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Human Metabolome Database Version 2.5

 

Showing metabocard for SM(d18:1/18:0) (HMDB01348)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-23 23:45:18
Accession Number HMDB01348
Secondary Accession Numbers HMDB12099
Common Name SM(d18:1/18:0)
Description Sphingomyelin (d18:1/18:0) or SM(d18:1/18:0) is a type of sphingolipid found in animal cell membranes, especially in the membranous myelin sheath which surrounds some nerve cell axons. It usually consists of phosphorylcholine and ceramide. SM(18:1/18:0) consists of oleic acid attached to the C1 position and stearic acid attached to the C2 position. In humans, sphingomyelin is the only membrane phospholipid not derived from glycerol. Like all sphingolipids, SPH has a ceramide core (sphingosine bonded to a fatty acid via an amide linkage). In addition it contains one polar head group, which is either phosphocholine or phosphoethanolamine. The plasma membrane of cells is highly enriched in sphingomyelin and is considered largely to be found in the exoplasmic leaflet of the cell membrane. However, there is some evidence that there may also be a sphingomyelin pool in the inner leaflet of the membrane. Moreover, neutral sphingomyelinase-2 - an enzyme that breaks down sphingomyelin into ceramide has been found to localise exclusively to the inner leaflet further suggesting that there may be sphingomyelin present there. Sphingomyelin can accumulate in a rare hereditary disease called Niemann-Pick Disease, types A and B. Niemann-Pick disease is a genetically-inherited disease caused by a deficiency in the enzyme Sphingomyelinase, which causes the accumulation of Sphingomyelin in spleen, liver, lungs, bone marrow, and the brain, causing irreversible neurological damage. SMs play a role in signal transduction. Sphingomyelins are synthesized by the transfer of phosphorylcholine from phosphatidylcholine to a ceramide in a reaction catalyzed by sphingomyelin synthase.
Synonyms
  1. N-(octadecanoyl)-sphing-4-enine-1-phosphocholine
  2. N-Acyl-4-sphingenyl-1-O-phosphorylcholine
  3. N-Acyl-D-sphingosine-1-phosphocholine
  4. Sphingomyelin
  5. Sphingomyelin (d18:1/18:0)
Chemical IUPAC Name 2-[hydroxy-[(E,2S,3R)-3-hydroxy-2-(octadecanoylamino)octadec-4-enoxy]phosphoryl]oxyethyl-trimethyl-azanium
Chemical Formula C41H84N2O6P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Lipids
Class
  • Sphingolipids
Sub Class
  • Sphingomyelins
Family
  • Mammalian Metabolite
Species
  • cation
  • secondary alcohol
  • quaternary ammonium salt
  • secondary carboxylic acid amide
  • phosphoric acid ester
  • alkene
Biofunction
  • Second messenger
  • Component of Glycosphingolipid metabolism
Application
Source
  • Endogenous
Average Molecular Weight 732.089
Monoisotopic Molecular Weight 731.606689
Isomeric SMILES CCCCCCCCCCCCCCCCCC(=O)N[C@@H](COP(O)(=O)OCC[N+](C)(C)C)[C@H](O)C=CCCCCCCCCCCCCC
Canonical SMILES CCCCCCCCCCCCCCCCCC(=O)NC(COP(O)(=O)OCC[N+](C)(C)C)C(O)C=CCCCCCCCCCCCCC
KEGG Compound ID C00550 Link Image
BioCyc ID SPHINGO-MYELIN Link Image
BiGG ID Not Available
Wikipedia Link Sphingomyelin Link Image
NuGOwiki Link HMDB01348 Link Image
Metagene Link HMDB01348 Link Image
METLIN ID 176 Link Image
PubChem Compound 5283588 Link Image
PubChem Substance 11039040 Link Image
ChEBI ID 17636 Link Image
CAS Registry Number 85187-10-6
InChI Identifier InChI=1/C41H83N2O6P/c1-6-8-10-12-14-16-18-20-21-23-25-27-29-31-33-35-41(45)42-39(38-49-50(46,47)48-37-36-43(3,4)5)40(44)34-32-30-28-26-24-22-19-17-15-13-11-9-7-2/h32,34,39-40,44H,6-31,33,35-38H2,1-5H3,(H-,42,45,46,47)/p+1/b34-32+/t39-,40+/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility null Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity null Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
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 Not Available
Biofluid Location
  • Blood
  • Breast Milk
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Brain
Erythrocyte
Liver
Nervous Tissues
Spleen
Concentrations (Normal)
Biofluid Blood
Value 298.0 +/- 24.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1145 +/- 67 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Concentration of total sphingomyelin in Breastfeeding women after 165–180 days of lactation
References
  • Ilcol YO, Ozbek R, Hamurtekin E, Ulus IH: Choline status in newborns, infants, children, breast-feeding women, breast-fed infants and human breast milk. J Nutr Biochem. 2005 Aug;16(8):489-99. [PubMed Link Image]
Biofluid Blood
Value 1364 +/- 106 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Concentration of total sphingomyelin in Breastfeeding women after 12-28 days of lactation
References
  • Ilcol YO, Ozbek R, Hamurtekin E, Ulus IH: Choline status in newborns, infants, children, breast-feeding women, breast-fed infants and human breast milk. J Nutr Biochem. 2005 Aug;16(8):489-99. [PubMed Link Image]
Biofluid Breast Milk
Value 124 +/- 9 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Holmes-McNary MQ, Cheng WL, Mar MH, Fussell S, Zeisel SH: Choline and choline esters in human and rat milk and in infant formulas. Am J Clin Nutr. 1996 Oct;64(4):572-6. [PubMed Link Image]
Biofluid CSF
Value 0.340 +/- 0.154 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Mandal, R. et al. (in preparation)
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. Harzer K, Massenkeil G, Frohlich E: Concurrent increase of cholesterol, sphingomyelin and glucosylceramide in the spleen from non-neurologic Niemann-Pick type C patients but also patients possibly affected with other lipid trafficking disorders. FEBS Lett. 2003 Feb 27;537(1-3):177-81. [PubMed Link Image]
  2. He X, Chen F, McGovern MM, Schuchman EH: A fluorescence-based, high-throughput sphingomyelin assay for the analysis of Niemann-Pick disease and other disorders of sphingomyelin metabolism. Anal Biochem. 2002 Jul 1;306(1):115-23. [PubMed Link Image]
  3. Reichl D, Sterchi JM: Human peripheral lymph lipoproteins are enriched in sphingomyelin. Biochim Biophys Acta. 1992 Jul 9;1127(1):28-32. [PubMed Link Image]
  4. Nelson JC, Jiang XC, Tabas I, Tall A, Shea S: Plasma sphingomyelin and subclinical atherosclerosis: findings from the multi-ethnic study of atherosclerosis. Am J Epidemiol. 2006 May 15;163(10):903-12. Epub 2006 Apr 12. [PubMed Link Image]
  5. Chen H, Born E, Mathur SN, Johlin FC Jr, Field FJ: Sphingomyelin content of intestinal cell membranes regulates cholesterol absorption. Evidence for pancreatic and intestinal cell sphingomyelinase activity. Biochem J. 1992 Sep 15;286 ( Pt 3):771-7. [PubMed Link Image]
  6. Liu KZ, Mantsch HH: Simultaneous quantitation from infrared spectra of glucose concentrations, lactate concentrations, and lecithin/sphingomyelin ratios in amniotic fluid. Am J Obstet Gynecol. 1999 Mar;180(3 Pt 1):696-702. [PubMed Link Image]
  7. Horter MJ, Sondermann S, Reinecke H, Bogdanski J, Woltering A, Kerber S, Breithardt G, Assmann G, Von Eckardstein A: Associations of HDL phospholipids and paraoxonase activity with coronary heart disease in postmenopausal women. Acta Physiol Scand. 2002 Oct;176(2):123-30. [PubMed Link Image]
  8. Tanaka K, Nishizawa K, Yamamoto H, Naruto T, Izeki E, Taga T, Shimada M, Saeki Y: Analysis of very long-chain fatty acids and plasmalogen in the erythrocyte membrane: a simple method for the detection of peroxisomal disorders and discrimination between adrenoleukodystrophy and Zellweger syndrome. Neuropediatrics. 1990 Aug;21(3):119-23. [PubMed Link Image]
  9. Cribier S, Morrot G, Neumann JM, Devaux PF: Lateral diffusion of erythrocyte phospholipids in model membranes comparison between inner and outer leaflet components. Eur Biophys J. 1990;18(1):33-41. [PubMed Link Image]
  10. Nyberg L, Duan RD, Axelson J, Nilsson A: Identification of an alkaline sphingomyelinase activity in human bile. Biochim Biophys Acta. 1996 Mar 29;1300(1):42-8. [PubMed Link Image]
  11. Whitworth NS, Magann EF, Morrison JC: Evaluation of fetal lung maturity in diamniotic twins. Am J Obstet Gynecol. 1999 Jun;180(6 Pt 1):1438-41. [PubMed Link Image]
  12. de Oliveira JS, Zaharenko AJ, de Freitas JC, Konno K, de Andrade SA, Portaro FC, Richardson M, Sant'anna OA, Tambourgi DV: Caissarolysin I (Bcs I), a new hemolytic toxin from the Brazilian sea anemone Bunodosoma caissarum: purification and biological characterization. Biochim Biophys Acta. 2006 Mar;1760(3):453-61. Epub 2006 Jan 17. [PubMed Link Image]
  13. Omarini LP, Frank-Burkhardt SE, Seemayer TA, Mentha G, Terrier F: Niemann-Pick disease type C: nodular splenomegaly. Abdom Imaging. 1995 Mar-Apr;20(2):157-60. [PubMed Link Image]
  14. Berna L, Asfaw B, Conzelmann E, Cerny B, Ledvinova J: Determination of urinary sulfatides and other lipids by combination of reversed-phase and thin-layer chromatographies. Anal Biochem. 1999 May 1;269(2):304-11. [PubMed Link Image]
  15. He X, Chen F, Gatt S, Schuchman EH: An enzymatic assay for quantifying sphingomyelin in tissues and plasma from humans and mice with Niemann-Pick disease. Anal Biochem. 2001 Jun 15;293(2):204-11. [PubMed Link Image]
  16. Feki NC, Therond P, Couturier M, Limea G, Legrand A, Jouannet P, Auger J: Human sperm lipid content is modified after migration into human cervical mucus. Mol Hum Reprod. 2004 Feb;10(2):137-42. [PubMed Link Image]
  17. Wang C, Yang J, Gao P, Lu X, Xu G: Identification of phospholipid structures in human blood by direct-injection quadrupole-linear ion-trap mass spectrometry. Rapid Commun Mass Spectrom. 2005;19(17):2443-53. [PubMed Link Image]
  18. Otterbach B, Stoffel W: Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease). Cell. 1995 Jun 30;81(7):1053-61. [PubMed Link Image]
  19. Haughey NJ, Cutler RG, Tamara A, McArthur JC, Vargas DL, Pardo CA, Turchan J, Nath A, Mattson MP: Perturbation of sphingolipid metabolism and ceramide production in HIV-dementia. Ann Neurol. 2004 Feb;55(2):257-67. [PubMed Link Image]
  20. Fujiwaki T, Yamaguchi S, Tasaka M, Sakura N, Taketomi T: Application of delayed extraction-matrix-assisted laser desorption ionization time-of-flight mass spectrometry for analysis of sphingolipids in pericardial fluid, peritoneal fluid and serum from Gaucher disease patients. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Aug 25;776(1):115-23. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
  2. N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
  3. Phosphatidylcholine:ceramide cholinephosphotransferase 2
  4. Phosphatidylcholine:ceramide cholinephosphotransferase 1
  5. Sphingomyelin phosphodiesterase
  6. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
  7. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
  8. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  9. Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
  10. Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
  11. Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
  12. Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
  13. Sphingomyelin phosphodiesterase 2
  14. Proactivator polypeptide
  15. Ganglioside GM2 activator
  16. T-cell surface glycoprotein CD1e, membrane-associated
  17. Epididymal secretory protein E1
  18. Antigen-presenting glycoprotein CD1d
  19. GPI mannosyltransferase 1
  20. Phosphatidylinositol-glycan biosynthesis class W protein
  21. Phosphatidylinositol-glycan biosynthesis class X protein
  22. GPI mannosyltransferase 4
  23. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  24. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
  25. Sphingomyelin phosphodiesterase 3
  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
  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. Sphingomyelin phosphodiesterase 4
  39. Non-lysosomal glucosylceramidase
  40. cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
  41. Sphingomyelin synthase-related protein 1
  42. GPI-anchor transamidase
  43. Glycosylphosphatidylinositol anchor attachment 1 protein
  44. Protein PLEKHA9
  45. Glycolipid transfer protein domain-containing protein 2
  46. Putative uncharacterized protein PLEKHA8
  47. Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
  48. T-cell surface glycoprotein CD1a
  49. Glycolipid transfer protein domain-containing protein 1
  50. T-cell surface glycoprotein CD1c
  51. Lipopolysaccharide-binding protein
  52. Putative uncharacterized protein DKFZp434L0435
  53. T-cell surface glycoprotein CD1b
  54. Glycolipid transfer protein
Enzyme 1 [top]
Enzyme 1 ID 5671
Enzyme 1 Name Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
Enzyme 1 Synonyms
  1. Forssman glycolipid synthase-like protein
Enzyme 1 Gene Name GBGT1
Enzyme 1 Protein Sequence >Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQP
VVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGK
YTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETS
MRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFP
YERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESH
LNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
Enzyme 1 Number of Residues 347
Enzyme 1 Molecular Weight 40126.9
Enzyme 1 Theoretical pI 8.63
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • membrane
Enzyme 1 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 1 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 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 6-26
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 6272650 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q8N5D6 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GBGT1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1044 bp
ATGCATCGCCGGAGACTGGCCCTGGGTCTGGGGTTCTGCCTGTTGGCGGGCACAAGCCTC
AGTGTCCTGTGGGTGTATCTTGAGAACTGGCTGCCAGTCTCCTATGTCCCCTATTATCTC
CCCTGCCCAGAGATCTTCAACATGAAGCTGCACTACAAGAGGGAGAAGCCACTCCAGCCC
GTGGTATGGTCACAGTACCCTCAGCCCAAGCTGCTGGAGCACAGGCCCACACAGCTGCTG
ACACTCACACCCTGGTTGGCGCCCATCGTCTCCGAGGGAACCTTCAACCCAGAGCTTCTG
CAGCACATCTACCAGCCACTGAACCTGACCATTGGGGTCACGGTGTTTGCCGTGGGGAAG
TACACTCATTTCATCCAGTCCTTCCTGGAGTCAGCCGAGGAGTTCTTCATGCGTGGGTAC
CGGGTGCACTACTACATCTTCACTGACAACCCTGCAGCCGTTCCCGGGGTCCCGCTGGGT
CCCCACCAGCTTCTCAGCTCCATCCCCATCCAGGGTCACTCCCACTGGGAGGAGACATCC
ATGCGCCGGATGGAGACCATCAGCCAGCACATTGCTAAGAGGGCTCACCGGGAGGTGGAC
TACTTTTTCTGCCTTGATGTGGACATGGTGTTTCGGAACCCGTGGGGCCCTGAGACCTTG
GGAGACCTGGTGGCTGCCATTCACCCAAGCTACTACGCCGTTCCCCGCCAGCAGTTCCCC
TATGAGCGCAGGCGTGTTTCCACTGCCTTTGTGGCAGACAGGGAAGGGGACTTCTATTAT
GGTGGGGCAGTCTTCGGGGGGCAGGTGGCCAGGGTATATGAGTTTACTAGGGGCTGCCAC
ATGGCCATCCTGGCGGACAAGGCCAATGGCATCATGGCTGCCTGGCGGGAGGAAAGCCAC
CTGAACCGTCACTTCATCTCAAACAAGCCGTCCAAGGTGCTGTCCCCCGAGTACCTCTGG
GACGACAGGAAGCCCCAGCCACCCAGCCTGAAGCTGATCCGCTTTTCTACACTGGACAAG
GATATCAGCTGCCTGAGGAGCTGA
Enzyme 1 GenBank Gene ID AF163572 Link Image
Enzyme 1 GeneCard ID GBGT1 Link Image
Enzyme 1 GenAtlas ID GBGT1 Link Image
Enzyme 1 HGNC ID HGNC:20460 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9q34.13-q34.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5829
Enzyme 2 Name N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Enzyme 2 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class L protein
  2. PIG-L
Enzyme 2 Gene Name PIGL
Enzyme 2 Protein Sequence >N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
Enzyme 2 Number of Residues 252
Enzyme 2 Molecular Weight 28531.0
Enzyme 2 Theoretical pI 8.23
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Involved in N-acetylglucosaminylphosphatidylinositol de
Enzyme 2 Specific Function Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate [RN:R03482 R05917]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 2-22
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4239986 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9Y2B2 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PIGL_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
Enzyme 2 GenBank Gene ID AB017165 Link Image
Enzyme 2 GeneCard ID PIGL Link Image
Enzyme 2 GenAtlas ID PIGL Link Image
Enzyme 2 HGNC ID HGNC:8966 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 17p12-p11.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6049
Enzyme 3 Name Phosphatidylcholine:ceramide cholinephosphotransferase 2
Enzyme 3 Synonyms
  1. Sphingomyelin synthase 2
Enzyme 3 Gene Name SGMS2
Enzyme 3 Protein Sequence >Phosphatidylcholine:ceramide cholinephosphotransferase 2
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
Enzyme 3 Number of Residues 365
Enzyme 3 Molecular Weight 42279.8
Enzyme 3 Theoretical pI 9.00
Enzyme 3 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Required for cell growth
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 80-100 128-148 159-179 206-226 248-268 275-295
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q8NHU3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SMS2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1098 bp
ATGGATATCATAGAGACAGCAAAACTTGAAGAACATTTGGAAAATCAACCCAGTGATCCT
ACGAACACTTATGCAAGACCCGCTGAACCTGTTGAAGAAGAAAACAAAAATGGCAATGGT
AAACCCAAGAGCTTATCCAGTGGGCTGCGAAAAGGCACCAAAAAGTACCCGGACTATATC
CAAATTGCTATGCCCACTGAATCAAGGAACAAATTTCCACTAGAGTGGTGGAAAACGGGC
ATTGCCTTCATATATGCAGTTTTCAACCTCGTCTTGACAACCGTCATGATCACAGTTGTA
CATGAGAGGGTCCCTCCCAAGGAGCTTAGCCCTCCACTCCCAGACAAGTTTTTTGATTAC
ATTGATAGGGTGAAATGGGCATTTTCTGTATCAGAAATAAATGGGATTATATTAGTTGGA
TTATGGATCACCCAGTGGCTGTTTCTGAGATACAAGTCAATAGTGGGACGCAGATTCTGT
TTTATTATTGGAACTTTATACCTGTATCGCTGCATTACAATGTATGTTACTACTCTACCT
GTGCCTGGAATGCATTTCCAGTGTGCTCCAAAGCTCAATGGAGACTCTCAGGCAAAAGTT
CAACGGATTCTACGATTGATTTCTGGTGGTGGATTGTCCATAACTGGATCACATATCTTA
TGTGGAGACTTCCTCTTCAGCGGTCACACGGTTACGCTGACACTGACTTATTTGTTCATC
AAAGAATATTCGCCTCGTCACTTCTGGTGGTATCATTTAATCTGCTGGCTGCTGAGTGCT
GCCGGGATCATCTGCATTCTTGTAGCACACGAACACTACACTATCGATGTGATCATTGCT
TATTATATCACAACACGACTGTTTTGGTGGTACCATTCAATGGCCAATGAAAAGAACTTG
AAGGTCTCTTCACAGACTAATTTCTTATCTCGAGCATGGTGGTTCCCCATCTTTTATTTT
TTTGAGAAAAATGTACAAGGCTCAATTCCTTGCTGCTTCTCCTGGCCGCTGTCTTGGCCT
CCTGGCTGCTTCAAATCATCATGCAAAAAGTATTCACGGGTTCAGAAGATTGGTGAAGAC
AATGAGAAATCGACCTGA
Enzyme 3 GenBank Gene ID AF452717 Link Image
Enzyme 3 GeneCard ID SGMS2 Link Image
Enzyme 3 GenAtlas ID SGMS2 Link Image
Enzyme 3 HGNC ID HGNC:28395 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q25
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed Link Image]
  4. Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed Link Image]
  5. Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed Link Image]
  6. Tani M, Kuge O: Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes. Biochem Biophys Res Commun. 2009 Apr 10;381(3):328-32. Epub 2009 Feb 20. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6054
Enzyme 4 Name Phosphatidylcholine:ceramide cholinephosphotransferase 1
Enzyme 4 Synonyms
  1. Medulla oblongata-derived protein
  2. Protein Mob
  3. Sphingomyelin synthase 1
  4. Transmembrane protein 23
Enzyme 4 Gene Name SGMS1
Enzyme 4 Protein Sequence >Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
Enzyme 4 Number of Residues 419
Enzyme 4 Molecular Weight 49207.3
Enzyme 4 Theoretical pI 8.51
Enzyme 4 GO Classification
Function
  • catalytic activity
Process
Component
  • cell part
  • membrane
Enzyme 4 General Function Involved in catalytic activity
Enzyme 4 Specific Function Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. Required for cell growth
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 142-162 190-210 221-241 282-302 310-330
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 29789379 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q86VZ5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SMS1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1242 bp
ATGAAGGAAGTGGTTTATTGGTCACCCAAGAAGGTGGCAGACTGGCTGCTGGAGAATGCT
ATGCCAGAATACTGTGAGCCTCTGGAGCATTTCACAGGCCAGGACTTGATCAACCTAACC
CAAGAGGATTTCAAAAAACCCCCCTTGTGCCGAGTCTCCTCTGACAATGGGCAGCGGCTC
CTGGACATGATAGAAACCCTGAAAATGGAGCACCATTTGGAAGCACACAAGAACGGCCAT
GCCAATGGGCACCTCAACATTGGCGTAGACATCCCCACCCCCGACGGCAGCTTCAGCATC
AAGATTAAACCCAACGGGATGCCAAATGGGTATAGGAAAGAGATGATAAAGATCCCCATG
CCAGAACTGGAGCGCTCTCAGTACCCCATGGAGTGGGGCAAGACTTTTCTGGCCTTTCTT
TATGCACTTTCCTGTTTCGTTCTCACCACAGTGATGATCTCGGTCGTCCACGAACGAGTA
CCTCCTAAGGAGGTGCAGCCTCCACTACCGGACACATTTTTTGACCATTTTAACCGGGTG
CAGTGGGCCTTTTCTATTTGTGAAATTAATGGCATGATCCTTGTAGGACTCTGGTTAATT
CAGTGGCTGCTCTTAAAATACAAGTCTATTATTAGCAGAAGATTTTTCTGCATAGTTGGC
ACGCTGTACCTGTATCGGTGTATTACAATGTATGTAACTACACTCCCAGTACCTGGTATG
CATTTCAACTGTTCTCCGAAGCTTTTCGGAGACTGGGAAGCCCAACTGCGAAGAATAATG
AAGCTCATTGCTGGAGGTGGCTTGTCTATCACTGGCTCTCACAACATGTGTGGGGACTAT
CTGTACAGCGGCCACACGGTCATGCTAACACTTACCTACTTATTTATCAAAGAGTATTCC
CCTCGGCGACTCTGGTGGTATCACTGGATTTGCTGGCTTCTCAGCGTAGTTGGAATCTTC
TGTATTCTCTTAGCGCATGACCACTACACTGTGGACGTGGTGGTGGCATATTACATCACC
ACGAGACTCTTCTGGTGGTATCACACTATGGCCAATCAGCAAGTGCTAAAGGAAGCTTCC
CAGATGAACCTCCTGGCCAGGGTGTGGTGGTACAGGCCATTTCAGTACTTTGAAAAGAAT
GTCCAAGGAATTGTACCTCGATCTTACCATTGGCCTTTCCCCTGGCCAGTAGTCCACCTC
AGTAGGCAAGTTAAATACAGCCGGCTGGTGAATGACACATAA
Enzyme 4 GenBank Gene ID Not Available
Enzyme 4 GeneCard ID SGMS1 Link Image
Enzyme 4 GenAtlas ID SGMS1 Link Image
Enzyme 4 HGNC ID HGNC:29799 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 10q11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T: Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J Biol Chem. 2004 Apr 30;279(18):18688-93. Epub 2004 Feb 19. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA: Human gene MOB: structure specification and aspects of transcriptional activity. Gene. 2004 Sep 1;338(2):257-65. [PubMed Link Image]
  5. Vladychenskaya IP, Dergunova LV, Limborska SA: In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein. Biomol Eng. 2002 Feb;18(6):263-8. [PubMed Link Image]
  6. Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed Link Image]
  7. Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed Link Image]
  8. Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6055
Enzyme 5 Name Sphingomyelin phosphodiesterase
Enzyme 5 Synonyms
  1. Acid sphingomyelinase
  2. aSMase
Enzyme 5 Gene Name SMPD1
Enzyme 5 Protein Sequence >Sphingomyelin phosphodiesterase
MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALSDSRVLWAPAEAH
PLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLC
NLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPT
VPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPG
AGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVT
ALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRT
LRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKV
HIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAF
LAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYILNLTQANIPGAIPHWQLLYRAR
ETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSAR
ADSPALCRHLMPDGSLPEAQSLWPRPLFC
Enzyme 5 Number of Residues 629
Enzyme 5 Molecular Weight 69751.3
Enzyme 5 Theoretical pI 7.30
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
  • sphingomyelin phosphodiesterase activity
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • sphingomyelin catabolic process
  • sphingomyelin metabolic process
Component
Enzyme 5 General Function Involved in hydrolase activity
Enzyme 5 Specific Function Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Isoform 2 and isoform 3 have lost catalytic activity
Enzyme 5 Pathways
Enzyme 5 Reactions
  • sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-46
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 179095 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P17405 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ASM_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1890 bp
ATGCCCCGCTACGGAGCGTCACTCCGCCAGAGCTGCCCCAGGTCCGGCCGGGAGCAGGGA
CAAGACGGGACCGCCGGAGCCCCCGGACTCCTTTGGATGGGCCTGGTGCTGGCGCTGGCG
CTGGCGCTGGCGCTGGCTCTGTCTGACTCTCGGGTTCTCTGGGCTCCGGCAGAGGCTCAC
CCTCTTTCTCCCCAAGGCCATCCTGCCAGGTTACATCGCATAGTGCCCCGGCTCCGAGAT
GTCTTTGGGTGGGGGAACCTCACCTGCCCAATCTGCAAAGGTCTATTCACCGCCATCAAC
CTCGGGCTGAAGAAGGAACCCAATGTGGCTCGCGTGGGCTCCGTGGCCATCAAGCTGTGC
AATCTGCTGAAGATAGCACCACCTGCCGTGTGCCAATCCATTGTCCACCTCTTTGAGGAT
GACATGGTGGAGGTGTGGAGACGCTCAGTGCTGAGCCCATCTGAGGCCTGTGGCCTGCTC
CTGGGCTCCACCTGTGGGCACTGGGACATTTTCTCATCTTGGAACATCTCTTTGCCTACT
GTGCCGAAGCCGCCCCCCAAACCCCCTAGCCCCCCAGCCCCAGGTGCCCCTGTCAGCCGC
ATCCTCTTCCTCACTGACCTGCACTGGGATCATGACTACCTGGAGGGCACGGACCCTGAC
TGTGCAGACCCACTGTGCTGCCGCCGGGGTTCTGGCCTGCCGCCCGCATCCCGGCCAGGT
GCCGGATACTGGGGCGAATACAGCAAGTGTGACCTGCCCCTGAGGACCCTGGAGAGCCTG
TTGAGTGGGCTGGGCCCAGCCGGCCCTTTTGATATGGTGTACTGGACAGGAGACATCCCC
GCACATGATGTCTGGCACCAGACTCGTCAGGACCAACTGCGGGCCCTGACCACCGTCACA
GCACTTGTGAGGAAGTTCCTGGGGCCAGTGCCAGTGTACCCTGCTGTGGGTAACCATGAA
AGCATACCTGTCAATAGCTTCCCTCCCCCCTTCATTGAGGGCAACCACTCCTCCCGCTGG
CTCTATGAAGCGATGGCCAAGGCTTGGGAGCCCTGGCTGCCTGCCGAAGCCCTGCGCACC
CTCAGAATTGGGGGGTTCTATGCTCTTTCCCCATACCCCGGTCTCCGCCTCATCTCTCTC
AATATGAATTTTTGTTCCCGTGAGAACTTCTGGCTCTTGATCAACTCCACGGATCCCGCA
GGACAGCTCCAGTGGCTGGTGGGGGAGCTTCAGGCTGCTGAGGATCGAGGAGACAAAGTG
CATATAATTGGCCACATTCCCCCAGGGCACTGTCTGAAGAGCTGGAGCTGGAATTATTAC
CGAATTGTAGCCAGGTATGAGAACACCCTGGCTGCTCAGTTCTTTGGCCACACTCATGTG
GATGAATTTGAGGTCTTCTATGATGAAGAGACTCTGAGCCGGCCGCTGGCTGTAGCCTTC
CTGGCACCCAGTGCAACTACCTACATCGGCCTTAATCCTGGTTACCGTGTGTACCAAATA
GATGGAAACTACTCCAGGAGCTCTCACGTGGTCCTGGACCATGAGACCTACATCCTGAAT
CTGACCCAGGCAAACATACCGGGAGCCATACCGCACTGGCAGCTTCTCTACAGGGCTCGA
GAAACCTATGGGCTGCCCAACACACTGCCTACCGCCTGGCACAACCTGGTATATCGCATG
CGGGGCGACATGCAACTTTTCCAGACCTTCTGGTTTCTCTACCATAAGGGCCACCCACCC
TCGGAGCCCTGTGGCACGCCCTGCCGTCTGGCTACTCTTTGTGCCCAGCTCTCTGCCCGT
GCTGACAGCCCTGCTCTGTGCCGCCACCTGATGCCAGATGGGAGCCTCCCAGAGGCCCAG
AGCCTGTGGCCAAGGCCACTGTTTTGCTAG
Enzyme 5 GenBank Gene ID M59916 Link Image
Enzyme 5 GeneCard ID SMPD1 Link Image
Enzyme 5 GenAtlas ID SMPD1 Link Image
Enzyme 5 HGNC ID HGNC:11120 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 11p15.4-p15.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Schuchman EH, Suchi M, Takahashi T, Sandhoff K, Desnick RJ: Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs. J Biol Chem. 1991 May 5;266(13):8531-9. [PubMed Link Image]
  2. Newrzella D, Stoffel W: Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene. Biol Chem Hoppe Seyler. 1992 Dec;373(12):1233-8. [PubMed Link Image]
  3. Schuchman EH, Levran O, Pereira LV, Desnick RJ: Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1). Genomics. 1992 Feb;12(2):197-205. [PubMed Link Image]
  4. Ida H, Rennert OM, Eto Y, Chan WY: Cloning of a human acid sphingomyelinase cDNA with a new mutation that renders the enzyme inactive. J Biochem (Tokyo). 1993 Jul;114(1):15-20. [PubMed Link Image]
  5. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  6. Quintern LE, Schuchman EH, Levran O, Suchi M, Ferlinz K, Reinke H, Sandhoff K, Desnick RJ: Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts. EMBO J. 1989 Sep;8(9):2469-73. [PubMed Link Image]
  7. Ferlinz K, Hurwitz R, Moczall H, Lansmann S, Schuchman EH, Sandhoff K: Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis. Eur J Biochem. 1997 Jan 15;243(1-2):511-7. [PubMed Link Image]
  8. Lansmann S, Schuette CG, Bartelsen O, Hoernschemeyer J, Linke T, Weisgerber J, Sandhoff K: Human acid sphingomyelinase. Eur J Biochem. 2003 Mar;270(6):1076-88. [PubMed Link Image]
  9. Dastani Z, Ruel IL, Engert JC, Genest J Jr, Marcil M: Sphingomyelin phosphodiesterase-1 (SMPD1) coding variants do not contribute to low levels of high-density lipoprotein cholesterol. BMC Med Genet. 2007 Dec 18;8:79. [PubMed Link Image]
  10. Ferlinz K, Hurwitz R, Sandhoff K: Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A. Biochem Biophys Res Commun. 1991 Sep 30;179(3):1187-91. [PubMed Link Image]
  11. Levran O, Desnick RJ, Schuchman EH: Niemann-Pick disease: a frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3748-52. [PubMed Link Image]
  12. Levran O, Desnick RJ, Schuchman EH: Niemann-Pick type B disease. Identification of a single codon deletion in the acid sphingomyelinase gene and genotype/phenotype correlations in type A and B patients. J Clin Invest. 1991 Sep;88(3):806-10. [PubMed Link Image]
  13. Levran O, Desnick RJ, Schuchman EH: Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients. Blood. 1992 Oct 15;80(8):2081-7. [PubMed Link Image]
  14. Takahashi T, Desnick RJ, Takada G, Schuchman EH: Identification of a missense mutation (S436R) in the acid sphingomyelinase gene from a Japanese patient with type B Niemann-Pick disease. Hum Mutat. 1992;1(1):70-1. [PubMed Link Image]
  15. Takahashi T, Suchi M, Desnick RJ, Takada G, Schuchman EH: Identification and expression of five mutations in the human acid sphingomyelinase gene causing types A and B Niemann-Pick disease. Molecular evidence for genetic heterogeneity in the neuronopathic and non-neuronopathic forms. J Biol Chem. 1992 Jun 25;267(18):12552-8. [PubMed Link Image]
  16. Sperl W, Bart G, Vanier MT, Christomanou H, Baldissera I, Steichen-Gersdorf E, Paschke E: A family with visceral course of Niemann-Pick disease, macular halo syndrome and low sphingomyelin degradation rate. J Inherit Metab Dis. 1994;17(1):93-103. [PubMed Link Image]
  17. Schuchman EH: Two new mutations in the acid sphingomyelinase gene causing type a Niemann-pick disease: N389T and R441X. Hum Mutat. 1995;6(4):352-4. [PubMed Link Image]
  18. Takahashi T, Suchi M, Sato W, Ten SB, Sakuragawa N, Desnick RJ, Schuchman EH, Takada G: Identification and expression of a missense mutation (Y446C) in the acid sphingomyelinase gene from a Japanese patient with type A Niemann-Pick disease. Tohoku J Exp Med. 1995 Oct;177(2):117-23. [PubMed Link Image]
  19. Ida H, Rennert OM, Maekawa K, Eto Y: Identification of three novel mutations in the acid sphinogomyelinase gene of Japanese patients with Niemann-Pick disease type A and B. Hum Mutat. 1996;7(1):65-7. [PubMed Link Image]
  20. Pavlu H, Elleder M: Two novel mutations in patients with atypical phenotypes of acid sphingomyelinase deficiency. J Inherit Metab Dis. 1997 Aug;20(4):615-6. [PubMed Link Image]
  21. Simonaro CM, Desnick RJ, McGovern MM, Wasserstein MP, Schuchman EH: The demographics and distribution of type B Niemann-Pick disease: novel mutations lead to new genotype/phenotype correlations. Am J Hum Genet. 2002 Dec;71(6):1413-9. Epub 2002 Oct 4. [PubMed Link Image]
  22. Sikora J, Pavlu-Pereira H, Elleder M, Roelofs H, Wevers RA: Seven novel acid sphingomyelinase gene mutations in Niemann-Pick type A and B patients. Ann Hum Genet. 2003 Jan;67(Pt 1):63-70. [PubMed Link Image]
  23. Ricci V, Stroppiano M, Corsolini F, Di Rocco M, Parenti G, Regis S, Grossi S, Biancheri R, Mazzotti R, Filocamo M: Screening of 25 Italian patients with Niemann-Pick A reveals fourteen new mutations, one common and thirteen private, in SMPD1. Hum Mutat. 2004 Jul;24(1):105. [PubMed Link Image]
  24. Pittis MG, Ricci V, Guerci VI, Marcais C, Ciana G, Dardis A, Gerin F, Stroppiano M, Vanier MT, Filocamo M, Bembi B: Acid sphingomyelinase: identification of nine novel mutations among Italian Niemann Pick type B patients and characterization of in vivo functional in-frame start codon. Hum Mutat. 2004 Aug;24(2):186-7. [PubMed Link Image]
  25. Dardis A, Zampieri S, Filocamo M, Burlina A, Bembi B, Pittis MG: Functional in vitro characterization of 14 SMPD1 mutations identified in Italian patients affected by Niemann Pick Type B disease. Hum Mutat. 2005 Aug;26(2):164. [PubMed Link Image]
  26. Pavlu-Pereira H, Asfaw B, Poupctova H, Ledvinova J, Sikora J, Vanier MT, Sandhoff K, Zeman J, Novotna Z, Chudoba D, Elleder M: Acid sphingomyelinase deficiency. Phenotype variability with prevalence of intermediate phenotype in a series of twenty-five Czech and Slovak patients. A multi-approach study. J Inherit Metab Dis. 2005;28(2):203-27. [PubMed Link Image]
  27. Mussig K, Harzer K, Mayrhofer H, Krageloh-Mann I, Haring HU, Machicao F: Clinical findings in Niemann-Pick disease type B. Intern Med J. 2006 Feb;36(2):135-6. [PubMed Link Image]
  28. Rodriguez-Pascau L, Gort L, Schuchman EH, Vilageliu L, Grinberg D, Chabas A: Identification and characterization of SMPD1 mutations causing Niemann-Pick types A and B in Spanish patients. Hum Mutat. 2009 Jul;30(7):1117-22. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6223
Enzyme 6 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
Enzyme 6 Synonyms
  1. Beta-1,3-glucuronyltransferase 1
  2. Glucuronosyltransferase P
  3. GlcAT-P
  4. UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
  5. GlcUAT-P
Enzyme 6 Gene Name B3GAT1
Enzyme 6 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSD
RDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVV
EDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRET
FPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVG
WKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPK
AANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
Enzyme 6 Number of Residues 334
Enzyme 6 Molecular Weight 38255.7
Enzyme 6 Theoretical pI 10.03
Enzyme 6 GO Classification
Function
  • UDP-glycosyltransferase activity
  • catalytic activity
  • galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
  • glucuronosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
  • cell part
  • membrane
Enzyme 6 General Function Involved in galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
Enzyme 6 Specific Function Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo- orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity:stearoyl- sphingomyelin was the most effective, followed by palmitoyl- sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group
Enzyme 6 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 6 Reactions
  • UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O- beta-D-xylosylprotein [RN:R04607 R05928]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 7-27
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 8051678 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9P2W7 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B3GA1_HUMAN Link Image
Enzyme 6 PDB ID 1V84 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1005 bp
ATGCCGAAGAGACGGGACATCCTAGCGATCGTCCTCATCGTGCTGCCCTGGACTCTGCTC
ATCACTGTCTGGCACCAGAGCACCCTCGCACCCCTGCTCGCGGTACATAAGGATGAGGGC
AGTGACCCCCGACGCGAAACGCCGCCCGGCGCCGACCCCAGGGAGTACTGCACGTCTGAC
CGCGACATCGTGGAGGTGGTGCGCACCGAGTACGTGTACACGCGGCCCCCGCCATGGTCC
GACACGCTGCCCACCATCCACGTGGTGACGCCCACCTACAGCCGCCCGGTGCAGAAGGCC
GAGCTGACGCGCATGGCCAACACGCTGCTGCACGTGCCCAACCTCCACTGGCTGGTGGTG
GAGGATGCGCCGCGCCGGACGCCGCTGACCGCGCGCCTGCTGCGCGACACCGGCCTCAAC
TACACGCACCTGCACGTGGAGACGCCCCGCAACTACAAGCTGCGCGGAGACGCCCGCGAC
CCACGCATCCCGCGGGGCACCATGCAGCGCAACCTGGCCCTGCGCTGGCTGCGCGAGACC
TTCCCGCGCAACTCCAGCCAGCCTGGCGTGGTCTACTTCGCCGACGACGACAACACCTAC
AGCCTGGAGCTCTTCGAAGAGATGCGCAGCACCAGGAGGGTGTCCGTGTGGCCCGTCGCC
TTCGTGGGTGGCCTGCGGTACGAGGCCCCACGGGTGAACGGGGCAGGGAAGGTGGTCCGC
TGGAAGACGGTGTTTGACCCCCACCGGCCATTTGCAATAGACATGGCTGGATTTGCCGTC
AACCTGCGGCTCATTCTGCAGCGAAGCCAGGCCTACTTCAAGCTGCGAGGTGTGAAGGGA
GGCTACCAGGAAAGCAGCCTCCTTCGAGAACTTGTCACCCTCAACGACCTGGAGCCCAAG
GCAGCCAACTGCACCAAGATCCTGGTGTGGCACACACGGACAGAGAAGCCAGTGCTGGTG
AATGAGGGCAAGAAGGGCTTCACTGACCCCTCGGTGGAGATCTGA
Enzyme 6 GenBank Gene ID AB029396 Link Image
Enzyme 6 GeneCard ID B3GAT1 Link Image
Enzyme 6 GenAtlas ID B3GAT1 Link Image
Enzyme 6 HGNC ID HGNC:921 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 11q25
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Mitsumoto Y, Oka S, Sakuma H, Inazawa J, Kawasaki T: Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope. Genomics. 2000 Apr 15;65(2):166-73. [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. Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R: Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1. J Biol Chem. 2004 May 21;279(21):22693-703. Epub 2004 Mar 1. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6228
Enzyme 7 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
Enzyme 7 Synonyms
  1. N-acetylglucosamyl transferase component GPI1
  2. Phosphatidylinositol-glycan biosynthesis class Q protein
  3. PIG-Q
Enzyme 7 Gene Name PIGQ
Enzyme 7 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL
Enzyme 7 Number of Residues 760
Enzyme 7 Molecular Weight 84081.4
Enzyme 7 Theoretical pI 8.08
Enzyme 7 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 7 General Function Involved in phosphatidylinositol N-acetylglucosaminyltransferase activity
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 [RN:R02654 R05916]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 278-298 349-371 378-400 446-468 475-497
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 22538453 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9BRB3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PIGQ_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2283 bp
ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGACGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGCCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTCGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGATAAACCCACTGCCCTACAGCCGCGTGGT
GCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTGTG
CCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAGGA
CTGAGGGAACTGCTGGCTCGCCTGGCACCACCACACGGCCACAGCCAGCCATCTGCTCTG
CCAGGGTGGCACCAGCTCAGCTGGCGCATGTCCTGTGCTTTGTGGACGCTGCTGTGTGCT
CCTGAACACGGCAGGCCCTGCTATCACACCTTGGGCTTGGAGGTCATTGGGAGTGAGCAG
ATGTGGGGGTGGCCAGCCAGGCTGGCCGCACTCCATCACTGGCACTGCCTGCCTTGGGAC
CCGCTTCCCACCTGCTGCGGTCACCATGGTGGCGAGCACAGCAACCCCAGGTGTCCAGAG
CACTGCCCCATGCCCACCCTGTGTACCCAGGTCCAGAGGGTCCGTCCACCACAGCAGCCC
CAGGTGGAGGGCTGGTCTCCCTGGGGGCTCCCCAGTGGCTCTGCCCTGGCTGTGGGGGTG
GAGGGACCTTGCCAGGATGAACCCCCCAGTCCCAGGCACCCTCTAGCTCCCTCAGCCGAA
CAGCACCCTGCATCTGGGGGATTGAAGCAGTCGCTGACCCCCGTCCCCAGCGGGCCCGGG
CCCTCACTCCCTGAACCACACGGGGTTTATTTGCGGATGTTCCCTGGAGAGGTCGCTTTG
TGA
Enzyme 7 GenBank Gene ID NM_148920.1 Link Image
Enzyme 7 GeneCard ID PIGQ Link Image
Enzyme 7 GenAtlas ID PIGQ Link Image
Enzyme 7 HGNC ID HGNC:14135 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 16p13.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6229
Enzyme 8 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 8 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol-glycan biosynthesis class A protein
  3. PIG-A
Enzyme 8 Gene Name PIGA
Enzyme 8 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 8 Number of Residues 484
Enzyme 8 Molecular Weight 54126.1
Enzyme 8 Theoretical pI 8.41
Enzyme 8 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 8 General Function Involved in biosynthetic process
Enzyme 8 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor 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 [RN:R02654 R05916]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 422-442
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 23398601 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID BC038236 Link Image
Enzyme 8 GeneCard ID PIGA Link Image
Enzyme 8 GenAtlas ID PIGA Link Image
Enzyme 8 HGNC ID HGNC:8957 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6230
Enzyme 9 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
Enzyme 9 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class H protein
  2. PIG-H
Enzyme 9 Gene Name PIGH
Enzyme 9 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP
Enzyme 9 Number of Residues 188
Enzyme 9 Molecular Weight 21080.4
Enzyme 9 Theoretical pI 6.72
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Involved in phosphatidylinositol N-acetylglucosaminyltr
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 [RN:R02654 R05916]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 189054281 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q14442 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PIGH_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >567 bp
ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA
Enzyme 9 GenBank Gene ID AK314108 Link Image
Enzyme 9 GeneCard ID PIGH Link Image
Enzyme 9 GenAtlas ID PIGH Link Image
Enzyme 9 HGNC ID HGNC:8964 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 14q24.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6231
Enzyme 10 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
Enzyme 10 Synonyms
  1. Down syndrome critical region protein 5
  2. Down syndrome critical region protein C
  3. Phosphatidylinositol-glycan biosynthesis class P protein
  4. PIG-P
Enzyme 10 Gene Name PIGP
Enzyme 10 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
MVPRSTSLTLIVFLFHRLSKAPGKMVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFI
PESWLNSLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNYAK
NQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN
Enzyme 10 Number of Residues 158
Enzyme 10 Molecular Weight 18089.1
Enzyme 10 Theoretical pI 9.20
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Involved in phosphatidylinositol N-acetylglucosaminyltr
Enzyme 10 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 10 Pathways Not Available
Enzyme 10 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 40-60 80-100
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 24497597 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P57054 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PIGP_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >477 bp
ATGGTGCCACGGAGCACATCGCTGACGCTGATTGTGTTCCTTTTCCACAGATTGTCTAAA
GCCCCAGGAAAAATGGTGGAAAATTCACCGTCGCCATTGCCAGAAAGAGCGATTTATGGC
TTTGTTCTTTTCTTAAGCTCCCAATTTGGCTTCATACTTTACCTCGTGTGGGCCTTTATT
CCTGAATCTTGGCTAAACTCTTTAGGTTTAACCTATTGGCCTCAAAAATATTGGGCAGTT
GCATTACCTGTCTACCTCCTTATTGCTATAGTAATTGGCTACGTGCTCTTGTTTGGGATT
AACATGATGAGTACCTCTCCACTCGACTCCATCCATACAATCACAGATAACTATGCAAAA
AATCAACAGCAGAAGAAATACCAAGAGGAGGCCATTCCAGCCTTAAGAGATATTTCTATT
AGTGAAGTAAACCAAATGTTCTTTCTTGCAGCCAAAGAACTTTACACCAAAAACTGA
Enzyme 10 GenBank Gene ID NM_153681.2 Link Image
Enzyme 10 GeneCard ID PIGP Link Image
Enzyme 10 GenAtlas ID PIGP Link Image
Enzyme 10 HGNC ID HGNC:3046 Link Image
Enzyme 10 Chromosome Location 2
Enzyme 10 Locus 21q22.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  6. 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]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6232
Enzyme 11 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
Enzyme 11 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class C protein
  2. PIG-C
Enzyme 11 Gene Name PIGC
Enzyme 11 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
Enzyme 11 Number of Residues 297
Enzyme 11 Molecular Weight 33582.2
Enzyme 11 Theoretical pI 8.55
Enzyme 11 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • phosphatidylinositol N-acetylglucosaminyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 11 General Function Involved in phosphatidylinositol N-acetylglucosaminyltransferase activity
Enzyme 11 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 11 Pathways Not Available
Enzyme 11 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 51-71 80-100 154-174 239-259
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 2547042 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q92535 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PIGC_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >894 bp
ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTTCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA
Enzyme 11 GenBank Gene ID AB000360 Link Image
Enzyme 11 GeneCard ID PIGC Link Image
Enzyme 11 GenAtlas ID PIGC Link Image
Enzyme 11 HGNC ID HGNC:8960 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1q23-q25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6378
Enzyme 12 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
Enzyme 12 Synonyms
  1. E-NPP 7
  2. NPP-7
  3. Alkaline sphingomyelin phosphodiesterase
  4. Intestinal alkaline sphingomyelinase
  5. Alk-SMase
Enzyme 12 Gene Name ENPP7
Enzyme 12 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
MRGLAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARD
GVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWD
NGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVM
AWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLN
LIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDAL
KDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDM
DMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALP
PDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA
Enzyme 12 Number of Residues 458
Enzyme 12 Molecular Weight 51493.4
Enzyme 12 Theoretical pI 6.88
Enzyme 12 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 12 General Function Involved in catalytic activity
Enzyme 12 Specific Function Converts sphingomyelin to ceramide. Also has phospholipase C activity toward palmitoyl lyso-phosphocholine. Does not appear to have nucleotide pyrophosphatase activity
Enzyme 12 Pathways
Enzyme 12 Reactions
  • sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-21
Enzyme 12 Transmembrane Regions
  • 434-454
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 45545421 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q6UWV6 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ENPP7_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1377 bp
ATGAGAGGCCTGGCCGTCCTCCTCACTGTGGCTCTGGCCACGCTCCTGGCTCCCGGGGCC
GGAGCACCGGTACAAAGTCAGGGCTCCCAGAACAAGCTGCTCCTGGTGTCCTTCGACGGC
TTCCGCTGGAACTACGACCAGGATGTGGACACCCCCAACCTGGACGCCATGGCCCGAGAC
GGGGTGAAGGCACGCTACATGACCCCCGCCTTTGTCACCATGACCAGCCCCTGCCACTTC
ACCCTGGTCACCGGCAAATATATCGAGAACCACGGGGTGGTTCACAACATGTACTACAAC
ACCACCAGCAAGGTGAAGCTGCCCTACCACGCCACGCTGGGCATCCAGAGGTGGTGGGAC
AACGGCAGCGTGCCCATCTGGATCACAGCCCAGAGGCAGGGCCTGAGGGCTGGCTCCTTC
TTCTACCCGGGCGGGAACGTCACCTACCAAGGGGTGGCTGTGACGCGGAGCCGGAAAGAA
GGCATCGCACACAACTACAAAAATGAGACGGAGTGGAGAGCGAACATCGACACAGTGATG
GCGTGGTTCACAGAGGAGGACCTGGATCTGGTCACACTCTACTTCGGGGAGCCGGACTCC
ACGGGCCACAGGTACGGCCCCGAGTCCCCGGAGAGGAGGGAGATGGTGCGGCAGGTGGAC
CGGACCGTGGGCTACCTCCGGGAGAGCATCGCGCGCAACCACCTCACAGACCGCCTCAAC
CTGATCATCACATCCGACCACGGCATGACGACCGTGGACAAACGGGCTGGCGACCTGGTT
GAATTCCACAAGTTCCCCAACTTCACCTTCCGGGACATCGAGTTTGAGCTCCTGGACTAC
GGACCAAACGGGATGCTGCTCCCTAAAGAAGGGAGGCTGGAGAAGGTGTACGATGCCCTC
AAGGACGCCCACCCCAAGCTCCACGTCTACAAGAAGGAGGCGTTCCCCGAGGCCTTCCAC
TACGCCAACAACCCCAGGGTCACACCCCTGCTGATGTACAGCGACCTTGGCTACGTCATC
CATGGGAGAATTAACGTCCAGTTCAACAATGGGGAGCACGGCTTTGACAACAAGGACATG
GACATGAAGACCATCTTCCGCGCTGTGGGCCCTAGCTTCAGGGCGGGCCTGGAGGTGGAG
CCCTTTGAGAGCGTCCACGTGTACGAGCTCATGTGCCGGCTGCTGGGCATCGTGCCCGAG
GCCAACGATGGGCACCTAGCTACTCTGCTGCCCATGCTGCACACAGAATCTGCTCTTCCG
CCTGATGGAAGGCCTACTCTCCTGCCCAAGGGAAGATCTGCTCTCCCGCCCAGCAGCAGG
CCCCTCCTCGTGATGGGACTGCTGGGGACCGTGATTCTTCTGTCTGAGGTCGCATAA
Enzyme 12 GenBank Gene ID NM_178543.3 Link Image
Enzyme 12 GeneCard ID ENPP7 Link Image
Enzyme 12 GenAtlas ID ENPP7 Link Image
Enzyme 12 HGNC ID HGNC:23764 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 17q25.3
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Duan RD, Bergman T, Xu N, Wu J, Cheng Y, Duan J, Nelander S, Palmberg C, Nilsson A: Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family. J Biol Chem. 2003 Oct 3;278(40):38528-36. Epub 2003 Jul 28. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
  6. Duan RD, Cheng Y, Hansen G, Hertervig E, Liu JJ, Syk I, Sjostrom H, Nilsson A: Purification, localization, and expression of human intestinal alkaline sphingomyelinase. J Lipid Res. 2003 Jun;44(6):1241-50. Epub 2003 Apr 1. [PubMed Link Image]
  7. Wu J, Cheng Y, Nilsson A, Duan RD: Identification of one exon deletion of intestinal alkaline sphingomyelinase in colon cancer HT-29 cells and a differentiation-related expression of the wild-type enzyme in Caco-2 cells. Carcinogenesis. 2004 Aug;25(8):1327-33. Epub 2004 Mar 11. [PubMed Link Image]
  8. Wu J, Hansen GH, Nilsson A, Duan RD: Functional studies of human intestinal alkaline sphingomyelinase by deglycosylation and mutagenesis. Biochem J. 2005 Feb 15;386(Pt 1):153-60. [PubMed Link Image]
  9. 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6379
Enzyme 13 Name Sphingomyelin phosphodiesterase 2
Enzyme 13 Synonyms
  1. Lyso-platelet-activating factor-phospholipase C
  2. Lyso-PAF-PLC
  3. Neutral sphingomyelinase
  4. N-SMase
  5. nSMase
Enzyme 13 Gene Name SMPD2
Enzyme 13 Protein Sequence >Sphingomyelin phosphodiesterase 2
MKPNFSLRLRIFNLNCWGIPYLSKHRADRMRRLGDFLNQESFDLALLEEVWSEQDFQYLR
QKLSPTYPAAHHFRSGIIGSGLCVFSKHPIQELTQHIYTLNGYPYMIHHGDWFSGKAVGL
LVLHLSGMVLNAYVTHLHAEYNRQKDIYLAHRVAQAWELAQFIHHTSKKADVVLLCGDLN
MHPEDLGCCLLKEWTGLHDAYLETRDFKGSEEGNTMVPKNCYVSQQELKPFPFGVRIDYV
LYKAVSGFYISCKSFETTTGFDPHRGTPLSDHEALMATLFVRHSPPQQNPSSTHGPAERS
PLMCVLKEAWTELGLGMAQARWWATFASYVIGLGLLLLALLCVLAAGGGAGEAAILLWTP
SVGLVLWAGAFYLFHVQEVNGLYRAQAELQHVLGRAREAQDLGPEPQPALLLGQQEGDRT
KEQ
Enzyme 13 Number of Residues 423
Enzyme 13 Molecular Weight 47645.3
Enzyme 13 Theoretical pI 6.98
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Involved in metal ion binding
Enzyme 13 Specific Function Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2- lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso- sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF
Enzyme 13 Pathways
Enzyme 13 Reactions
  • sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 330-350 354-374
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3021428 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O60906 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name NSMA_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1272 bp
ATGAAGCTCAACTTCTCCCTGCGACTGCGGATCTTCAACCTCAACTGCTGGGGCATTCCG
TACTTGAGCAAGCACCGGGCCGACCGCATGAGGCGCCTGGGAGACTTTCTGAACCAGGAG
AGCTTCGACCTGGCTTTGCTGGAGGAGGTGTGGAGTGAGCAGGACTTCCAGTACCTGAGA
CAGAAGCTGTCACCTACCTACCCAGCTGCACACCACTTCCGGAGCGGAATCATTGGCAGT
GGCCTCTGTGTCTTCTCCAAACATCCAATCCAGGAGCTTACCCAGCACATCTACACTCTC
AATGGCTACCCCTACATGATCCATCATGGTGACTGGTTCAGTGGGAAGGCTGTGGGGCTG
CTGGTGCTCCATCTAAGTGGCATGGTGCTCAACGCCTATGTGACCCATCTCCATGCCGAA
TACAATCGACAGAAGGACATCTACCTAGCACATCGTGTGGCCCAAGCTTGGGAATTGGCC
CAGTTCATCCACCACACATCCAAGAAGGCAGACGTGGTTCTGTTGTGTGGAGACCTCAAC
ATGCACCCAGAAGACCTGGGCTGCTGCCTGCTGAAGGAGTGGACAGGGCTTCATGATGCC
TATCTTGAAACTCGGGACTTCAAGGGCTCTGAGGAAGGCAACACAATGGTACCCAAGAAC
TGCTACGTCAGCCAGCAGGAGCTGAAGCCATTTCCCTTTGGTGTCCGCATTGACTACGTG
CTTTACAAGGCAGTTTCTGGGTTTTACATCTCCTGTAAGAGTTTTGAAACCACTACAGGC
TTTGACCCTCACAGTGGCACCCCCCTCTCTGATCATGAAGCCCTGATGGCTACTCTGTTT
GTGAGGCACAGCCCCCCACAGCAGAACCCCAGCTCTACCCACGGACCAGCAGAGAGGTCG
CCGTTGATGTGTGTGCTAAAGGAGGCCTGGACGGAGCTGGGTCTGGGCATGGCTCAGGCT
CGCTGGTGGGCCACCTTCGCTAGCTATGTGATTGGCCTGGGGCTGCTTCTCCTGGCACTG
CTGTGTGTCCTGGCGGCTGGAGGAGGGGCCGGGGAAGCTGCCATACTGCTCTGGACCCCC
AGTGTAGGGCTGGTGCTGTGGGCAGGTGCATTCTACCTCTTCCACGTACAGGAGGTCAAT
GGCTTATATAGGGCCCAGGCTGAGCTCCAGCATGTGCTAGGAAGGGCAAGGGAGGCCCAG
GATCTGGGCCCAGAGCCTCAGCCAGCCCTACTCCTGGGGCAGCAGGAGGGGGACAGAACT
AAAGAACAATAA
Enzyme 13 GenBank Gene ID AJ222801 Link Image
Enzyme 13 GeneCard ID SMPD2 Link Image
Enzyme 13 GenAtlas ID SMPD2 Link Image
Enzyme 13 HGNC ID HGNC:11121 Link Image
Enzyme 13 Chromosome Location 6
Enzyme 13 Locus 6q21
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Tomiuk S, Hofmann K, Nix M, Zumbansen M, Stoffel W: Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling? Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3638-43. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sawai H, Domae N, Nagan N, Hannun YA: Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C. J Biol Chem. 1999 Dec 31;274(53):38131-9. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 7010
Enzyme 14 Name Proactivator polypeptide
Enzyme 14 Synonyms
  1. Saposin-A
  2. Protein A
  3. Saposin-B-Val
  4. Saposin-B
  5. Cerebroside sulfate activator
  6. CSAct
  7. Dispersin
  8. Sphingolipid activator protein 1
  9. SAP-1
  10. Sulfatide/GM1 activator
  11. Saposin-C
  12. A1 activator
  13. Co-beta-glucosidase
  14. Glucosylceramidase activator
  15. Sphingolipid activator protein 2
  16. SAP-2
  17. Saposin-D
  18. Component C
  19. Protein C
Enzyme 14 Gene Name PSAP
Enzyme 14 Protein Sequence >Proactivator polypeptide
MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKS
LPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDI
IKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLY
PQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADI
CKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVE
PIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEV
VDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLD
RNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIG
ACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN
Enzyme 14 Number of Residues 524
Enzyme 14 Molecular Weight 58112.1
Enzyme 14 Theoretical pI 4.82
Enzyme 14 GO Classification
Function
Process
  • cellular lipid metabolic process
  • lipid metabolic process
  • membrane lipid metabolic process
  • metabolic process
  • primary metabolic process
  • sphingolipid metabolic process
Component
  • intracellular membrane-bounded organelle
  • lysosome
  • lytic vacuole
  • membrane-bounded organelle
  • organelle
  • vacuole
Enzyme 14 General Function Involved in lipid metabolic process
Enzyme 14 Specific Function Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12)
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-16
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 16306656 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P07602 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name SAP_HUMAN Link Image
Enzyme 14 PDB ID 1N69 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1575 bp
ATGTACGCCCTCTTCCTCCTGGCCAGCCTCCTGGGCGCGGCTCTAGCCGGCCCGGTCCTT
GGACTGAAAGAATGCACCAGGGGCTCGGCAGTGTGGTGCCAGAATGTGAAGACGGCGTCC
GACTGCGGGGCAGTGAAGCACTGCCTGCAGACCGTTTGGAACAAGCCAACAGTGAAATCC
CTTCCCTGCGACATATGCAAAGACGTTGTCACCGCAGCTGGTGATATGCTGAAGGACAAT
GCCACTGAGGAGGAGATCCTTGTTTACTTGGAGAAGACCTGTGACTGGCTTCCGAAACCG
AACATGTCTGCTTCATGCAAGGAGATAGTGGACTCCTACCTCCCTGTCATCCTGGACATC
ATTAAAGGAGAAATGAGCCGTCCTGGGGAGGTGTGCTCTGCTCTCAACCTCTGCGAGTCT
CTCCAGAAGCACCTAGCAGAGCTGAATCACCAGAAGCAGCTGGAGTCCAATAAGATCCCA
GAGCTGGACATGACTGAGGTGGTGGCCCCCTTCATGGCCAACATCCCTCTCCTCCTCTAC
CCTCAGGACGGCCCCCGCAGCAAGCCCCAGCCAAAGGATAATGGGGACGTTTGCCAGGAC
TGCATTCAGATGGTGACTGACATCCAGACTGCTGTACGGACCAACTCCACCTTTGTCCAG
GCCTTGGTGGAACATGTCAAGGAGGAGTGTGACCGCCTGGGCCCTGGCATGGCCGACATA
TGCAAGAACTATATCAGCCAGTATTCTGAAATTGCTATCCAGATGATGATGCACATGCAA
CCCAAGGAGATCTGTGCGCTGGTTGGGTTCTGTGATGAGGTGAAAGAGATGCCCATGCAG
ACTCTGGTCCCCGCCAAAGTGGCCTCCAAGAATGTCATCCCTGCCCTGGAACTGGTGGAG
CCCATTAAGAAGCACGAGGTCCCAGCAAAGTCTGATGTTTACTGTGAGGTGTGTGAATTC
CTGGTGAAGGAGGTGACCAAGCTGATTGACAACAACAAGACTGAGAAAGAAATACTCGAC
GCTTTTGACAAAATGTGCTCGAAGCTGCCGAAGTCCCTGTCGGAAGAGTGCCAGGAGGTG
GTGGACACGTACGGCAGCTCCATCCTGTCCATCCTGCTGGAGGAGGTCAGCCCTGAGCTG
GTGTGCAGCATGCTGCACCTCTGCTCTGGCACGCGGCTGCCTGCACTGACCGTTCACGTG
ACTCAGCCAAAGGACGGTGGCTTCTGCGAAGTGTGCAAGAAGCTGGTGGGTTATTTGGAT
CGCAACCTGGAGAAAAACAGCACCAAGCAGGAGATCCTGGCTGCTCTTGAGAAAGGCTGC
AGCTTCCTGCCAGACCCTTACCAGAAGCAGTGTGATCAGTTTGTGGCAGAGTACGAGCCC
GTGCTGATCGAGATCCTGGTGGAGGTGATGGATCCTTCCTTCGTGTGCTTGAAAATTGGA
GCCTGCCCCTCGGCCCATAAGCCCTTGTTGGGAACTGAGAAGTGTATATGGGGCCCAAGC
TACTGGTGCCAGAACACAGAGACAGCAGCCCAGTGCAATGCTGTCGAGCATTGCAAACGC
CATGTGTGGAACTAG
Enzyme 14 GenBank Gene ID BC001503 Link Image
Enzyme 14 GeneCard ID PSAP Link Image
Enzyme 14 GenAtlas ID PSAP Link Image
Enzyme 14 HGNC ID HGNC:9498 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 10q21-q22
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Rorman EG, Grabowski GA: Molecular cloning of a human co-beta-glucosidase cDNA: evidence that four sphingolipid hydrolase activator proteins are encoded by single genes in humans and rats. Genomics. 1989 Oct;5(3):486-92. [PubMed Link Image]
  2. Nakano T, Sandhoff K, Stumper J, Christomanou H, Suzuki K: Structure of full-length cDNA coding for sulfatide activator, a Co-beta-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. J Biochem (Tokyo). 1989 Feb;105(2):152-4. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. O'Brien JS, Kretz KA, Dewji N, Wenger DA, Esch F, Fluharty AL: Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. Science. 1988 Aug 26;241(4869):1098-101. [PubMed Link Image]
  5. Rorman EG, Scheinker V, Grabowski GA: Structure and evolution of the human prosaposin chromosomal gene. Genomics. 1992 Jun;13(2):312-8. [PubMed Link Image]
  6. Hiraiwa M, O'Brien JS, Kishimoto Y, Galdzicka M, Fluharty AL, Ginns EI, Martin BM: Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins). Arch Biochem Biophys. 1993 Jul;304(1):110-6. [PubMed Link Image]
  7. Kondoh K, Hineno T, Sano A, Kakimoto Y: Isolation and characterization of prosaposin from human milk. Biochem Biophys Res Commun. 1991 Nov 27;181(1):286-92. [PubMed Link Image]
  8. Holtschmidt H, Sandhoff K, Furst W, Kwon HY, Schnabel D, Suzuki K: The organization of the gene for the human cerebroside sulfate activator protein. FEBS Lett. 1991 Mar 25;280(2):267-70. [PubMed Link Image]
  9. Morimoto S, Martin BM, Yamamoto Y, Kretz KA, O'Brien JS, Kishimoto Y: Saposin A: second cerebrosidase activator protein. Proc Natl Acad Sci U S A. 1989 May;86(9):3389-93. [PubMed Link Image]
  10. Tyynela J, Palmer DN, Baumann M, Haltia M: Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis. FEBS Lett. 1993 Sep 6;330(1):8-12. [PubMed Link Image]
  11. Dewji NN, Wenger DA, O'Brien JS: Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8652-6. [PubMed Link Image]
  12. Dewji N, Wenger D, Fujibayashi S, Donoviel M, Esch F, Hill F, O'Brien JS: Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator. Biochem Biophys Res Commun. 1986 Jan 29;134(2):989-94. [PubMed Link Image]
  13. Kleinschmidt T, Christomanou H, Braunitzer G: Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1). Biol Chem Hoppe Seyler. 1988 Dec;369(12):1361-5. [PubMed Link Image]
  14. 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]
  15. Kleinschmidt T, Christomanou H, Braunitzer G: Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant. Biol Chem Hoppe Seyler. 1987 Dec;368(12):1571-8. [PubMed Link Image]
  16. Morimoto S, Martin BM, Kishimoto Y, O'Brien JS: Saposin D: a sphingomyelinase activator. Biochem Biophys Res Commun. 1988 Oct 14;156(1):403-10. [PubMed Link Image]
  17. Furst W, Machleidt W, Sandhoff K: The precursor of sulfatide activator protein is processed to three different proteins. Biol Chem Hoppe Seyler. 1988 May;369(5):317-28. [PubMed Link Image]
  18. Fluharty AL, Lombardo C, Louis A, Stevens RL, Whitelegge J, Waring AJ, To T, Fluharty CB, Faull KF: Preparation of the cerebroside sulfate activator (CSAct or saposin B) from human urine. Mol Genet Metab. 1999 Nov;68(3):391-403. [PubMed Link Image]
  19. Vaccaro AM, Salvioli R, Barca A, Tatti M, Ciaffoni F, Maras B, Siciliano R, Zappacosta F, Amoresano A, Pucci P: Structural analysis of saposin C and B. Complete localization of disulfide bridges. J Biol Chem. 1995 Apr 28;270(17):9953-60. [PubMed Link Image]
  20. Faull KF, Johnson J, Kim MJ, To T, Whitelegge JP, Stevens RL, Fluharty CB, Fluharty AL: Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein. J Mass Spectrom. 2000 Dec;35(12):1416-24. [PubMed Link Image]
  21. Tatti M, Salvioli R, Ciaffoni F, Pucci P, Andolfo A, Amoresano A, Vaccaro AM: Structural and membrane-binding properties of saposin D. Eur J Biochem. 1999 Jul;263(2):486-94. [PubMed Link Image]
  22. Ahn VE, Faull KF, Whitelegge JP, Higginson J, Fluharty AL, Prive GG: Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B. Protein Expr Purif. 2003 Jan;27(1):186-93. [PubMed Link Image]
  23. Faull KF, Whitelegge JP, Higginson J, To T, Johnson J, Krutchinsky AN, Standing KG, Waring AJ, Stevens RL, Fluharty CB, Fluharty AL: Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties. J Mass Spectrom. 1999 Oct;34(10):1040-54. [PubMed Link Image]
  24. 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]
  25. Ahn VE, Faull KF, Whitelegge JP, Fluharty AL, Prive GG: Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):38-43. Epub 2002 Dec 23. [PubMed Link Image]
  26. Gieselmann V, Zlotogora J, Harris A, Wenger DA, Morris CP: Molecular genetics of metachromatic leukodystrophy. Hum Mutat. 1994;4(4):233-42. [PubMed Link Image]
  27. Rafi MA, Zhang XL, DeGala G, Wenger DA: Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy. Biochem Biophys Res Commun. 1990 Jan 30;166(2):1017-23. [PubMed Link Image]
  28. Kretz KA, Carson GS, Morimoto S, Kishimoto Y, Fluharty AL, O'Brien JS: Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2541-4. [PubMed Link Image]
  29. Holtschmidt H, Sandhoff K, Kwon HY, Harzer K, Nakano T, Suzuki K: Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. J Biol Chem. 1991 Apr 25;266(12):7556-60. [PubMed Link Image]
  30. Schnabel D, Schroder M, Furst W, Klein A, Hurwitz R, Zenk T, Weber J, Harzer K, Paton BC, Poulos A, et al.: Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. J Biol Chem. 1992 Feb 15;267(5):3312-5. [PubMed Link Image]
  31. Schnabel D, Schroder M, Sandhoff K: Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. FEBS Lett. 1991 Jun 17;284(1):57-9. [PubMed Link Image]
  32. Regis S, Filocamo M, Corsolini F, Caroli F, Keulemans JL, van Diggelen OP, Gatti R: An Asn > Lys substitution in saposin B involving a conserved amino acidic residue and leading to the loss of the single N-glycosylation site in a patient with metachromatic leukodystrophy and normal arylsulphatase A activity. Eur J Hum Genet. 1999 Feb-Mar;7(2):125-30. [PubMed Link Image]
  33. Wrobe D, Henseler M, Huettler S, Pascual Pascual SI, Chabas A, Sandhoff K: A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD). J Inherit Metab Dis. 2000 Feb;23(1):63-76. [PubMed Link Image]
  34. Hulkova H, Cervenkova M, Ledvinova J, Tochackova M, Hrebicek M, Poupetova H, Befekadu A, Berna L, Paton BC, Harzer K, Boor A, Smid F, Elleder M: A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation. Hum Mol Genet. 2001 Apr 15;10(9):927-40. [PubMed Link Image]
  35. Spiegel R, Bach G, Sury V, Mengistu G, Meidan B, Shalev S, Shneor Y, Mandel H, Zeigler M: A mutation in the saposin A coding region of the prosaposin gene in an infant presenting as Krabbe disease: first report of saposin A deficiency in humans. Mol Genet Metab. 2005 Feb;84(2):160-6. [PubMed Link Image]
  36. Tylki-Szymanska A, Czartoryska B, Vanier MT, Poorthuis BJ, Groener JA, Lugowska A, Millat G, Vaccaro AM, Jurkiewicz E: Non-neuronopathic Gaucher disease due to saposin C deficiency. Clin Genet. 2007 Dec;72(6):538-42. Epub 2007 Oct 7. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 7061
Enzyme 15 Name Ganglioside GM2 activator
Enzyme 15 Synonyms
  1. Cerebroside sulfate activator protein
  2. GM2-AP
  3. Shingolipid activator protein 3
  4. SAP-3
  5. Ganglioside GM2 activator isoform short
Enzyme 15 Gene Name GM2A
Enzyme 15 Protein Sequence >Ganglioside GM2 activator
MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIV
PGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIP
TGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKR
LGCIKIAASLKGI
Enzyme 15 Number of Residues 193
Enzyme 15 Molecular Weight 20838.1
Enzyme 15 Theoretical pI 4.96
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Involved in sphingolipid activator protein activity
Enzyme 15 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 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function Not Available
Enzyme 15 Signals
  • 1-23
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 4587479 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P17900 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name SAP3_HUMAN Link Image
Enzyme 15 PDB ID 1PUB Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >582 bp
ATGCAGTCCCTGATGCAGGCTCCCCTCCTGATCGCCCTGGGCTTGCTTCTCGCGACCCCT
GCGCAAGCCCACCTGAAAAAGCCATCCCAGCTCAGTAGCTTTTCCTGGGATAACTGTGAT
GAAGGGAAGGACCCTGCGGTGATCAGAAGCCTGACTCTGGAGCCTGACCCCATCGTCGTT
CCTGGAAATGTGACCCTCAGTGTCGTGGGCAGCACCAGTGTCCCCCTGAGTTCTCCTCTG
AAGGTGGATTTAGTTTTGGAGAAGGAGGTGGCTGGCCTCTGGATCAAGATCCCATGCACA
GACTACATTGGCAGCTGTACCTTTGAACACTTCTGTGATGTGCTTGACATGTTAATTCCT
ACTGGGGAGCCCTGCCCAGAGCCCCTGCGTACCTATGGGCTTCCTTGCCACTGTCCCTTC
AAAGAAGGAACCTACTCACTGCCCAAGAGCGAATTCGTTGTGCCTGACCTGGAGCTGCCC
AGTTGGCTCACCACCGGGAACTACCGCATAGAGAGCGTCCTGAGCAGCAGTGGGAAGCGT
CTGGGCTGCATCAAGATCGCTGCCTCTCTAAAGGGCATATAG
Enzyme 15 GenBank Gene ID AF124719 Link Image
Enzyme 15 GeneCard ID GM2A Link Image
Enzyme 15 GenAtlas ID GM2A Link Image
Enzyme 15 HGNC ID HGNC:4367 Link Image
Enzyme 15 Chromosome Location 5
Enzyme 15 Locus 5q33.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 7905
Enzyme 16 Name T-cell surface glycoprotein CD1e, membrane-associated
Enzyme 16 Synonyms
  1. hCD1e
  2. R2G1
  3. CD1e antigen
  4. T-cell surface glycoprotein CD1e, soluble
  5. sCD1e
Enzyme 16 Gene Name CD1E
Enzyme 16 Protein Sequence >T-cell surface glycoprotein CD1e, membrane-associated
MLLLFLLFEGLCCPGENTAAPQALQSYHLAAEEQLSFRMLQTSSFANHSWAHSEGSGWLG
DLQTHGWDTVLGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYP
FEIQILAGCRMNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKE
ILQSLLGHTCPRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPV
WVMWMRGEQEQRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIH
WGGYSIFLILICLTVIVTLVILVVVDSRLKKQSSNKNILSPHTPSPVFLMGANTQDTKNS
RHQFCLAQVSWIKNRVLKKWKTRLNQLW
Enzyme 16 Number of Residues 388
Enzyme 16 Molecular Weight 43626.1
Enzyme 16 Theoretical pI 8.69
Enzyme 16 GO Classification
Function
Process
  • antigen processing and presentation
  • immune response
  • immune system process
Component
  • cell part
  • membrane
Enzyme 16 General Function Involved in immune response
Enzyme 16 Specific Function T-cell surface glycoprotein CD1e, soluble is required for the presentation of glycolipid antigens on the cell surface. The membrane-associated form is not active
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-19
Enzyme 16 Transmembrane Regions
  • 305-325
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 8249469 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P15812 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name CD1E_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1164 bp
ATGCTGCTCCTGTTCCTCCTCTTCGAGGGTCTCTGCTGTCCTGGGGAAAATACAGCAGCT
CCCCAGGCTCTACAATCCTATCATCTAGCAGCAGAGGAGCAGCTGTCCTTCCGCATGCTC
CAAACTTCCTCCTTTGCCAACCACAGCTGGGCACACAGTGAGGGCTCAGGATGGCTGGGT
GACCTGCAGACTCATGGCTGGGACACTGTCTTGGGCACCATCCGCTTTCTGAAGCCCTGG
TCCCATGGAAACTTCAGCAAGCAGGAGCTGAAAAACTTACAGTCACTGTTCCAGTTATAC
TTCCATAGTTTTATCCGGATAGTGCAAGCTTCTGCTGGTCAATTTCAGCTTGAATACCCC
TTCGAGATCCAGATATTAGCTGGCTGTAGAATGAATGCCCCACAAATCTTCTTAAATATG
GCATATCAAGGGTCAGATTTCCTGAGTTTCCAAGGAATTTCCTGGGAGCCATCTCCAGGA
GCAGGGATCCGGGCCCAGAACATCTGTAAAGTGCTCAATCGCTACCTAGATATTAAGGAA
ATACTGCAAAGCCTTCTTGGTCACACCTGCCCTCGATTTCTAGCGGGGCTCATGGAAGCA
GGGGAGTCAGAACTGAAACGGAAAGTGAAGCCAGAGGCCTGGCTGTCCTGTGGCCCCAGT
CCTGGCCCTGGCCGTCTGCAGCTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTG
TGGGTGATGTGGATGCGGGGTGAGCAGGAGCAGCGGGGCACTCAGCGAGGGGACGTCCTG
CCTAATGCTGACGAGACATGGTATCTCCGAGCAACCCTGGATGTGGCGGCTGGGGAGGCA
GCTGGCCTGTCCTGTCGGGTGAAACACAGCAGTCTAGGGGGCCATGATCTAATCATCCAT
TGGGGTGGATATTCCATCTTTCTCATCCTGATCTGTTTGACTGTGATAGTTACCCTGGTC
ATATTGGTTGTAGTTGACTCACGGTTAAAAAAACAGAGTTCAAATAAGAACATTCTTTCT
CCCCACACACCCAGCCCTGTCTTTCTCATGGGAGCCAACACTCAGGACACCAAGAATTCA
AGACATCAGTTCTGCTTGGCACAAGTATCGTGGATCAAAAACAGAGTATTGAAGAAGTGG
AAGACACGCCTAAACCAACTCTGG
Enzyme 16 GenBank Gene ID AJ289111 Link Image
Enzyme 16 GeneCard ID CD1E Link Image
Enzyme 16 GenAtlas ID CD1E Link Image
Enzyme 16 HGNC ID HGNC:1638 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 1q22-q23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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. Angenieux C, Salamero J, Fricker D, Cazenave JP, Goud B, Hanau D, de La Salle H: Characterization of CD1e, a third type of CD1 molecule expressed in dendritic cells. J Biol Chem. 2000 Dec 1;275(48):37757-64. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. 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. Tamouza R, Sghiri R, Ramasawmy R, Neonato MG, Mombo LE, Poirier JC, Schaeffer V, Fortier C, Labie D, Girot R, Toubert A, Krishnamoorthy R, Charron D: Two novel CD1 E alleles identified in black African individuals. Tissue Antigens. 2002 May;59(5):417-20. [PubMed Link Image]
  7. 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]
  8. 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]
  9. de la Salle H, Mariotti S, Angenieux C, Gilleron M, Garcia-Alles LF, Malm D, Berg T, Paoletti S, Maitre B, Mourey L, Salamero J, Cazenave JP, Hanau D, Mori L, Puzo G, De Libero G: Assistance of microbial glycolipid antigen processing by CD1e. Science. 2005 Nov 25;310(5752):1321-4. [PubMed Link Image]
  10. Maitre B, Angenieux C, Salamero J, Hanau D, Fricker D, Signorino F, Proamer F, Cazenave JP, Goud B, Tourne S, de la Salle H: Control of the intracellular pathway of CD1e. Traffic. 2008 Apr;9(4):431-45. Epub 2008 Jan 15. [PubMed Link Image]
  11. Maitre B, Angenieux C, Wurtz V, Layre E, Gilleron M, Collmann A, Mariotti S, Mori L, Fricker D, Cazenave JP, van Dorsselaer A, Gachet C, de Libero G, Puzo G, Hanau D, de la Salle H: The assembly of CD1e is controlled by an N-terminal propeptide which is processed in endosomal compartments. Biochem J. 2009 May 1;419(3):661-8. [PubMed Link Image]
  12. Tourne S, Maitre B, Collmann A, Layre E, Mariotti S, Signorino-Gelo F, Loch C, Salamero J, Gilleron M, Angenieux C, Cazenave JP, Mori L, Hanau D, Puzo G, De Libero G, de la Salle H: Cutting edge: a naturally occurring mutation in CD1e impairs lipid antigen presentation. J Immunol. 2008 Mar 15;180(6):3642-6. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 8178
Enzyme 17 Name Epididymal secretory protein E1
Enzyme 17 Synonyms
  1. Human epididymis-specific protein 1
  2. He1
  3. Niemann-Pick disease type C2 protein
Enzyme 17 Gene Name NPC2
Enzyme 17 Protein Sequence >Epididymal secretory protein E1
MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVT
FTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYP
SIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL
Enzyme 17 Number of Residues 151
Enzyme 17 Molecular Weight 16570.1
Enzyme 17 Theoretical pI 7.77
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Involved in cholesterol binding
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
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 12803417 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 BC002532 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 1
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. 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. 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]
  4. Leong WF, Chow VT: Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006 Apr;8(4):565-80. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
  8. Park WD, O'Brien JF, Lundquist PA, Kraft DL, Vockley CW, Karnes PS, Patterson MC, Snow K: Identification of 58 novel mutations in Niemann-Pick disease type C: correlation with biochemical phenotype and importance of PTC1-like domains in NPC1. Hum Mutat. 2003 Oct;22(4):313-25. [PubMed Link Image]
  9. Chikh K, Rodriguez C, Vey S, Vanier MT, Millat G: Niemann-Pick type C disease: subcellular location and functional characterization of NPC2 proteins with naturally occurring missense mutations. Hum Mutat. 2005 Jul;26(1):20-8. [PubMed Link Image]
  10. Millat G, Bailo N, Molinero S, Rodriguez C, Chikh K, Vanier MT: Niemann-Pick C disease: use of denaturing high performance liquid chromatography for the detection of NPC1 and NPC2 genetic variations and impact on management of patients and families. Mol Genet Metab. 2005 Sep-Oct;86(1-2):220-32. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 8289
Enzyme 18 Name Antigen-presenting glycoprotein CD1d
Enzyme 18 Synonyms
  1. R3G1
  2. CD1d antigen
Enzyme 18 Gene Name CD1D
Enzyme 18 Protein Sequence >Antigen-presenting glycoprotein CD1d
MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSN
DSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGC
EVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLL
NGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMR
GEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYT
SMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL
Enzyme 18 Number of Residues 335
Enzyme 18 Molecular Weight 37717.0
Enzyme 18 Theoretical pI 8.28
Enzyme 18 GO Classification
Function
Process
  • antigen processing and presentation
  • immune response
  • immune system process
Component
  • cell part
  • membrane
Enzyme 18 General Function Involved in immune response
Enzyme 18 Specific Function Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-19
Enzyme 18 Transmembrane Regions
  • 302-322
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 619800 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P15813 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name CD1D_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1008 bp
ATGGGGTGCCTGCTGTTTCTGCTGCTCTGGGCGCTCCTCCAGGCTTGGGGAAGCGCTGAA
GTCCCGCAAAGGCTTTTCCCCCTCCGCTGCCTCCAGATCTCGTCCTTCGCCAATAGCAGC
TGGACGCGCACCGACGGCTTGGCGTGGCTGGGGGAGCTGCAGACGCACAGCTGGAGCAAC
GACTCGGACACCGTCCGCTCTCTGAAGCCTTGGTCCCAGGGCACGTTCAGCGACCAGCAG
TGGGAGACGCTGCAGCATATATTTCGGGTTTATCGAAGCAGCTTCACCAGGGACGTGAAG
GAATTCGCCAAAATGCTACGCTTATCCTATCCCTTGGAGCTCCAGGTGTCCGCTGGCTGT
GAGGTGCACCCTGGGAACGCCTCAAATAACTTCTTCCATGTAGCATTTCAAGGAAAAGAT
ATCCTGAGTTTCCAAGGAACTTCTTGGGAGCCAACCCAAGAGGCCCCACTTTGGGTAAAC
TTGGCCATTCAAGTGCTCAACCAGGACAAGTGGACGAGGGAAACAGTGCAGTGGCTCCTT
AATGGCACCTGCCCCCAATTTGTCAGTGGCCTCCTTGAGTCAGGGAAGTCGGAACTGAAG
AAGCAAGTGAAGCCCAAGGCCTGGCTGTCCCGTGGCCCCAGTCCTGGCCCTGGCCGTCTG
CTGCTGGTGTGCCATGTCTCAGGATTCTACCCAAAGCCTGTATGGGTGAAGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCCAGGGGACATCCTGCCCAATGCTGACGAGACA
TGGTATCTCCGAGCAACCCTGGATGTGGTGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGGTGGGAGCTACACC
TCCATGGGCTTGATTGCCTTGGCAGTCCTGGCGTGCTTGCTGTTCCTCCTCATTGTGGGC
TTTACCTCCCGGTTTAAGAGGCAAACTTCCTATCAGGGCGTCCTGTGA
Enzyme 18 GenBank Gene ID J04142 Link Image
Enzyme 18 GeneCard ID CD1D Link Image
Enzyme 18 GenAtlas ID CD1D Link Image
Enzyme 18 HGNC ID HGNC:1637 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1q22-q23
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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. 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. Rodionov DG, Nordeng TW, Pedersen K, Balk SP, Bakke O: A critical tyrosine residue in the cytoplasmic tail is important for CD1d internalization but not for its basolateral sorting in MDCK cells. J Immunol. 1999 Feb 1;162(3):1488-95. [PubMed Link Image]
  8. Kang SJ, Cresswell P: Regulation of intracellular trafficking of human CD1d by association with MHC class II molecules. EMBO J. 2002 Apr 2;21(7):1650-60. [PubMed Link Image]
  9. Brutkiewicz RR: CD1d ligands: the good, the bad, and the ugly. J Immunol. 2006 Jul 15;177(2):769-75. [PubMed Link Image]
  10. Chen X, Wang X, Keaton JM, Reddington F, Illarionov PA, Besra GS, Gumperz JE: Distinct endosomal trafficking requirements for presentation of autoantigens and exogenous lipids by human CD1d molecules. J Immunol. 2007 May 15;178(10):6181-90. [PubMed Link Image]
  11. 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]
  12. Koch M, Stronge VS, Shepherd D, Gadola SD, Mathew B, Ritter G, Fersht AR, Besra GS, Schmidt RR, Jones EY, Cerundolo V: The crystal structure of human CD1d with and without alpha-galactosylceramide. Nat Immunol. 2005 Aug;6(8):819-26. Epub 2005 Jul 10. [PubMed Link Image]
  13. Borg NA, Wun KS, Kjer-Nielsen L, Wilce MC, Pellicci DG, Koh R, Besra GS, Bharadwaj M, Godfrey DI, McCluskey J, Rossjohn J: CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor. Nature. 2007 Jul 5;448(7149):44-9. Epub 2007 Jun 20. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 8469
Enzyme 19 Name GPI mannosyltransferase 1
Enzyme 19 Synonyms
  1. GPI mannosyltransferase I
  2. GPI-MT-I
  3. Phosphatidylinositol-glycan biosynthesis class M protein
  4. PIG-M
Enzyme 19 Gene Name PIGM
Enzyme 19 Protein Sequence >GPI mannosyltransferase 1
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
Enzyme 19 Number of Residues 423
Enzyme 19 Molecular Weight 49459.2
Enzyme 19 Theoretical pI 9.31
Enzyme 19 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 19 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 19 Specific Function Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 18-38 80-100 139-161 170-190 226-246 288-308 315-337 339-350 358-378 385-405
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 11414879 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9H3S5 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PIGM_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 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 19 GenBank Gene ID AB028127 Link Image
Enzyme 19 GeneCard ID PIGM Link Image
Enzyme 19 GenAtlas ID PIGM Link Image
Enzyme 19 HGNC ID HGNC:18858 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 1q23.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. 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. Almeida AM, Murakami Y, Layton DM, Hillmen P, Sellick GS, Maeda Y, Richards S, Patterson S, Kotsianidis I, Mollica L, Crawford DH, Baker A, Ferguson M, Roberts I, Houlston R, Kinoshita T, Karadimitris A: Hypomorphic promoter mutation in PIGM causes inherited glycosylphosphatidylinositol deficiency. Nat Med. 2006 Jul;12(7):846-51. Epub 2006 Jun 11. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8495
Enzyme 20 Name Phosphatidylinositol-glycan biosynthesis class W protein
Enzyme 20 Synonyms
  1. PIG-W
Enzyme 20 Gene Name PIGW
Enzyme 20 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class W protein
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
Enzyme 20 Number of Residues 504
Enzyme 20 Molecular Weight 56881.3
Enzyme 20 Theoretical pI 9.44
Enzyme 20 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 20 General Function Involved in transferase activity, transferring acyl groups
Enzyme 20 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 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 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 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 31339065 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q7Z7B1 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PIGW_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1515 bp
ATGTCTGAAAAGCAGATGAAGGAAGCTTTTGTCAGTAACCTCAATGGAACCACCGTGCTG
GAAATCACCCAGGGATTGTGCTTTCCTGCATTCTGTATCCTGTGCAGAGGGTTCCTGATC
ATTTTCTCACAGTACTTGTGTTCTTTTTCACCTACCTGGAAAACTAGATTCCTCACTGAC
TTTGTTGTCCTAATAGTTCCCATGGTAGCCACTTTGACCATTTGGGCTTCATTTATCCTC
CTTGAGCTTCTCGGTGTAATTATCTTTGGGGCAGGGCTGTTGTATCAAATATACCGAAGG
AGGACCTGCTATGCCAGACTGCCTTTCCTAAAAATCCTTGAAAAATTCTTGAACATCAGT
CTAGAATCAGAATACAATCCAGCCATCTCCTGTTTCCGTGTAATTACCAGTGCGTTTACT
GCTATTGCTATTTTGGCTGTGGACTTCCCACTTTTTCCCAGAAGATTTGCCAAAACTGAG
CTCTATGGGACAGGAGCAATGGATTTTGGAGTAGGTGGCTTTGTTTTTGGGTCTGCAATG
GTTTGTCTAGAGGTCAGGAGGAGAAAATATATGGAAGGGTCCAAATTGCATTACTTTACA
AACTCATTGTACTCTGTTTGGCCATTAGTCTTCCTAGGAATCGGACGATTAGCCATTATA
AAATCAATAGGCTATCAGGAACATTTAACAGAGTATGGAGTTCACTGGAACTTTTTCTTT
ACCATAATAGTTGTGAAATTGATAACACCACTGCTGTTGATTATTTTTCCCCTAAATAAG
TCCTGGATTATTGCCCTCGGCATTACTGTATTATACCAGCTAGCCCTTGACTTTACCTCA
CTGAAGAGGTTAATATTATATGGCACTGATGGTAGTGGCACACGGGTTGGTCTATTAAAT
GCCAACCGCGAAGGAATAATCTCTACCCTGGGGTATGTGGCAATACACATGGCTGGTGTG
CAAACAGGGTTATATATGCATAAGAACCGATCACATATCAAAGACTTGATAAAAGTAGCC
TGTTTTCTTTTACTGGCAGCTATTAGCCTCTTCATATCTCTTTACGTAGTTCAAGTAAAT
GTAGAAGCAGTATCTCGAAGAATGGCAAATTTAGCCTTTTGTATTTGGATAGTTGCTTCT
AGCCTGATCCTTCTTAGTAGTTTATTACTGGGTGATATAATTTTGAGTTTTGCCAAATTT
CTAATTAAAGGAGCTCTAGTACCATGTTCTTGGAAACTTATCCAGTCACCTGTTACAAAT
AAAAAGCATTCAGAATCTCTAGTCCCTGAAGCCGAAAGAATGGAACCCAGTCTTTGTTTA
ATCACAGCTCTAAACAGAAAACAGTTAATATTTTTCTTGCTGTCAAATATAACAACTGGC
CTGATCAACCTGATGGTAGATACATTACACAGCAGTACCTTGTGGGCCTTATTTGTGGTC
AATCTCTATATGTTTTCCAACTGTTTAATTGTATATGTACTATATTTGCAAGATAAGACT
GTACAATTTTGGTGA
Enzyme 20 GenBank Gene ID AB097818 Link Image
Enzyme 20 GeneCard ID PIGW Link Image
Enzyme 20 GenAtlas ID PIGW Link Image
Enzyme 20 HGNC ID HGNC:23213 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 17q12
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Murakami Y, Siripanyapinyo U, Hong Y, Kang JY, Ishihara S, Nakakuma H, Maeda Y, Kinoshita T: PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor. Mol Biol Cell. 2003 Oct;14(10):4285-95. Epub 2003 Jun 13. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 8621
Enzyme 21 Name Phosphatidylinositol-glycan biosynthesis class X protein
Enzyme 21 Synonyms
  1. PIG-X
Enzyme 21 Gene Name PIGX
Enzyme 21 Protein Sequence >Phosphatidylinositol-glycan biosynthesis class X protein
MAARVAAVRAAAWLLLGAATGLTRGPAAAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALENEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
Enzyme 21 Number of Residues 258
Enzyme 21 Molecular Weight 28788.1
Enzyme 21 Theoretical pI 6.30
Enzyme 21 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • membrane
  • organelle membrane
Enzyme 21 General Function Involved in GPI anchor biosynthetic process
Enzyme 21 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 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function Not Available
Enzyme 21 Signals
  • 1-21
Enzyme 21 Transmembrane Regions
  • 231-251
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 261490706 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8TBF5 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PIGX_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >777 bp
CTGGCGGCTCGGGTGGCGGCGGTTCGGGCGGCCGCCTGGCTGCTCCTCGGGGCGGCGACC
GGGCTCACGCGCGGGCCCGCCGCGGCCTTCACCGCCGCGCGCTCTGACGCCGGCATAAGG
GCCATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGAC
CTTTTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACCTGCCGTCTCTTA
ATTAAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGA
GAGAGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAAC
TATTTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGAC
TGTTTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGA
GAAGCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCG
ATTTTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGAGAATGAGGAT
ATCTGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTT
CCAGTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATC
CTGTGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
Enzyme 21 GenBank Gene ID NM_017861.3 Link Image
Enzyme 21 GeneCard ID PIGX Link Image
Enzyme 21 GenAtlas ID PIGX Link Image
Enzyme 21 HGNC ID HGNC:26046 Link Image
Enzyme 21 Chromosome Location 3
Enzyme 21 Locus 3q29
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Ashida H, Hong Y, Murakami Y, Shishioh N, Sugimoto N, Kim YU, Maeda Y, Kinoshita T: Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I. Mol Biol Cell. 2005 Mar;16(3):1439-48. Epub 2005 Jan 5. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 8625
Enzyme 22 Name GPI mannosyltransferase 4
Enzyme 22 Synonyms
  1. GPI mannosyltransferase IV
  2. GPI-MT-IV
  3. Phosphatidylinositol-glycan biosynthesis class Z protein
  4. PIG-Z
  5. SMP3 homolog
  6. hSMP3
Enzyme 22 Gene Name PIGZ
Enzyme 22 Protein Sequence >GPI mannosyltransferase 4
MQICGSSVASVAAGTSFQVLGPVCWQQLDLKMAVRVLWGGLSLLRVLWCLLPQTGYVHPD
EFFQSPEVMAEDILGVQAARPWEFYPSSSCRSVLFPLLISGSTFWLLRLWEELGPWPGLV
SGYALLVGPRLLLTALSFALDGAVYHLAPPMGADRWNALALLSGSYVTLVFYTRTFSNTI
EGLLFTWLLVLVSSHVTWGPTRKEPAPGPRWRSWLLGGIVAAGFFNRPTFLAFAVVPLYL
WGTRGATNPGLKSLTREALVLLPGATLTAAVFVATDSWYFSSPATSRNLVLTPVNFLHYN
LNPQNLARHGTHARLTHLAVNGFLLFGVLHAQALQAAWQQLQVGLQASAQMGLLRALGAR
SLLSSPRSYLLLLYFMPLALLSAFSHQEARFLIPLLVPLVLLCSPQTQPVPWKGTVVLFN
ALGALLFGCLHQGGLVPGLEYLEQVVHAPVLPSTPTHYTLLFTHTYMPPRHLLHLPGLGA
PVEVVDMGGTEDWALCQTLKSFTRQPACQVAGGPWLCRLFVVTPGTTRRAVEKCSFPFKN
ETLLFPHLTLEDPPALSSLLSGAWRDHLSLHIVELGEET
Enzyme 22 Number of Residues 579
Enzyme 22 Molecular Weight 63472.6
Enzyme 22 Theoretical pI 8.28
Enzyme 22 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 22 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 22 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 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 131-151 156-173 180-200 216-236 258-278 369-389 391-411 416-436
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 30581137 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q86VD9 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PIGZ_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1740 bp
ATGCAGATCTGTGGATCCAGCGTAGCATCTGTAGCAGCTGGGACATCATTCCAGGTTTTG
GGCCCGGTGTGTTGGCAACAACTGGATCTGAAGATGGCAGTCAGGGTGCTTTGGGGTGGT
CTCAGCCTGCTCCGAGTGCTGTGGTGTCTCCTTCCGCAGACGGGCTATGTGCACCCAGAT
GAGTTCTTCCAGTCCCCTGAGGTGATGGCAGAGGACATCCTGGGCGTTCAGGCCGCGCGG
CCCTGGGAGTTTTACCCCAGCAGCTCCTGCCGCTCGGTGCTCTTCCCCCTGCTGATCTCT
GGTTCCACCTTCTGGCTGCTCAGGCTCTGGGAGGAGCTGGGGCCGTGGCCTGGCCTGGTG
AGCGGCTATGCGCTGCTGGTGGGGCCTCGACTCCTCCTCACTGCCCTTTCCTTTGCTCTG
GACGGGGCCGTGTACCACCTGGCCCCGCCGATGGGGGCGGATCGCTGGAACGCCCTGGCC
CTGCTGTCTGGTTCCTACGTCACCCTGGTCTTCTACACAAGGACCTTCTCCAACACCATT
GAGGGACTCCTCTTCACGTGGCTGCTGGTGCTGGTATCCTCCCATGTAACGTGGGGCCCT
ACACGCAAGGAGCCGGCGCCGGGTCCACGGTGGCGCAGCTGGCTTCTTGGAGGCATTGTG
GCTGCTGGCTTCTTCAACCGGCCCACCTTTCTGGCCTTTGCTGTGGTCCCCCTCTACCTC
TGGGGCACTCGTGGAGCCACAAACCCTGGTTTGAAGTCTCTGACCCGGGAGGCCCTGGTG
CTGCTCCCTGGGGCAGCCCTCACAGCAGCGGTGTTTGTGGCCACGGACAGCTGGTATTTC
TCCAGCCCCGCTACATCCAGGAACCTTGTCCTGACACCTGTCAACTTCTTGCACTACAAC
CTGAATCCCCAAAACCTGGCGAGACATGGCACGCACGCGCGGCTCACTCACCTGGCAGTC
AACGGCTTCCTGCTCTTCGGGGTGCTGCATGCCCAGGCCCTGCAGGCTGCGTGGCAACGG
CTGCAAGTCGGCCTCCAGGCCTCTGCACAAATGGGCCTCCTGAGGGCACTGGGTGCCCGG
AGCCTGCTGTCCAGCCCCAGGTCCTATCTCCTTCTCCTCTACTTCATGCCTCTGGCCCTG
CTATCTGCCTTTAGCCACCAGGAGGCTCGGTTCCTGATTCCCCTCCTGGTCCCCCTGGTC
CTGCTTTGTAGTCCACAGACGCAGCCTGTGCCTTGGAAGGGCACTGTGGTCCTCTTCAAC
GCCCTCGGTGCCCTCCTCTTCGGCTGCCTGCATCAGGGGGGCCTGGTGCCTGGCCTGGAG
TACCTGGAGCAGGTGGTCCATGCCCCTGTGCTCCCAAGCACACCCACCCACTACACACTC
CTCTTCACTCACACCTACATGCCCCCCCGGCACCTCCTACACCTCCCAGGCCTGGGGGCA
CCAGTGGAGGTGGTGGACATGGGGGGGACTGAGGACTGGGCCCTGTGCCAAACCCTGAAA
AGCTTCACCAGACAACCAGCCTGCCAAGTGGCTGGTGGGCCATGGCTCTGCCGCCTCTTT
GTGGTAACCCCTGGCACCACCAGGCGTGCCGTGGAGAAGTGCAGCTTCCCCTTCAAGAAT
GAAACACTTTTATTTCCCCATCTGACCCTGGAGGATCCACCAGCCCTGTCCTCCTTGCTG
AGTGGGGCTTGGAGGGACCACCTCAGTCTTCACATTGTGGAGCTGGGGGAAGAAACCTGA
Enzyme 22 GenBank Gene ID NM_025163.2 Link Image
Enzyme 22 GeneCard ID PIGZ Link Image
Enzyme 22 GenAtlas ID PIGZ Link Image
Enzyme 22 HGNC ID HGNC:30596 Link Image
Enzyme 22 Chromosome Location 3
Enzyme 22 Locus 3q29
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Taron BW, Colussi PA, Wiedman JM, Orlean P, Taron CH: Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo. J Biol Chem. 2004 Aug 20;279(34):36083-92. Epub 2004 Jun 18. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 10050
Enzyme 23 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
Enzyme 23 Synonyms
  1. Phosphoinositide phospholipase C-delta-3
  2. Phospholipase C-delta-3
  3. PLC-delta-3
Enzyme 23 Gene Name PLCD3
Enzyme 23 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
Enzyme 23 Number of Residues 789
Enzyme 23 Molecular Weight 89257.5
Enzyme 23 Theoretical pI 6.97
Enzyme 23 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 23 General Function Involved in calcium ion binding
Enzyme 23 Specific Function Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow
Enzyme 23 Pathways
Enzyme 23 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein Not Available
Enzyme 23 UniProtKB/Swiss-Prot ID Q8N3E9 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PLCD3_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >2370 bp
ATGCTGTGCGGCCGCTGGAGGCGTTGCCGCCGCCCGCCCGAGGAGCCCCCGGTGGCCGCC
CAGGTCGCAGCCCAAGTCGCGGCGCCGGTCGCTCTCCCGTCCCCGCCGACTCCCTCCGAT
GGCGGCACCAAGAGGCCCGGGCTGCGGGCGCTGAAGAAGATGGGCCTGACGGAGGACGAG
GACGTGCGCGCCATGCTGCGGGGCTCCCGGCTCCGCAAGATCCGCTCGCGCACGTGGCAC
AAGGAGCGGCTGTACCGGCTGCAGGAGGACGGCCTGAGCGTGTGGTTCCAGCGGCGCATC
CCGCGTGCGCCATCGCAGCACATCTTCTTCGTGCAGCACATCGAGGCGGTCCGCGAGGGC
CACCAGTCCGAGGGCCTGCGGCGCTTCGGGGGTGCCTTCGCGCCAGCGCGCTGCCTCACC
ATCGCCTTCAAGGGCCGCCGCAAGAACCTGGACCTGGCGGCGCCCACGGCTGAGGAAGCG
CAGCGCTGGGTGCGCGGTCTGACCAAGCTCCGCGCGCGCCTGGACGCCATGAGCCAGCGC
GAGCGGCTAGACCACTGGATCCACTCCTATCTGCACCGGGCTGACTCCAACCAGGACAGC
AAGATGAGCTTCAAGGAGATCAAGAGCCTGCTGAGAATGGTCAACGTGGACATGAACGAC
ATGTACGCCTACCTCCTCTTCAAGGAGTGTGACCACTCCAACAACGACCGTCTAGAGGGG
GCTGAGATCGAGGAGTTCCTGCGGCGGCTGCTGAAGCGGCCGGAGCTGGAGGAGATCTTC
CATCAGTACTCGGGCGAGGACCGCGTGCTGAGTGCCCCTGAGCTGCTGGAGTTCCTGGAG
GACCAGGGCGAGGAGGGCGCCACACTGGCCCGCGCCCAGCAGCTCATTCAGACCTATGAG
CTCAACGAGACAGCCAAGCAGCATGAGCTGATGACACTGGATGGCTTCATGATGTACCTG
TTGTCGCCGGAGGGGGCTGCCTTGGACAACACCCACACGTGTGTGTTCCAGGACATGAAC
CAGCCCCTTGCCCACTACTTCATCTCTTCCTCCCACAACACCTATCTGACTGACTCCCAG
ATCGGGGGGCCCAGCAGCACCGAGGCCTATGTTAGGGCCTTTGCCCAGGGATGCCGCTGC
GTGGAGCTGGACTGCTGGGAGGGGCCAGGAGGGGAGCCCGTCATCTATCATGGCCATACC
CTCACCTCCAAGATTCTCTTCCGGGACGTGGTCCAAGCCGTGCGCGACCATGCCTTCACG
CTGTCCCCTTACCCTGTCATCCTATCCCTGGAGAACCACTGCGGGCTGGAGCAGCAGGCT
GCCATGGCCCGCCACCTCTGCACCATCCTGGGGGACATGCTGGTGACACAGGCGCTGGAC
TCCCCAAATCCCGAGGAGCTGCCATCCCCAGAGCAGCTGAAGGGCCGGGTCCTGGTGAAG
GGAAAGAAGTTGCCCGCTGCTCGGAGCGAGGATGGCCGGGCTCTGTCGGATCGGGAGGAG
GAGGAGGAGGATGACGAGGAGGAAGAAGAGGAGGTGGAGGCTGCAGCGCAGAGGCGGCTG
GCCAAGCAGATCTCCCCGGAGCTGTCGGCCCTGGCTGTGTACTGCCACGCCACCCGCCTG
CGGACCCTGCACCCTGCCCCCAACGCCCCACAACCCTGCCAGGTCAGCTCCCTCAGCGAG
CGCAAAGCCAAGAAACTCATTCGGGAGGCAGGGAACAGCTTTGTCAGGCACAATGCCCGC
CAGCTGACCCGCGTGTACCCGCTGGGGCTGCGGATGAACTCAGCCAACTACAGTCCCCAG
GAGATGTGGAACTCGGGCTGTCAGCTGGTGGCCTTGAACTTCCAGACGCCAGGCTACGAG
ATGGACCTCAATGCCGGGCGCTTCCTAGTCAATGGGCAGTGTGGCTACGTCCTAAAACCT
GCCTGCCTGCGGCAACCTGACTCGACCTTTGACCCCGAGTACCCAGGACCTCCCAGAACC
ACTCTCAGCATCCAGGTGCTGACTGCACAGCAGCTGCCCAAGCTGAATGCCGAGAAGCCA
CACTCCATTGTGGACCCCCTGGTGCGCATTGAGATCCATGGGGTGCCCGCAGACTGTGCC
CGGCAGGAGACTGACTACGTGCTCAACAATGGCTTCAACCCCCGCTGGGGGCAGACCCTG
CAGTTCCAGCTGCGGGCTCCGGAGCTGGCACTGGTCCGGTTTGTGGTGGAAGATTATGAC
GCCACCTCCCCCAATGACTTTGTGGGCCAGTTTACACTGCCTCTTAGCAGCCTAAAGCAA
GGGTACCGCCACATACACCTGCTTTCCAAGGACGGGGCCTCACTGTCACCAGCCACGCTC
TTCATCCAAATCCGCATCCAGCGCTCCTGA
Enzyme 23 GenBank Gene ID AK074240 Link Image
Enzyme 23 GeneCard ID PLCD3 Link Image
Enzyme 23 GenAtlas ID PLCD3 Link Image
Enzyme 23 HGNC ID HGNC:9061 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 17q21.31
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. 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. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  5. Pawelczyk T, Matecki A: Expression, purification and kinetic properties of human recombinant phospholipase C delta 3. Acta Biochim Pol. 1997;44(2):221-9. [PubMed Link Image]
  6. Ghosh S, Pawelczyk T, Lowenstein JM: Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties. Protein Expr Purif. 1997 Mar;9(2):262-78. [PubMed Link Image]
  7. Pawelczyk T, Matecki A: Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium. Eur J Biochem. 1998 Oct 1;257(1):169-77. [PubMed Link Image]
  8. Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):209-10. [PubMed Link Image]
  9. Pawelczyk T, Matecki A: Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes. Eur J Biochem. 1999 Jun;262(2):291-8. [PubMed Link Image]
  10. Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH: Downregulation of phospholipase C delta3 by cAMP and calcium. Biochem Biophys Res Commun. 2001 Aug 17;286(2):274-80. [PubMed Link Image]
  11. Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W: Membrane targeting of C2 domains of phospholipase C-delta isoforms. J Biol Chem. 2002 Feb 1;277(5):3568-75. Epub 2001 Nov 12. [PubMed Link Image]
  12. Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed Link Image]
  13. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  14. Naito Y, Okada M, Yagisawa H: Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006 Dec;140(6):785-91. Epub 2006 Oct 14. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 11996
Enzyme 24 Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
Enzyme 24 Synonyms
  1. BGnT-5
  2. Beta-1,3-Gn-T5
  3. Beta-1,3-N-acetylglucosaminyltransferase 5
  4. Beta3Gn-T5
  5. Lactotriaosylceramide synthase
  6. Lc(3)Cer synthase
  7. Lc3 synthase
Enzyme 24 Gene Name B3GNT5
Enzyme 24 Protein Sequence >UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
Enzyme 24 Number of Residues 378
Enzyme 24 Molecular Weight 44052.3
Enzyme 24 Theoretical pI 8.00
Enzyme 24 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 24 General Function Involved in galactosyltransferase activity
Enzyme 24 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 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 15-35
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 13568434 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q9BYG0 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name B3GN5_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1137 bp
ATGAGAATGTTGGTTAGTGGCAGAAGAGTCAAAAAATGGCAGTTAATTATTCAGTTATTT
GCTACTTGTTTTTTAGCGAGCCTCATGTTTTTTTGGGAACCAATCGATAATCACATTGTG
AGCCATATGAAGTCATATTCTTACAGATACCTCATAAATAGCTATGACTTTGTGAATGAT
ACCCTGTCTCTTAAGCACACCTCAGCGGGGCCTCGCTACCAATACTTGATTAACCACAAG
GAAAAGTGTCAAGCTCAAGACGTCCTCCTTTTACTGTTTGTAAAAACTGCTCCTGAAAAC
TATGATCGACGTTCCGGAATTAGAAGGACGTGGGGCAATGAAAATTATGTTCGGTCTCAG
CTGAATGCCAACATCAAAACTCTGTTTGCCTTAGGAACTCCTAATCCACTGGAGGGAGAA
GAACTACAAAGAAAACTGGCTTGGGAAGATCAAAGGTACAATGATATAATTCAGCAAGAC
TTTGTTGATTCTTTCTACAATCTTACTCTGAAATTACTTATGCAGTTCAGTTGGGCAAAT
ACCTATTGTCCACATGCCAAATTTCTTATGACTGCTGATGATGACATATTTATTCACATG
CCAAATCTGATTGAGTACCTTCAAAGTTTAGAACAAATTGGTGTTCAAGACTTTTGGATT
GGTCGTGTTCATCGTGGTGCCCCTCCCATTAGAGATAAAAGCAGCAAATACTACGTGTCC
TATGAAATGTACCAGTGGCCAGCTTACCCTGACTACACAGCCGGAGCTGCCTATGTAATC
TCCGGTGATGTAGCTGCCAAAGTCTATGAGGCATCACAGACACTAAATTCAAGTCTTTAC
ATAGACGATGTGTTCATGGGCCTCTGTGCCAATAAAATAGGGATAGTACCGCAGGACCAT
GTGTTTTTTTCTGGAGAGGGTAAAACTCCTTATCATCCCTGCATCTATGAAAAAATGATG
ACATCTCATGGACACTTAGAAGATCTCCAGGACCTTTGGAAGAATGCTACAGATCCTAAA
GTAAAAACCATTTCCAAAGGTTTTTTTGGTCAAATATACTGCAGATTAATGAAGATAATT
CTCCTTTGTAAAATTAGCTATGTGGACACATACCCTTGTAGGGCTGCGTTTATCTAA
Enzyme 24 GenBank Gene ID AB045278 Link Image
Enzyme 24 GeneCard ID B3GNT5 Link Image
Enzyme 24 GenAtlas ID B3GNT5 Link Image
Enzyme 24 HGNC ID HGNC:15684 Link Image
Enzyme 24 Chromosome Location 3
Enzyme 24 Locus 3q28
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 12250
Enzyme 25 Name Sphingomyelin phosphodiesterase 3
Enzyme 25 Synonyms
  1. Neutral sphingomyelinase 2
  2. nSMase-2
  3. nSMase2
  4. Neutral sphingomyelinase II
Enzyme 25 Gene Name SMPD3
Enzyme 25 Protein Sequence >Sphingomyelin phosphodiesterase 3
MVLYTTPFPNSCLSALHCVSWALIFPCYWLVDRLAASFIPTTYEKRQRADDPCCLQLLCT
ALFTPIYLALLVASLPFAFLGFLFWSPLQSARRPYIYSRLEDKGLAGGAALLSEWKGTGP
GKSFCFATANVCLLPDSLARVNNLFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSIS
AASFSSLVSPQGGDGVARAVPGSIKRTASVEYKGDGGRHPGDEAANGPASGDPVDSSSPE
DACIVRIGGEEGGRPPEADDPVPGGQARNGAGGGPRGQTPNHNQQDGDSGSLGSPSASRE
SLVKGRAGPDTSASGEPGANSKLLYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFL
CLQEVFDKRAATKLKEQLHGYFEYILYDVGVYGCQGCCSFKCLNSGLLFASRYPIMDVAY
HCYPNKCNDDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPQEDSAIRCGQLDLLQ
DWLADFRKSTSSSSAANPEELVAFDVVCGDFNFDNCSSDDKLEQQHSLFTHYRDPCRLGP
GEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSSGQKGRKELLK
GNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSSGEEEA
Enzyme 25 Number of Residues 655
Enzyme 25 Molecular Weight 71080.1
Enzyme 25 Theoretical pI 5.53
Enzyme 25 GO Classification Not Available
Enzyme 25 General Function Involved in metal ion binding
Enzyme 25 Specific Function Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization
Enzyme 25 Pathways
Enzyme 25 Reactions
  • sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 11-31 65-85
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 8247250 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q9NY59 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name NSMA2_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1968 bp
ATGGTTTTGTACACGACCCCCTTTCCTAACAGCTGTCTGTCCGCCCTGCACTGTGTGTCC
TGGGCCCTTATCTTTCCATGCTACTGGCTGGTGGACCGGCTCGCTGCCTCCTTCATACCC
ACCACCTACGAGAAGCGCCAGCGGGCAGACGACCCGTGCTGCCTGCAGCTGCTCTGCACT
GCCCTCTTCACGCCCATCTACCTGGCCCTCCTGGTGGCCTCGCTGCCCTTTGCGTTTCTC
GGCTTTCTCTTCTGGTCCCCACTGCAGTCGGCCCGCCGGCCCTACATCTATTCACGGCTG
GAAGACAAGGGCCTGGCCGGTGGGGCAGCCCTGCTCAGTGAATGGAAGGGCACGGGGCCT
GGCAAAAGCTTCTGCTTTGCCACTGCCAACGTCTGCCTCCTGCCCGACTCACTCGCCAGG
GTCAACAACCTTTTTAACACCCAAGCGCGGGCCAAGGAGATCGGGCAGAGAATCCGCAAT
GGGGCCGCCCGGCCCCAGATCAAAATTTACATCGACTCCCCCACCAATACCTCCATCAGC
GCCGCTAGCTTCAGCAGCCTGGTGTCACCACAGGGCGGCGATGGGGTGGCCCGGGCCGTC
CCCGGGAGCATTAAGAGGACAGCCTCTGTGGAGTACAAGGGTGACGGTGGGCGGCACCCC
GGTGACGAGGCTGCCAACGGCCCAGCCTCTGGGGACCCTGTCGACAGCAGCAGCCCGGAG
GATGCCTGCATCGTGCGCATCGGTGGCGAGGAGGGCGGCCGGCCACCTGAAGCTGACGAC
CCTGTGCCTGGGGGCCAGGCCAGGAACGGAGCTGGCGGGGGCCCAAGGGGCCAGACGCCC
AACCATAATCAGCAGGACGGGGATTCAGGGAGCCTGGGCAGCCCCTCGGCCTCCCGGGAG
TCCCTGGTGAAGGGGCGAGCTGGGCCAGACACCAGTGCCAGCGGGGAGCCAGGTGCCAAC
AGCAAGCTCCTGTACAAGGCCTCGGTGGTGAAGAAGGCGGCTGCACGCAGGAGGCGGCAC
CCCGACGAGGCCTTCGACCATGAGGTCTCCGCCTTCTTCCCCGCCAACCTGGACTTCCTG
TGCCTGCAGGAGGTGTTTGACAAGCGAGCAGCCACCAAATTGAAAGAGCAGCTGCACGGC
TACTTCGAGTACATCCTGTACGACGTCGGGGTCTACGGCTGCCAGGGCTGCTGCAGCTTC
AAGTGTCTCAACAGCGGCCTCCTCTTTGCCAGCCGCTACCCCATCATGGACGTGGCCTAT
CACTGTTACCCCAACAAGTGTAACGACGATGCCCTGGCCTCTAAGGGAGCTCTGTTTCTC
AAGGTGCAGGTGGGAAGCACACCTCAGGACCAAAGAATCGTCGGGTACATCGCCTGCACA
CACCTGCATGCCCCACAAGAGGACAGCGCCATCCGGTGTGGGCAGCTGGACCTGCTTCAG
GACTGGCTGGCTGATTTCCGAAAATCTACCTCCTCGTCCAGCGCAGCCAACCCCGAGGAG
CTGGTGGCATTTGACGTCGTCTGTGGAGATTTCAACTTTGATAACTGCTCCTCTGACGAC
AAGCTGGAGCAGCAACACTCCCTGTTCACCCACTACAGGGACCCCTGCCGCCTGGGGCCT
GGTGAGGAGAAGCCGTGGGCCATCGGTACTCTGCTGGACACGAACGGCCTGTACGATGAG
GATGTGTGCACCCCCGACAACCTGCAGAAGGTCCTGGAGAGTGAGGAGGGCCGCAGGGAG
TACCTGGCGTTTCCCACCAGCAAGAGCTCGGGCCAGAAGGGGCGGAAGGAGCTGCTGAAG
GGCAACGGCCGGCGCATCGACTACATGCTGCATGCAGAGGAGGGGCTGTGCCCAGACTGG
AAGGCCGAGGTGGAAGAATTCAGTTTTATCACCCAGCTGTCCGGCCTGACGGACCACCTG
CCAGTAGCCATGCGACTGATGGTGTCTTCGGGGGAGGAGGAGGCATAG
Enzyme 25 GenBank Gene ID AJ250460 Link Image
Enzyme 25 GeneCard ID SMPD3 Link Image
Enzyme 25 GenAtlas ID SMPD3 Link Image
Enzyme 25 HGNC ID HGNC:14240 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 16q22.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Hofmann K, Tomiuk S, Wolff G, Stoffel W: Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5895-900. [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. Miura Y, Gotoh E, Nara F, Nishijima M, Hanada K: Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases. FEBS Lett. 2004 Jan 16;557(1-3):288-92. [PubMed Link Image]
  4. Marchesini N, Osta W, Bielawski J, Luberto C, Obeid LM, Hannun YA: Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells. J Biol Chem. 2004 Jun 11;279(24):25101-11. Epub 2004 Mar 29. [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. Beta3GalT5
  4. b3Gal-T5
  5. Beta-3-Gx-T5
  6. UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5
  7. UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5
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 36188.9
Enzyme 26 Theoretical pI 9.02
Enzyme 26 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 26 General Function Involved in galactosyltransferase activity
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 Not Available
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 >933 bp
ATGGCTTTCCCGAAGATGAGATTGATGTATATTTGCCTTCTGGTTCTGGGGGCTCTTTGT
TTGTATTTTAGCATGTACAGTCTAAATCCTTTCAAAGAACAGTCCTTTGTTTACAAGAAA
GACGGGAACTTCCTTAAGCTCCCAGATACAGACTGCAGGCAGACACCTCCCTTCCTCGTC
CTGCTGGTGACCTCATCCCACAAACAGTTGGCTGAGCGCATGGCCATCCGGCAGACGTGG
GGGAAAGAGAGGATGGTGAAGGGAAAGCAGCTGAAGACATTCTTCCTCCTGGGGACCACC
AGCAGTGCAGCGGAAACGAAAGAGGTGGACCAGGAGAGCCAGCGACACGGGGACATTATC
CAGAAGGATTTCCTAGACGTCTATTACAATCTGACCCTGAAGACCATGATGGGCATAGAA
TGGGTCCATCGCTTTTGTCCTCAGGCGGCGTTTGTGATGAAAACAGACTCAGACATGTTC
ATCAATGTTGACTATCTGACTGAACTGCTTCTGAAGAAAAACAGAACAACCAGGTTTTTC
ACTGGCTTCTTGAAACTCAATGAGTTTCCCATCAGGCAGCCATTCAGCAAGTGGTTTGTC
AGTAAATCTGAATATCCGTGGGACAGGTACCCACCATTCTGCTCCGGCACCGGCTACGTG
TTTTCTGGCGACGTGGCGAGTCAGGTGTACAATGTCTCCAAGAGCGTCCCATACATTAAA
CTGGAAGACGTGTTTGTGGGGCTCTGCCTCGAAAGGCTGAACATCAGATTGGAGGAGCTC
CACTCCCAGCCGACCTTTTTTCCAGGGGGCTTACGCTTCTCCGTATGCCTCTTCAGGAGG
ATCGTGGCCTGCCACTTCATCAAGCCTCGGACTCTCTTGGACTACTGGCAGGCTCTAGAG
AATTCCCGGGGGGAAGATTGTCCGCCTGTCTGA
Enzyme 26 GenBank Gene ID AB020337 Link Image
Enzyme 26 GeneCard ID B3GALT5 Link Image
Enzyme 26 GenAtlas ID B3GALT5 Link Image
Enzyme 26 HGNC ID HGNC:920 Link Image
Enzyme 26 Chromosome Location 2
Enzyme 26 Locus 21q22.3
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. Dunn CA, Medstrand P, Mager DL: An endogenous retroviral long terminal repeat is the dominant promoter for human beta1,3-galactosyltransferase 5 in the colon. Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12841-6. Epub 2003 Oct 8. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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 65055.9
Enzyme 27 Theoretical pI 9.57
Enzyme 27 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 27 General Function Involved in transferase activity, transferring glycosyl groups
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 62898221 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 >1665 bp
ATGAGGAGGCCCCTAAGCAAGTGCGGAATGGAGCCGGGGGGCGGAGATGCCAGCCTCACT
TTGCATGGTCTCCAGAACCGCTCCCACGGCAAGATAAAGCTGCGAAAGAGAAAGTCTACC
TTGTACTTCAACACCCAGGAGAAGAGCGCCAGGCGCCGCGGGGATCTTCTTGGAGAAAAT
ATTTATCTGCTCTTGTTTACCATAGCTTTACGAATATTAAACTGCTTTTTAGTGCAGACA
AGTTTTGTTCCAGATGAATACTGGCAGTCTCTTGAAGTTTCACATCACATGGTTTTCAAT
TATGGTTATTTGACTTGGGAATGGACAGAGAGACTGAGGAGTTACACTTATCCCTTAATC
TTTGCAAGCATTTACAAGATTCTTCATCTTTTAGGGAAAGATAGTGTTCAGTTGCTGATT
TGGATTCCTAGACTTGCCCAAGCACTTCTGTCTGCTGTAGCAGATGTGAGACTTTACTCA
TTAATGAAGCAACTAGAAAATCAGGAAGTGGCAAGATGGGTGTTTTTTTGCCAGTTGTGC
TCCTGGTTCACATGGTATTGCTGTACCAGAACCCTTACAAACACCATGGAAATTGTTCTC
ACTATAATTGCTCTTTTCTACTATCCTTTGGAAGGTTCAAAGTCTATGAACAGTGTCAAA
TACTCATCCCTGGTGGCACTTGCCTTCATAATTCGTCCCACAGCTGTCATTCTGTGGACA
CCTTTGCTCTTCAGACATTTCTGTCAAGAACCAAGAAAGCTTGATCTTATTCTACATCAT
TTTTTACCTGTAGGCTTTGTTACTTTGAGTTTGTCTCTGATGATTGATCGTATTTTTTTT
GGCCAATGGACTCTGGTTCAATTTAATTTTTTGAAATTTAACGTGCTGCAGAACTTGGGA
ACATTTTATGGTTCTCATCCATGGCACTGGTACTTCAGTCAAGGATTTCCAGTTATCTTG
GGTACTCACTTACCCTTCTTTATTCATGGCTGCTATCTAGCACCAAAGAGATACCGGATA
CTTTTGGTGACTGTGCTGTGGACACTGCTTGTTTATAGCATGTTGAGCCACAAAGAATTC
AGGTTTATTTATCCAGTTTTACCATTCTGTATGGTGTTCTGTGGATACTCATTAACCCAC
CTGAAAACATGGAAGAAACCAGCTCTAAGTTTCCTGTTTTTATCAAATTTGTTCCTCGCC
CTTTATACTGGTTTAGTTCATCAACGAGGTACTCTTGATGTCATGAGTCATATTCAAAAA
GTTTGTTACAACAATCCCAATAAATCTTCAGCTTCAATATTTATAATGATGCCTTGCCAC
TCTACTCCTTATTACAGCCATGTTCACTGCCCACTTCCCATGAGATTTCTCCAGTGCCCG
CCAGACCTGACTGGAAAAAGTCATTATCTTGATGAAGCAGATGTATTTTACCTAAATCCC
TTAAACTGGTTACATAGAGAGTTTCATGATGATGCATCATTGCCTACTCACTTGATCACC
TTCAGCATTTTGGAAGAGGAAATAAGCGCTTTCCTAATTTCAAGCAATTATAAAAGAACT
GCTGTTTTCTTCCACACTCACTTGCCAGAGGGTCGAATTGGAAGTCACATATATGTCTAT
GAACGGAAGTTAAAAGGGAAATTCAACATGAAGATGAAATTCTGA
Enzyme 27 GenBank Gene ID AK223330 Link Image
Enzyme 27 GeneCard ID PIGB Link Image
Enzyme 27 GenAtlas ID PIGB Link Image
Enzyme 27 HGNC ID HGNC:8959 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 15q21-q22
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]
  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. Mohney RP, Knez JJ, Ravi L, Sevlever D, Rosenberry TL, Hirose S, Medof ME: Glycoinositol phospholipid anchor-defective K562 mutants with biochemical lesions distinct from those in Thy-1- murine lymphoma mutants. J Biol Chem. 1994 Mar 4;269(9):6536-42. [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 24889.3
Enzyme 28 Theoretical pI 8.64
Enzyme 28 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 28 General Function Involved in GPI anchor biosynthetic process
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 4505797 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 >660 bp
ATGAAAGATAACGATATCAAGAGACTACTGTATACCCATCTTTTATGCATATTTTCAATT
ATCCTAAGTGTCTTCATTCCATCACTCTTCTTGGAGAACTTCTCAATATTGGAAACACAC
TTGACATGGTTGTGCATCTGTTCTGGTTTTGTAACTGCTGTCAATCTAGTACTATATTTA
GTAGTGAAACCAAATACATCCTCTAAAAGAAGTTCATTATCACACAAGGTAACTGGATTT
TTGAAATGCTGTATCTACTTTCTTATGTCTTGTTTCTCCTTTCATGTAATTTTTGTTCTG
TATGGAGCACCACTGATAGAGTTGGCATTGGAAACATTTTTATTTGCAGTTATTTTGTCT
ACTTTTACTACTGTGCCTTGCTTATGTTTGTTAGGACCAAACCTCAAAGCATGGCTAAGA
GTGTTCAGTAGAAATGGAGTTACATCCATATGGGAGAATAGTCTCCAGATCACTACAATT
TCTAGCTTTGTAGGAGCATGGCTTGGAGCACTTCCTATTCCACTGGATTGGGAAAGACCA
TGGCAGGTATGGCCCATCTCCTGTACGCTTGGAGCGACCTTTGGCTACGTGGCTGGCCTT
GTTATTTCACCACTCTGGATATACTGGAATAGAAAGCAACTTACATACAAGAACAATTAA
Enzyme 28 GenBank Gene ID NM_002643.3 Link Image
Enzyme 28 GeneCard ID PIGF Link Image
Enzyme 28 GenAtlas ID PIGF Link Image
Enzyme 28 HGNC ID HGNC:8962 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 2p21-p16
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]
  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. Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T: GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9728-34. Epub 2005 Jan 4. [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. GPI7 homolog
  2. hGPI7
  3. Phosphatidylinositol-glycan biosynthesis class G protein
  4. PIG-G
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 108171.7
Enzyme 29 Theoretical pI 7.15
Enzyme 29 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 29 General Function Involved in catalytic activity
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 >2952 bp
ATGCGGCTGGGCTCCGGGACTTTCGCTACCTGTTGCGTAGCGATCGAGGTGCTAGGGATC
GCGGTCTTCCTTCGGGGATTCTTCCCGGCTCCCGTTCGTTCCTCTGCCAGAGCGGAACAC
GGAGCGGAGCCCCCAGCGCCCGAACCCTCGGCTGGAGCCAGTTCTAACTGGACCACGCTG
CCACCACCTCTCTTCAGTAAAGTTGTTATTGTTCTGATAGATGCCTTGAGAGATGATTTT
GTGTTTGGGTCAAAGGGTGTGAAATTTATGCCCTACACAACTTACCTTGTGGAAAAAGGA
GCATCTCACAGTTTTGTGGCTGAAGCAAAGCCACCTACAGTTACTATGCCTCGAATCAAG
GCATTGATGACGGGGAGCCTTCCTGGCTTTGTCGACGTCATCAGGAACCTCAATTCTCCT
GCACTGCTGGAAGACAGTGTGATAAGACAAGCAAAAGCAGCTGGAAAAAGAATAGTCTTT
TATGGAGATGAAACCTGGGTTAAATTATTCCCAAAGCATTTTGTGGAATATGATGGAACA
ACCTCATTTTTCGTGTCAGATTACACAGAGGTGGATAATAATGTCACGAGGCATTTGGAT
AAAGTATTAAAAAGAGGAGATTGGGACATATTAATCCTCCACTACCTGGGGCTGGACCAC
ATTGGCCACATTTCAGGGCCCAACAGCCCCCTGATTGGGCAGAAGCTGAGCGAGATGGAC
AGCGTGCTGATGAAGATCCACACCTCACTGCAGTCGAAGGAGAGAGAGACGCCTTTACCC
AATTTGCTGGTTCTTTGTGGTGACCATGGCATGTCTGAAACAGGAAGTCACGGGGCCTCC
TCCACCGAGGAGGTGAATACACCTCTGATTTTAATCAGTTCTGCGTTTGAAAGGAAACCC
GGTGATATCCGACATCCAAAGCACGTCCAACAGACGGATGTGGCTGCGACACTGGCGATA
GCACTTGGCTTACCGATTCCAAAAGACAGTGTAGGGAGCCTCCTATTCCCAGTTGTGGAA
GGAAGACCAATGAGAGAGCAGTTGAGATTTTTACATTTGAATACAGTGCAGCTTAGTAAA
CTGTTGCAAGAGAATGTGCCGTCATATGAAAAAGATCCTGGGTTTGAGCAGTTTAAAATG
TCAGAAAGATTGCATGGGAACTGGATCAGACTGTACTTGGAGGAAAAGCATTCAGAAGTC
CTATTCAACCTGGGCTCCAAGGTTCTCAGGCAGTACCTGGATGCTCTGAAGACGCTGAGC
TTGTCCCTGAGTGCACAAGTGGCCCAGTACGACATCTATTCGATGATGGTGGGGACTGTC
GTGGTTTTGGAGGTTCTCACCCTGCTCCTGCTCAGCGTCCCACAGGCACTGCGCAGAAAG
GCTGAGCTGGAAGTCCCACTGTCATCTCCTGGGTTTTCTCTGCTCTTTTATTTGGTGATC
CTGGTTCTTTCGGCCGTTCACGTCATTGTGTGCACCTCAGCTGAAAGTTCGTGCTACTTC
TGTGGCCTCTCGTGGCTGGCGGCAGGTGGGGTGATGGTGCTGGCCTCGGCGCTGCTGTGT
GTGATTGTGTCTGTTCTGACCAACGTGCTCGTGGGTGGAAACACCCCAAGGAAGAACCCC
ATGCATCCCAGCTCAAGGTGGTCAGAGCTAGACCTTCTTATTCTGTTGGGGACGGCGGGC
CACGTCTTGAGCCTGGGCGCCAGCAGCTTCGTGGAGGAGGAGCACCAGACCTGGTACTTC
CTTGTGAACACCCTGTGTCTAGCTCTGAGCCAAGAAACCTACAGAAACTACTTTCTGGGA
GATGACGGTGAGCCTCCGTGTGGCCTCTGTGTGGAACAAGGGCATGACGGGGCCACAGCA
GCGTGGCAGGACGGGCCTGGCTGTGATGTCCTGGAGCGAGACAAAGGCCACGGAAGCCCC
TCTACCTCCGAAGTGCTCAGAGGCCGCGAGAAGTGGATGGTGCTGGCCAGTCCGTGGCTA
ATACTGGCCTGCTGCCGGCTGCTGCGCTCCCTAAACCAGACAGGTGTGCAGTGGGCTCAC
CGGCCTGACCTCGGCCACTGGCTCACCAGCTCTGACCACAAAGCCGAGCTCTCTGTCCTG
GCTGCCCTCTCCCTCCTCGTAGTTTTTGTGCTGGTGCAGAGGGGGTGCTCCCCTGTGTCC
AAGGCTGCCCTGGCGCTGGGGCTGCTGGGCGTCTACTGCTACCGGGCGGCCATCGGGAGT
GTCCGGTTCCCGTGGCGGCCGGACAGCAAGGACATTTCCAAGGGTATTATTGAAGCTCGT
TTTGTTTATGTCTTTGTCCTTGGCATTCTGTTCACGGGCACCAAAGACTTACTTAAATCT
CAAGTCATTGCTGCAGACTTCAAACTCAAGACTGTAGGTTTATGGGAGATATATAGTGGA
TTAGTTCTTCTGGCAGCCTTGCTCTTTAGACCACATAATCTTCCGGTCTTAGCATTTAGC
CTCTTGATTCAGACTCTAATGACTAAATTCATCTGGAAGCCCCTGAGACACGATGCAGCT
GAGATTACTGTGATGCATTATTGGTTTGGTCAAGCATTCTTCTATTTTCAGGGCAACTCC
AACAACATTGCCACCGTGGACATCTCCGCAGGCTTCGTGGGCTTAGACACCTACGTGGAA
ATCCCAGCCGTGCTCCTGACAGCGTTTGGGACGTACGCAGGGCCTGTGCTGTGGGCCAGC
CACTTAGTGCACTTCCTGAGCTCAGAAACACGCAGTGGTTCAGCACTGAGTCATGCTTGC
TTCTGCTACGCACTGATTTGTTCTATTCCAGTTTTCACGTACATCGTTTTGGTGACATCT
CTGCGTTATCATTTATTTATATGGAGTGTATTTTCTCCAAAACTTCTCTACGAGGGAATG
CACCTGCTCATTACAGCTGCTGTCTGTGTATTCTTCACGGCAATGGATCAAACCAGACTC
ACACAGTCTTAG
Enzyme 29 GenBank Gene ID AB162713 Link Image
Enzyme 29 GeneCard ID PIGG Link Image
Enzyme 29 GenAtlas ID PIGG Link Image
Enzyme 29 HGNC ID HGNC:25985 Link Image
Enzyme 29 Chromosome Location 4
Enzyme 29 Locus 4p16.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T: GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9728-34. Epub 2005 Jan 4. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. 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 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 12950
Enzyme 30 Name GPI ethanolamine phosphate transferase 1
Enzyme 30 Synonyms
  1. MCD4 homolog
  2. Phosphatidylinositol-glycan biosynthesis class N protein
  3. PIG-N
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 105809.2
Enzyme 30 Theoretical pI 8.87
Enzyme 30 GO Classification
Function
  • catalytic activity
  • transferase activity
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • membrane
  • organelle membrane
Enzyme 30 General Function Involved in catalytic activity
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 >2796 bp
ATGCTGCTGTTCTTTACTTTGGGATTGCTTATACATTTTGTGTTCTTCGCCTCCATCTTT
GACATTTATTTTACATCTCCTTTGGTTCATGGAATGACTCCTCAGTTTACACCATTGCCT
CCTCCAGCGAGAAGATTAGTGTTGTTTGTTGCTGATGGCCTTCGAGCAGATGCACTTTAC
GAATTAGATGAAAATGGAAACTCTAGAGCACCGTTTATTAGGAATATCATAATGCATGAA
GGCAGCTGGGGCATATCTCATACACGTGTGCCAACAGAATCTCGGCCAGGTCATGTAGCT
CTGATAGCTGGGTTTTATGAAGATGTCAGTGCAGTTGCCAAAGGATGGAAGGAAAATCCT
GTAGAGTTTGATTCTCTTTTTAATGAAAGTAAATACACATGGAGCTGGGGAAGCCCAGAT
ATCCTGCCTATGTTTGCCAAAGGTGCTAGTGGAGACCACGTTTATACATATAGTTATGAT
GCTAAAAGAGAGGATTTTGGTGCTCAAGATGCAACAAAACTGGATACGTGGGTTTTTGAT
AATGTTAAGGACTTCTTTCATCATGCCAGAAACAACCAGTCTTTGTTTTCTAAAATAAAT
GAAGAGAAAATAGTTTTTTTCTTACATTTATTAGGAATAGATACAAACGGACATGCTCAT
CGACCATCCTCGAGAGACTACAAGCACAATATTAAAAAAGTTGATGATGGAGTTAAAGAA
ATCGTGTCTATGTTTAACCACTTCTATGGAAATGATGGGAAAACAACATTTATCTTTACC
TCTGACCATGGAATGACAGACTGGGGTTCCCATGGGGCTGGTCATCCTTCAGAGACTTTA
ACTCCTTTAGTCACTTGGGGAGCTGGAATCAAGTATCCCCAAAGAGTATCAGCTCAGCAA
TTTGATGATGCATTTTTGAAAGAGTGGAGATTGGAGAATTGGAAGAGGCTAGATGTCAAT
CAGGCTGATATTGCACCATTGATGACTTCCCTTATTGGAGTTCCCTTTCCTCTTAACTCA
GTGGGAATCCTTCCTGTGGATTATCTTAACAACACTGATCTCTTCAAAGCAGAGAGCATG
TTTACAAATGCAGTACAGATTCTTGAACAGTTCAAGGTGAAAATGACTCAGAAGAAAGAA
GTTACTTTACCATTTTTGTTTACACCATTTAAACTGCTTTCTGATTCCAAACAGTTCAAC
ATTTTAAGAAAAGCAAGATCTTATATAAAACACAGAAAGTTTGATGAAGTGGTCTCCCTT
TGCAAGGAGCTAATTCATCTTGCATTGAAAGGATTGTCCTATTATCACACATATGACAGA
TTCTTTTTGGGCGTCAATGTTGTTATTGGTTTTGTGGGATGGATATCTTATGCCTCTTTG
TTGATCATCAAGTCTCATTCCAACCTTATAAAAGGTGTTAGTAAAGAAGTGAAGAAACCA
AGCCATCTCCTGCCTTGTAGTTTTGTAGCTATTGGCATTTTAGTAGCATTTTTTCTGCTG
ATTCAAGCCTGTCCCTGGACATATTATGTATATGGTTTGTTGCCACTGCCAATATGGTAT
GCGGTTCTAAGAGAATTTCAAGTTATTCAGGACCTTGTTGTATCAGTGTTGACCTATCCT
CTGAGCCATTTTGTTGGGTACCTGTTAGCCTTTACCCTGGGAATTGAAGTATTAGTTCTC
AGTTTTTTCTACCGCTATATGCTTACCGCTGGACTTACTGCCTTTGCAGCTTGGCCATTT
CTCACTCGGCTGTGGACTCGAGCAAAGATGACCTCACTGAGTTGGACTTTCTTCTCTTTG
CTCCTGGCAGTGTTCCCACTGATGCCGGTTGTAGGTCGAAAGCCAGACATCTCTCTAGTG
ATGGGTGCAGGCTTGCTGGTTCTTCTGTTATCCCTGTGTGTTGTAACATCTCTCATGAAA
AGAAAAGATAGCTTTATAAAGGAAGAGCTATTGGTACATCTGTTACAGGTGCTGAGCACA
GTGCTCTCCATGTATGTTGTGTATAGCACTCAGAGTAGTTTACTCAGGAAGCAAGGACTG
CCTCTCATGAATCAAATTATTAGCTGGGCAACATTAGCCTCTTCCTTGGTTGTGCCACTA
CTGAGTTCTCCAGTTCTCTTTCAGCGATTGTTCAGCATACTTCTTTCATTGATGTCAACC
TACCTACTTCTAAGCACAGGGTATGAAGCTCTCTTTCCACTAGTGTTGTCTTGTTTGATG
TTTGTCTGGATAAACATAGAACAAGAAACTCTACAACAATCTGGTGTTTGCTGTAAACAA
AAGCTCACCAGTATCCAGTTCTCTTATAATACTGATATAACTCAGTTTCGACAGCTATAT
CTGGATGACATCCGTAGGGCCTTTTTCCTTGTTTTCTTCTTAGTGACAGCATTTTTTGGA
ACTGGAAATATAGCTTCTATTAACAGCTTTGATCTTGCCTCTGTCTATTGCTTTCTGACT
GTGTTCAGTCCTTTTATGATGGGAGCCCTGATGATGTGGAAGATTTTAATCCCCTTTGTT
CTTGTTATGTGTGCTTTTGAAGCAGTTCAGTTGACTACTCAGTTATCGTCAAAAAGCCTT
TTTCTCATTGTTCTCGTCATATCAGACATTATGGCTTTGCATTTTTTCTTCTTGGTCAAG
GATTATGGCAGCTGGCTTGATATTGGGACAAGCATCAGCCACTATGTGATTGTCATGTCC
ATGACCATCTTTTTGGTGTTCCTCAATGGCCTGGCCCAGCTGCTCACAACGAAGAAACTC
AGACTATGTGGCAAACCCAAAAGTCACTTCATGTGA
Enzyme 30 GenBank Gene ID AF109219 Link Image
Enzyme 30 GeneCard ID PIGN Link Image
Enzyme 30 GenAtlas ID PIGN Link Image
Enzyme 30 HGNC ID HGNC:8967 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 18q21.33
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]
  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. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 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 118697.6
Enzyme 31 Theoretical pI 8.18
Enzyme 31 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 31 General Function Involved in catalytic activity
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 23397648 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 >3270 bp
ATGCAGAAAGCCTCAGTGTTGCTCTTCCTGGCCTGGGTCTGCTTCCTCTTCTACGCTGGC
ATTGCCCTCTTCACCAGTGGCTTCCTGCTCACCCGTTTGGAGCTCACCAACCATAGCAGC
TGCCAAGAGCCCCCAGGCCCTGGGTCCCTGCCATGGGGGAGCCAAGGGAAACCTGGGGCC
TGCTGGATGGCTTCCCGATTTTCGCGGGTTGTGTTGGTGCTGATAGATGCTCTGCGATTT
GACTTCGCCCAGCCCCAGCATTCACACGTGCCTAGAGAGCCTCCTGTCTCCCTACCCTTC
CTGGGCAAACTAAGCTCCTTGCAGAGGATCCTGGAGATTCAGCCCCACCATGCCCGGCTC
TACCGATCTCAGGTTGACCCTCCTACCACCACCATGCAGCGCCTCAAGGCCCTCACCACT
GGCTCACTGCCTACCTTTATTGATGCTGGTAGTAACTTCGCCAGCCACGCCATAGTGGAA
GACAATCTCATTAAGCAGCTCACCAGTGCAGGAAGGCGTGTAGTCTTCATGGGAGATGAT
ACCTGGAAAGACCTTTTCCCTGGTGCTTTCTCCAAAGCTTTCTTCTTCCCATCCTTCAAT
GTCAGAGACCTAGACACAGTGGACAATGGCATCCTGGAACACCTCTACCCCACCATGGAC
AGTGGTGAATGGGACGTGCTGATTGCTCACTTCCTGGGTGTGGACCACTGTGGCCACAAG
CATGGCCCTCACCACCCTGAAATGGCCAAGAAACTTAGCCAGATGGACCAGGTGATCCAG
GGACTTGTGGAGCGTCTGGAGAATGACACACTGCTGGTAGTGGCTGGGGACCATGGGATG
ACCACAAATGGAGACCATGGAGGGGACAGTGAGCTGGAGGTCTCAGCTGCTCTCTTTCTG
TATAGCCCCACAGCAGTCTTCCCCAGCACCCCACCAGAGGAGCCAGAGGTGATTCCTCAA
GTTAGCCTTGTGCCCACGCTGGCCCTGCTGCTGGGCCTGCCCATCCCATTTGGGAATATC
GGGGAAGTGATGGCTGAGCTATTCTCAGGGGGTGAGGACTCCCAGCCCCACTCCTCTGCT
TTAGCCCAAGCCTCAGCTCTCCATCTCAATGCTCAGCAGGTGTCCCGATTTCTTCATACC
TACTCAGCTGCTACTCAGGACCTTCAAGCTAAGGAGCTTCATCAGCTGCAGAACCTCTTC
TCCAAGGCCTCTGCTGACTACCAGTGGCTTCTCCAGAGCCCCAAGGGGGCTGAGGCGACA
CTGCCGACTGTGATTGCTGAGCTGCAGCAGTTCCTGCGGGGAGCTCGGGCCATGTGCATC
GAGTCTTGGGCTCGTTTCTCTCTGGTCCGCATGGCGGGGGGTACTGCTCTCTTGGCTGCT
TCCTGCTTTATCTGCCTGCTGGCATCTCAGTGGGCAATATCCCCAGGCTTTCCATTCTGC
CCTCTACTCCTGACACCTGTGGCCTGGGGCCTGGTTGGGGCCATAGCGTATGCTGGACTC
CTGGGAACTATTGAGCTGAAGCTAGATCTAGTGCTTCTAGGGGCTGTGGCTGCAGTGAGC
TCATTCCTCCCTTTTCTGTGGAAAGCCTGGGCTGGCTGGGGGTCCAAGAGGCCCCTGGCA
ACCCTGTTTCCCATCCCTGGGCCCGTCCTGTTACTCCTGCTGTTTCGCTTGGCTGTGTTC
TTCTCTGATAGTTTTGTTGTAGCTGAGGCCAGGGCCACCCCCTTCCTTTTGGGCTCATTC
ATCCTGCTCCTGGTTGTCCAGCTTCACTGGGAGGGCCAGCTGCTTCCACCTAAGCTACTC
ACAATGCCCCGCCTTGGCACTTCAGCCACAACAAACCCCCCACGGCACAATGGTGCATAT
GCCCTGAGGCTTGGAATTGGGTTGCTTTTATGTACAAGGCTAGCTGGGCTTTTTCATCGT
TGCCCTGAAGAGACACCTGTTTGCCACTCCTCTCCCTGGCTGAGTCCTCTGGCATCCATG
GTGGGTGGTCGAGCCAAGAATTTGTGGTATGGAGCTTGTGTGGCGGCGCTGGTGGCCCTG
TTAGCTGCCGTGCGCTTGTGGCTTCGCCGCTATGGTAATCTCAAGAGCCCCGAGCCACCC
ATGCTCTTTGTGCGCTGGGGACTGCCCCTAATGGCATTGGGTACTGCTGCCTACTGGGCA
TTGGCGTCGGGGGCAGATGAGGCTCCCCCCCGTCTCCGGGTCCTGGTCTCTGGGGCATCC
ATGGTGCTGCCTCGGGCTGTAGCAGGGCTGGCTGCTTCAGGGCTCGCGCTGCTGCTCTGG
AAGCCTGTGACAGTGCTGGTGAAGGCTGGGGCAGGCGCTCCAAGGACCAGGACTGTCCTC
ACTCCCTTCTCAGGCCCCCCCACTTCTCAAGCTGACTTGGATTATGTGGTCCCTCAAATC
TACCGACACATGCAGGAGGAGTTCCGGGGCCGGTTAGAGAGGACCAAATCTCAGGGTCCC
CTGACTGTGGCTGCTTATCAGTTGGGGAGTGTCTACTCAGCTGCTATGGTCACAGCCCTC
ACCCTGTTGGCCTTCCCACTTCTGCTGTTGCATGCGGAGCGCATCAGCCTTGTGTTCCTG
CTTCTGTTTCTGCAGAGCTTCCTTCTCCTACATCTGCTTGCTGCTGGGATACCCGTCACC
ACCCCTGGTCCTTTTACTGTGCCATGGCAGGCAGTCTCGGCTTGGGCCCTCATGGCCACA
CAGACCTTCTACTCCACAGGCCACCAGCCTGTCTTTCCAGCCATCCATTGGCATGCAGCC
TTCGTGGGATTCCCAGAGGGTCATGGCTCCTGTACTTGGCTGCCTGCTTTGCTAGTGGGA
GCCAACACCTTTGCCTCCCACCTCCTCTTTGCAGTAGGTTGCCCACTGCTCCTGCTCTGG
CCTTTCCTGTGTGAGAGTCAAGGGCTGCGGAAGAGACAGCAGCCCCCAGGGAATGAAGCT
GATGCCAGAGTCAGACCCGAGGAGGAAGAGGAGCCACTGATGGAGATGCGGCTCCGGGAT
GCGCCTCAGCACTTCTATGCAGCACTGCTGCAGCTGGGCCTCAAGTACCTCTTTATCCTT
GGTATTCAGATTCTGGCCTGTGCCTTGGCAGCCTCCATCCTTCGCAGGCATCTCATGGTC
TGGAAAGTGTTTGCCCCTAAGTTCATATTTGAGGCTGTGGGCTTCATTGTGAGCAGCGTG
GGACTTCTCCTGGGCATAGCTTTGGTGATGAGAGTGGATGGTGCTGTGAGCTCCTGGTTC
AGGCAGCTATTTCTGGCCCAGCAGAGGTAG
Enzyme 31 GenBank Gene ID NM_032634.2 Link Image
Enzyme 31 GeneCard ID PIGO Link Image
Enzyme 31 GenAtlas ID PIGO Link Image
Enzyme 31 HGNC ID HGNC:23215 Link Image
Enzyme 31 Chromosome Location 9
Enzyme 31 Locus 9p13.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 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 61655.5
Enzyme 32 Theoretical pI 6.46
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Involved in protein binding
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
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 >1668 bp
ATGGCGGCCGCCGGGGCTGCGGCTACACACCTAGAGGTGGCCCGGGGCAAGCGCGCCGCC
CTCTTCTTCGCTGCGGTGGCCATCGTGCTGGGGCTACCGCTCTGGTGGAAGACCACGGAG
ACCTACCGGGCCTCGTTGCCTTACTCCCAGATCAGTGGCCTGAATGCCCTTCAGCTCCGC
CTCATGGTGCCTGTCACTGTCGTGTTTACGCGGGAGTCAGTGCCCCTGGACGACCAGGAG
AAGCTGCCCTTCACCGTTGTGCATGAAAGAGAGATTCCTCTGAAATACAAAATGAAAATC
AAATGCCGTTTCCAGAAGGCCTATCGGAGGGCTTTGGACCATGAGGAGGAGGCCCTGTCA
TCGGGCAGTGTGCAAGAGGCAGAAGCCATGTTAGATGAGCCTCAGGAACAAGCGGAGGGC
TCCCTGACTGTGTACGTGATATCTGAACACTCCTCACTTCTTCCCCAGGACATGATGAGC
TACATTGGGCCCAAGAGGACAGCAGTGGTGCGGGGGATAATGCACCGGGAGGCCTTTAAC
ATCATTGGCCGCCGCATAGTCCAGGTGGCCCAGGCCATGTCTTTGACTGAGGATGTGCTT
GCTGCTGCTCTGGCTGACCACCTTCCAGAGGACAAGTGGAGCGCTGAGAAGAGGCGGCCT
CTCAAGTCCAGCTTGGGCTATGAGATCACCTTCAGTTTACTCAACCCAGACCCCAAGTCC
CATGATGTCTACTGGGACATTGAGGGGGCTGTCCGGCGCTATGTGCAACCTTTCCTGAAT
GCCCTCGGTGCCGCTGGCAACTTCTCTGTGGACTCTCAGATTCTTTACTATGCAATGTTG
GGGGTGAATCCCCGCTTTGACTCAGCTTCCTCCAGCTACTATTTGGACATGCACAGCCTC
CCCCATGTCATCAACCCAGTGGAGTCCCGGCTGGGATCCAGTGCTGCCTCCTTGTACCCT
GTGCTCAACTTTCTACTCTACGTGCCTGAGCTTGCACACTCACCGCTGTACATTCAGGAC
AAGGATGGCGCTCCAGTGGCCACCAATGCCTTCCATAGTCCCCGCTGGGGTGGCATTATG
GTATATAATGTTGACTCCAAAACCTATAATGCCTCAGTGCTGCCAGTGAGAGTCGAGGTG
GACATGGTGCGAGTGATGGAGGTGTTCCTGGCACAGTTGCGGTTGCTCTTTGGGATTGCT
CAGCCCCAGCTGCCTCCAAAATGCCTGCTTTCAGGGCCTACGAGTGAAGGGCTAATGACC
TGGGAGCTAGACCGGCTGCTCTGGGCTCGGTCAGTGGAGAACCTGGCCACAGCCACCACC
ACCCTTACCTCCCTGGCGCAGCTTCTGGGCAAGATCAGCAACATTGTCATTAAGGACGAC
GTGGCATCTGAGGTGTACAAGGCTGTAGCTGCCGTCCAGAAGTCGGCAGAAGAGTTGGCG
TCTGGGCACCTGGCATCTGCCTTTGTCGCCAGCCAGGAAGCTGTGACATCCTCTGAGCTT
GCCTTCTTTGACCCGTCACTCCTCCACCTCCTTTATTTCCCTGATGACCAGAAGTTTGCC
ATCTACATCCCACTCTTCCTGCCTATGGCTGTGCCCATCCTCCTGTCCCTGGTCAAGATC
TTCCTGGAGACCCGCAAGTCCTGGAGAAAGCCTGAGAAGACAGACTGA
Enzyme 32 GenBank Gene ID AB057723 Link Image
Enzyme 32 GeneCard ID PIGS Link Image
Enzyme 32 GenAtlas ID PIGS Link Image
Enzyme 32 HGNC ID HGNC:14937 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 17p13.2
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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 12953
Enzyme 33 Name GPI transamidase component PIG-T
Enzyme 33 Synonyms
  1. Phosphatidylinositol-glycan biosynthesis class T protein
Enzyme 33 Gene Name PIGT
Enzyme 33 Protein Sequence >GPI transamidase component PIG-T
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQR
EGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTV
TDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREV
VCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQ
TLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPP
TTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSG
YGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQ
DRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVA
AKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCY
GSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
Enzyme 33 Number of Residues 578
Enzyme 33 Molecular Weight 65699.0
Enzyme 33 Theoretical pI 8.49
Enzyme 33 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • macromolecular complex
  • membrane part
  • protein complex
Enzyme 33 General Function Involved in protein binding
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 >1737 bp
ATGGCGGCGGCTATGCCGCTTGCTCTGCTCGTCCTGTTGCTCCTGGGGCCCGGCGGCTGG
TGCCTTGCAGAACCCCCACGCGACAGCCTGCGGGAGGAACTTGTCATCACCCCGCTGCCT
TCCGGGGACGTAGCCGCCACATTCCAGTTCCGCACGCGCTGGGATTCGGAGCTTCAGCGG
GAAGGAGTGTCCCATTACAGGCTCTTTCCCAAAGCCCTGGGGCAGCTGATCTCCAAGTAT
TCTCTACGGGAGCTGCACCTGTCATTCACACAAGGCTTTTGGAGGACCCGATACTGGGGG
CCACCCTTCCTGCAGGCCCCATCAGGTGCAGAGCTGTGGGTCTGGTTCCAAGACACTGTC
ACTGATGTGGATAAATCTTGGAAGGAGCTCAGTAATGTCCTCTCAGGGATCTTCTGCGCC
TCTCTCAACTTCATCGACTCCACCAACACAGTCACTCCCACTGCCTCCTTCAAACCCCTG
GGTCTGGCCAATGACACTGACCACTACTTTCTGCGCTATGCTGTGCTGCCGCGGGAGGTG
GTCTGCACCGAAAACCTCACCCCCTGGAAGAAGCTCTTGCCCTGTAGTTCCAAGGCAGGC
CTCTCTGTGCTGCTGAAGGCAGATCGCTTGTTCCACACCAGCTACCACTCCCAGGCAGTG
CATATCCGCCCTGTTTGCAGAAATGCACGCTGTACTAGCATCTCCTGGGAGCTGAGGCAG
ACCCTGTCAGTTGTATTTGATGCCTTCATCACGGGGCAGGGAAAGAAAGACTGGTCCCTC
TTCCGGATGTTCTCCCGAACCCTCACGGAGCCCTGCCCCCTGGCTTCAGAGAGCCGAGTC
TATGTGGACATCACCACCTACAACCAGGACAACGAGACATTAGAGGTGCACCCACCCCCG
ACCACTACATATCAGGACGTCATCCTAGGCACTCGGAAGACCTATGCCATCTATGACTTG
CTTGACACCGCCATGATCAACAACTCTCGAAACCTCAACATCCAGCTCAAGTGGAAGAGA
CCCCCAGAGAATGAGGCCCCCCCAGTGCCCTTCCTGCATGCCCAGCGGTACGTGAGTGGC
TATGGGCTGCAGAAGGGGGAGCTGAGCACACTGCTGTACAACACCCACCCATACCGGGCC
TTCCCGGTGCTGCTGCTGGACACCGTACCCTGGTATCTGCGGCTGTATGTGCACACCCTC
ACCATCACCTCCAAGGGCAAGGAGAACAAACCAAGTTACATCCACTACCAGCCTGCCCAG
GACCGGCTGCAACCCCACCTCCTGGAGATGCTGATTCAGCTGCCGGCCAACTCAGTCACC
AAGGTTTCCATCCAGTTTGAGCGGGCGCTGCTGAAGTGGACCGAGTACACGCCAGATCCT
AACCATGGCTTCTATGTCAGCCCATCTGTCCTCAGCGCCCTTGTGCCCAGCATGGTAGCA
GCCAAGCCAGTGGACTGGGAAGAGAGTCCCCTCTTCAACAGCCTGTTCCCAGTCTCTGAT
GGCTCTAACTACTTTGTGCGGCTCTACACGGAGCCGCTGCTGGTGAACCTGCCGACACCG
GACTTCAGCATGCCCTACAACGTGATCTGCCTCACGTGCACTGTGGTGGCCGTGTGCTAT
GGCTCCTTCTACAATCTCCTCACCCGAACCTTCCACATCGAGGAGCCCCGCACAGGTGGC
CTGGCCAAGCGGCTGGCCAACCTTATCCGGCGCGCCCGAGGTGTCCCCCCACTCTGA
Enzyme 33 GenBank Gene ID AB057724 Link Image
Enzyme 33 GeneCard ID PIGT Link Image
Enzyme 33 GenAtlas ID PIGT Link Image
Enzyme 33 HGNC ID HGNC:14938 Link Image
Enzyme 33 Chromosome Location 2
Enzyme 33 Locus 20q12-q13.12
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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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 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. Cell division cycle protein 91-like 1
  2. Protein CDC91-like 1
  3. GPI transamidase component PIG-U
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 50051.2
Enzyme 34 Theoretical pI 7.82
Enzyme 34 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 34 General Function Involved in GPI anchor biosynthetic process
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 >1308 bp
ATGGCGGCTCCCTTGGTCCTGGTGCTGGTGGTGGCTGTGACAGTGCGGGCGGCCTTGTTC
CGCTCCAGTCTGGCCGAGTTCATTTCCGAGCGGGTGGAGGTGGTGTCCCCACTGAGCTCT
TGGAAGAGAGTGGTTGAAGGCCTTTCACTGTTGGACTTGGGAGTATCTCCGTATTCTGGA
GCAGTATTTCATGAAACTCCATTAATAATATACCTCTTTCATTTCCTAATTGACTATGCT
GAATTGGTGTTTATGATAACTGATGCACTCACTGCTATTGCCCTGTATTTTGCAATCCAG
GACTTCAATAAAGTTGTGTTTAAAAAGCAGAAACTCCTCCTAGAACTGGACCAGTATGCC
CCAGATGTGGCCGAACTCATCCGGACCCCTATGGAAATGCGTTACATCCCTTTGAAAGTG
GCCCTGTTCTATCTCTTAAATCCTTACACGATTTTGTCTTGTGTTGCCAAGTCTACCTGT
GCCATCAACAACACCCTCATTGCTTTCTTCATTTTGACTACGATAAAAGGCAGTGCTTTC
CTCAGTGCTATTTTTCTTGCCTTAGCGACATACCAGTCTCTGTACCCACTCACCTTGTTT
GTCCCAGGACTCCTCTATCTCCTCCAGCGGCAGTACATACCTGTGAAAATGAAGAGCAAA
GCCTTCTGGATCTTTTCTTGGGAGTATGCCATGATGTATGTGGGAAGCCTAGTGGTAATC
ATTTGCCTCTCCTTCTTCCTTCTCAGCTCTTGGGATTTCATCCCCGCAGTCTATGGCTTT
ATACTTTCTGTTCCAGATCTCACTCCAAACATTGGTCTTTTCTGGTACTTCTTTGCAGAG
ATGTTTGAGCACTTCAGCCTCTTCTTTGTATGTGTGTTTCAGATCAACGTCTTCTTCTAC
ACCATCCCCTTAGCCATAAAGCTAAAGGAGCACCCCATCTTCTTCATGTTTATCCAGATC
GCTGTCATCGCCATCTTTAAGTCCTACCCGACAGTGGGGGACGTGGCGCTCTACATGGCC
TTCTTCCCCGTGTGGAACCATCTCTACAGATTCCTGAGAAACATCTTTGTCCTCACCTGC
ATCATCATCGTCTGTTCCCTGCTCTTCCCTGTCCTGTGGCACCTCTGGATTTATGCAGGA
AGTGCCAACTCTAATTTCTTTTATGCCATCACACTGACCTTCAACGTTGGGCAGATCCTG
CTCATCTCTGATTACTTCTATGCCTTCCTGCGGCGGGAGTACTACCTCACACATGGCCTC
TACTTGACCGCCAAGGATGGCACAGAGGCCATGCTCGTGCTCAAGTAG
Enzyme 34 GenBank Gene ID AB086842 Link Image
Enzyme 34 GeneCard ID PIGU Link Image
Enzyme 34 GenAtlas ID PIGU Link Image
Enzyme 34 HGNC ID HGNC:15791 Link Image
Enzyme 34 Chromosome Location 2
Enzyme 34 Locus 20q11.22
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Hong Y, Ohishi K, Kang JY, Tanaka S, Inoue N, Nishimura J, Maeda Y, Kinoshita T: Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. Mol Biol Cell. 2003 May;14(5):1780-9. Epub 2003 Jan 26. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
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 55712.1
Enzyme 35 Theoretical pI 8.03
Enzyme 35 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • GPI anchor biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
  • cell part
  • endoplasmic reticulum membrane
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 35 General Function Involved in transferase activity, transferring hexosyl groups
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 Not Available
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 >1482 bp
ATGTGGCCCCAGGACCCATCCCGGAAGGAGGTGCTGAGGTTTGCAGTCAGCTGCCGTATC
CTGACTCTGATGCTGCAGGCCCTCTTCAATGCCATCACCCCAGATCACCATGCAGAAGCC
TTCTCTCCTCCTCGCCTGGCCCCCTCAGGCTTTGTGGACCAACTCGTGGAAGGTCTTCTG
GGCGGCCTGTCTCACTGGGATGCTGAACACTTCTTGTTCATTGCTGAGCATGGCTACCTG
TATGAGCACAACTTTGCCTTCTTTCCTGGTTTCCCCTTGGCCCTGCTGGTGGGGACTGAA
CTGTTGAGACCCTTACGGGGGTTACTGAGTCTACGCAGTTGCCTGCTGATTTCGGTAGCA
TCACTCAATTTCTTGTTCTTCATGTTGGCTGCAGTTGCACTTCATGACCTGGGTTGTCTG
GTTTTGCACTGTCCCCACCAGTCCTTTTATGCAGCTCTGCTTTTCTGTCTCAGCCCTGCC
AATGTCTTCCTGGCAGCTGGTTACTCAGAAGCTTTGTTTGCCCTCCTGACATTCAGTGCC
ATGGGGCAGCTGGAGAGGGGCCGAGTCTGGACTAGTGTACTCCTCTTTGCCTTTGCCACT
GGGGTACGCTCCAACGGGCTGGTCAGTGTTGGCTTCCTCATGCATTCTCAATGCCAAGGC
TTTTTCTCTTCTCTAACGATGCTGAATCCTCTGAGACAGCTCTTTAAGCTGATGGCCTCT
CTGTTTCTGTCGGTGTTCACACTTGGCCTTCCCTTTGCCCTCTTTCAGTATTATGCCTAC
ACCCAATTCTGTCTGCCAGGCTCAGCCCGCCCCATTCCTGAGCCTTTGGTACAGTTAGCT
GTAGACAAGGGCTACCGGATTGCAGAGGGAAATGAACCGCCTTGGTGCTTCTGGGATGTT
CCACTAATATACAGCTATATCCAGGATGTCTACTGGAATGTTGGCTTTTTGAAATACTAT
GAGCTCAAGCAGGTGCCCAATTTTCTACTGGCTGCACCAGTGGCTATACTGGTTGCCTGG
GCAACTTGGACATACGTGACCACTCACCCTTGGCTCTGCCTTACACTTGGGCTGCAAAGG
AGCAAGAACAATAAGACCCTAGAGAAGCCCGATCTTGGATTCCTCAGTCCTCAGGTGTTT
GTGTACGTGGTCCACGCTGCAGTGCTGCTGCTGTTTGGAGGTCTGTGCATGCATGTTCAG
GTTCTCACCAGGTTTTTGGGCTCCTCCACTCCTATTATGTACTGGTTTCCAGCTCACTTG
CTTCAGGATCAAGAGCCGCTGTTGAGATCCTTAAAGACTGTGCCTTGGAAGCCTCTTGCA
GAGGACTCCCCACCAGGACAAAAGGTCCCCAGAAATCCTATCATGGGACTTTTGTATCAC
TGGAAAACCTGTTCTCCAGTCACACGATACATTCTAGGCTACTTCCTGACTTACTGGCTC
CTGGGACTACTCCTACATTGCAACTTCCTGCCTTGGACATGA
Enzyme 35 GenBank Gene ID AK000484 Link Image
Enzyme 35 GeneCard ID PIGV Link Image
Enzyme 35 GenAtlas ID PIGV Link Image
Enzyme 35 HGNC ID HGNC:26031 Link Image
Enzyme 35 Chromosome Location 1
Enzyme 35 Locus 1p36.11
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Fabre AL, Orlean P, Taron CH: Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly. FEBS J. 2005 Mar;272(5):1160-8. [PubMed Link Image]
  5. Kang JY, Hong Y, Ashida H, Shishioh N, Murakami Y, Morita YS, Maeda Y, Kinoshita T: PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9489-97. Epub 2004 Dec 28. [PubMed Link Image]
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 8057.5
Enzyme 36 Theoretical pI 7.41
Enzyme 36 GO Classification Not Available
Enzyme 36 General Function Involved in GPI anchor biosynthetic process
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 >216 bp
ATGTTTCTGTCTCTTCCTACGTTGACTGTTCTTATTCCACTGGTTTCTTTAGCAGGACTG
TTCTACTCAGCCTCTGTGGAAGAAAACTTCCCACAGGGCTGCACTAGCACAGCCAGCCTT
TGCTTTTACAGCCTGCTCTTGCCTATTACCATACCAGTGTATGTATTCTTCCACCTTTGG
ACTTGGATGGGTATTAAACTCTTCAGGCATAATTGA
Enzyme 36 GenBank Gene ID AB206972 Link Image
Enzyme 36 GeneCard ID PIGY Link Image
Enzyme 36 GenAtlas ID PIGY Link Image
Enzyme 36 HGNC ID HGNC:28213 Link Image
Enzyme 36 Chromosome Location 4
Enzyme 36 Locus 4q22.1
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [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 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. PH domain-containing family A member 8
  2. Phosphatidylinositol-four-phosphate adapter protein 2
  3. FAPP-2
  4. Phosphoinositol 4-phosphate adapter protein 2
  5. hFAPP2
  6. 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 58306.0
Enzyme 37 Theoretical pI 4.89
Enzyme 37 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 37 General Function Involved in glycolipid transporter activity
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 308153327 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 >1560 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAATAATGCATATGGTAAAACA
TTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCTTTAAGGGCAGCT
CCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGACCACCAGAAAGAA
GCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCCATGGAGAAGCAG
CTGGCCATACTGGACACTTTATATGAGGTCCACGGGCTGGAATCTGATGAGGTGGTATGA
Enzyme 37 GenBank Gene ID NM_001197026.1 Link Image
Enzyme 37 GeneCard ID PLEKHA8 Link Image
Enzyme 37 GenAtlas ID PLEKHA8 Link Image
Enzyme 37 HGNC ID HGNC:30037 Link Image
Enzyme 37 Chromosome Location 7
Enzyme 37 Locus 7p21-p11.2
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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. 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]
  5. Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS, Daniele T, Marra P, Lucocq JM, De Matteis MA: FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat Cell Biol. 2004 May;6(5):393-404. Epub 2004 Apr 25. [PubMed Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 14494
Enzyme 38 Name Sphingomyelin phosphodiesterase 4
Enzyme 38 Synonyms
  1. Neutral sphingomyelinase 3
  2. nSMase-3
  3. nSMase3
  4. Neutral sphingomyelinase III
Enzyme 38 Gene Name SMPD4
Enzyme 38 Protein Sequence >Sphingomyelin phosphodiesterase 4
MAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPAKELHTIFPWLVESIFGSLD
GVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKA
SIQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTS
DCAYFILVDRYLSWFLPTEGSVPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRH
ISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLSVSS
ALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSP
LEEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSD
SQPRCVSEKWAPFVQENLLMYTKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAE
MIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAVTDASFKVKSHVYSLEGQDC
KYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYT
ANDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCI
VGEDGLILTPLGRYQIINGLRRFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFA
GQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVAGHTRGPRLSLRFLGSYRTL
VSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
Enzyme 38 Number of Residues 827
Enzyme 38 Molecular Weight 93350.8
Enzyme 38 Theoretical pI 8.04
Enzyme 38 GO Classification Not Available
Enzyme 38 General Function Involved in metal ion binding
Enzyme 38 Specific Function Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide
Enzyme 38 Pathways
Enzyme 38 Reactions
  • sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
Enzyme 38 Pfam Domain Function Not Available
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 783-803
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 102467481 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q9NXE4 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name NSMA3_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2601 bp
ATGACGACTTTCGGCGCCGTGGCGGAATGGCGGCTTCCATCTCTGAGGCGAGCGACGCTA
TGGATCCCACAGTGGTTTGCTAAGAAGGCCATTTTCAACTCTCCACTGGAGGCTGCTATG
GCGTTCCCTCACCTGCAGCAGCCCAGCTTTCTACTGGCTAGCCTGAAAGCTGACTCTATA
AATAAGCCCTTTGCACAGCAGTGCCAAGACTTGGTTAAAGTCATTGAGGACTTTCCAGCA
AAGGAGCTGCACACCATCTTCCCATGGCTGGTAGAAAGCATTTTTGGCAGCCTAGATGGT
GTCCTCGTTGGCTGGAACCTCCGCTGCTTACAGGGGCGCGTGAATCCTGTGGAGTACAGC
ATCGTGATGGAATTTCTCGACCCTGGTGGCCCAATGATGAAGTTGGTTTATAAGCTTCAA
GCTGAAGACTATAAGTTCGACTTTCCTGTCTCCTACTTGCCTGGTCCTGTGAAGGCGTCC
ATCCAGGAGTGCATCCTCCCTGACAGTCCTCTGTACCACAACAAGGTCCAGTTCACCCCT
ACTGGGGGCCTTGGTCTGAACTTGGCCCTGAATCCGTTCGAGTATTACATATTCTTCTTT
GCCTTGAGCCTCATCACTCAGAAGCCACTTCCTGTGTCCCTCCACGTCCGTACTTCAGAC
TGTGCCTATTTCATCCTGGTGGACAGGTACCTGTCATGGTTCCTGCCCACCGAAGGCAGT
GTGCCCCCACCACTCTCCTCCAGCCCAGGGGGGACCAGCCCCTCACCACCTCCCAGGACA
CCAGCCATACCCTTTGCTTCCTATGGCCTCCACCACACTAGCCTCCTAAAGCGACACATC
TCTCATCAGACGTCTGTGAATGCAGACCCCGCCTCCCACGAGATCTGGAGGTCAGAAACT
CTGCTCCAGGTTTTTGTTGAAATGTGGCTTCATCACTATTCCTTGGAGATGTATCAAAAA
ATGCAGTCCCCTCATGCCAAGCTGGAGGTTCTGCACTACCGACTCAGTGTCTCCAGCGCC
CTCTACAGCCCCGCCCAACCCAGCCTCCAGGCCCTCCACGCCTACCAAGAGTCGTTCACG
CCTACTGAGGAGCATGTGTTGGTGGTGCGCCTGCTGCTGAAGCACCTGCACGCCTTTGCC
AACAGCCTGAAGCCAGAGCAGGCCTCACCCTCCGCCCACTCCCACGCCACCAGCCCCCTG
GAGGAGTTCAAACGGGCTGCTGTCCCGAGGTTCGTCCAGCAGAAACTCTACCTCTTCTTG
CAGCATTGCTTTGGCCACTGGCCCCTGGACGCATCGTTCAGAGCTGTCCTGGAGATGTGG
CTGAGCTACCTGCAGCCGTGGCGGTACGCGCCTGACAAGCAGGCTCCGGGCAGCGACTCC
CAGCCCCGGTGTGTGTCGGAGAAATGGGCACCCTTTGTCCAGGAGAACCTGCTGATGTAC
ACCAAGTTGTTTGTGGGCTTTCTGAACCGCGCGCTCCGCACAGACCTGGTCAGCCCCAAG
CACGCGCTCATGGTGTTCCGAGTGGCCAAAGTCTTTGCCCAGCCCAACCTGGCTGAGATG
ATTCAGAAAGGTGAGCAGCTATTCCTGGAGCCAGAGCTGGTCATCCCCCACCGCCAGCAC
CGACTCTTCACGGCCCCCACATTCACTGGGAGCTTCCTGTCACCCTGGCCACCAGCGGTC
ACTGATGCCTCCTTCAAGGTGAAGAGCCACGTCTACAGCCTGGAGGGCCAGGACTGCAAG
TACACCCCGATGTTTGGGCCCGAGGCCCGCACCCTGGTCCTGCGCCTCGCTCAGCTCATC
ACACAGGCCAAACACACAGCCAAGTCCATCTCCGACCAGTGTGCGGAGAGCCCGGCTGGC
CACTCCTTCCTCTCATGGCTGGGCTTTAGCTCCATGGACACCAATGGCTCCTACACAGCC
AACGACCTGGACGAGATGGGGCAAGACAGTGTCCGGAAGACAGATGAATACCTGGAGAAG
GCCCTGGAGTACCTGCGCCAGATATTCCGGCTCAGCGAAGCGCAGCTCAGGCAGTTCACA
CTCGCCTTGGGCACCACCCAGGATGAGAATGGAAAAAAGCAACTCCCCGACTGCATCGTG
GGTGAGGACGGACTCATCCTTACGCCCCTGGGGCGGTACCAGATCATCAATGGGCTGCGA
AGGTTTGAAATTGAGTACCAGGGGGACCCGGAGCTGCAGCCCATCCGGAGCTATGAGATC
GCCAGCTTGGTCCGCACACTCTTTAGGCTGTCGTCTGCCATCAACCACAGATTTGCAGGA
CAGATGGCGGCTCTGTGTTCCCGGGATGACTTCCTCGGCAGCTTCTGTCGCTACCACCTC
ACAGAACCTGGGCTGGCCAGCAGGCACCTGCTGAGCCCTGTGGGGCGGAGGCAGGTGGCC
GGCCACACCCGCGGCCCCAGGCTCAGCCTGCGCTTCCTGGGCAGTTACCGGACGCTGGTC
TCGCTGCTGCTGGCCTTCTTCGTGGCCTCTCTGTTCTGCGTCGGGCCCCTCCCATGCACG
CTGCTGCTCACCCTGGGCTATGTCCTCTACGCCTCTGCCATGACACTGCTGACCGAGCGG
GGGAAGCTGCACCAGCCCTGA
Enzyme 38 GenBank Gene ID Not Available
Enzyme 38 GeneCard ID SMPD4 Link Image
Enzyme 38 GenAtlas ID SMPD4 Link Image
Enzyme 38 HGNC ID HGNC:32949 Link Image
Enzyme 38 Chromosome Location 2
Enzyme 38 Locus 2q21.1
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Krut O, Wiegmann K, Kashkar H, Yazdanpanah B, Kronke M: Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein. J Biol Chem. 2006 May 12;281(19):13784-93. Epub 2006 Mar 3. [PubMed Link Image]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  8. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 14925
Enzyme 39 Name Non-lysosomal glucosylceramidase
Enzyme 39 Synonyms
  1. NLGase
  2. Beta-glucocerebrosidase 2
  3. Beta-glucosidase 2
  4. Glucosylceramidase 2
Enzyme 39 Gene Name GBA2
Enzyme 39 Protein Sequence >Non-lysosomal glucosylceramidase
MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCC
NPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLR
YLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMY
QHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQ
LPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDD
APGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQ
QVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFG
AKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSAL
FNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVH
FYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDD
EPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDK
DHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILS
RGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVR
ALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWE
GFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASW
PKVKQGTGLRTGPMFGPKEAMANLSPE
Enzyme 39 Number of Residues 927
Enzyme 39 Molecular Weight 104648.1
Enzyme 39 Theoretical pI 5.74
Enzyme 39 GO Classification
Function
  • catalytic activity
  • glucosylceramidase activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • cellular lipid metabolic process
  • glucosylceramide catabolic process
  • glucosylceramide metabolic process
  • glycolipid metabolic process
  • glycosylceramide metabolic process
  • lipid metabolic process
  • membrane lipid metabolic process
  • metabolic process
  • primary metabolic process
  • sphingolipid metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 39 General Function Involved in catalytic activity
Enzyme 39 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 39 Pathways Not Available
Enzyme 39 Reactions
  • D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine [RN:R01498]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • 688-708
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 24308251 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q9HCG7 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name GBA2_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 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 39 GenBank Gene ID NM_020944.2 Link Image
Enzyme 39 GeneCard ID GBA2 Link Image
Enzyme 39 GenAtlas ID GBA2 Link Image
Enzyme 39 HGNC ID HGNC:18986 Link Image
Enzyme 39 Chromosome Location 9
Enzyme 39 Locus 9p13.3
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Matern H, Heinemann H, Legler G, Matern S: Purification and characterization of a microsomal bile acid beta-glucosidase from human liver. J Biol Chem. 1997 Apr 25;272(17):11261-7. [PubMed Link Image]
  8. Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marle J, Overkleeft HS, Wennekes T, Aerts JM: Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J Biol Chem. 2007 Jan 12;282(2):1305-12. Epub 2006 Nov 14. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 16484
Enzyme 40 Name cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name MGC26963
Enzyme 40 Protein Sequence >cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
Enzyme 40 Number of Residues 365
Enzyme 40 Molecular Weight 42281
Enzyme 40 Theoretical pI 9.00
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function Not Available
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein Not Available
Enzyme 40 UniProtKB/Swiss-Prot ID B2RA61 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name B2RA61_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence Not Available
Enzyme 40 GenBank Gene ID AK314049 Link Image
Enzyme 40 GeneCard ID B2RA61 Link Image
Enzyme 40 GenAtlas ID Not Available
Enzyme 40 HGNC ID Not Available
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 17301
Enzyme 41 Name Sphingomyelin synthase-related protein 1
Enzyme 41 Synonyms
  1. SMSr
  2. Sterile alpha motif domain-containing protein 8
  3. SAM domain-containing protein 8
Enzyme 41 Gene Name SAMD8
Enzyme 41 Protein Sequence >Sphingomyelin synthase-related protein 1
MAGPNQLCIRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIK
VLGDIKRLMLSVRKLQKIHIDVLEEMGYNSDSPMGSMTPFISALQSTDWLCNGELSHDCD
GPITDLNSDQYQYMNGKNKHSVRRLDPEYWKTILSCIYVFIVFGFTSFIMVIVHERVPDM
QTYPPLPDIFLDSVPRIPWAFAMTEVCGMILCYIWLLVLLLHKHRSILLRRLCSLMGTVF
LLRCFTMFVTSLSVPGQHLQCTGKIYGSVWEKLHRAFAIWSGFGMTLTGVHTCGDYMFSG
HTVVLTMLNFFVTEYTPRSWNFLHTLSWVLNLFGIFFILAAHEHYSIDVFIAFYITTRLF
LYYHTLANTRAYQQSRRARIWFPMFSFFECNVNGTVPNEYCWPFSKPAIMKRLIG
Enzyme 41 Number of Residues 415
Enzyme 41 Molecular Weight 48320.2
Enzyme 41 Theoretical pI 8.13
Enzyme 41 GO Classification Not Available
Enzyme 41 General Function Involved in sphingomyelin biosynthetic process
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • 153-173 201-221 232-252 277-297 322-342 347-367
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 292658773 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q96LT4 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name SAMD8_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1248 bp
ATGGCAGGTCCTAATCAACTCTGCATTCGCCGCTGGACTACCAAGCATGTAGCTGTGTGG
CTGAAGGATGAAGGCTTTTTTGAATATGTGGACATTTTATGCAATAAGCACCGACTTGAT
GGAATCACATTGCTAACATTGACTGAATATGATCTCCGGTCTCCTCCTCTGGAAATCAAA
GTCTTAGGGGACATTAAAAGGTTAATGCTCTCAGTCCGAAAATTGCAGAAAATACATATT
GATGTTTTAGAAGAGATGGGCTACAACAGTGACAGTCCCATGGGTTCCATGACCCCTTTC
ATCAGTGCTCTTCAGAGTACAGACTGGCTCTGTAATGGGGAGCTTTCCCATGACTGTGAC
GGACCCATAACTGACTTGAATTCTGATCAGTACCAGTACATGAATGGTAAAAACAAACAT
TCTGTTCGAAGATTGGACCCAGAATACTGGAAGACTATACTGAGTTGTATATATGTTTTT
ATAGTATTTGGATTTACATCTTTCATTATGGTTATAGTCCATGAGCGAGTGCCTGACATG
CAGACCTATCCACCACTCCCAGATATATTCTTAGACAGCGTTCCTAGAATCCCATGGGCC
TTTGCCATGACGGAAGTATGTGGCATGATTCTGTGCTATATTTGGCTCCTGGTTCTTCTT
CTTCACAAGCACAGGTCAATACTTCTGCGAAGGCTCTGTAGTCTGATGGGAACTGTATTC
TTGCTTCGCTGCTTTACCATGTTTGTGACCTCCCTCTCCGTGCCAGGACAACACCTGCAG
TGTACTGGAAAGATATATGGCAGTGTATGGGAGAAATTACATCGAGCCTTTGCCATTTGG
AGTGGCTTTGGTATGACCCTGACTGGCGTTCACACATGTGGAGATTACATGTTTAGTGGC
CACACAGTCGTCCTAACTATGCTGAATTTCTTTGTCACCGAATATACACCAAGAAGCTGG
AATTTCTTGCACACTTTATCCTGGGTTCTCAACCTCTTTGGAATCTTCTTCATCTTGGCT
GCCCATGAACATTATTCTATTGATGTGTTTATTGCTTTTTATATAACAACAAGACTCTTT
TTGTACTACCATACTCTGGCCAATACCAGAGCATATCAGCAGAGTAGGAGAGCAAGGATT
TGGTTTCCCATGTTCTCTTTTTTTGAATGCAATGTTAATGGCACAGTACCTAATGAATAT
TGTTGGCCATTTTCAAAACCAGCAATAATGAAAAGACTAATTGGATGA
Enzyme 41 GenBank Gene ID NM_001174156.1 Link Image
Enzyme 41 GeneCard ID SAMD8 Link Image
Enzyme 41 GenAtlas ID SAMD8 Link Image
Enzyme 41 HGNC ID HGNC:26320 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 10q22.2
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 17337
Enzyme 42 Name GPI-anchor transamidase
Enzyme 42 Synonyms
  1. GPI transamidase
  2. GPI8 homolog
  3. hGPI8
  4. Phosphatidylinositol-glycan biosynthesis class K protein
  5. PIG-K
Enzyme 42 Gene Name PIGK
Enzyme 42 Protein Sequence >GPI-anchor transamidase
MAVTDSLSRAATVLATVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYR
HVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVD
YRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITN
IELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPA
IGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLI
TDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEKLMEPLKYAEQLPVAQIIHQKPK
LKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
Enzyme 42 Number of Residues 395
Enzyme 42 Molecular Weight 45251.4
Enzyme 42 Theoretical pI 6.09
Enzyme 42 GO Classification
Function
  • catalytic activity
  • cysteine-type endopeptidase activity
  • endopeptidase activity
  • hydrolase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
Enzyme 42 General Function Involved in cysteine-type endopeptidase activity
Enzyme 42 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 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • 1-27
Enzyme 42 Transmembrane Regions
  • 368-388
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 2558891 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q92643 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name GPI8_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1188 bp
ATGGCCGTCACCGACAGCCTCAGCCGGGCTGCGACTGTCTTGGCAACTGTGTTGCTCTTG
TCCTTCGGCAGCGTGGCCGCTAGTCATATCGAGGATCAAGCAGAACAATTCTTTAGAAGT
GGCCATACAAACAACTGGGCTGTTCTGGTGTGTACATCCCGATTCTGGTTTAATTATCGA
CATGTTGCAAATACCCTTTCTGTTTATAGAAGTGTCAAGAGGCTAGGTATTCCTGACAGT
CACATTGTCCTAATGCTTGCAGATGATATGGCCTGTAATCCTAGAAATCCCAAACCAGCT
ACAGTGTTTAGTCACAAGAATATGGAACTAAATGTGTATGGAGATGATGTGGAAGTGGAT
TATAGAAGTTATGAGGTAACTGTGGAGAATTTTTTACGGGTATTAACTGGGAGGATCCCA
CCTAGTACTCCTCGGTCAAAACGTCTTCTTTCTGATGACAGAAGCAATATTCTAATTTAT
ATGACAGGGCATGGTGGAAATGGTTTCTTAAAATTTCAAGATTCTGAAGAAATTACCAAC
ATAGAACTCGCGGATGCTTTTGAACAAATGTGGCAGAAAAGACGCTACAATGAGCTACTG
TTTATTATTGATACTTGCCAAGGAGCATCCATGTATGAACGATTTTATTCTCCTAACATA
ATGGCTCTAGCTAGTAGTCAAGTGGGAGAAGATTCACTCTCGCATCAACCTGATCCTGCA
ATTGGAGTCCATCTTATGGATAGATACACATTTTATGTCTTGGAATTTTTGGAAGAAATT
AACCCAGCTAGCCAAACTAATATGAATGACCTTTTTCAGGTATGTCCCAAAAGTCTGTGT
GTGTCTACTCCTGGACATCGCACTGATCTTTTTCAGAGGGATCCTAAAAATGTACTGATA
ACTGATTTCTTTGGAAGTGTACGGAAAGTGGAAATTACAACAGAGACTATTAAATTGCAA
CAGGATTCAGAAATCATGGAAAGCAGCTATAAGGAAGACCAGATGGATGAGAAACTAATG
GAACCTCTGAAATATGCTGAACAACTTCCTGTAGCTCAGATAATACACCAGAAACCGAAG
CTGAAAGACTGGCATCCTCCTGGGGGCTTTATTCTGGGATTATGGGCACTTATTATCATG
GTTTTCTTCAAAACTTATGGAATTAAGCATATGAAGTTCATTTTTTAG
Enzyme 42 GenBank Gene ID AF022913 Link Image
Enzyme 42 GeneCard ID PIGK Link Image
Enzyme 42 GenAtlas ID PIGK Link Image
Enzyme 42 HGNC ID HGNC:8965 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 1p31.1
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 17782
Enzyme 43 Name Glycosylphosphatidylinositol anchor attachment 1 protein
Enzyme 43 Synonyms
  1. GPI anchor attachment protein 1
  2. GAA1 protein homolog
  3. hGAA1
Enzyme 43 Gene Name GPAA1
Enzyme 43 Protein Sequence >Glycosylphosphatidylinositol anchor attachment 1 protein
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMV
EEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHE
RYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDI
VFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVE
GLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASG
RPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLY
LLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQ
GVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPH
NTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGP
RTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLF
PLLSLGLYPCWLLFWNVLFWK
Enzyme 43 Number of Residues 621
Enzyme 43 Molecular Weight 67622.5
Enzyme 43 Theoretical pI 8.16
Enzyme 43 GO Classification
Function
Process
Component
  • GPI-anchor transamidase complex
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • macromolecular complex
  • membrane part
  • protein complex
Enzyme 43 General Function Involved in tubulin binding
Enzyme 43 Specific Function Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • 25-45 369-389 428-448 459-479 496-516 544-564 600-620
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 5572751 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID O43292 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name GPAA1_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 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
CGGACCCTCTATGCTGCCCTGCTGGTGCTGACCAGCCCGGCAGCCACGCTCCTTGGCAGC
CTGTTCCTGTGGCGGGAGCTGCAGGAGGCGCCACTGTCACTGGCCGAGGGCTGGCAGCTC
TTCCTGGCAGCGCTAGCCCAGGGTGTGCTGGAGCACCACACCTACGGCGCCCTGCTCTTC
CCACTGCTGTCCCTGGGCCTCTACCCCTGCTGGCTGCTTTTCTGGAATGTGCTCTTCTGG
AAGTGA
Enzyme 43 GenBank Gene ID AB002135 Link Image
Enzyme 43 GeneCard ID GPAA1 Link Image
Enzyme 43 GenAtlas ID GPAA1 Link Image
Enzyme 43 HGNC ID HGNC:4446 Link Image
Enzyme 43 Chromosome Location 8
Enzyme 43 Locus 8q24.3
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 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 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 17783
Enzyme 44 Name Protein PLEKHA9
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name PLEKHA9
Enzyme 44 Protein Sequence >Protein PLEKHA9
MSELRLCCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAA
FTSELLYHTPPGSPQLAMLKSSKMKHPIIPIHNSLERQTELSTCENGSLNMEINGEEEIL
MKNKNSLYLKSAEIDCSISSEENTDDNITVQGEIMKEDRMENLKNHDNNLSQSGSDSSCS
PECLWEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCCAVVPVLDKLGPTVFAP
VKMDLVENIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLK
GFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGD
HRKEAFSIGMQRDLSLYLPAMKKQMAILDAL
Enzyme 44 Number of Residues 391
Enzyme 44 Molecular Weight 43538.3
Enzyme 44 Theoretical pI 4.76
Enzyme 44 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 44 General Function Involved in glycolipid transporter activity
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 4050073 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID O95397 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name PKHA9_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 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 44 GenBank Gene ID AF103731 Link Image
Enzyme 44 GeneCard ID PLEKHA9 Link Image
Enzyme 44 GenAtlas ID PLEKHA9 Link Image
Enzyme 44 HGNC ID HGNC:30222 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 12q
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 17784
Enzyme 45 Name Glycolipid transfer protein domain-containing protein 2
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name GLTPD2
Enzyme 45 Protein Sequence >Glycolipid transfer protein domain-containing protein 2
MGVAARPPALRHWFSHSIPLAIFALLLLYLSVRSLGARSGCGPRAQPCVPGETAPFQVRQ
ESGTLEAPERKQPPCLGPRGMLGRMMRRFHASLKPEGDVGLSPYLAGWRALVEFLTPLGS
VFAFATREAFTKVTDLEARVHGPDAEHYWSLAAMAAWERRAGLLEQPGAAPRDPTRSSGS
RTLLLLHRALRWSQLCLHRVATGALGGPEAGVQCSDAYRAALGPHHPWLVRQTARLAFLA
FPGRRRLLELACPGATEAEARAALLRAAGTLEDVYNRTQSLLAERGLLQLA
Enzyme 45 Number of Residues 291
Enzyme 45 Molecular Weight 31641.2
Enzyme 45 Theoretical pI 10.54
Enzyme 45 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 45 General Function Involved in glycolipid transporter activity
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 304571945 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID A6NH11 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name GLTD2_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >876 bp
ATGGGAGTGGCGGCGCGGCCCCCAGCCCTGCGGCACTGGTTCAGCCACTCAATTCCTCTC
GCTATCTTCGCGCTGCTGCTGCTTTATCTCAGTGTTCGGAGCCTAGGCGCCCGCTCGGGC
TGCGGACCCAGGGCGCAGCCCTGCGTTCCAGGGGAAACGGCGCCCTTCCAGGTCCGGCAG
GAGTCGGGAACCCTGGAGGCCCCGGAGAGGAAACAGCCTCCGTGTCTGGGCCCTCGGGGG
ATGCTGGGCCGCATGATGAGGCGGTTCCACGCCAGTCTGAAACCCGAAGGGGATGTGGGG
CTGTCGCCGTACCTGGCGGGATGGAGGGCACTCGTCGAGTTCCTGACTCCCCTCGGCTCC
GTCTTCGCCTTCGCCACTAGGGAGGCCTTCACCAAGGTGACAGACCTGGAGGCTCGGGTG
CACGGCCCGGACGCGGAGCACTACTGGTCGCTGGTGGCCATGGCGGCGTGGGAGCGGAGG
GCGGGACTGCTGGAGCAGCCGGGGGCGGCCCCCCGGGACCCGACCCGGAGCTCGGGCTCT
CGCACGCTGCTCCTGCTGCACCGCGCGCTGCGCTGGTCCCAGCTCTGCCTCCACCGGGTG
GCGACCGGCGCGCTGGGAGGCCCGGAAGCGGGCGTGCAGTGCAGCGACGCCTACCGTGCG
GCCCTGGGTCCGCATCACCCCTGGCTGGTCCGACAGACCGCCCGCCTCGCCTTCCTCGCC
TTCCCGGGTCGCCGCCGCCTGCTGGAGCTGGCGTGTCCCGGAGCCACCGAGGCGGAGGCG
CGGGCCGCGCTGCTCCGGGCCGCCGGCACCTTGGAGGATGTCTACAACCGCACCCAGAGC
CTGCTGGCCGAGCGCGGCCTGCTCCAGCTGGCCTAA
Enzyme 45 GenBank Gene ID NM_001014985.2 Link Image
Enzyme 45 GeneCard ID GLTPD2 Link Image
Enzyme 45 GenAtlas ID GLTPD2 Link Image
Enzyme 45 HGNC ID HGNC:33756 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 17p13.2
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 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 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 17785
Enzyme 46 Name Putative uncharacterized protein PLEKHA8
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name PLEKHA8
Enzyme 46 Protein Sequence >Putative uncharacterized protein PLEKHA8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALSVGMWV
Enzyme 46 Number of Residues 439
Enzyme 46 Molecular Weight 49308.8
Enzyme 46 Theoretical pI 4.67
Enzyme 46 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 46 General Function Involved in glycolipid transporter activity
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 14249174 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID B5MDU3 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name B5MDU3_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1323 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAGAAATCCAACAGAAAACACT
TGA
Enzyme 46 GenBank Gene ID NM_032639 Link Image
Enzyme 46 GeneCard ID PLEKHA8 Link Image
Enzyme 46 GenAtlas ID PLEKHA8 Link Image
Enzyme 46 HGNC ID HGNC:30037 Link Image
Enzyme 46 Chromosome Location 7
Enzyme 46 Locus 7p21-p11.2
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 17786
Enzyme 47 Name Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
Enzyme 47 Synonyms
  1. SubName: cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
Enzyme 47 Gene Name PLEKHA8
Enzyme 47 Protein Sequence >Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTVKEGDHQKE
AFSIGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV
Enzyme 47 Number of Residues 519
Enzyme 47 Molecular Weight 58260.9
Enzyme 47 Theoretical pI 4.76
Enzyme 47 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 47 General Function Involved in glycolipid transporter activity
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 194378422 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID B4DH00 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name B4DH00_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 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 47 GenBank Gene ID AK294857 Link Image
Enzyme 47 GeneCard ID PLEKHA8 Link Image
Enzyme 47 GenAtlas ID PLEKHA8 Link Image
Enzyme 47 HGNC ID HGNC:30037 Link Image
Enzyme 47 Chromosome Location 7
Enzyme 47 Locus 7p21-p11.2
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 17787
Enzyme 48 Name T-cell surface glycoprotein CD1a
Enzyme 48 Synonyms
  1. T-cell surface antigen T6/Leu-6
  2. hTa1 thymocyte antigen
  3. CD1a antigen
Enzyme 48 Gene Name CD1A
Enzyme 48 Protein Sequence >T-cell surface glycoprotein CD1a
MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSN
SSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCE
LHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLS
DTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRG
EQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSV
GFIILAVIVPLLLLIGLALWFRKRCFC
Enzyme 48 Number of Residues 327
Enzyme 48 Molecular Weight 37077.1
Enzyme 48 Theoretical pI 6.79
Enzyme 48 GO Classification
Function
Process
  • antigen processing and presentation
  • immune response
  • immune system process
Component
  • MHC class I protein complex
  • MHC protein complex
  • cell part
  • macromolecular complex
  • membrane
  • protein complex
Enzyme 48 General Function Involved in immune response
Enzyme 48 Specific Function Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • 1-16
Enzyme 48 Transmembrane Regions
  • 301-321
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 180036 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P06126 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name CD1A_HUMAN Link Image
Enzyme 48 PDB ID 1ONQ Link Image
Enzyme 48 PDB File Show
Enzyme 48 3D Structure
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >984 bp
ATGCTGTTTTTGCTACTTCCATTGTTAGCTGTTCTCCCAGGTGATGGCAATGCAGACGGG
CTCAAGGAGCCTCTCTCCTTCCATGTCATCTGGATCGCATCCTTTTACAACCATTCCTGG
AAACAAAATCTGGTCTCAGGTTGGCTGAGTGATTTGCAGACTCATACCTGGGACAGCAAT
TCCAGCACCATCGTTTTCCTGTGGCCCTGGTCCAGGGGAAACTTCAGCAATGAGGAGTGG
AAGGAACTGGAAACATTATTCCGTATACGCACCATTCGGTCATTTGAGGGAATTCGTAGA
TACGCCCATGAATTGCAGTTTGAATATCCTTTTGAGATACAGGTGACAGGAGGCTGTGAG
CTGCACTCTGGAAAGGTCTCAGGAAGCTTCTTGCAGTTAGCTTATCAAGGATCAGACTTT
GTGAGCTTCCAGAACAATTCATGGTTGCCATATCCAGTGGCTGGGAATATGGCCAAGCAT
TTCTGCAAAGTGCTCAATCAGAATCAGCATGAAAATGACATAACACACAATCTTCTCAGT
GACACCTGCCCACGTTTCATCTTGGGTCTTCTTGATGCAGGAAAGGCACATCTCCAGCGG
CAAGTGAAGCCCGAGGCCTGGCTGTCCCATGGCCCCAGTCCTGGCCCTGGCCATCTGCAG
CTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGT
GAGCAGGAGCAGCAGGGCACTCAGCGAGGGGACATCTTGCCCAGTGCTGATGGGACATGG
TATCTCCGCGCAACCCTGGAGGTGGCCGCTGGGGAGGCAGCTGACCTGTCCTGTCGGGTG
AAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGAGCATCACAGTTCCGTG
GGCTTCATCATCTTGGCGGTGATAGTGCCTTTACTTCTTCTGATAGGTCTTGCGCTTTGG
TTCAGGAAACGCTGTTTCTGTTAA
Enzyme 48 GenBank Gene ID M28825 Link Image
Enzyme 48 GeneCard ID CD1A Link Image
Enzyme 48 GenAtlas ID CD1A Link Image
Enzyme 48 HGNC ID HGNC:1634 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 1q22-q23
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. 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. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 17788
Enzyme 49 Name Glycolipid transfer protein domain-containing protein 1
Enzyme 49 Synonyms Not Available
Enzyme 49 Gene Name GLTPD1
Enzyme 49 Protein Sequence >Glycolipid transfer protein domain-containing protein 1
MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSK
LRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQL
FLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPP
EQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Enzyme 49 Number of Residues 214
Enzyme 49 Molecular Weight 24364.8
Enzyme 49 Theoretical pI 7.23
Enzyme 49 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 49 General Function Involved in glycolipid transporter activity
Enzyme 49 Specific Function Not Available
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 56204961 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q5TA50 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name GLTD1_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >645 bp
ATGGATGACTCGGAGACAGGTTTCAATCTGAAAGTCGTCCTGGTCAGTTTCAAGCAGTGT
CTCGATGAGAAGGAAGAGGTCTTGCTGGACCCCTACATTGCCAGCTGGAAGGGCCTGGTC
AGGTTTCTGAACAGCCTGGGCACCATCTTCTCATTCATCTCCAAGGACGTGGTCTCCAAG
CTGCGGATCATGGAGCGCCTCAGGGGCGGCCCGCAGAGCGAGCACTACCGCAGCCTGCAG
GCCATGGTGGCCCACGAGCTGAGCAACCGGCTGGTGGACCTGGAGCGCCGCTCCCACCAC
CCGGAGTCTGGCTGCCGGACGGTGCTGCGCCTGCACCGCGCCCTGCACTGGCTGCAGCTG
TTCCTGGAGGGCCTGCGTACCAGCCCCGAGGACGCACGCACCTCCGCGCTCTGCGCCGAC
TCCTACAACGCCTCGCTGGCCGCCTACCACCCCTGGGTCGTGCGCCGCGCCGTCACCGTG
GCCTTCTGCACGCTGCCCACACGCGAGGTCTTCCTGGAGGCCATGAACGTGGGGCCCCCG
GAGCAGGCCGTGCAGATGCTAGGCGAGGCCCTCCCCTTCATCCAGCGTGTCTACAACGTC
TCCCAGAAGCTCTACGCCGAGCACTCCCTGCTGGACCTGCCCTAG
Enzyme 49 GenBank Gene ID AL139287 Link Image
Enzyme 49 GeneCard ID GLTPD1 Link Image
Enzyme 49 GenAtlas ID GLTPD1 Link Image
Enzyme 49 HGNC ID HGNC:28116 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1p36.33
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 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 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 17789
Enzyme 50 Name T-cell surface glycoprotein CD1c
Enzyme 50 Synonyms
  1. CD1c antigen
Enzyme 50 Gene Name CD1C
Enzyme 50 Protein Sequence >T-cell surface glycoprotein CD1c
MLFLQFLLLALLLPGGDNADASQEHVSFHVIQIFSFVNQSWARGQGSGWLDELQTHGWDS
ESGTIIFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGC
ELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNL
IRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWM
RNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWGHHF
SMNWIALVVIVPLVILIVLVLWFKKHCSYQDIL
Enzyme 50 Number of Residues 333
Enzyme 50 Molecular Weight 37653.7
Enzyme 50 Theoretical pI 6.09
Enzyme 50 GO Classification
Function
Process
  • antigen processing and presentation
  • immune response
  • immune system process
Component
  • cell part
  • membrane
Enzyme 50 General Function Involved in immune response
Enzyme 50 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 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • 1-17
Enzyme 50 Transmembrane Regions
  • 303-323
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 110618227 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID P29017 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name CD1C_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1002 bp
ATGCTGTTTCTGCAGTTTCTGCTGCTAGCTCTTCTTCTCCCAGGTGGTGACAATGCAGAC
GCATCCCAGGAACACGTCTCCTTCCATGTCATCCAGATCTTCTCATTTGTCAACCAATCC
TGGGCACGAGGTCAGGGCTCAGGATGGCTGGACGAGTTGCAGACTCATGGCTGGGACAGT
GAATCAGGCACAATAATTTTCCTGCATAACTGGTCCAAGGGCAACTTCAGCAATGAAGAG
TTGTCAGACCTAGAGTTGTTATTTCGTTTCTACCTCTTTGGATTAACTCGGGAGATTCAA
GACCATGCAAGTCAAGATTACTCGAAATATCCCTTTGAAGTACAGGTGAAAGCGGGCTGT
GAGCTGCATTCTGGAAAGAGCCCAGAAGGCTTCTTTCAGGTAGCTTTCAACGGATTAGAT
TTACTGAGTTTCCAGAATACAACATGGGTGCCATCTCCAGGCTGTGGAAGTTTGGCCCAA
AGTGTCTGTCATCTACTCAATCATCAGTATGAAGGCGTCACAGAAACAGTGTATAATCTC
ATAAGAAGCACTTGCCCCCGATTTCTCTTGGGTCTCCTGGATGCAGGGAAGATGTATGTA
CACAGGCAAGTGAGGCCAGAAGCCTGGCTGTCCAGTCGCCCCAGCCTTGGGTCTGGCCAG
CTGTTGCTGGTTTGTCATGCCTCCGGCTTCTACCCAAAGCCTGTTTGGGTGACATGGATG
CGGAATGAACAGGAGCAACTGGGCACTAAACATGGTGATATTCTTCCTAATGCTGATGGG
ACATGGTATCTTCAGGTGATCCTGGAGGTGGCATCTGAGGAGCCTGCTGGCCTGTCTTGT
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTTT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
Enzyme 50 GenBank Gene ID NM_001765.2 Link Image
Enzyme 50 GeneCard ID CD1C Link Image
Enzyme 50 GenAtlas ID CD1C Link Image
Enzyme 50 HGNC ID HGNC:1636 Link Image
Enzyme 50 Chromosome Location 1
Enzyme 50 Locus 1q22-q23
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 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 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 17790
Enzyme 51 Name Lipopolysaccharide-binding protein
Enzyme 51 Synonyms
  1. LBP
Enzyme 51 Gene Name LBP
Enzyme 51 Protein Sequence >Lipopolysaccharide-binding protein
MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLP
DFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRK
SFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNL
FHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATA
QMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLN
FSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDP
YMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFN
AELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMR
V
Enzyme 51 Number of Residues 481
Enzyme 51 Molecular Weight 53383.0
Enzyme 51 Theoretical pI 6.68
Enzyme 51 GO Classification
Function
  • binding
  • lipid binding
Process
Component
Enzyme 51 General Function Involved in lipid binding
Enzyme 51 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 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • 1-25
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 2653817 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID P18428 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name LBP_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >1446 bp
ATGGGGGCCTTGGCAAGAGCCCTGCCGTCCATACTGCTGGCATTGCTGCTTACGTCCACC
CCAGAGGCTCTGGGTGCCAACCCCGGCTTGGTCGCCAGGATCACCGACAAGGGACTGCAG
TATGCGGCCCAGGAGGGGCTATTGGCTCTGCAGAGTGAGCTGCTCAGGATCACGCTGCCT
GACTTCACCGGGGACTTGAGGATCCCCCACGTCGGCCGTGGGCGCTATGAGTTCCACAGC
CTGAAGATCCACAGCTGTGAGCTGCTTCACTCTGCGCTGAGGCCTGTCCCCGGCCAGGGC
CTGAGTCTCAGCATCTCCGACTCCTCCATCCGGGTCCAGGGCAGGTGGAAGGTGCGCAAG
TCATTCTTCAAACTACAGGGCTTCTTTGATGTCAGTGTCAAGGGCATCAGCATTTCGGTC
AACCTCCTGTTGGGCAGCGAGTCCTCCGGGAGGCCCACAGTTACTGCCTCCAGCTGCAGC
AGTGACATCGCTGACGTGGAGGTGGACATGTCGGGAGACTTGGGGTGGCTGTTGAACCTC
TTCCACAACCAGATTGAGTCCAAGTTCCAGAAAGTACTGGAGAGCAGGATTTGCGAAATG
ATCCAGAAATCGGTGTCCTCCGATCTACAGCCTTATCTCCAAACTCTGCCAGTTACAACA
GAGATTGACAGTTTCGCCGACATTGATTATAGCTTAGTGGAAGCCCCTCGGGCAACAGCC
CAGATGCTGGAGGTGATGTTTAAGGGTGAAATCTTTCATCGTAACCACAGTTCTCCAGTT
ACCCTCCTTGCTGCAGTCATGAGCCTTCCTGAGGAACACAACAAAATGGTCTACTTTGCC
ATCTCGGATTATGTCTTCAACACGGCCAGCCTGGTTTATCATGAGGAAGGATATCTGAAC
TTCTCCATCACAGATGACATGATACCGCCTGACTCTAATATCCGACTGACCACCAAGTCC
TTCCGACCCTTCGTCCCACGGTTAGCCAGGCTCTACCCCAACATGAACCTGGAACTCCAG
GGATCAGTGCCCTCTGCTCCGCTCCTGAACTTCAGCCCTGGGAATCTGTCTGTGGACCCC
TATATGGAGATAGATGCCTTTGTGCACCTGCCCAGCTCCAGCAAGGAGCCTGTCTTCCGG
CTCAGTGTGGCCACTAATGTGTCCGCCACCTTGACCTTCAATACCAGCAAGATCACTGGG
TTCCTGAAGCCAGGAAAGGTAAAAGTGGAACTGAAAGAATCCAAAGTTGGACTATTCAAT
GCAGAGCTGTTGGAAGCGCTCCTCAACTATTACATCCTTAACACCTTCTACCCCAAGTTC
AATGATAAGTTGGCCGAAGGCTTCCCCCTTCCTCTGCTGAAGCGTGTTCAGCTCTACGAC
CTTGGGCTGCAGATCCATAAGGACTTCCTGTTCTTGGGTGCCAATGTCCAATACATGAGA
GTTTGA
Enzyme 51 GenBank Gene ID AF013512 Link Image
Enzyme 51 GeneCard ID LBP Link Image
Enzyme 51 GenAtlas ID LBP Link Image
Enzyme 51 HGNC ID HGNC:6517 Link Image
Enzyme 51 Chromosome Location 2
Enzyme 51 Locus 20q11.23
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 17791
Enzyme 52 Name Putative uncharacterized protein DKFZp434L0435
Enzyme 52 Synonyms Not Available
Enzyme 52 Gene Name DKFZp434L0435
Enzyme 52 Protein Sequence >Putative uncharacterized protein DKFZp434L0435
VAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
Enzyme 52 Number of Residues 55
Enzyme 52 Molecular Weight 6175.1
Enzyme 52 Theoretical pI 4.41
Enzyme 52 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 52 General Function Involved in glycolipid transporter activity
Enzyme 52 Specific Function Not Available
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function Not Available
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 50978454 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q9UFH6 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name Q9UFH6_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >168 bp
GTGGCCTTCTGCACGCTGCCCACACGCGAGGTCTTCCTGGAGGCCATGAACGTGGGGCCC
CCGGAGCAGGCCGTGCAGATGCTAGGCGAGGCCCTCCCCTTCATCCAGCGTGTCTACAAC
GTCTCCCAGAAGCTCTACGCCGAGCACTCCCTGCTGGACCTGCCCTAG
Enzyme 52 GenBank Gene ID AL122073 Link Image
Enzyme 52 GeneCard ID DKFZp434L0435 Link Image
Enzyme 52 GenAtlas ID DKFZp434L0435 Link Image
Enzyme 52 HGNC ID HGNC:28116 Link Image
Enzyme 52 Chromosome Location Not Available
Enzyme 52 Locus Not Available
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References Not Available
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 17792
Enzyme 53 Name T-cell surface glycoprotein CD1b
Enzyme 53 Synonyms
  1. CD1b antigen
Enzyme 53 Gene Name CD1B
Enzyme 53 Protein Sequence >T-cell surface glycoprotein CD1b
MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDS
DSGTAIFLKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDFQMKYPFEIQGIAGC
ELHSGGAIVSFLRGALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQGIMETVRILL
YETCPRYLLGVLNAGKADLQRQVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVWVMWMR
GEQEQQGTQLGDILPNANWTWYLRATLDVADGEAAGLSCRVKHSSLEGQDIILYWRNPTS
IGSIVLAIIVPSLLLLLCLALWYMRRRSYQNIP
Enzyme 53 Number of Residues 333
Enzyme 53 Molecular Weight 36939.1
Enzyme 53 Theoretical pI 6.24
Enzyme 53 GO Classification
Function
Process
  • antigen processing and presentation
  • immune response
  • immune system process
Component
  • cell part
  • membrane
Enzyme 53 General Function Involved in immune response
Enzyme 53 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 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • 1-17
Enzyme 53 Transmembrane Regions
  • 304-324
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 55859606 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID P29016 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name CD1B_HUMAN Link Image
Enzyme 53 PDB ID 1UQS Link Image
Enzyme 53 PDB File Show
Enzyme 53 3D Structure
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >1002 bp
ATGCTGTTTCTGCAGTTTCTGCTGCTAGCTCTTCTTCTCCCAGGTGGTGACAATGCAGAC
GCATCCCAGGAACACGTCTCCTTCCATGTCATCCAGATCTTCTCATTTGTCAACCAATCC
TGGGCACGAGGTCAGGGCTCAGGATGGCTGGACGAGTTGCAGACTCATGGCTGGGACAGT
GAATCAGGCACAATAATTTTCCTGCATAACTGGTCCAAGGGCAACTTCAGCAATGAAGAG
TTGTCAGACCTAGAGTTGTTATTTCGTTTCTACCTCTTTGGATTAACTCGGGAGATTCAA
GACCATGCAAGTCAAGATTACTCGAAATATCCCTTTGAAGTACAGGTGAAAGCGGGCTGT
GAGCTGCATTCTGGAAAGAGCCCAGAAGGCTTCTTTCAGGTAGCTTTCAACGGATTAGAT
TTACTGAGTTTCCAGAATACAACATGGGTGCCATCTCCAGGCTGTGGAAGTTTGGCCCAA
AGTGTCTGTCATCTACTCAATCATCAGTATGAAGGCGTCACAGAAACAGTGTATAATCTC
ATAAGAAGCACTTGCCCCCGATTTCTCTTGGGTCTCCTGGATGCAGGGAAGATGTATGTA
CACAGGCAAGTGAGGCCAGAAGCCTGGCTGTCCAGTCGCCCCAGCCTTGGGTCTGGCCAG
CTGTTGCTGGTTTGTCATGCCTCCGGCTTCTACCCAAAGCCTGTTTGGGTGACATGGATG
CGGAATGAACAGGAGCAACTGGGCACTAAACATGGTGATATTCTTCCTAATGCTGATGGG
ACATGGTATCTTCAGGTGATCCTGGAGGTGGCATCTGAGGAGCCTGCTGGCCTGTCTTGT
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTTT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
Enzyme 53 GenBank Gene ID AL121986 Link Image
Enzyme 53 GeneCard ID CD1B Link Image
Enzyme 53 GenAtlas ID CD1B Link Image
Enzyme 53 HGNC ID HGNC:1635 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 1q22-q23
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 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 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 17793
Enzyme 54 Name Glycolipid transfer protein
Enzyme 54 Synonyms
  1. GLTP
Enzyme 54 Gene Name GLTP
Enzyme 54 Protein Sequence >Glycolipid transfer protein
MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVY
DTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENH
PNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKI
RLFLVNYTATIDVIYEMYTQMNAELNYKV
Enzyme 54 Number of Residues 209
Enzyme 54 Molecular Weight 23849.6
Enzyme 54 Theoretical pI 7.49
Enzyme 54 GO Classification
Function
  • binding
  • glycolipid binding
  • glycolipid transporter activity
  • lipid binding
  • lipid transporter activity
  • substrate-specific transporter activity
  • transporter activity
Process
  • establishment of localization
  • glycolipid transport
  • lipid transport
  • transport
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 54 General Function Involved in glycolipid transporter activity
Enzyme 54 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 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 Not Available
Enzyme 54 UniProtKB/Swiss-Prot ID Q9NZD2 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name GLTP_HUMAN Link Image
Enzyme 54 PDB ID 1SX6 Link Image
Enzyme 54 PDB File Show
Enzyme 54 3D Structure
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >630 bp
ATGGCGCTGCTGGCGGAGCACTTGCTGAAGCCGCTGCCCGCGGACAAGCAGATCGAGACC
GGGCCCTTCCTCGAGGCGGTGTCCCACCTGCCGCCCTTCTTCGATTGCCTTGGGTCCCCA
GTGTTTACTCCCATCAAGGCAGACATAAGCGGCAACATCACGAAAATCAAAGCTGTGTAC
GACACCAACCCAGCCAAGTTCCGGACCCTGCAGAACATCCTGGAGGTGGAGAAAGAAATG
TATGGAGCAGAGTGGCCCAAAGTAGGGGCCACACTGGCGCTGATGTGGCTGAAAAGAGGC
CTCCGCTTCATCCAGGTCTTCCTCCAGAGCATCTGCGACGGGGAGCGGGACGAGAACCAC
CCCAACCTCATCCGTGTCAACGCCACCAAGGCCTACGAGATGGCCCTCAAGAAGTACCAT
GGCTGGATCGTGCAGAAGATCTTCCAGGCAGCACTGTACGCAGCACCCTATAAGTCTGAC
TTCCTGAAAGCGCTCTCCAAGGGGCAGAATGTTACGGAGGAGGAGTGCCTGGAGAAGATC
CGCCTCTTCCTAGTCAACTACACGGCGACCATCGATGTCATCTACGAGATGTACACCCAG
ATGAACGCTGAGCTCAACTACAAGGTGTAG
Enzyme 54 GenBank Gene ID AF209704 Link Image
Enzyme 54 GeneCard ID GLTP Link Image
Enzyme 54 GenAtlas ID GLTP Link Image
Enzyme 54 HGNC ID HGNC:24867 Link Image
Enzyme 54 Chromosome Location 1
Enzyme 54 Locus 12q24.11
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Li XM, Malakhova ML, Lin X, Pike HM, Chung T, Molotkovsky JG, Brown RE: Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy. Biochemistry. 2004 Aug 10;43(31):10285-94. [PubMed Link Image]
  2. Zou X, Chung T, Lin X, Malakhova ML, Pike HM, Brown RE: Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution. BMC Genomics. 2008 Feb 8;9:72. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rao CS, Lin X, Pike HM, Molotkovsky JG, Brown RE: Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses. Biochemistry. 2004 Nov 2;43(43):13805-15. [PubMed Link Image]
  6. Tuuf J, Mattjus P: Human glycolipid transfer protein--intracellular localization and effects on the sphingolipid synthesis. Biochim Biophys Acta. 2007 Nov;1771(11):1353-63. Epub 2007 Sep 21. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
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Enzyme 54 Metabolite References Not Available