGCTATTGCTACG
GACACGGTAGCCAACCTGAGCAGAGGTCCAGAACCTCCCTTTTTCAAACAATTAATAGTT
CCATTAATTCCTAGTATTGTGGATAGAGCACCAAAAGGCAGAACTTTCGGGGATGTCCTG
CAGCCAGCAAAACCTGAATACAGAGTGGGGGAAGTTGCTGAAGTTATATTTGTAGGTGCT
AACCCGAAGAATTCAGTACAAAACCAGACCCATCAGACCTTCCTCACTGTGGAGAAATAT
GAGGCTACTTCAACATCGTGGCAGATAGTGTGTAATGATGCCTCCTGGGAGACTCGTTTT
TATTGGCACAAGGGACTCCTGGGTCTGAGTAATGCAACAGTGGAATGGCATATTCCAGAC
ACTGCCCAGCCTGGAATCTACAGAATAAGATATTTTGGACACAATCGGAAGCAGGACATT
CTGAAGCCTGCTGTCATACTTTCATTTGAAGGCACTTCCCCGGCTTTTGAAGTTGTAACT
ATTTAG
Enzyme 42 GenBank Gene ID AY049008 Link Image
Enzyme 42 GeneCard ID Q9NR71 Link Image
Enzyme 42 GenAtlas ID ASAH2 Link Image
Enzyme 42 HGNC ID HGNC:18860 Link Image
Enzyme 42 Chromosome Location 10
Enzyme 42 Locus 10q11.21
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Choi MS, Anderson MA, Zhang Z, Zimonjic DB, Popescu N, Mukherjee AB: Neutral ceramidase gene: role in regulating ceramide-induced apoptosis. Gene. 2003 Oct 2;315:113-22. [PubMed Link Image]
  2. El Bawab S, Roddy P, Qian T, Bielawska A, Lemasters JJ, Hannun YA: Molecular cloning and characterization of a human mitochondrial ceramidase. J Biol Chem. 2000 Jul 14;275(28):21508-13. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 14925
Enzyme 43 Name Non-lysosomal glucosylceramidase
Enzyme 43 Synonyms
  1. NLGase
  2. Glucosylceramidase 2
  3. Beta-glucocerebrosidase 2
  4. Beta-glucosidase 2
Enzyme 43 Gene Name GBA2
Enzyme 43 Protein Sequence >Non-lysosomal glucosylceramidase
MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCC
NPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLR
YLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMY
QHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQ
LPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDD
APGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQ
QVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFG
AKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSAL
FNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVH
FYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDD
EPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDK
DHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILS
RGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVR
ALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWE
GFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASW
PKVKQGTGLRTGPMFGPKEAMANLSPE
Enzyme 43 Number of Residues 927
Enzyme 43 Molecular Weight 104650
Enzyme 43 Theoretical pI 5.74
Enzyme 43 GO Classification Not Available
Enzyme 43 General Function Not Available
Enzyme 43 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 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • 688-708
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 16215453 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q9HCG7 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name GBA2_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 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 43 GenBank Gene ID AJ309567 Link Image
Enzyme 43 GeneCard ID Q9HCG7 Link Image
Enzyme 43 GenAtlas ID GBA2 Link Image
Enzyme 43 HGNC ID HGNC:18986 Link Image
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 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 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 15257
Enzyme 44 Name Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name SPHK1
Enzyme 44 Protein Sequence >Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
MDPVVGCGRGLFGFVFSAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAE
ISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLC
SLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSV
LSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASP
VVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMH
LFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMV
SEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL
Enzyme 44 Number of Residues 398
Enzyme 44 Molecular Weight 43945
Enzyme 44 Theoretical pI 7.33
Enzyme 44 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 44 General Function Lipid transport and metabolism
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 14495625 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q96GK1 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name Q96GK1_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 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 44 GenBank Gene ID BC009419 Link Image
Enzyme 44 GeneCard ID Q96GK1 Link Image
Enzyme 44 GenAtlas ID SPHK1 Link Image
Enzyme 44 HGNC ID HGNC:11240 Link Image
Enzyme 44 Chromosome Location 17
Enzyme 44 Locus 17q25.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 15258
Enzyme 45 Name ASAH1 protein
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name Not Available
Enzyme 45 Protein Sequence >ASAH1 protein
MNCCIGLGEKARGSHRASYPSLSALFTEASILGFGSFAVKAQWTEDCRKSTYPPSGPTVF
PAVIRYRGAVPWYTINLDLPPYKRWHELMLDKAPVPGLLGNFPGPFEEEMKGIAAVTDIP
LGEIISFNIFYELFTVCTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLT
VNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDA
MWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYE
LDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNK
LTVYTTLIDVTKGQFETYLRDCPDPCIGW
Enzyme 45 Number of Residues 389
Enzyme 45 Molecular Weight 44004
Enzyme 45 Theoretical pI 7.70
Enzyme 45 GO Classification Not Available
Enzyme 45 General Function Not Available
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 16877108 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q96AS2 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name Q96AS2_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1170 bp
ATGAACTGCTGCATCGGGCTGGGAGAGAAGGCTCGCGGGTCCCACCGGGCCTCCTACCCA
AGTCTCAGCGCGCTTTTCACCGAGGCCTCAATTCTGGGATTTGGCAGCTTTGCTGTGAAA
GCCCAATGGACAGAGGACTGCAGAAAATCAACCTATCCTCCTTCAGGACCAACTGTCTTC
CCTGCTGTTATAAGGTACAGAGGTGCAGTTCCATGGTACACCATAAATCTTGACTTACCA
CCCTACAAAAGATGGCATGAATTGATGCTTGACAAGGCACCAGTGCCTGGCCTACTTGGC
AACTTTCCTGGCCCTTTTGAAGAGGAAATGAAGGGTATTGCCGCTGTTACTGATATACCT
TTAGGAGAGATTATTTCATTCAATATTTTTTATGAATTATTTACCGTTTGTACTTCAATA
GTAGCAGAAGACAAAAAAGGTCATCTAATACATGGGAGAAACATGGATTTTGGAGTATTT
CTTGGGTGGAACATAAATAATGATACCTGGGTCATAACTGAGCAACTAAAACCTTTAACA
GTGAATTTGGATTTCCAAAGAAACAACAAAACTGTCTTCAAGGCTTCAAGCTTTGCTGGC
TATGTGGGCATGTTAACAGGATTCAAACCAGGACTGTTCAGTCTTACACTGAATGAACGT
TTCAGTATAAATGGTGGTTATCTGGGTATTCTAGAATGGATTCTGGGAAAGAAAGATGCC
ATGTGGATAGGGTTCCTCACTAGAACAGTTCTGGAAAATAGCACAAGTTATGAAGAAGCC
AAGAATTTATTGACCAAGACCAAGATATTGGCCCCAGCCTACTTTATCCTGGGAGGCAAC
CAGTCTGGGGAAGGTTGTGTGATTACACGAGACAGAAAGGAATCATTGGATGTATATGAA
CTCGATGCTAAGCAGGGTAGATGGTATGTGGTACAAACAAATTATGACCGTTGGAAACAT
CCCTTCTTCCTTGATGATCGCAGAACGCCTGCAAAGATGTGTTTGAACCGCACCAGCCAA
GAGAATATCTCATTTGAAACCATGTATGATGTCCTGTCAACAAAACCTGTCCTCAACAAG
CTGACCGTATACACAACCTTGATAGATGTTACCAAAGGTCAATTCGAAACTTACCTGCGG
GACTGCCCTGACCCTTGTATAGGTTGGTGA
Enzyme 45 GenBank Gene ID BC016828 Link Image
Enzyme 45 GeneCard ID Q96AS2 Link Image
Enzyme 45 GenAtlas ID Not Available
Enzyme 45 HGNC ID HGNC:735 Link Image
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs Not Available
Enzyme 45 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 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 16543
Enzyme 46 Name cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name PPAP2B
Enzyme 46 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 46 Number of Residues 311
Enzyme 46 Molecular Weight 35116
Enzyme 46 Theoretical pI 9.40
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Lipid transport and metabolism
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID B2R651 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name B2R651_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 AK312439 Link Image
Enzyme 46 GeneCard ID B2R651 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 16867
Enzyme 47 Name Alkaline ceramidase 1
Enzyme 47 Synonyms
  1. Alkaline CDase-1
  2. AlkCDase 1
  3. N-acylsphingosine amidohydrolase 3
  4. Acylsphingosine deacylase 3
Enzyme 47 Gene Name ASAH3
Enzyme 47 Protein Sequence >Alkaline ceramidase 1
MPSIFAYQSSEVDWCESNFQYSELVAEFYNTFSNIPFFIFGPLMMLLMHPYAQKRSRYIY
VVWVLFMIIGLFSMYFHMTLSFLGQLLDEIAILWLLGSGYSIWMPRCYFPSFLGGNRSQF
IRLVFITTVVSTLLSFLRPTVNAYALNSIALHILYIVCQEYRKTSNKELRHLIEVSVVLW
AVALTSWISDRLLCSFWQRIHFFYLHSIWHVLISITFPYGMVTMALVDANYEMPGETLKV
RYWPRDSWPVGLPYVEIRGDDKDC
Enzyme 47 Number of Residues 264
Enzyme 47 Molecular Weight 31096
Enzyme 47 Theoretical pI 7.16
Enzyme 47 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • cellular lipid metabolism
  • ceramide metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • sphingoid metabolism
  • sphingolipid metabolism
Component
  • Golgi membrane
  • cell
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo- phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • 28-48 58-78 82-102 120-137 139-159 177-197 207-227
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID Q8TDN7 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name ASAH3_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 AF347024 Link Image
Enzyme 47 GeneCard ID Q8TDN7 Link Image
Enzyme 47 GenAtlas ID ASAH3 Link Image
Enzyme 47 HGNC ID HGNC:18356 Link Image
Enzyme 47 Chromosome Location 19
Enzyme 47 Locus 19p13.3
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Mao C, Xu R, Szulc ZM, Bielawski J, Becker KP, Bielawska A, Galadari SH, Hu W, Obeid LM: Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides. J Biol Chem. 2003 Aug 15;278(33):31184-91. Epub 2003 Jun 3. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 17071
Enzyme 48 Name Sphingosine 1-phosphate receptor 3
Enzyme 48 Synonyms
  1. S1P receptor 3
  2. S1P3
  3. Sphingosine 1-phosphate receptor Edg-3
  4. S1P receptor Edg-3
  5. Endothelial differentiation G-protein coupled receptor 3
Enzyme 48 Gene Name S1PR3
Enzyme 48 Protein Sequence >Sphingosine 1-phosphate receptor 3
MATALPPRLQPVRGNETLREHYQYVGKLAGRLKEASEGSTLTTVLFLVICSFIVLENLMV
LIAIWKNNKFHNRMYFFIGNLALCDLLAGIAYKVNILMSGKKTFSLSPTVWFLREGSMFV
ALGASTCSLLAIAIERHLTMIKMRPYDANKRHRVFLLIGMCWLIAFTLGALPILGWNCLH
NLPDCSTILPLYSKKYIAFCISIFTAILVTIVILYARIYFLVKSSSRKVANHNNSERSMA
LLRTVVIVVSVFIACWSPLFILFLIDVACRVQACPILFKAQWFIVLAVLNSAMNPVIYTL
ASKEMRRAFFRLVCNCLVRGRGARASPIQPALDPSRSKSSSSNNSSHSPKVKEDLPHTAP
SSCIMDKNAALQNGIFCN
Enzyme 48 Number of Residues 378
Enzyme 48 Molecular Weight 42251
Enzyme 48 Theoretical pI 10.19
Enzyme 48 GO Classification
Function
  • G-protein coupled receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • 41-65 73-101 116-134 154-179 196-216 244-265 282-302
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID Q99500 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name S1PR3_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence Not Available
Enzyme 48 GenBank Gene ID X83864 Link Image
Enzyme 48 GeneCard ID Q99500 Link Image
Enzyme 48 GenAtlas ID S1PR3 Link Image
Enzyme 48 HGNC ID HGNC:3167 Link Image
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Yamaguchi F, Tokuda M, Hatase O, Brenner S: Molecular cloning of the novel human G protein-coupled receptor (GPCR) gene mapped on chromosome 9. Biochem Biophys Res Commun. 1996 Oct 14;227(2):608-14. [PubMed Link Image]
  2. An S, Bleu T, Huang W, Hallmark OG, Coughlin SR, Goetzl EJ: Identification of cDNAs encoding two G protein-coupled receptors for lysosphingolipids. FEBS Lett. 1997 Nov 17;417(3):279-82. [PubMed Link Image]
  3. Himmel HM, Meyer Zu Heringdorf D, Graf E, Dobrev D, Kortner A, Schuler S, Jakobs KH, Ravens U: Evidence for Edg-3 receptor-mediated activation of I(K.ACh) by sphingosine-1-phosphate in human atrial cardiomyocytes. Mol Pharmacol. 2000 Aug;58(2):449-54. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 17337
Enzyme 49 Name GPI-anchor transamidase
Enzyme 49 Synonyms
  1. GPI transamidase
  2. Phosphatidylinositol-glycan biosynthesis class K protein
  3. PIG-K
  4. hGPI8
Enzyme 49 Gene Name PIGK
Enzyme 49 Protein Sequence >GPI-anchor transamidase
MAVTDSLSRAATVLATVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYR
HVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVD
YRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITN
IELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPA
IGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLI
TDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEKLMEPLKYAEQLPVAQIIHQKPK
LKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
Enzyme 49 Number of Residues 395
Enzyme 49 Molecular Weight 45251.4
Enzyme 49 Theoretical pI 6.09
Enzyme 49 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 49 General Function Involved in cysteine-type endopeptidase activity
Enzyme 49 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 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-27
Enzyme 49 Transmembrane Regions
  • 368-388
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 1518259 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q92643 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name GPI8_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence Not Available
Enzyme 49 GenBank Gene ID Y07596 Link Image
Enzyme 49 GeneCard ID PIGK Link Image
Enzyme 49 GenAtlas ID Not Available
Enzyme 49 HGNC ID HGNC:8965 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1p31.1
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 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 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 17782
Enzyme 50 Name Glycosylphosphatidylinositol anchor attachment 1 protein
Enzyme 50 Synonyms
  1. GPI anchor attachment protein 1
  2. GAA1 protein homolog
  3. hGAA1
Enzyme 50 Gene Name GPAA1
Enzyme 50 Protein Sequence >Glycosylphosphatidylinositol anchor attachment 1 protein
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMV
EEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHE
RYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDI
VFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVE
GLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASG
RPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLY
LLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQ
GVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPH
NTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGP
RTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLF
PLLSLGLYPCWLLFWNVLFWK
Enzyme 50 Number of Residues 621
Enzyme 50 Molecular Weight 67622.5
Enzyme 50 Theoretical pI 8.16
Enzyme 50 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • protein complex
Enzyme 50 General Function Involved in tubulin binding
Enzyme 50 Specific Function Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • 25-45 369-389 428-448 459-479 496-516 544-564 600-620
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 2706632 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID O43292 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name GPAA1_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 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 50 GenBank Gene ID AB006969 Link Image
Enzyme 50 GeneCard ID GPAA1 Link Image
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID HGNC:4446 Link Image
Enzyme 50 Chromosome Location 8
Enzyme 50 Locus 8q24.3
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 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 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 17783
Enzyme 51 Name Protein PLEKHA9
Enzyme 51 Synonyms Not Available
Enzyme 51 Gene Name PLEKHA9
Enzyme 51 Protein Sequence >Protein PLEKHA9
MSELRLCCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAA
FTSELLYHTPPGSPQLAMLKSSKMKHPIIPIHNSLERQTELSTCENGSLNMEINGEEEIL
MKNKNSLYLKSAEIDCSISSEENTDDNITVQGEIMKEDRMENLKNHDNNLSQSGSDSSCS
PECLWEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCCAVVPVLDKLGPTVFAP
VKMDLVENIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLK
GFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGD
HRKEAFSIGMQRDLSLYLPAMKKQMAILDAL
Enzyme 51 Number of Residues 391
Enzyme 51 Molecular Weight 43538.3
Enzyme 51 Theoretical pI 4.76
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Involved in glycolipid binding
Enzyme 51 Specific Function Not Available
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 4050073 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID O95397 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name PKHA9_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 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 51 GenBank Gene ID AF103731 Link Image
Enzyme 51 GeneCard ID PLEKHA9 Link Image
Enzyme 51 GenAtlas ID Not Available
Enzyme 51 HGNC ID HGNC:30222 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 12q
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 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 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 17784
Enzyme 52 Name Glycolipid transfer protein domain-containing protein 2
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name GLTPD2
Enzyme 52 Protein Sequence >Glycolipid transfer protein domain-containing protein 2
MGVAARPPALRHWFSHSIPLAIFALLLLYLSVRSLGARSGCGPRAQPCVPGETAPFQVRQ
ESGTLEAPERKQPPCLGPRGMLGRMMRRFHASLKPEGDVGLSPYLAGWRALVEFLTPLGS
VFAFATREAFTKVTDLEARVHGPDAEHYWSLAAMAAWERRAGLLEQPGAAPRDPTRSSGS
RTLLLLHRALRWSQLCLHRVATGALGGPEAGVQCSDAYRAALGPHHPWLVRQTARLAFLA
FPGRRRLLELACPGATEAEARAALLRAAGTLEDVYNRTQSLLAERGLLQLA
Enzyme 52 Number of Residues 291
Enzyme 52 Molecular Weight 31641.2
Enzyme 52 Theoretical pI 10.54
Enzyme 52 GO Classification Not Available
Enzyme 52 General Function Involved in glycolipid binding
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 152061018 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID A6NH11 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name GLTD2_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence Not Available
Enzyme 52 GenBank Gene ID BC150536 Link Image
Enzyme 52 GeneCard ID GLTPD2 Link Image
Enzyme 52 GenAtlas ID Not Available
Enzyme 52 HGNC ID HGNC:33756 Link Image
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 17p13.2
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 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 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 17785
Enzyme 53 Name Putative uncharacterized protein PLEKHA8
Enzyme 53 Synonyms Not Available
Enzyme 53 Gene Name PLEKHA8
Enzyme 53 Protein Sequence >Putative uncharacterized protein PLEKHA8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALSVGMWV
Enzyme 53 Number of Residues 439
Enzyme 53 Molecular Weight 49308.8
Enzyme 53 Theoretical pI 4.67
Enzyme 53 GO Classification Not Available
Enzyme 53 General Function Involved in glycolipid binding
Enzyme 53 Specific Function Not Available
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID B5MDU3 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name B5MDU3_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence Not Available
Enzyme 53 GenBank Gene ID AC007285 Link Image
Enzyme 53 GeneCard ID PLEKHA8 Link Image
Enzyme 53 GenAtlas ID Not Available
Enzyme 53 HGNC ID HGNC:30037 Link Image
Enzyme 53 Chromosome Location 7
Enzyme 53 Locus 7p21-p11.2
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References Not Available
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 17786
Enzyme 54 Name cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
Enzyme 54 Synonyms
  1. SubName: Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
Enzyme 54 Gene Name PLEKHA8
Enzyme 54 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 54 Number of Residues 519
Enzyme 54 Molecular Weight 58260.9
Enzyme 54 Theoretical pI 4.76
Enzyme 54 GO Classification Not Available
Enzyme 54 General Function Involved in glycolipid binding
Enzyme 54 Specific Function Not Available
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 194378422 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID B4DH00 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name B4DH00_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 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 54 GenBank Gene ID AK294857 Link Image
Enzyme 54 GeneCard ID PLEKHA8 Link Image
Enzyme 54 GenAtlas ID Not Available
Enzyme 54 HGNC ID HGNC:30037 Link Image
Enzyme 54 Chromosome Location 7
Enzyme 54 Locus 7p21-p11.2
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References Not Available
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 17787
Enzyme 55 Name T-cell surface glycoprotein CD1a
Enzyme 55 Synonyms
  1. T-cell surface antigen T6/Leu-6
  2. hTa1 thymocyte antigen
  3. CD1a antigen
Enzyme 55 Gene Name CD1A
Enzyme 55 Protein Sequence >T-cell surface glycoprotein CD1a
MLFLLLPLLAVLPGDGNADGLKEPLSFHVIWIASFYNHSWKQNLVSGWLSDLQTHTWDSN
SSTIVFLWPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCE
LHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLS
DTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRG
EQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSV
GFIILAVIVPLLLLIGLALWFRKRCFC
Enzyme 55 Number of Residues 327
Enzyme 55 Molecular Weight 37172.2
Enzyme 55 Theoretical pI 6.79
Enzyme 55 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 55 General Function Involved in antigen processing and presentation
Enzyme 55 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 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • 1-16
Enzyme 55 Transmembrane Regions
  • 301-321
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 180036 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P06126 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name CD1A_HUMAN Link Image
Enzyme 55 PDB ID 1ONQ Link Image
Enzyme 55 PDB File Show
Enzyme 55 3D Structure
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >984 bp
ATGCTGTTTTTGCTACTTCCATTGTTAGCTGTTCTCCCAGGTGATGGCAATGCAGACGGG
CTCAAGGAGCCTCTCTCCTTCCATGTCATCTGGATCGCATCCTTTTACAACCATTCCTGG
AAACAAAATCTGGTCTCAGGTTGGCTGAGTGATTTGCAGACTCATACCTGGGACAGCAAT
TCCAGCACCATCGTTTTCCTGTGGCCCTGGTCCAGGGGAAACTTCAGCAATGAGGAGTGG
AAGGAACTGGAAACATTATTCCGTATACGCACCATTCGGTCATTTGAGGGAATTCGTAGA
TACGCCCATGAATTGCAGTTTGAATATCCTTTTGAGATACAGGTGACAGGAGGCTGTGAG
CTGCACTCTGGAAAGGTCTCAGGAAGCTTCTTGCAGTTAGCTTATCAAGGATCAGACTTT
GTGAGCTTCCAGAACAATTCATGGTTGCCATATCCAGTGGCTGGGAATATGGCCAAGCAT
TTCTGCAAAGTGCTCAATCAGAATCAGCATGAAAATGACATAACACACAATCTTCTCAGT
GACACCTGCCCACGTTTCATCTTGGGTCTTCTTGATGCAGGAAAGGCACATCTCCAGCGG
CAAGTGAAGCCCGAGGCCTGGCTGTCCCATGGCCCCAGTCCTGGCCCTGGCCATCTGCAG
CTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGT
GAGCAGGAGCAGCAGGGCACTCAGCGAGGGGACATCTTGCCCAGTGCTGATGGGACATGG
TATCTCCGCGCAACCCTGGAGGTGGCCGCTGGGGAGGCAGCTGACCTGTCCTGTCGGGTG
AAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGAGCATCACAGTTCCGTG
GGCTTCATCATCTTGGCGGTGATAGTGCCTTTACTTCTTCTGATAGGTCTTGCGCTTTGG
TTCAGGAAACGCTGTTTCTGTTAA
Enzyme 55 GenBank Gene ID M28825 Link Image
Enzyme 55 GeneCard ID CD1A Link Image
Enzyme 55 GenAtlas ID Not Available
Enzyme 55 HGNC ID HGNC:1634 Link Image
Enzyme 55 Chromosome Location 1
Enzyme 55 Locus 1q22-q23
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 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 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 17788
Enzyme 56 Name Glycolipid transfer protein domain-containing protein 1
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name GLTPD1
Enzyme 56 Protein Sequence >Glycolipid transfer protein domain-containing protein 1
MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSK
LRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQL
FLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPP
EQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Enzyme 56 Number of Residues 214
Enzyme 56 Molecular Weight 24364.8
Enzyme 56 Theoretical pI 7.23
Enzyme 56 GO Classification Not Available
Enzyme 56 General Function Involved in glycolipid binding
Enzyme 56 Specific Function Not Available
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein Not Available
Enzyme 56 UniProtKB/Swiss-Prot ID Q5TA50 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name GLTD1_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence Not Available
Enzyme 56 GenBank Gene ID CR599582 Link Image
Enzyme 56 GeneCard ID GLTPD1 Link Image
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID HGNC:28116 Link Image
Enzyme 56 Chromosome Location 1
Enzyme 56 Locus 1p36.33
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 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 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 17789
Enzyme 57 Name T-cell surface glycoprotein CD1c
Enzyme 57 Synonyms
  1. CD1c antigen
Enzyme 57 Gene Name CD1C
Enzyme 57 Protein Sequence >T-cell surface glycoprotein CD1c
MLFLQFLLLALLLPGGDNADASQEHVSFHVIQIFSFVNQSWARGQGSGWLDELQTHGWDS
ESGTIIFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGC
ELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNL
IRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWM
RNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWGHHF
SMNWIALVVIVPLVILIVLVLWFKKHCSYQDIL
Enzyme 57 Number of Residues 333
Enzyme 57 Molecular Weight 37653.7
Enzyme 57 Theoretical pI 6.09
Enzyme 57 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 57 General Function Involved in antigen processing and presentation
Enzyme 57 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 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • 1-17
Enzyme 57 Transmembrane Regions
  • 303-323
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 180066 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID P29017 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name CD1C_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1002 bp
ATGCTGTTTCTGCAGTTTCTGCTGCTAGCTCTTCTTCTCCCAGGTGGTGACAATGCAGAC
GCATCCCAGGAACACGTCTCCTTCCATGTCATCCAGATCTTCTCATTTGTCAACCAATCC
TGGGCACGAGGTCAGGGCTCAGGATGGCTGGACGAGTTGCAGACTCATGGCTGGGACAGT
GAATCAGGCACAATAATTTTCCTGCATAACTGGTCCAAGGGCAACTTCAGCAATGAAGAG
TTGTCAGACCTAGAGTTGTTATTTCGTTTCTACCTCTTTGGATTAACTCGGGAGATTCAA
GACCATGCAAGTCAAGATTACTCGAAATATCCCTTTGAAGTACAGGTGAAAGCGGGCTGT
GAGCTGCATTCTGGAAAGAGCCCAGAAGGCTTCTTTCAGGTAGCTTTCAACGGATTAGAT
TTACTGAGTTTCCAGAATACAACATGGGTGCCATCTCCAGGCTGTGGAAGTTTGGCCCAA
AGTGTCTGTCATCTACTCAATCATCAGTATGAAGGCGTCACAGAAACAGTGTATAATCTC
ATAAGAAGCACTTGCCCCCGATTTCTCTTGGGTCTCCTGGATGCAGGGAAGATGTATGTA
CACAGGCAAGTGAGGCCAGAAGCCTGGCTGTCCAGTCGCCCCAGCCTTGGGTCTGGCCAG
CTGTTGCTGGTTTGTCATGCCTCCGGCTTCTACCCAAAGCCTGTTTGGGTGACATGGATG
CGGAATGAACAGGAGCAACTGGGCACTAAACATGGTGATATTCTTCCTAATGCTGATGGG
ACATGGTATCTTCAGGTGATCCTGGAGGTGGCATCTGAGGAGCCTGCTGGCCTGTCTTGT
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTCT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
Enzyme 57 GenBank Gene ID M28827 Link Image
Enzyme 57 GeneCard ID CD1C Link Image
Enzyme 57 GenAtlas ID Not Available
Enzyme 57 HGNC ID HGNC:1636 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 1q22-q23
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 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 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 17790
Enzyme 58 Name Lipopolysaccharide-binding protein
Enzyme 58 Synonyms
  1. LBP
Enzyme 58 Gene Name LBP
Enzyme 58 Protein Sequence >Lipopolysaccharide-binding protein
MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLP
DFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRK
SFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNL
FHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATA
QMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLN
FSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDP
YMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFN
AELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMR
V
Enzyme 58 Number of Residues 481
Enzyme 58 Molecular Weight 53383.0
Enzyme 58 Theoretical pI 6.68
Enzyme 58 GO Classification
Function
  • binding
  • lipid binding
Process
Component
Enzyme 58 General Function Involved in Gram-negative bacterial cell surface binding
Enzyme 58 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 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • 1-25
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 186966 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID P18428 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name LBP_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence Not Available
Enzyme 58 GenBank Gene ID M35533 Link Image
Enzyme 58 GeneCard ID LBP Link Image
Enzyme 58 GenAtlas ID Not Available
Enzyme 58 HGNC ID HGNC:6517 Link Image
Enzyme 58 Chromosome Location 2
Enzyme 58 Locus 20q11.23-q12
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 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 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 17791
Enzyme 59 Name Putative uncharacterized protein DKFZp434L0435
Enzyme 59 Synonyms Not Available
Enzyme 59 Gene Name DKFZp434L0435
Enzyme 59 Protein Sequence >Putative uncharacterized protein DKFZp434L0435
VAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Enzyme 59 Number of Residues 55
Enzyme 59 Molecular Weight 6175.1
Enzyme 59 Theoretical pI 4.41
Enzyme 59 GO Classification Not Available
Enzyme 59 General Function Involved in glycolipid binding
Enzyme 59 Specific Function Not Available
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function Not Available
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 50978454 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q9UFH6 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name Q9UFH6_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence Not Available
Enzyme 59 GenBank Gene ID AL122073 Link Image
Enzyme 59 GeneCard ID DKFZp434L0435 Link Image
Enzyme 59 GenAtlas ID Not Available
Enzyme 59 HGNC ID HGNC:28116 Link Image
Enzyme 59 Chromosome Location Not Available
Enzyme 59 Locus Not Available
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References Not Available
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 17792
Enzyme 60 Name T-cell surface glycoprotein CD1b
Enzyme 60 Synonyms
  1. CD1b antigen
Enzyme 60 Gene Name CD1B
Enzyme 60 Protein Sequence >T-cell surface glycoprotein CD1b
MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDS
DSGTAIFLKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDFQMKYPFEIQGIAGC
ELHSGGAIVSFLRGALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQGIMETVRILL
YETCPRYLLGVLNAGKADLQRQVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVWVMWMR
GEQEQQGTQLGDILPNANWTWYLRATLDVADGEAAGLSCRVKHSSLEGQDIILYWRNPTS
IGSIVLAIIVPSLLLLLCLALWYMRRRSYQNIP
Enzyme 60 Number of Residues 333
Enzyme 60 Molecular Weight 36939.1
Enzyme 60 Theoretical pI 6.24
Enzyme 60 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 60 General Function Involved in protein binding
Enzyme 60 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 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • 1-17
Enzyme 60 Transmembrane Regions
  • 304-324
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 180056 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID P29016 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name CD1B_HUMAN Link Image
Enzyme 60 PDB ID 1UQS Link Image
Enzyme 60 PDB File Show
Enzyme 60 3D Structure
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >1002 bp
ATGCTGCTGCTGCCATTTCAACTGTTAGCTGTTCTCTTTCCTGGTGGTAACAGTGAACAT
GCCTTCCAGGGGCCGACCTCCTTTCATGTTATCCAGACCTCGTCCTTTACCAATAGTACC
TGGGCACAAACTCAAGGCTCAGGCTGGTTGGATGATTTGCAGATTCATGGCTGGGATAGC
GACTCAGGCACTGCCATATTCCTGAAGCCTTGGTCTAAAGGTAACTTTAGTGATAAGGAG
GTTGCTGAGTTAGAGGAGATATTCCGAGTCTACATCTTTGGATTCGCTCGAGAAGTACAA
GACTTTGCCGGTGATTTCCAGATGAAATACCCCTTTGAGATCCAGGGCATAGCAGGCTGT
GAGCTACATTCTGGAGGTGCCATAGTAAGCTTCCTGAGGGGAGCTCTAGGAGGATTGGAT
TTCCTGAGTGTCAAGAATGCTTCATGTGTGCCTTCCCCAGAAGGTGGCAGCAGGGCACAG
AAATTCTGTGCACTAATCATACAATATCAAGGTATCATGGAAACTGTGAGAATTCTCCTC
TATGAAACCTGCCCCCGATATCTCTTGGGCGTCCTCAATGCAGGAAAAGCAGATCTGCAA
AGACAAGTGAAGCCTGAGGCCTGGCTGTCCAGTGGCCCCAGTCCTGGACCTGGCCGTCTG
CAGCTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCTAGGGGACATCCTGCCCAATGCTAACTGGACA
TGGTATCTCCGAGCAACCCTGGATGTGGCAGATGGGGAGGCGGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTTTAGAGGGCCAGGACATCATCCTCTACTGGAGAAACCCCACCTCC
ATTGGCTCAATTGTTTTGGCAATAATAGTGCCTTCCTTGCTCCTTTTGCTATGCCTTGCA
TTATGGTATATGAGGCGCCGGTCATATCAGAATATCCCATGA
Enzyme 60 GenBank Gene ID M28826 Link Image
Enzyme 60 GeneCard ID CD1B Link Image
Enzyme 60 GenAtlas ID Not Available
Enzyme 60 HGNC ID HGNC:1635 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 1q22-q23
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 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 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 17793
Enzyme 61 Name Glycolipid transfer protein
Enzyme 61 Synonyms
  1. GLTP
Enzyme 61 Gene Name GLTP
Enzyme 61 Protein Sequence >Glycolipid transfer protein
MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVY
DTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENH
PNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKI
RLFLVNYTATIDVIYEMYTQMNAELNYKV
Enzyme 61 Number of Residues 209
Enzyme 61 Molecular Weight 23849.6
Enzyme 61 Theoretical pI 7.49
Enzyme 61 GO Classification Not Available
Enzyme 61 General Function Involved in glycolipid binding
Enzyme 61 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 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 6959686 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q9NZD2 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name GLTP_HUMAN Link Image
Enzyme 61 PDB ID 1SX6 Link Image
Enzyme 61 PDB File Show
Enzyme 61 3D Structure
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >630 bp
ATGGCGCTGCTGGCGGAGCACTTGCTGAAGCCGCTGCCCGCGGACAAGCAGATCGAGACC
GGGCCCTTCCTCGAGGCGGTGTCCCACCTGCCGCCCTTCTTCGATTGCCTTGGGTCCCCA
GTGTTTACTCCCATCAAGGCAGACATAAGCGGCAACATCACGAAAATCAAAGCTGTGTAC
GACACCAACCCAGCCAAGTTCCGGACCCTGCAGAACATCCTGGAGGTGGAGAAAGAAATG
TATGGAGCAGAGTGGCCCAAAGTAGGGGCCACACTGGCGCTGATGTGGCTGAAAAGAGGC
CTCCGCTTCATCCAGGTCTTCCTCCAGAGCATCTGCGACGGGGAGCGGGACGAGAACCAC
CCCAACCTCATCCGTGTCAACGCCACCAAGGCCTACGAGATGGCCCTCAAGAAGTACCAT
GGCTGGATCGTGCAGAAGATCTTCCAGGCAGCACTGTACGCAGCACCCTATAAGTCTGAC
TTCCTGAAAGCGCTCTCCAAGGGGCAGAATGTTACGGAGGAGGAGTGCCTGGAGAAGATC
CGCCTCTTCCTAGTCAACTACACGGCGACCATCGATGTCATCTACGAGATGTACACCCAG
ATGAACGCTGAGCTCAACTACAAGGTGTAG
Enzyme 61 GenBank Gene ID AF209704 Link Image
Enzyme 61 GeneCard ID GLTP Link Image
Enzyme 61 GenAtlas ID Not Available
Enzyme 61 HGNC ID HGNC:24867 Link Image
Enzyme 61 Chromosome Location 1
Enzyme 61 Locus 12q24.11
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 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]
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Enzyme 61 Metabolite References Not Available