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Human Metabolome Database Version 2.5

 

Showing metabocard for Phosphoadenosine phosphosulfate (HMDB01134)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:31
Accession Number HMDB01134
Secondary Accession Numbers Not Available
Common Name Phosphoadenosine phosphosulfate
Description 3'-Phosphoadenosine-5'-phosphosulfate. Key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from sulfate ion and ATP in a two-step process. This compound also is an important step in the process of sulfur fixation in plants and microorganisms.
Synonyms
  1. 3'-Phospho-5'-adenylyl sulfate
  2. 3'-Phosphoadenosine 5'-phosphosulfate
  3. 3'-Phosphoadenylyl sulfate
  4. 3'-phosphoadenosine-5'-phosphosulfate
  5. 3'-phosphoadenylyl-sulfate
  6. 5-phosphoadenosine 3-phosphosulfate
  7. PAPS
  8. Phosphoadenosine Phosphosulfate
  9. Phosphoadenosine phosphosulfic acid
Chemical IUPAC Name 6-amino-9-[3-hydroxy-5-[(hydroxy-sulfooxy-phosphoryl)oxymethyl]-4-phosphonooxy-oxolan-2-yl]-purine
Chemical Formula C10H15N5O13P2S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • sulfuric acid
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Androgen and estrogen metabolism
  • Component of Chondroitin / Heparan sulfate biosynthesis
  • Component of Glycosphingolipid metabolism
  • Component of Sulfur metabolism
Application
Source
  • Endogenous
Average Molecular Weight 507.264
Monoisotopic Molecular Weight 506.986237
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OS(O)(=O)=O)[C@@H](OP(O)(O)=O)[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC(COP(O)(=O)OS(O)(=O)=O)C(OP(O)(O)=O)C1O
KEGG Compound ID C00053 Link Image
BioCyc ID PAPS Link Image
BiGG ID 33679 Link Image
Wikipedia Link Phosphoadenosine phosphosulfate Link Image
NuGOwiki Link HMDB01134 Link Image
Metagene Link HMDB01134 Link Image
METLIN ID 6028 Link Image
PubChem Compound 990 Link Image
PubChem Substance 3056 Link Image
ChEBI ID 17980 Link Image
CAS Registry Number 482-67-7
InChI Identifier InChI=1/C10H15N5O13P2S/c11-8-5-9(13-2-12-8)15(3-14-5)10-6(16)7(27-29(17,18)19)4(26-10)1-25-30(20,21)28-31(22,23)24/h2-4,6-7,10,16H,1H2,(H,20,21)(H2,11,12,13)(H2,17,18,19)(H,22,23,24)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Lin, Chun-Hung; Shen, Gwo-Jenn; Garcia-Junceda, Eduardo; Wong, Chi-Huey. Enzymic Synthesis and Regeneration of 3'-Phosphoadenosine 5'-Phosphosulfate (PAPS) for Regioselective Sulfation of Oligosaccharides. Journal of the American Chemical Society (1995),
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.65 [Predicted by ALOGPS]; -5.6 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • golgi apparatus
Biofluid Location Not Available
Tissue Location
Tissue References
Kidney
Liver
Platelet
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Sulfate/Sulfite Metabolism SMP00041 Link Image map00920 Link Image
General References
  1. Emmi L, Bergamini C, Spinelli A, Liotta F, Marchione T, Caldini A, Fanelli A, De Cristofaro MT, Dal Pozzo G: Possible pathogenetic role of activated platelets in the primary antiphospholipid syndrome involving the central nervous system. Ann N Y Acad Sci. 1997 Aug 14;823:188-200. [PubMed Link Image]
  2. Fanelli A, Bergamini C, Rapi S, Caldini A, Spinelli A, Buggiani A, Emmi L: Flow cytometric detection of circulating activated platelets in primary antiphospholipid syndrome. Correlation with thrombocytopenia and anticardiolipin antibodies. Lupus. 1997;6(3):261-7. [PubMed Link Image]
  3. Joseph JE, Harrison P, Mackie IJ, Isenberg DA, Machin SJ: Increased circulating platelet-leucocyte complexes and platelet activation in patients with antiphospholipid syndrome, systemic lupus erythematosus and rheumatoid arthritis. Br J Haematol. 2001 Nov;115(2):451-9. [PubMed Link Image]
  4. Suarez IM, Diaz RA, Aguayo Canela D, Pujol de la Llave E: Correction of severe thrombocytopenia with chloroquine in the primary antiphospholipid syndrome. Lupus. 1996 Feb;5(1):81-3. [PubMed Link Image]
  5. Khoo BY, Sit KH, Wong KP: Does PAPS generation determine the overall sulfate conjugation in human platelets? Life Sci. 1988;42(23):2389-95. [PubMed Link Image]
  6. Wong KP, Khoo BY, Sit KH: Biosynthesis of PAPS in vitro by human liver. Measurement by two independent assay procedures. Biochem Pharmacol. 1991 Jan 1;41(1):63-9. [PubMed Link Image]
  7. Cappiello M, Franchi M, Rane A, Pacifici GM: Sulphotransferase and its substrate: adenosine-3'-phosphate-5'-phosphosulphate in human fetal liver and placenta. Dev Pharmacol Ther. 1990;14(1):62-5. [PubMed Link Image]
  8. Cappiello M, Franchi M, Giuliani L, Pacifici GM: Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3'-phosphate 5'-phosphosulphate in human tissues. Eur J Clin Pharmacol. 1989;37(3):317-20. [PubMed Link Image]
  9. Carlier M, Squifflet JP, Pirson Y, Gribomont B, Alexandre GP: Maximal hydration during anesthesia increases pulmonary arterial pressures and improves early function of human renal transplants. Transplantation. 1982 Oct;34(4):201-4. [PubMed Link Image]
  10. Wikipedia Link Image
Metabolic Enzymes
  1. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
  3. Carbohydrate sulfotransferase 3
  4. Carbohydrate sulfotransferase 13
  5. Carbohydrate sulfotransferase 12
  6. Galactosylceramide sulfotransferase
  7. Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
  8. 3'(2'),5'-bisphosphate nucleotidase 1
  9. Heparan sulfate glucosamine 3-O-sulfotransferase 1
  10. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
  11. Estrogen sulfotransferase
  12. Heparan sulfate glucosamine 3-O-sulfotransferase 5
  13. Heparan sulfate glucosamine 3-O-sulfotransferase 2
  14. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
  15. Protein-tyrosine sulfotransferase 2
  16. Sulfotransferase family cytosolic 2B member 1
  17. Sulfotransferase 1A3/1A4
  18. Carbohydrate sulfotransferase 7
  19. Heparan-sulfate 6-O-sulfotransferase 1
  20. Heparan-sulfate 6-O-sulfotransferase 2
  21. Adenosine 3'-phospho 5'-phosphosulfate transporter 1
  22. Heparan-sulfate 6-O-sulfotransferase 3
  23. Carbohydrate sulfotransferase 15
  24. cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
  25. Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2
  26. Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
  27. cDNA FLJ75927, highly similar to Homo sapiens carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11), mRNA (Carbohydrate (Chondroitin 4) sulfotransferase 11, isoform CRA_a)
  28. Carbohydrate (Chondroitin 4) sulfotransferase 12
  29. Tyrosylprotein sulfotransferase 1
  30. cDNA FLJ76340, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 5 (HS3ST5), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 5)
  31. cDNA FLJ77168, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1 (HS3ST3A1), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3A1)
  32. cDNA FLJ90057 fis, clone HEMBA1003101, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
  33. cDNA FLJ39504 fis, clone PROST2017203, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 1 (EC 2.8.2.23)
  34. Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a
  35. Adenosine 3'-phospho 5'-phosphosulfate transporter 2
Enzyme 1 [top]
Enzyme 1 ID 5351
Enzyme 1 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 1 Synonyms
  1. E-NPP 1
  2. Membrane component chromosome 6 surface marker 1
  3. Phosphodiesterase I/nucleotide pyrophosphatase 1
  4. Plasma-cell membrane glycoprotein PC-1
  5. Alkaline phosphodiesterase I
  6. Nucleotide pyrophosphatase
  7. NPPase
Enzyme 1 Gene Name ENPP1
Enzyme 1 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 1 Number of Residues 925
Enzyme 1 Molecular Weight 104923.6
Enzyme 1 Theoretical pI 7.14
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • pattern binding
  • polysaccharide binding
  • receptor activity
  • scavenger receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • immune response
  • immune system process
  • metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 77-97
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 170650661 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2778 bp
ATGGAGCGCGACGGCTGCGCGGGGGGCGGGAGCCGCGGCGGCGAGGGCGGGCGCGCTCCC
CGGGAGGGCCCGGCGGGGAACGGCCGCGATCGGGGCCGCAGCCACGCTGCCGAGGCGCCC
GGGGACCCGCAGGCGGCCGCGTCCTTGCTGGCCCCTATGGACGTGGGGGAGGAGCCGCTG
GAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCCAACACCTATAAAGTACTCTCGCTG
GTATTGTCAGTATGTGTGTTAACAACAATACTTGGTTGTATATTTGGGTTGAAACCAAGC
TGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGTTTCGAGAGAACATTTGGGAACTGT
CGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGCTGTTTAGATTACCAGGAGACGTGC
ATAGAACCAGAACATATATGGACTTGCAACAAATTCAGGTGTGGTGAGAAAAGGTTGACC
AGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGACAAGGGCGACTGCTGCATCAACTAC
AGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAAGAACCATGTGAGAGCATTAATGAG
CCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACCCTCTTATTTTCTTTGGATGGATTC
AGGGCAGAATATTTACACACTTGGGGTGGACTTCTTCCTGTTATTAGCAAACTAAAAAAA
TGTGGAACATATACTAAAAACATGAGACCGGTATATCCAACAAAAACTTTCCCCAATCAC
TACAGCATTGTCACCGGATTGTATCCAGAATCTCATGGCATAATCGACAATAAAATGTAT
GATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGTAAAGAGAAATTTAATCCTGAGTGG
TACAAAGGAGAACCAATTTGGGTCACAGCTAAGTATCAAGGCCTCAAGTCTGGCACATTT
TTCTGGCCAGGATCAGATGTGGAAATTAACGGAATTTTCCCAGACATCTATAAAATGTAT
AATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCTGTTCTTCAGTGGCTACAGCTTCCT
AAAGATGAAAGACCACACTTTTACACTCTGTATTTAGAAGAACCAGATTCTTCAGGTCAT
TCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCCTTGCAGAGGGTTGATGGTATGGTT
GGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTGCACAGATGCCTGAACCTCATCCTT
ATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAGAAATACATATATCTGAATAAATAT
TTGGGGGATGTTAAAAATATTAAAGTTATCTATGGACCTGCAGCTCGATTGAGACCCTCT
GATGTCCCAGATAAATACTATTCATTTAACTATGAAGGCATTGCCCGAAATCTTTCTTGC
CGGGAACCAAACCAGCACTTCAAACCTTACCTGAAACATTTCTTACCTAAGCGTTTGCAC
TTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTCTATTTGGACCCTCAGTGGCAACTT
GCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGTGGATTTCATGGCTCTGACAATGTA
TTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGACCTGGATTCAAGCATGGCATTGAG
GCTGACACCTTTGAAAACATTGAAGTCTATAACTTAATGTGTGATTTACTGAATTTGACA
CCGGCTCCTAATAACGGAACTCATGGAAGTCTTAACCACCTTCTAAAGAATCCTGTTTAT
ACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTACAGTGCCCCTTCACAAGAAACCCC
AGAGATAACCTTGGCTGCTCATGTAACCCTTCGATTTTGCCGATTGAGGATTTTCAAACA
CAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATTAAGCATGAAACTTTACCCTATGGA
AGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGTCTTCTTTCCCAGCACCAGTTTATG
AGTGGATACAGCCAAGACATCTTAATGCCCCTTTGGACATCCTATACCGTGGACAGAAAT
GACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTGTACCAGGACTTTAGAATTCCTCTT
AGTCCTGTCCATAAATGTTCATTTTATAAAAATAACACCAAAGTGAGTTACGGGTTCCTC
TCCCCACCACAACTAAATAAAAATTCAAGTGGAATATATTCTGAAGCTTTGCTTACTACA
AATATAGTGCCAATGTACCAGAGTTTTCAAGTTATATGGCGCTACTTTCATGACACCCTA
CTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAATGTCGTCAGTGGTCCTGTGTTTGAC
TTTGATTATGATGGACGTTGTGATTCCTTAGAGAATCTGAGGCAAAAAAGAAGAGTCATC
CGTAACCAAGAAATTTTGATTCCAACTCACTTCTTTATTGTGCTAACAAGCTGTAAAGAT
ACATCTCAGACGCCTTTGCACTGTGAAAACCTAGACACCTTAGCTTTCATTTTGCCTCAC
AGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAGCATGACTCCTCATGGGTTGAAGAA
TTGTTAATGTTACACAGAGCACGGATCACAGATGTTGAGCACATCACTGGACTCAGCTTC
TATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTAAAGTTGAAAACACATTTGCCAACC
TTTAGCCAAGAAGACTGA
Enzyme 1 GenBank Gene ID NM_006208.2 Link Image
Enzyme 1 GeneCard ID ENPP1 Link Image
Enzyme 1 GenAtlas ID ENPP1 Link Image
Enzyme 1 HGNC ID HGNC:3356 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6q22-q23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  6. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  7. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  8. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  9. Bello V, Goding JW, Greengrass V, Sali A, Dubljevic V, Lenoir C, Trugnan G, Maurice M: Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Mol Biol Cell. 2001 Oct;12(10):3004-15. [PubMed Link Image]
  10. Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed Link Image]
  11. 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]
  12. 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]
  13. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
  14. Rutsch F, Ruf N, Vaingankar S, Toliat MR, Suk A, Hohne W, Schauer G, Lehmann M, Roscioli T, Schnabel D, Epplen JT, Knisely A, Superti-Furga A, McGill J, Filippone M, Sinaiko AR, Vallance H, Hinrichs B, Smith W, Ferre M, Terkeltaub R, Nurnberg P: Mutations in ENPP1 are associated with 'idiopathic' infantile arterial calcification. Nat Genet. 2003 Aug;34(4):379-81. [PubMed Link Image]
  15. Cheng KS, Chen MR, Ruf N, Lin SP, Rutsch F: Generalized arterial calcification of infancy: different clinical courses in two affected siblings. Am J Med Genet A. 2005 Jul 15;136(2):210-3. [PubMed Link Image]
  16. Bacci S, Ludovico O, Prudente S, Zhang YY, Di Paola R, Mangiacotti D, Rauseo A, Nolan D, Duffy J, Fini G, Salvemini L, Amico C, Vigna C, Pellegrini F, Menzaghi C, Doria A, Trischitta V: The K121Q polymorphism of the ENPP1/PC-1 gene is associated with insulin resistance/atherogenic phenotypes, including earlier onset of type 2 diabetes and myocardial infarction. Diabetes. 2005 Oct;54(10):3021-5. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5426
Enzyme 2 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Enzyme 2 Synonyms
  1. E-NPP 3
  2. Phosphodiesterase I beta
  3. PD-Ibeta
  4. Phosphodiesterase I/nucleotide pyrophosphatase 3
  5. CD203c antigen
  6. Alkaline phosphodiesterase I
  7. Nucleotide pyrophosphatase
  8. NPPase
Enzyme 2 Gene Name ENPP3
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Enzyme 2 Number of Residues 875
Enzyme 2 Molecular Weight 100123.5
Enzyme 2 Theoretical pI 6.55
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • pattern binding
  • polysaccharide binding
  • receptor activity
  • scavenger receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • immune response
  • immune system process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD
Enzyme 2 Pathways
Enzyme 2 Reactions
  • a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 12-30
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2465540 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14638 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENPP3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2628 bp
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
Enzyme 2 GenBank Gene ID AF005632 Link Image
Enzyme 2 GeneCard ID ENPP3 Link Image
Enzyme 2 GenAtlas ID ENPP3 Link Image
Enzyme 2 HGNC ID HGNC:3358 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Buhring HJ, Seiffert M, Giesert C, Marxer A, Kanz L, Valent P, Sano K: The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3. Blood. 2001 May 15;97(10):3303-5. [PubMed Link Image]
  5. Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed Link Image]
  6. Buhring HJ, Streble A, Valent P: The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell activation and allergy diagnosis. Int Arch Allergy Immunol. 2004 Apr;133(4):317-29. Epub 2004 Mar 17. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5519
Enzyme 3 Name Carbohydrate sulfotransferase 3
Enzyme 3 Synonyms
  1. Chondroitin 6-O-sulfotransferase 1
  2. C6ST-1
  3. Chondroitin 6-sulfotransferase
  4. Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0
  5. GST-0
Enzyme 3 Gene Name CHST3
Enzyme 3 Protein Sequence >Carbohydrate sulfotransferase 3
MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALA
DANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKE
EEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGAN
AAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKK
VFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLV
RDPRAVLASRMVAFAGKYKTWKKWLDDEGQDGLREEEVQRLRGNCESIRLSAELGLRQPA
WLRGRYMLVRYEDVARGPLQKAREMYRFAGIPLTPQVEDWIQKNTQAAHDGSGIYSTQKN
SSEQFEKWRFSMPFKLAQVVQAACGPAMRLFGYKLARDAAALTNRSVSLLEERGTFWVT
Enzyme 3 Number of Residues 479
Enzyme 3 Molecular Weight 54705.5
Enzyme 3 Theoretical pI 8.75
Enzyme 3 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • Golgi membrane
  • cell part
  • membrane
  • organelle membrane
Enzyme 3 General Function Involved in sulfotransferase activity
Enzyme 3 Specific Function Catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen
Enzyme 3 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 3 Reactions
  • 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 21-38
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 3510308 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q7LGC8 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CHST3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1440 bp
ATGGAGAAAGGACTCACTTTGCCCCAGGACTGCCGGGACTTTGTGCACAGCCTGAAGATG
AGAAGCAAATACGCCCTTTTCTTGGTTTTTGTGGTGATAGTTTTTGTCTTCATCGAAAAG
GAAAATAAAATCATATCAAGGGTCTCAGACAAGCTGAAGCAGATTCCCCAAGCTCTAGCA
GATGCCAACAGCACCGACCCAGCCCTGATCTTAGCTGAGAACGCATCTCTCTTGTCCCTG
AGCGAGCTCGATTCAGCCTTCTCCCAGCTTCAGAGCCGTCTCCGCAACCTCAGCTTGCAG
CTGGGCGTGGAGCCAGCCATGGAGGCCGCAGGGGAGGAAGAGGAAGAGCAGAGAAAGGAG
GAGGAGCCGCCCAGACCGGCCGTGGCGGGGCCCCGGCGCCACGTGCTGCTCATGGCCACC
ACGCGCACCGGCTCCTCGTTCGTGGGCGAGTTCTTCAACCAGCAGGGCAACATCTTCTAC
CTCTTCGAGCCGCTGTGGCACATCGAGCGCACAGTGTCCTTCGAGCCGGGGGGCGCCAAC
GCCGCGGGCTCGGCCCTGGTGTACCGCGACGTGCTCAAGCAGCTCTTCCTGTGCGACCTG
TACGTGCTGGAGCACTTCATCACGCCGCTGCCCGAGGACCACCTGACTCAGTTCATGTTC
CGCCGGGGCTCCAGCCGCTCCCTGTGCGAGGACCCCGTCTGTACGCCCTTCGTCAAGAAG
GTCTTCGAGAAGTACCACTGCAAGAACCGCCGCTGCGGCCCCCTCAACGTGACGCTGGCC
GCAGAGGCCTGCCGCCGCAAGGAGCACATGGCCCTCAAGGCGGTGCGCATCCGGCAGCTG
GAGTTCCTGCAGCCGCTGGCCGAGGACCCCCGCCTGGACCTGCGCGTCATCCAGCTGGTG
CGCGACCCCCGGGCCGTGCTGGCCTCGCGCATGGTGGCCTTCGCCGGCAAGTATAAGACC
TGGAAGAAGTGGCTGGACGACGAGGGCCAGGACGGCCTGAGGGAAGAGGAGGTGCAGCGG
CTGCGGGGCAACTGCGAGAGCATCCGCCTGTCCGCGGAGCTGGGGCTGCGGCAGCCCGCC
TGGCTGCGGGGCCGCTACATGCTGGTGCGCTACGAGGACGTGGCACGCGGGCCGCTGCAG
AAGGCCCGCGAGATGTACCCGTTCGCCGGCATCCCCCTGACCCCGCAGGTGGAAGACTGG
ATCCAAAAGAACACGCAGGCGGCCCACGACGGCAGCGGCATCTACTCCACGCAGAAGAAC
TCCTCGGAGCAGTTCGAGAAGTGGCGCTTCAGCATGCCCTTCAAGCTGGCCCAGGTGGTG
CAGGCCCCGTGCGGCCCTGCCATGCGCCTCTTCGGCTACAAACTGGCGCGGGACGCCGCC
GCCCTCACCAACCGCTCAGTCAGCCTGCTGGAGGAGAGGGGCACCTTCTGGGTCACGTAG
Enzyme 3 GenBank Gene ID AB012192 Link Image
Enzyme 3 GeneCard ID CHST3 Link Image
Enzyme 3 GenAtlas ID CHST3 Link Image
Enzyme 3 HGNC ID HGNC:1971 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 10q22.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Fukuta M, Kobayashi Y, Uchimura K, Kimata K, Habuchi O: Molecular cloning and expression of human chondroitin 6-sulfotransferase. Biochim Biophys Acta. 1998 Jul 30;1399(1):57-61. [PubMed Link Image]
  2. Tsutsumi K, Shimakawa H, Kitagawa H, Sugahara K: Functional expression and genomic structure of human chondroitin 6-sulfotransferase. FEBS Lett. 1998 Dec 18;441(2):235-41. [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. Thiele H, Sakano M, Kitagawa H, Sugahara K, Rajab A, Hohne W, Ritter H, Leschik G, Nurnberg P, Mundlos S: Loss of chondroitin 6-O-sulfotransferase-1 function results in severe human chondrodysplasia with progressive spinal involvement. Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):10155-60. Epub 2004 Jun 23. [PubMed Link Image]
  5. Hermanns P, Unger S, Rossi A, Perez-Aytes A, Cortina H, Bonafe L, Boccone L, Setzu V, Dutoit M, Sangiorgi L, Pecora F, Reicherter K, Nishimura G, Spranger J, Zabel B, Superti-Furga A: Congenital joint dislocations caused by carbohydrate sulfotransferase 3 deficiency in recessive Larsen syndrome and humero-spinal dysostosis. Am J Hum Genet. 2008 Jun;82(6):1368-74. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5520
Enzyme 4 Name Carbohydrate sulfotransferase 13
Enzyme 4 Synonyms
  1. Chondroitin 4-O-sulfotransferase 3
  2. Chondroitin 4-sulfotransferase 3
  3. C4ST-3
  4. C4ST3
Enzyme 4 Gene Name CHST13
Enzyme 4 Protein Sequence >Carbohydrate sulfotransferase 13
MGRRCCRRRVLAAACLGAALLLLCAAPRSLRPAFGNRALGSSWLGGEKRSPLQKLYDLDQ
DPRSTLAKVHRQRRDLLNSACSRHSRRQRLLQPEDLRHVLVDDAHGLLYCYVPKVACTNW
KRVLLALSGQARGDPRAISAQEAHAPGRLPSLADFSPAEINRRLRAYLAFLFVREPFERL
ASAYRNKLARPYSAAFQRRYGARIVQRLRPRALPDARARGHDVRFAEFLAYLLDPRTRRE
EPFNEHWERAHALCHPCRLRYDVVGKFETLAEDAAFVLGLAGASDLSFPGPPRPRGAAAS
RDLAARLFRDISPFYQRRLFDLYKMDFLLFNYSAPSYLRLL
Enzyme 4 Number of Residues 341
Enzyme 4 Molecular Weight 38919.3
Enzyme 4 Theoretical pI 11.00
Enzyme 4 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate biosynthetic process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 4 General Function Involved in sulfotransferase activity
Enzyme 4 Specific Function Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan
Enzyme 4 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
  • Sulfate and Sulfite Metabolism (map00920 Link Image)
Enzyme 4 Reactions
  • 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate [RN:R02180]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 10-30
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 22651777 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8NET6 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name CHSTD_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1026 bp
ATGGGGAGGCGCTGCTGCCGGCGGCGCGTGCTGGCGGCCGCCTGTCTGGGCGCCGCGCTC
CTGCTCCTATGCGCCGCGCCCCGCTCCCTGCGCCCGGCATTTGGAAACAGAGCCCTGGGC
TCCAGCTGGCTTGGTGGGGAGAAGAGAAGCCCCCTGCAGAAGCTCTATGACCTGGATCAG
GACCCGCGCTCGACCCTGGCGAAGGTGCACCGTCAGCGGCGCGACCTGCTGAACAGCGCC
TGTAGCCGCCACTCACGCCGGCAGCGCCTGCTACAGCCGGAGGACCTGCGGCACGTGCTG
GTGGACGACGCGCATGGCCTGCTCTACTGCTACGTGCCCAAGGTGGCCTGCACCAACTGG
AAGCGCGTGCTGCTGGCGCTGAGCGGCCAAGCCCGCGGCGACCCGCGCGCCATCTCCGCG
CAAGAGGCGCACGCGCCTGGCCGCCTGCCCTCACTGGCCGACTTCAGCCCCGCCGAGATC
AACCGGCGCCTGCGCGCCTACTTGGCCTTCCTGTTCGTGCGGGAGCCCTTCGAGCGCCTG
GCATCGGCTTACCGCAACAAGCTCGCGCGCCCCTACAGCGCCGCCTTCCAGAGGCGCTAC
GGTGCACGCATCGTTCAGCGCCTGCGGCCGCGCGCGCTCCCCGACGCCCGGGCCCGCGGC
CACGACGTGCGCTTCGCGGAGTTCCTGGCCTACCTGCTGGACCCGCGCACGCGGCGTGAG
GAGCCCTTCAACGAGCACTGGGAGCGCGCGCACGCGCTCTGCCACCCGTGTCGCCTCCGC
TACGACGTCGTGGGCAAGTTCGAGACGCTGGCGGAGGACGCGGCCTTCGTGCTGGGCCTG
GCGGGCGCATCCGACCTGAGCTTCCCTGGGCCGCCGCGGCCCCGGGGAGCCGCCGCCTCC
CGCGACCTGGCAGCGCGCCTCTTCCGGGACATCAGCCCCTTCTACCAGCGGCGCCTCTTC
GACCTCTACAAGATGGACTTCCTGCTTTTCAACTACTCCGCCCCCTCCTACCTGCGGCTG
CTCTAG
Enzyme 4 GenBank Gene ID AY120869 Link Image
Enzyme 4 GeneCard ID CHST13 Link Image
Enzyme 4 GenAtlas ID CHST13 Link Image
Enzyme 4 HGNC ID HGNC:21755 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3q21.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Kang HG, Evers MR, Xia G, Baenziger JU, Schachner M: Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases. J Biol Chem. 2002 Sep 20;277(38):34766-72. Epub 2002 Jun 21. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5521
Enzyme 5 Name Carbohydrate sulfotransferase 12
Enzyme 5 Synonyms
  1. Chondroitin 4-O-sulfotransferase 2
  2. Chondroitin 4-sulfotransferase 2
  3. C4ST-2
  4. C4ST2
  5. Sulfotransferase Hlo
Enzyme 5 Gene Name CHST12
Enzyme 5 Protein Sequence >Carbohydrate sulfotransferase 12
MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDREL
TADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQ
QAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKR
VMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTK
FLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSF
ANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDR
QLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
Enzyme 5 Number of Residues 414
Enzyme 5 Molecular Weight 48413.9
Enzyme 5 Theoretical pI 9.69
Enzyme 5 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate biosynthetic process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 5 General Function Involved in sulfotransferase activity
Enzyme 5 Specific Function Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor
Enzyme 5 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
  • Sulfate and Sulfite Metabolism (map00920 Link Image)
Enzyme 5 Reactions
  • 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate [RN:R02180]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 6-26
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 8925968 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9NRB3 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CHSTC_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1245 bp
ATGACCAAGGCCCGGCTGTTCCGGCTGTGGCTGGTGCTGGGGTCGGTGTTCATGATCCTG
CTGATCATCGTGTACTGGGACAGCGCAAGCGCCGCGCACTTCTACTTGCACACGTCCTTC
TCTAAGCCGCACACAGGGCCGCCGCTGCCCACGCCCGGGCCGGACAGGGACAGGGAGCTC
ACGGCCGACTCCGATGTCGACGAGTTTCTGGACAAGTTTCTCAGTGCTGGCGTGAAGCAG
AGCGACCTTCCCAGAAAGGAGACGGAGCAGCCGCTTGCGCCGGGGAGCATGGAGGAGAGC
GTGAGAGGCTACGACTGGTCCCCGCGCGACGCCCGGCGCAGCCCAGACCAGGGCCGGCAG
CAGGCGGAGCGGAGGAGCGTGCTGCGGGGCTTCTGCGCCAACTCCAGCCTGGCCTTCCCC
ACCAAGGAGCGCGCATTCGACGACATCCCCAACTCGGAGCTGAGCCACCTGATCGTGGAC
GACCGGCACGGGGCCATCTACTGCTACGTGCCCAAGGTGGCCTGCACCAACTGGAAGCGC
GTGATGATCGTGCTGAGCGGAAGCCTGCTGCACCGCGGTGCGCCCTACCGCGACCCGCTG
CGCATCCCGCGCGAGCACGTGCACAACGCCAGCGCGCACCTGACCTTCAACAAGTTCTGG
CGCCGCTACGGGAAGCTCTCCCGCCACCTCATGAAGGTCAAGCTCAAGAAGTACACCAAG
TTCCTCTTCGTGCGCGACCCCTTCGTGCGCCTGATCTCCGCCTTCCGCAGCAAGTTCGAG
CTGGAGAACGAGGAGTTCTACCGCAAGTTCGCCGTGCCCATGCTGCGGCTGTACGCCAAC
CACACAAGCCTGCCCGCCTCGGCGCGCGAGGCCTTCCGCGCTGGCCTCAAGGTGTCCTTC
GCCAACTTCATCCAGTACCTGCTGGACCCGCACACGGAGAAGCTGGCGCCCTTCAACGAG
CACTGGCGGCAGGTGTACCGCCTCTGCCACCCGTGCCAGATCGACTACGACTTCGTGGGG
AAGCTGGAGACTCTGGACGAGGACGCCGCGCAGCTGCTGCAGCTACTCCAGGTGGACCGG
CAGCTCCGCTTCCCCCCGAGCTACCGGAACAGGACCGCCAGCAGCTGGGAGGAGGACTGT
TTCGCCAAGATCCCCCTGGCCTGGAGGCAGCAGCTGTATAAACTCTACGAGGCCGACTTT
GTTCTCTTCGGCTACCCCAAGCCCGAAAACCTCCTCCGAGACTGA
Enzyme 5 GenBank Gene ID AF239822 Link Image
Enzyme 5 GeneCard ID CHST12 Link Image
Enzyme 5 GenAtlas ID CHST12 Link Image
Enzyme 5 HGNC ID HGNC:17423 Link Image
Enzyme 5 Chromosome Location 7
Enzyme 5 Locus 7p22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Hiraoka N, Nakagawa H, Ong E, Akama TO, Fukuda MN, Fukuda M: Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family. J Biol Chem. 2000 Jun 30;275(26):20188-96. [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. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [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. Mikami T, Mizumoto S, Kago N, Kitagawa H, Sugahara K: Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor: implication of differential roles in dermatan sulfate biosynthesis. J Biol Chem. 2003 Sep 19;278(38):36115-27. Epub 2003 Jul 7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5554
Enzyme 6 Name Galactosylceramide sulfotransferase
Enzyme 6 Synonyms
  1. GalCer sulfotransferase
  2. 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase
  3. 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
  4. Cerebroside sulfotransferase
Enzyme 6 Gene Name GAL3ST1
Enzyme 6 Protein Sequence >Galactosylceramide sulfotransferase
MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPE
AVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTF
FARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPV
VPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHIL
EVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAW
NMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDE
AMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDF
LRW
Enzyme 6 Number of Residues 423
Enzyme 6 Molecular Weight 48763.6
Enzyme 6 Theoretical pI 8.78
Enzyme 6 GO Classification
Function
  • catalytic activity
  • galactose 3-O-sulfotransferase activity
  • galactosylceramide sulfotransferase activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
  • Golgi apparatus
  • cell part
  • integral to membrane
  • intracellular membrane-bounded organelle
  • intrinsic to membrane
  • membrane part
  • membrane-bounded organelle
  • organelle
Enzyme 6 General Function Involved in galactosylceramide sulfotransferase activity
Enzyme 6 Specific Function Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate [RN:R04017 R06279]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 15-35
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 6714628 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q99999 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name G3ST1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1272 bp
ATGCTGCCACCGCAGAAGAAGCCCTGGGAGTCCATGGCTAAGGGGCTGGTGCTGGGCGCG
CTCTTCACTAGTTTCCTGCTGCTGGTGTACTCCTATGCCGTGCCCCCGCTGCATGCCGGC
CTGGCCTCCACGACCCCGGAGGCCGCAGCGTCCTGCTCTCCACCTGCACTCGAGCCAGAG
GCAGTGATCCGGGCCAACGGCTCGGCGGGGGAGTGCCAGCCGCGGCGCAACATCGTGTTC
TTGAAGACGCACAAGACGGCCAGCAGCACCCTGCTCAACATCCTGTTCCGCTTCGGCCAG
AAGCACCGGCTCAAGTTCGCCTTCCCTAACGGCCGCAATGACTTCGACTACCCGACCTTC
TTCGCCCGCAGCCTGGTGCAGGACTATCGGCCCGGGGCCTGCTTCAACATCATCTGCAAC
CACATGCGCTTCCACTACGACGAGGTGCGCGGCCTGGTGCCGACCAACGCCATCTTCATC
ACGGTGCTCCGCGACCCCGCCCGCTTGTTCGAGTCCTCCTTCCACTACTTCGGGCCGGTG
GTGCCCCTCACGTGGAAGCTCTCGGCCGGCGACAAGCTGACCGAGTTCCTGCAAGACCCG
GATCGCTACTACGACCCCAACGGCTTCAATGCCCACTACCTCCGAAACCTGCTCTTCTTC
GACCTGGGCTATGACAACAGCCTGGACCCCAGCAGCCCGCAGGTGCAGGAGCACATCCTG
GAGGTGGAGCGTCGCTTCCACCTGGTGCTCCTTCAAGAGTACTTCGACGAGTCGCTGGTG
CTGCTGAAGGACCTGCTGTGCTGGGAGCTGGAGGACGTGCTCTACTTCAAGCTCAACGCC
CGCCGCGACTCGCCCGTGCCGCGGCTCTCGGGGGAGCTGTATGGGCGCGCCACCGCCTGG
AACATGCTGGACTCCCACCTCTACCGCCACTTCAACGCCAGCTTCTGGCGCAAGGTGGAG
GCCTTCGGGCGGGAGCGCATGGCCCGCGAGGTGGCCGCCCTGCGCCATGCCAACGAGCGC
ATGCGGACCATCTGCATCGACGGGGGCCACGCCGTGGACGCCGCCGCCATCCAGGACGAG
GCCATGCAGCCCTGGCAGCCGCTGGGCACCAAGTCCATCCTGGGCTACAACCTCAAGAAG
AGCATCGGGCAGCGGCACGCGCAGCTCTGCCGGCGCATGCTCACGCCCGAGATCCAGTAC
CTGATGGACCTCGGCGCCAACCTGTGGGTCACCAAGCTCTGGAAGTTCATTCGCGATTTC
CTGCGGTGGTGA
Enzyme 6 GenBank Gene ID AB029901 Link Image
Enzyme 6 GeneCard ID GAL3ST1 Link Image
Enzyme 6 GenAtlas ID GAL3ST1 Link Image
Enzyme 6 HGNC ID HGNC:24240 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 22q12.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Honke K, Tsuda M, Hirahara Y, Ishii A, Makita A, Wada Y: Molecular cloning and expression of cDNA encoding human 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase. J Biol Chem. 1997 Feb 21;272(8):4864-8. [PubMed Link Image]
  2. Tsuda M, Egashira M, Niikawa N, Wada Y, Honke K: Cancer-associated alternative usage of multiple promoters of human GalCer sulfotransferase gene. Eur J Biochem. 2000 May;267(9):2672-9. [PubMed Link Image]
  3. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  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. Honke K, Yamane M, Ishii A, Kobayashi T, Makita A: Purification and characterization of 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase from human renal cancer cells. J Biochem (Tokyo). 1996 Mar;119(3):421-7. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5575
Enzyme 7 Name Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
Enzyme 7 Synonyms
  1. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1
  2. 3-OST-3B
  3. Heparan sulfate 3-O-sulfotransferase 3B1
  4. h3-OST-3B
Enzyme 7 Gene Name HS3ST3B1
Enzyme 7 Protein Sequence >Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
MGQRLSGGRSCLDVPGRLLPQPPPPPPPVRRKLALLFAMLCVWLYMFLYSCAGSCAAAPG
LLLLGSGSRAAHDPPALATAPDGTPPRLPFRAPPATPLASGKEMAEGAASPEEQSPEVPD
SPSPISSFFSGSGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKG
LAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQ
TLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERL
ISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEI
DREVVRRLREFYRPFNLKFYQMTGHDFGWD
Enzyme 7 Number of Residues 390
Enzyme 7 Molecular Weight 43323.6
Enzyme 7 Theoretical pI 10.14
Enzyme 7 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 7 General Function Involved in sulfotransferase activity
Enzyme 7 Specific Function Transfers a sulfuryl group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 33-53
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4835725 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y662 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name HS3SB_HUMAN Link Image
Enzyme 7 PDB ID 1T8U Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1173 bp
ATGGGGCAGCGCCTGAGTGGCGGCAGATCTTGCCTCGATGTCCCCGGCCGGCTCCTACCG
CAGCCGCCGCCGCCCCCGCCGCCGGTGAGGAGGAAGCTCGCGCTGCTCTTCGCCATGCTC
TGCGTCTGGCTCTATATGTTCCTGTACTCGTGCGCCGGCTCCTGCGCCGCCGCGCCGGGG
CTGCTGCTCCTGGGCTCTGGGTCCCGCGCCGCACACGACCCGCCAGCCCTGGCCACAGCT
CCGGACGGGACGCCCCCCAGGCTGCCGTTCCGGGCGCCGCCAGCCACCCCACTGGCTTCA
GGCAAGGAGATGGCCGAGGGCGCTGCGAGCCCGGAGGAGCAGAGTCCCGAGGTGCCGGAC
TCCCCAAGCCCCATCTCCAGCTTTTTCAGTGGGTCTGGGAGCAAGCAGCTGCCGCAGGCC
ATCATCATCGGCGTGAAGAAGGGCGGCACGCGGGCGCTGCTGGAGTTTCTGCGCGTGCAC
CCCGACGTGCGCGCCGTGGGCGCCGAGCCCCATTTCTTCGATCGCAGCTACGACAAGGGC
CTCGCTTGGTACCGGGACCTGATGCCCAGAACCCTGGACGGGCAGATCACCATGGAGAAG
ACGCCCAGTTACTTCGTCACGCGGGAGGCCCCCGCGCGCATCTCGGCCATGTCCAAGGAC
ACCAAGCTCATCGTGGTGGTGCGGGACCCGGTGACCAGGGCCATCTCGGACTACACGCAG
ACGCTGTCCAAGCGGCCCGACATCCCCACCTTCGAGAGCTTGACGTTCAAAAACAGGACA
GCGGGCCTCATCGACACGTCGTGGAGCGCCATCCAGATCGGCATCTACGCCAAGCACCTG
GAGCACTGGCTGCGCCACTTCCCCATCCGCCAGATGCTCTTCGTGAGCGGCGAGCGGCTC
ATCAGCGACCCGGCCGGGGAGCTGGGCCGCGTGCAAGACTTCCTGGGCCTCAAGAGGATC
ATCACGGACAAGCACTTCTACTTCAACAAGACCAAGGGCTTCCCCTGCCTGAAGAAGGCG
GAGGGCAGCAGCCGGCCCCATTGCCTGGGCAAGACCAAGGGCAGGACCCATCCTGAGATC
GACCGCGAGGTGGTGCGCAGGCTGCGCGAGTTCTACCGGCCTTTCAACCTCAAGTTCTAC
CAGATGACCGGGCACGACTTTGGCTGGGATTGA
Enzyme 7 GenBank Gene ID AF105377 Link Image
Enzyme 7 GeneCard ID HS3ST3B1 Link Image
Enzyme 7 GenAtlas ID HS3ST3B1 Link Image
Enzyme 7 HGNC ID HGNC:5198 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 17p12
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD: Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. J Biol Chem. 1999 Feb 19;274(8):5170-84. [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. Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, Cohen GH, Eisenberg RJ, Rosenberg RD, Spear PG: A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell. 1999 Oct 1;99(1):13-22. [PubMed Link Image]
  5. Liu J, Shworak NW, Sinay P, Schwartz JJ, Zhang L, Fritze LM, Rosenberg RD: Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J Biol Chem. 1999 Feb 19;274(8):5185-92. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5578
Enzyme 8 Name 3'(2'),5'-bisphosphate nucleotidase 1
Enzyme 8 Synonyms
  1. Bisphosphate 3'-nucleotidase 1
  2. PAP-inositol-1,4-phosphatase
  3. PIP
Enzyme 8 Gene Name BPNT1
Enzyme 8 Protein Sequence >3'(2'),5'-bisphosphate nucleotidase 1
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
Enzyme 8 Number of Residues 308
Enzyme 8 Molecular Weight 33392.0
Enzyme 8 Theoretical pI 5.41
Enzyme 8 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 8 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 8 Specific Function Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4- trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6
Enzyme 8 Pathways
Enzyme 8 Reactions
  • adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate [RN:R00188]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID O95861 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name BPNT1_HUMAN Link Image
Enzyme 8 PDB ID 1JP4 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >927 bp
ATGGCTTCCAGTAACACTGTGTTGATGCGGTTGGTAGCCTCCGCATATTCTATTGCTCAA
AAGGCAGGAATGATAGTCAGACGTGTTATTGCTGAAGGAGACCTGGGTATTGTGGAGAAG
ACCTGTGCAACAGACCTGCAGACCAAAGCTGACCGATTGGCACAGATGAGCATATGTTCT
TCATTGGCCCGGAAATTCCCCAAACTCACAATTATAGGGGAAGAGGATCTGCCTTCTGAG
GAAGTGGATCAAGAGCTGATTGAAGACAGTCAGTGGGAAGAAATACTGAAGCAACCATGC
CCATCGCAGTACAGTGCTATTAAAGAAGAAGATCTCGTGGTCTGGGTTGATCCTCTGGAT
GGAACCAAGGAATATACCGAAGGTCTTCTTGACAATGTAACAGTTCTTATTGGAATTGCT
TATGAAGGAAAAGCCATAGCAGGAGTTATTAACCAGCCATATTACAACTATGAGGCAGGA
CCAGATGCTGTGTTGGGGAGGACAATCTGGGGAGTTTTAGGTTTAGGCGCCTTTGGGTTT
CAGCTGAAAGAAGTCCCTGCTGGGAAACACATTATCACAACTACTCGATCCCATAGCAAC
AAGTTGGTTACTGACTGTGTTGCTGCTATGAACCCCGATGCTGTGCTGCGAGTAGGAGGA
GCAGGAAATAAGATTATTCAGCTGATTGAAGGCAAAGCCTCTGCTTATGTATTTGCAAGT
CCTGGTTGTAAGAAGTGGGATACTTGTGCTCCAGAAGTTATTTTACATGCTGTGGGAGGC
AAGTTAACCGATATCCATGGGAATGTTCTTCAGTACCACAAGGATGTGAAGCATATGAAC
TCTGCAGGAGTCCTGGCCACACTGAGGAATTATGACTACTATGCAAGCCGAGTTCCAGAA
TCTATTAAAAATGCACTTGTTCCTTAA
Enzyme 8 GenBank Gene ID AF125042 Link Image
Enzyme 8 GeneCard ID BPNT1 Link Image
Enzyme 8 GenAtlas ID BPNT1 Link Image
Enzyme 8 HGNC ID HGNC:1096 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q41
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Spiegelberg BD, Xiong JP, Smith JJ, Gu RF, York JD: Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate. J Biol Chem. 1999 May 7;274(19):13619-28. [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. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5579
Enzyme 9 Name Heparan sulfate glucosamine 3-O-sulfotransferase 1
Enzyme 9 Synonyms
  1. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1
  2. 3-OST-1
  3. Heparan sulfate 3-O-sulfotransferase 1
  4. h3-OST-1
Enzyme 9 Gene Name HS3ST1
Enzyme 9 Protein Sequence >Heparan sulfate glucosamine 3-O-sulfotransferase 1
MAALLLGAVLLVAQPQLVPSRPAELGQQELLRKAGTLQDDVRDGVAPNGSAQQLPQTIII
GVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSHGLGWYLSQMPFSWPHQLTVEKT
PAYFTSPKVPERVYSMNPSIRLLLILRDPSERVLSDYTQVFYNHMQKHKPYPSIEEFLVR
DGRLNVDYKALNRSLYHVHMQNWLRFFPLRHIHIVDGDRLIRDPFPEIQKVERFLKLSPQ
INASNFYFNKTKGFYCLRDSGRDRCLHESKGRAHPQVDPKLLNKLHEYFHEPNKKFFELV
GRTFDWH
Enzyme 9 Number of Residues 307
Enzyme 9 Molecular Weight 35772.8
Enzyme 9 Theoretical pI 9.16
Enzyme 9 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 9 General Function Involved in sulfotransferase activity
Enzyme 9 Specific Function Rate limiting enzyme for synthesis of HSact. Performs the crucial step modification in the biosynthesis of anticoagulant heparan sulfate (HSact) that is to complete the structure of the antithrombin pentasaccharide binding site
Enzyme 9 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 9 Reactions
  • 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-20
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 2618973 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O14792 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name HS3S1_HUMAN Link Image
Enzyme 9 PDB ID 1VKJ Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >924 bp
ATGGCCGCGCTGCTCCTGGGCGCGGTGCTGCTGGTGGCCCAGCCCCAGCTAGTGCCTTCC
CGCCCCGCCGAGCTAGGCCAGCAGGAGCTTCTGCGGAAAGCGGGGACCCTCCAGGATGAC
GTCCGCGATGGCGTGGCCCCAAACGGCTCTGCCCAGCAGTTGCCGCAGACCATCATCATC
GGCGTGCGCAAGGGCGGCACGCGCGCACTGCTGGAGATGCTCAGCCTGCACCCCGACGTG
GCGGCCGCGGAGAACGAGGTCCACTTCTTCGACTGGGAGGAGCATTACAGCCACGGCTTG
GGCTGGTACCTCAGCCAGATGCCCTTCTCCTGGCCACACCAGCTCACAGTGGAGAAGACC
CCCGCGTATTTCACGTCGCCCAAAGTGCCTGAGCGAGTCTACAGCATGAACCCGTCCATC
CGGCTGCTGCTCATCCTGCGAGACCCGTCGGAGCGCGTGCTATCTGACTACACCCAAGTG
TTCTACAACCACATGCAGAAGCACAAGCCCTACCCGTCCATCGAGGAGTTCCTGGTGCGC
GATGGCAGGCTCAATGTGGACTACAAGGCCCTCAACCGCAGCCTCTACCACGTGCACATG
CAGAACTGGCTGCGCTTTTTCCCGCTGCGCCACATCCACATTGTGGACGGCGACCGCCTC
ATCAGGGACCCCTTCCCTGAGATCCAAAAGGTCGAGAGGTTCCTAAAGCTGTCGCCGCAG
ATCAATGCTTCGAACTTCTACTTTAACAAAACCAAGGGCTTTTACTGCCTGCGGGACAGC
GGCCGGGACCGCTGCTTACATGAGTCCAAAGGCCGGGCGCACCCCCAAGTCGATCCCAAA
CTACTCAATAAACTGCACGAATATTTTCATGAGCCAAATAAGAAGTTCTTCGAGCTTGTT
GGCAGAACATTTGACTGGCACTGA
Enzyme 9 GenBank Gene ID AF019386 Link Image
Enzyme 9 GeneCard ID HS3ST1 Link Image
Enzyme 9 GenAtlas ID HS3ST1 Link Image
Enzyme 9 HGNC ID HGNC:5194 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4p16
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Shworak NW, Liu J, Fritze LM, Schwartz JJ, Zhang L, Logeart D, Rosenberg RD: Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J Biol Chem. 1997 Oct 31;272(44):28008-19. [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. Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD: Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J Biol Chem. 1996 Oct 25;271(43):27072-82. [PubMed Link Image]
  5. Liu J, Shworak NW, Sinay P, Schwartz JJ, Zhang L, Fritze LM, Rosenberg RD: Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J Biol Chem. 1999 Feb 19;274(8):5185-92. [PubMed Link Image]
  6. Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD: Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. J Biol Chem. 1999 Feb 19;274(8):5170-84. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5581
Enzyme 10 Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
Enzyme 10 Synonyms
  1. PAPS synthase 1
  2. PAPSS 1
  3. Sulfurylase kinase 1
  4. SK 1
  5. SK1
  6. Sulfate adenylyltransferase
  7. ATP-sulfurylase
  8. Sulfate adenylate transferase
  9. SAT
  10. Adenylyl-sulfate kinase
  11. 3'-phosphoadenosine-5'-phosphosulfate synthase
  12. APS kinase
  13. Adenosine-5'-phosphosulfate 3'-phosphotransferase
  14. Adenylylsulfate 3'-phosphotransferase
Enzyme 10 Gene Name PAPSS1
Enzyme 10 Protein Sequence >Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA
Enzyme 10 Number of Residues 624
Enzyme 10 Molecular Weight 70832.7
Enzyme 10 Theoretical pI 6.85
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • adenylyltransferase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • nucleotidyltransferase activity
  • purine nucleoside binding
  • sulfate adenylyltransferase (ATP) activity
  • sulfate adenylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • sulfate assimilation
  • sulfur metabolic process
Component
Enzyme 10 General Function Involved in ATP binding
Enzyme 10 Specific Function Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 2673862 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O43252 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PAPS1_HUMAN Link Image
Enzyme 10 PDB ID 1X6V Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1875 bp
ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG
Enzyme 10 GenBank Gene ID Y10387 Link Image
Enzyme 10 GeneCard ID PAPSS1 Link Image
Enzyme 10 GenAtlas ID PAPSS1 Link Image
Enzyme 10 HGNC ID HGNC:8603 Link Image
Enzyme 10 Chromosome Location 4
Enzyme 10 Locus 4q24
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed Link Image]
  2. Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed Link Image]
  3. Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed Link Image]
  4. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [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. Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5582
Enzyme 11 Name Estrogen sulfotransferase
Enzyme 11 Synonyms
  1. EST-1
  2. Sulfotransferase 1E1
  3. ST1E1
  4. Sulfotransferase, estrogen-preferring
Enzyme 11 Gene Name SULT1E1
Enzyme 11 Protein Sequence >Estrogen sulfotransferase
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMI
YKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEK
DCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWE
KGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYT
TLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
Enzyme 11 Number of Residues 294
Enzyme 11 Molecular Weight 35126.2
Enzyme 11 Theoretical pI 6.61
Enzyme 11 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 11 General Function Involved in sulfotransferase activity
Enzyme 11 Specific Function May control the level of the estrogen receptor by sulfurylating free estradiol. Maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. Also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate [RN:R02350]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID P49888 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ST1E1_HUMAN Link Image
Enzyme 11 PDB ID 1G3M Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >885 bp
ATGAATTCTGAACTTGACTATTATGAAAAGTTTGAAGAAGTCCATGGGATTCTAATGTAT
AAAGATTTTGTCAAATATTGGGATAATGTGGAAGCGTTCCAGGCAAGACCAGATGATCTT
GTCATTGCCACCTACCCTAAATCTGGTACAACCTGGGTTAGTGAAATTGTGTATATGATC
TATAAAGAGGGTGATGTGGAAAAGTGCAAAGAAGATGTAATTTTTAATCGAATACCTTTC
CTGGAATGCAGAAAAGAAAACCTCATGAATGGAGTAAAACAATTAGATGAGATGAATTCT
CCTAGAATTGTGAAGACTCATTTGCCACCTGAACTTCTTCCTGCCTCATTTTGGGAAAAG
GATTGTAAGATAATCTATCTTTGCCGGAATGCAAAGGATGTGGCTGTTTCCTTTTATTAT
TTCTTTCTAATGGTGGCTGGTCATCCAAATCCTGGATCCTTTCCAGAGTTTGTGGAGAAA
TTCATGCAAGGACAGGTTCCTTATGGTTCCTGGTATAAACATGTAAAATCTTGGTGGGAA
AAGGGAAAGAGTCCACGTGTACTATTTCTTTTCTACGAAGACCTGAAAGAGGATATCAGA
AAAGAGGTGATAAAATTGATACATTTCCTGGAAAGGAAGCCATCAGAGGAGCTTGTGGAC
AGGATTATACATCATACTTCGTTCCAAGAGATGAAGAACAATCCATCCACAAATTACACA
ACACTGCCAGACGAAATTATGAACCAGAAATTGTCGCCCTTCATGAGAAAGGGAATTACA
GGAGACTGGAAAAATCACTTTACAGTAGCCCTGAATGAAAAATTTGATAAACATTATGAG
CAGCAAATGAAGGAATCTACACTGAAGTTTCGAACTGAGATCTAA
Enzyme 11 GenBank Gene ID U08098 Link Image
Enzyme 11 GeneCard ID SULT1E1 Link Image
Enzyme 11 GenAtlas ID SULT1E1 Link Image
Enzyme 11 HGNC ID HGNC:11377 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4q13.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Aksoy IA, Wood TC, Weinshilboum R: Human liver estrogen sulfotransferase: identification by cDNA cloning and expression. Biochem Biophys Res Commun. 1994 May 16;200(3):1621-9. [PubMed Link Image]
  2. Her C, Aksoy IA, Kimura S, Brandriff BF, Wasmuth JJ, Weinshilboum RM: Human estrogen sulfotransferase gene (STE): cloning, structure, and chromosomal localization. Genomics. 1995 Sep 1;29(1):16-23. [PubMed Link Image]
  3. Falany CN, Krasnykh V, Falany JL: Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J Steroid Biochem Mol Biol. 1995 Jun;52(6):529-39. [PubMed Link Image]
  4. Rubin GL, Harrold AJ, Mills JA, Falany CN, Coughtrie MW: Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy. Mol Hum Reprod. 1999 Nov;5(11):995-1002. [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. Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M: Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. [PubMed Link Image]
  7. Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M: Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect. 2003 Jun;111(7):884-8. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5587
Enzyme 12 Name Heparan sulfate glucosamine 3-O-sulfotransferase 5
Enzyme 12 Synonyms
  1. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5
  2. 3-OST-5
  3. Heparan sulfate 3-O-sulfotransferase 5
  4. h3-OST-5
Enzyme 12 Gene Name HS3ST5
Enzyme 12 Protein Sequence >Heparan sulfate glucosamine 3-O-sulfotransferase 5
MLFKQQAWLRQKLLVLGSLAVGSLLYLVARVGSLDRLQPICPIEGRLGGARTQAEFPLRA
LQFKRGLLHEFRKGNASKEQVRLHDLVQQLPKAIIIGVRKGGTRALLEMLNLHPAVVKAS
QEIHFFDNDENYGKGIEWYRKKMPFSYPQQITIEKSPAYFITEEVPERIYKMNSSIKLLI
IVREPTTRAISDYTQVLEGKERKNKTYYKFEKLAIDPNTCEVNTKYKAVRTSIYTKHLER
WLKYFPIEQFHVVDGDRLITEPLPELQLVEKFLNLPPRISQYNLYFNATRGFYCLRFNII
FNKCLAGSKGRIHPEVDPSVITKLRKFFHPFNQKFYQITGRTLNWP
Enzyme 12 Number of Residues 346
Enzyme 12 Molecular Weight 40407.9
Enzyme 12 Theoretical pI 10.31
Enzyme 12 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 12 General Function Involved in sulfotransferase activity
Enzyme 12 Specific Function Rate limiting enzyme for synthesis of HSact. Performs the crucial step modification in the biosynthesis of anticoagulant heparan sulfate (HSact) that is to complete the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA- GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O- sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry
Enzyme 12 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 12 Reactions
  • 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 13-32
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 23506319 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q8IZT8 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name HS3S5_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1041 bp
ATGCTATTCAAACAGCAGGCGTGGCTGAGACAGAAGCTCCTGGTGCTGGGAAGCCTTGCC
GTTGGGAGTCTCCTGTATCTAGTCGCCAGAGTTGGGAGCTTGGATAGGCTACAACCCATT
TGCCCCATTGAAGGTCGACTGGGTGGAGCCCGCACTCAGGCTGAATTCCCACTTCGCGCC
CTGCAGTTTAAGCGTGGCCTGCTGCACGAGTTCCGGAAGGGCAACGCTTCCAAGGAGCAG
GTTCGCCTCCATGACCTGGTCCAGCAGCTCCCCAAGGCCATTATCATTGGGGTGAGGAAA
GGAGGCACAAGGGCCCTGCTTGAAATGCTGAACCTACATCCGGCAGTAGTCAAAGCCTCT
CAAGAAATCCACTTTTTTGATAATGATGAGAATTATGGTAAGGGCATTGAGTGGTATAGG
AAAAAGATGCCTTTTTCCTACCCTCAGCAAATCACAATTGAAAAGAGCCCAGCATATTTT
ATCACAGAGGAGGTTCCAGAAAGGATTTACAAAATGAACTCATCCATCAAGTTGTTGATC
ATTGTCAGGGAGCCAACCACAAGAGCTATTTCTGATTATACTCAGGTGCTAGAGGGGAAG
GAGAGGAAGAACAAAACTTATTACAAGTTTGAGAAGCTGGCCATAGACCCTAATACATGC
GAAGTGAACACAAAATACAAAGCAGTAAGAACCAGCATCTACACCAAACATCTGGAAAGG
TGGTTGAAATACTTTCCAATTGAGCAATTTCATGTCGTCGATGGAGATCGCCTCATCACG
GAACCTCTGCCAGAACTTCAGCTCGTGGAGAAGTTCCTAAATCTGCCTCCAAGGATAAGT
CAATACAATTTATACTTCAATGCTACCAGAGGGTTTTACTGCTTGCGGTTTAATATTATC
TTTAATAAGTGCCTGGCGGGCAGCAAGGGGCGCATTCATCCAGAGGTGGACCCCTCTGTC
ATTACTAAATTGCGCAAATTCTTTCATCCTTTTAATCAAAAATTTTACCAGATCACTGGG
AGGACATTGAACTGGCCCTAA
Enzyme 12 GenBank Gene ID AF503292 Link Image
Enzyme 12 GeneCard ID HS3ST5 Link Image
Enzyme 12 GenAtlas ID HS3ST5 Link Image
Enzyme 12 HGNC ID HGNC:19419 Link Image
Enzyme 12 Chromosome Location 6
Enzyme 12 Locus 6q21
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Xia G, Chen J, Tiwari V, Ju W, Li JP, Malmstrom A, Shukla D, Liu J: Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1. J Biol Chem. 2002 Oct 4;277(40):37912-9. Epub 2002 Jul 23. [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. Mochizuki H, Yoshida K, Gotoh M, Sugioka S, Kikuchi N, Kwon YD, Tawada A, Maeyama K, Inaba N, Hiruma T, Kimata K, Narimatsu H: Characterization of a heparan sulfate 3-O-sulfotransferase-5, an enzyme synthesizing a tetrasulfated disaccharide. J Biol Chem. 2003 Jul 18;278(29):26780-7. Epub 2003 May 9. [PubMed Link Image]
  5. Duncan MB, Chen J, Krise JP, Liu J: The biosynthesis of anticoagulant heparan sulfate by the heparan sulfate 3-O-sulfotransferase isoform 5. Biochim Biophys Acta. 2004 Mar 17;1671(1-3):34-43. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5588
Enzyme 13 Name Heparan sulfate glucosamine 3-O-sulfotransferase 2
Enzyme 13 Synonyms
  1. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2
  2. 3-OST-2
  3. Heparan sulfate 3-O-sulfotransferase 2
  4. h3-OST-2
Enzyme 13 Gene Name HS3ST2
Enzyme 13 Protein Sequence >Heparan sulfate glucosamine 3-O-sulfotransferase 2
MAYRVLGRAGPPQPRRARRLLFAFTLSLSCTYLCYSFLCCCDDLGRSRLLGAPRCLRGPS
AGGQKLLQKSRPCDPSGPTPSEPSAPSAPAAAVPAPRLSGSNHSGSPKLGTKRLPQALIV
GVKKGGTRAVLEFIRVHPDVRALGTEPHFFDRNYGRGLDWYRSLMPRTLESQITLEKTPS
YFVTQEAPRRIFNMSRDTKLIVVVRNPVTRAISDYTQTLSKKPDIPTFEGLSFRNRTLGL
VDVSWNAIRIGMYVLHLESWLQYFPLAQIHFVSGERLITDPAGEMGRVQDFLGIKRFITD
KHFYFNKTKGFPCLKKTESSLLPRCLGKSKGRTHVQIDPEVIDQLREFYRPYNIKFYETV
GQDFRWE
Enzyme 13 Number of Residues 367
Enzyme 13 Molecular Weight 41500.6
Enzyme 13 Theoretical pI 10.39
Enzyme 13 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 13 General Function Involved in sulfotransferase activity
Enzyme 13 Specific Function Transfers a sulfuryl group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 20-39
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 4835719 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9Y278 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name HS3S2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1104 bp
ATGGCCTATAGGGTCCTGGGCCGCGCGGGGCCACCTCAGCCGCGGAGGGCGCGCAGGCTG
CTCTTCGCCTTCACGCTCTCGCTCTCCTGCACTTACCTGTGTTACAGCTTCCTGTGCTGC
TGCGACGACCTGGGTCGGAGCCGCCTCCTCGGCGCGCCTCGCTGCCTCCGCGGCCCCAGC
GCGGGCGGCCAGAAACTTCTCCAGAAGTCCCGCCCCTGTGATCCCTCCGGGCCGACGCCC
AGCGAGCCCAGCGCTCCCAGCGCGCCCGCCGCCGCCGTGCCCGCCCCTCGCCTCTCCGGT
TCCAACCACTCCGGCTCACCCAAGCTGGGTACCAAGCGGTTGCCCCAAGCCCTCATTGTG
GGCGTGAAGAAGGGGGGCACCCGGGCCGTGCTGGAGTTTATCCGAGTACACCCGGACGTG
CGGGCCTTGGGCACGGAACCCCACTTCTTTGACAGGAACTACGGCCGCGGGCTGGATTGG
TACAGGAGCCTGATGCCCAGGACCCTCGAGAGCCAGATCACGCTGGAGAAGACGCCCAGC
TACTTTGTCACTCAAGAGGCTCCTCGACGCATCTTCAACATGTCCCGAGACACCAAGCTG
ATCGTGGTTGTGCGGAACCCTGTGACCCGTGCCATCTCTGATTACACGCAGACACTCTCC
AAGAAGCCCGACATCCCGACCTTTGAGGGCCTCTCCTTCCGCAACCGCACCCTGGGCCTG
GTGGACGTGTCGTGGAACGCCATCCGCATCGGCATGTACGTGCTGCACCTGGAGAGCTGG
CTGCAGTACTTCCCGCTAGCTCAGATTCACTTCGTCAGTGGCGAGCGACTCATCACTGAC
CCGGCCGGCGAGATGGGGCGAGTCCAGGACTTCCTGGGCATTAAGAGATTCATCACGGAC
AAGCACTTCTATTTCAACAAGACCAAAGGATTCCCTTGCTTGAAAAAAACAGAATCGAGC
CTCCTGCCTCGATGCTTGGGCAAATCAAAAGGGAGAACTCATGTACAGATTGATCCTGAA
GTGATAGACCAGCTCCGAGAATTTTATAGACCGTATAATATCAAATTTTATGAAACCGTT
GGGCAGGACTTCAGGTGGGAATAA
Enzyme 13 GenBank Gene ID AF105374 Link Image
Enzyme 13 GeneCard ID HS3ST2 Link Image
Enzyme 13 GenAtlas ID HS3ST2 Link Image
Enzyme 13 HGNC ID HGNC:5195 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 16p12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD: Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. J Biol Chem. 1999 Feb 19;274(8):5170-84. [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. Liu J, Shworak NW, Sinay P, Schwartz JJ, Zhang L, Fritze LM, Rosenberg RD: Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J Biol Chem. 1999 Feb 19;274(8):5185-92. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5589
Enzyme 14 Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
Enzyme 14 Synonyms
  1. PAPS synthase 2
  2. PAPSS 2
  3. Sulfurylase kinase 2
  4. SK 2
  5. SK2
  6. Sulfate adenylyltransferase
  7. ATP-sulfurylase
  8. Sulfate adenylate transferase
  9. SAT
  10. Adenylyl-sulfate kinase
  11. 3'-phosphoadenosine-5'-phosphosulfate synthase
  12. APS kinase
  13. Adenosine-5'-phosphosulfate 3'-phosphotransferase
  14. Adenylylsulfate 3'-phosphotransferase
Enzyme 14 Gene Name PAPSS2
Enzyme 14 Protein Sequence >Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN
Enzyme 14 Number of Residues 614
Enzyme 14 Molecular Weight 69500.2
Enzyme 14 Theoretical pI 8.13
Enzyme 14 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • adenylyltransferase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • nucleotidyltransferase activity
  • purine nucleoside binding
  • sulfate adenylyltransferase (ATP) activity
  • sulfate adenylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • sulfate assimilation
  • sulfur metabolic process
Component
Enzyme 14 General Function Involved in ATP binding
Enzyme 14 Specific Function Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important role in skeletogenesis during postnatal growth
Enzyme 14 Pathways
Enzyme 14 Reactions
  • ATP + sulfate = diphosphate + adenylyl sulfate [RN:R00529]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 5052075 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O95340 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PAPS2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1845 bp
ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAAGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACTCGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCTAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA
Enzyme 14 GenBank Gene ID AF074331 Link Image
Enzyme 14 GeneCard ID PAPSS2 Link Image
Enzyme 14 GenAtlas ID PAPSS2 Link Image
Enzyme 14 HGNC ID HGNC:8604 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 10q24
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed Link Image]
  2. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed Link Image]
  3. Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [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. Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed Link Image]
  6. Noordam C, Dhir V, McNelis JC, Schlereth F, Hanley NA, Krone N, Smeitink JA, Smeets R, Sweep FC, Claahsen-van der Grinten HL, Arlt W: Inactivating PAPSS2 mutations in a patient with premature pubarche. N Engl J Med. 2009 May 28;360(22):2310-8. [PubMed Link Image]
  7. Xu ZH, Freimuth RR, Eckloff B, Wieben E, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (PAPSS2) pharmacogenetics: gene resequencing, genetic polymorphisms and functional characterization of variant allozymes. Pharmacogenetics. 2002 Jan;12(1):11-21. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5590
Enzyme 15 Name Protein-tyrosine sulfotransferase 2
Enzyme 15 Synonyms
  1. Tyrosylprotein sulfotransferase 2
  2. TPST-2
Enzyme 15 Gene Name TPST2
Enzyme 15 Protein Sequence >Protein-tyrosine sulfotransferase 2
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHV
EYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREK
LRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLL
MVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQ
LVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSK
WTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLK
GYFQVNQNSTSSHLGSS
Enzyme 15 Number of Residues 377
Enzyme 15 Molecular Weight 41911.5
Enzyme 15 Theoretical pI 9.42
Enzyme 15 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 15 General Function Involved in sulfotransferase activity
Enzyme 15 Specific Function Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • 9-25
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 3617846 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O60704 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name TPST2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1134 bp
ATGCGCCTGTCGGTGCGGAGGGTGCTGCTGGCAGCCGGCTGCGCCCTGGTCCTGGTGCTG
GCGGTTCAGCTGGGACAGCAGGTGCTAGAGTGCCGGGCGGTGCTGGCGGGCCTGCGGAGC
CCCCGGGGGGCCATGCGGCCTGAGCAGGAGGAGCTGGTGATGGTGGGCACCAACCACGTG
GAATACCGCTATGGCAAGGCCATGCCGCTCATCTTCGTGGGTGGCGTGCCTCGCAGTGGC
ACCACGTTGATGCGCGCCATGCTGGACGCCCACCCCGAGGTGCGCTGCGGCGAGGAGACC
CGCATCATCCCGCGCGTGCTGGCCATGCGCCAGGCCTGGTCCAAGTCTGGCCGTGAGAAG
CTGCGGCTGGATGAGGCGGGGGTGACGGATGAGGTGCTGGACGCCGCCATGCAGGCCTTC
ATCCTGGAGGTGATTGCCAAGCACGGAGAGCCGGCCCGCGTGCTCTGCAACAAGGACCCA
TTTACGCTCAAGTCCTCGGTCTACCTGTCGCGCCTGTTCCCCAACTCCAAGTTCCTGCTG
ATGGTGCGGGACGGCCGGGCCTCCGTGCACTCCATGATCACGCGCAAAGTCACCATTGCG
GGCTTTGACCTCAGCAGCTACCGTGACTGCCTCACCAAGTGGAACAAGGCCATCGAGGTG
ATGTACGCCCAGTGCATGGAGGTAGGCAAGGAGAAGTGCTTGCCTGTGTACTACGAGCAG
CTGGTGCTGCACCCCAGGCGCTCACTCAAGCTCATCCTCGACTTCCTCGGCATCGCCTGG
AGCGACGCTGTCCTCCACCATGAAGACCTCATTGGCAAGCCCGGTGGTGTCTCCCTGTCC
AAGATCGAGCGGTCCACGGACCAGGTCATCAAGCCTGTTAACCTGGAAGCGCTCTCCAAG
TGGACTGGCCACATCCCTGGGGATGTGGTGCGGGACATGGCCCAGATCGCCCCCATGCTG
GCTCAGCTCGGCTATGACCCTTATGCAAACCCCCCCAACTATGGCAACCCTGACCCCTTC
GTCATCAACAACACACAGCGGGTCTTGAAAGGGGACTATAAAACACCAGCCAATCTGAAA
GGATATTTTCAGGTGAACCAGAACAGCACCTCCTCCCACTTAGGAAGCTCGTGA
Enzyme 15 GenBank Gene ID AF049891 Link Image
Enzyme 15 GeneCard ID TPST2 Link Image
Enzyme 15 GenAtlas ID TPST2 Link Image
Enzyme 15 HGNC ID HGNC:12021 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 22q12.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Beisswanger R, Corbeil D, Vannier C, Thiele C, Dohrmann U, Kellner R, Ashman K, Niehrs C, Huttner WB: Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11134-9. [PubMed Link Image]
  2. Ouyang YB, Moore KL: Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans. J Biol Chem. 1998 Sep 18;273(38):24770-4. [PubMed Link Image]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  4. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  5. 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]
  6. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5591
Enzyme 16 Name Sulfotransferase family cytosolic 2B member 1
Enzyme 16 Synonyms
  1. ST2B1
  2. Sulfotransferase 2B1
  3. Alcohol sulfotransferase
  4. Hydroxysteroid sulfotransferase 2
Enzyme 16 Gene Name SULT2B1
Enzyme 16 Protein Sequence >Sulfotransferase family cytosolic 2B member 1
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS
Enzyme 16 Number of Residues 365
Enzyme 16 Molecular Weight 41307.3
Enzyme 16 Theoretical pI 5.05
Enzyme 16 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 16 General Function Involved in sulfotransferase activity
Enzyme 16 Specific Function Catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol
Enzyme 16 Pathways
Enzyme 16 Reactions
  • 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate [RN:R00629]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 31563386 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O00204 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name ST2B1_HUMAN Link Image
Enzyme 16 PDB ID 1Q1Q Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1098 bp
ATGGACGGGCCCGCCGAGCCCCAGATCCCGGGCTTGTGGGACACCTATGAAGATGACATC
TCGGAAATCAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAGGGCGTCCCCTTCCCC
GTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACCCAAGATGTGCGGGAC
GACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGGATGATCGAGATCATC
TGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTGCCCATCTGGGAGCGG
GCACCCTGGTGTGAGACCATTGTGGGTGCCTTCAGCCTCCCGGACCAGTACAGCCCCCGC
CTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTCTTCAGCTCCAAGGCC
AAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCCCTCTATCATTACTCC
AAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTCCTGAGGGACTTCCTC
AAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGCTGGCTTCGGATGAAG
GGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAGGACTTACAGGGCTCC
GTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAGGCACTGGGCTCCGTC
GTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCCAACTACACGCTGCTG
CCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAAGGGGTCTGCGGCGAC
TGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGTGCCTACCGCAAGCAG
ATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAGGACGGCAGCCCAGAT
CCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCCAACACCAGCCTGGAG
CGTGAGCCCAGACCCAACTCCAGCCCCAGCCCCAGCCCCGGCCAGGCCTCTGAGACCCCG
CACCCACGACCCTCATAA
Enzyme 16 GenBank Gene ID NM_177973.1 Link Image
Enzyme 16 GeneCard ID SULT2B1 Link Image
Enzyme 16 GenAtlas ID SULT2B1 Link Image
Enzyme 16 HGNC ID HGNC:11459 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 19q13.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Her C, Wood TC, Eichler EE, Mohrenweiser HW, Ramagli LS, Siciliano MJ, Weinshilboum RM: Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998 Nov 1;53(3):284-95. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Fuda H, Lee YC, Shimizu C, Javitt NB, Strott CA: Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem. 2002 Sep 27;277(39):36161-6. Epub 2002 Jul 26. [PubMed Link Image]
  5. Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC: Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5592
Enzyme 17 Name Sulfotransferase 1A3/1A4
Enzyme 17 Synonyms
  1. ST1A3/ST1A4
  2. Aryl sulfotransferase 1A3/1A4
  3. Catecholamine-sulfating phenol sulfotransferase
  4. HAST3
  5. M-PST
  6. Monoamine-sulfating phenol sulfotransferase
  7. Placental estrogen sulfotransferase
  8. Sulfotransferase, monoamine-preferring
  9. Thermolabile phenol sulfotransferase
  10. TL-PST
Enzyme 17 Gene Name SULT1A3
Enzyme 17 Protein Sequence >Sulfotransferase 1A3/1A4
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDM
IYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLD
QKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNY
TTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
Enzyme 17 Number of Residues 295
Enzyme 17 Molecular Weight 34196.0
Enzyme 17 Theoretical pI 5.88
Enzyme 17 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 17 General Function Involved in sulfotransferase activity
Enzyme 17 Specific Function Catalyzes the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs
Enzyme 17 Pathways
Enzyme 17 Reactions
  • 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate [RN:R01242]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID P50224 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name ST1A3_HUMAN Link Image
Enzyme 17 PDB ID 1CJM Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >888 bp
ATGGAGCTGATCCAGGACACCTCCCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAAGCCCGACCTGATGAC
CTGCTCATCAACACCTACCCCAAGTCTGGCACCACCTGGGTGAGCCAGATACTGGACATG
ATCTACCAGGGCGGCGACCTAGAGAAGTGTAACCGGGCTCCCATCTACGTACGGGTGCCC
TTCCTTGAGGTCAATGATCCAGGGGAACCCTCAGGGCTGGAGACTCTGAAAGACACACCG
CCCCCACGGCTCATCAAGTCACACCTGCCCCTGGCTCTGCTCCCTCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGAAACCCAAAGGACGTGGCGGTCTCCTACTAC
CATTTCCACCGTATGGAAAAGGCGCACCCTGAGCCTGGGACCTGGGACAGCTTCCTGGAA
AAGTTCATGGCTGGAGAAGTGTCCTACGGGTCCTGGTACCAGCACGTGCAGGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACCATG
GACTTCATGGTTCAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCCCCAGGAGCTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Enzyme 17 GenBank Gene ID L19956 Link Image
Enzyme 17 GeneCard ID SULT1A3 Link Image
Enzyme 17 GenAtlas ID SULT1A3 Link Image
Enzyme 17 HGNC ID HGNC:11455 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 16p11.2
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Zhu X, Veronese ME, Bernard CC, Sansom LN, McManus ME: Identification of two human brain aryl sulfotransferase cDNAs. Biochem Biophys Res Commun. 1993 Aug 31;195(1):120-7. [PubMed Link Image]
  2. Bernier F, Lopez Solache I, Labrie F, Luu-The V: Cloning and expression of cDNA encoding human placental estrogen sulfotransferase. Mol Cell Endocrinol. 1994 Feb;99(1):R11-5. [PubMed Link Image]
  3. Dooley TP, Probst P, Munroe PB, Mole SE, Liu Z, Doggett NA: Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM). Biochem Biophys Res Commun. 1994 Dec 15;205(2):1325-32. [PubMed Link Image]
  4. Wood TC, Aksoy IA, Aksoy S, Weinshilboum RM: Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1119-27. [PubMed Link Image]
  5. Aksoy IA, Weinshilboum RM: Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization. Biochem Biophys Res Commun. 1995 Mar 17;208(2):786-95. [PubMed Link Image]
  6. Jones AL, Hagen M, Coughtrie MW, Roberts RC, Glatt H: Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form. Biochem Biophys Res Commun. 1995 Mar 17;208(2):855-62. [PubMed Link Image]
  7. Bernier F, Leblanc G, Labrie F, Luu-The V: Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene. J Biol Chem. 1994 Nov 11;269(45):28200-5. [PubMed Link Image]
  8. 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]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. Aksoy IA, Callen DF, Apostolou S, Her C, Weinshilboum RM: Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2. Genomics. 1994 Sep 1;23(1):275-7. [PubMed Link Image]
  11. Veronese ME, Burgess W, Zhu X, McManus ME: Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies. Biochem J. 1994 Sep 1;302 ( Pt 2):497-502. [PubMed Link Image]
  12. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL: Crystal structure of human catecholamine sulfotransferase. J Mol Biol. 1999 Oct 29;293(3):521-30. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5989
Enzyme 18 Name Carbohydrate sulfotransferase 7
Enzyme 18 Synonyms
  1. Chondroitin 6-sulfotransferase 2
  2. C6ST-2
  3. Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5
  4. GST-5
  5. N-acetylglucosamine 6-O-sulfotransferase 4
  6. GlcNAc6ST-4
  7. Gn6st-4
Enzyme 18 Gene Name CHST7
Enzyme 18 Protein Sequence >Carbohydrate sulfotransferase 7
MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKGAEHCPGLQRSLGVWSLEAA
AAGEREQGAEARAAEEGGANQSPRFPSNLSGAVGEAVSREKQHIYVHATWRTGSSFLGEL
FNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAAR
APDTANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDTACERSCPPVAIRALEAE
CRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQ
VLRTRQRGDRFHRVLLAHGVGARPGGQSRALPAAPRADFFLTGALEVICEAWLRDLLFAR
GAPAWLRRRYLRLRYEDLVRQPRAQLRRLLRFSGLRALAALDAFALNMTRGAAYGADRPF
HLSARDAREAVHAWRERLSREQVRQVEAACAPAMRLLAYPRSGEEGDAEQPREGETPLEM
DADGAT
Enzyme 18 Number of Residues 486
Enzyme 18 Molecular Weight 54265.6
Enzyme 18 Theoretical pI 9.96
Enzyme 18 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • Golgi membrane
  • cell part
  • membrane
  • organelle membrane
Enzyme 18 General Function Involved in sulfotransferase activity
Enzyme 18 Specific Function Catalyzes the transfer of sulfate to position 6 of non- reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O- sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc
Enzyme 18 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 18 Reactions
  • 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 14-34
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 9309344 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NS84 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name CHST7_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1461 bp
ATGAAGGGCCGGCGGCGGCGACGCCGAGAGTACTGCAAGTTCGCGCTGCTGTTGGTGCTG
TACACGCTGGTGCTGTTGCTCGTCCCCTCCGTATTGGACGGCGGCCGCGACGGGGACAAG
GGCGCCGAGCACTGCCCCGGCCTGCAGCGCAGCCTGGGAGTGTGGAGCCTGGAGGCGGCG
GCGGCCGGCGAACGCGAGCAGGGAGCGGAGGCGCGGGCCGCCGAGGAAGGGGGCGCGAAC
CAGTCTCCTCGGTTCCCAAGCAACCTCAGCGGCGCTGTCGGGGAGGCAGTGTCTCGCGAG
AAGCAGCACATCTACGTGCATGCCACCTGGCGCACCGGCTCGTCCTTCCTGGGCGAACTC
TTTAACCAGCACCCGGACGTTTTCTACTTGTATGAGCCCATGTGGCATCTATGGCAGGCG
CTGTATCCGGGCGACGCCGAGAGCTTGCAGGGCGCGCTGCGCGACATGCTGCGTTCGCTC
TTCCGCTGCGACTTCTCCGTGCTGCGGCTGTACGCGCCGCCGGGGGACCCCGCTGCGCGC
GCCCCGGACACGGCCAATCTTACCACGGCCGCCCTCTTCCGCTGGCGGACTAACAAGGTC
ATCTGCTCGCCGCCACTGTGTCCTGGCGCACCCCGTGCCCGGGCCGAGGTGGGCCTCGTC
GAGGACACCGCCTGCGAGCGCAGCTGCCCACCCGTGGCGATACGCGCCCTGGAGGCCGAG
TGCCGAAAGTACCCGGTGGTGGTCATCAAGGACGTGCGCCTGCTCGATCTGGGCGTGCTG
GTGCCCCTGTTGCGTGATCCAGGCCTCAACCTGAAGGTGGTGCAGCTTTTCCGCGACCCG
AGGGCGGTGCACAACTCGCGCCTCAAGTCTAGGCAGGGACTGCTGCGCGAGAGCATCCAG
GTGCTGCGCACCCGCCAGAGGGGCGACCGCTTCCACCGTGTGCTGCTGGCGCACGGCGTG
GGTGCTCGCCCCGGGGGCCAGTCTCGCGCGCTGCCCGCCGCGCCGCGCGCCGATTTCTTC
CTGACCGGTGCGCTCGAGGTGATCTGCGAAGCCTGGCTGCGCGATCTGCTTTTCGCGCGC
GGCGCGCCCGCCTGGCTGCGGCGCCGCTACCTGAGGCTGCGCTATGAGGACCTGGTGCGG
CAGCCACGCGCCCAGCTGCGCCGCCTGCTGCGCTTCTCCGGGCTACGCGCGCTCGCAGCG
CTCGATGCCTTCGCGCTCAACATGACTCGCGGCGCGGCCTACGGCGCCGACCGGCCCTTC
CACCTGTCAGCGCGCGACGCCCGGGAGGCGGTGCACGCCTGGCGCGAGCGCCTGAGCCGA
GAGCAGGTGCGCCAGGTGGAGGTCGCCTGCGCTCCAGCCATGCGTCTGCTCGCCTACCCT
CGCAGCGGAGAGGAGGGCGACGCGGAGCAGCCCAGGGAAGGGGAGACGCCGCTGGAGATG
GATGCCGACGGCGCCACGTAG
Enzyme 18 GenBank Gene ID AB037187 Link Image
Enzyme 18 GeneCard ID CHST7 Link Image
Enzyme 18 GenAtlas ID CHST7 Link Image
Enzyme 18 HGNC ID HGNC:13817 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Uchimura K, Fasakhany F, Kadomatsu K, Matsukawa T, Yamakawa T, Kurosawa N, Muramatsu T: Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities. Biochem Biophys Res Commun. 2000 Aug 2;274(2):291-6. [PubMed Link Image]
  2. Kitagawa H, Fujita M, Ito N, Sugahara K: Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase. J Biol Chem. 2000 Jul 14;275(28):21075-80. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  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. Bhakta S, Bartes A, Bowman KG, Kao WM, Polsky I, Lee JK, Cook BN, Bruehl RE, Rosen SD, Bertozzi CR, Hemmerich S: Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5). J Biol Chem. 2000 Dec 22;275(51):40226-34. [PubMed Link Image]
  6. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 8511
Enzyme 19 Name Heparan-sulfate 6-O-sulfotransferase 1
Enzyme 19 Synonyms
  1. HS6ST-1
Enzyme 19 Gene Name HS6ST1
Enzyme 19 Protein Sequence >Heparan-sulfate 6-O-sulfotransferase 1
MRRRRAGGRTMVERASKFVLVVAGSVCFMLILYQYAGPGLSLGAPGGRAPPDDLDLFPTP
DPHYEKKYYFPVRELERSLRFDMKGDDVIVFLHIQKTGGTTFGRHLVQNVRLEVPCDCRP
GQKKCTCYRPNRRETWLFSRFSTGWSCGLHADWTELTNCVPGVLDRRDSAALRTPRKFYY
ITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPPCYEGTDWSGCTLQEFMD
CPYNLANNRQVRMLADLSLVGCYNLSFIPEGKRAQLLLESAKKNLRGMAFFGLTEFQRKT
QYLFERTFNLKFIRPFMQYNSTRAGGVEVDEDTIRRIEELNDLDMQLYDYAKDLFQQRYQ
YKRQLERREQRLRSREERLLHRAKEALPREDADEPGRVPTEDYMSHIIEKW
Enzyme 19 Number of Residues 411
Enzyme 19 Molecular Weight 48225.7
Enzyme 19 Theoretical pI 8.95
Enzyme 19 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate biosynthetic process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 19 General Function Involved in sulfotransferase activity
Enzyme 19 Specific Function 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 18-37
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 148747866 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O60243 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name H6ST1_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1236 bp
ATGCGGCGGCGGCGCGCCGGCGGCAGGACCATGGTTGAGCGCGCCAGCAAGTTCGTGCTG
GTGGTGGCGGGCTCGGTGTGCTTCATGCTCATCTTGTACCAGTACGCGGGCCCAGGACTG
AGCCTGGGCGCGCCCGGCGGCCGCGCGCCGCCCGACGACCTGGACCTGTTCCCCACACCC
GACCCCCACTACGAGAAGAAGTACTACTTCCCGGTCCGCGAGCTGGAGCGCTCGCTGCGC
TTCGACATGAAGGGCGACGACGTGATCGTCTTCCTGCACATCCAGAAGACGGGCGGCACC
ACCTTCGGCCGCCACCTCGTGCAGAACGTACGCCTCGAGGTGCCGTGCGACTGCCGGCCC
GGCCAGAAGAAGTGCACCTGCTACCGGCCCAACCGCCGCGAGACTTGGCTCTTCTCCCGC
TTCTCCACCGGCTGGAGCTGCGGGCTGCACGCCGACTGGACCGAGCTCACCAACTGCGTG
CCCGGCGTGCTGGACCGCCGCGACTCCGCCGCGCTGCGCACGCCCAGGAAGTTCTACTAC
ATCACCCTGCTACGAGACCCCGTGTCCCGCTACCTGAGCGAGTGGCGGCATGTGCAGAGG
GGTGCCACGTGGAAGACGTCGTTGCATATGTGTGATGGGCGCACGCCCACGCCTGAGGAG
CTGCCGCCCTGCTACGAGGGCACGGACTGGTCGGGCTGCACGCTACAGGAGTTCATGGAC
TGCCCGTACAACCTGGCCAACAACCGCCAGGTGCGCATGCTGGCCGACCTGAGCCTGGTG
GGCTGCTACAACCTGTCCTTCATCCCCGAGGGCAAGCGGGCCCAGCTGCTGCTCGAGAGC
GCCAAGAAGAACCTGCGGGGCATGGCCTTCTTCGGCCTGACCGAGTTCCAGCGCAAGACG
CAGTACCTGTTCGAGCGGACGTTCAACCTCAAGTTCATCCGGCCCTTCATGCAGTACAAT
AGCACGCGGGCGGGCGGCGTGGAGGTGGATGAAGACACCATCCGGCGCATCGAGGAGCTC
AACGACCTGGACATGCAGCTGTACGACTACGCCAAGGACCTCTTCCAGCAGCGCTACCAG
TACAAGCGGCAGCTGGAGCGCAGGGAGCAGCGCCTGAGGAGCCGCGAGGAGCGTCTGCTG
CACCGGGCCAAGGAGGCACTGCCGCGGGAGGATGCCGACGAGCCGGGCCGCGTGCCCACC
GAGGACTACATGAGCCACATCATTGAGAAGTGGTAG
Enzyme 19 GenBank Gene ID NM_004807.2 Link Image
Enzyme 19 GeneCard ID HS6ST1 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 2q21
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Habuchi H, Kobayashi M, Kimata K: Molecular characterization and expression of heparan-sulfate 6-sulfotransferase. Complete cDNA cloning in human and partial cloning in Chinese hamster ovary cells. J Biol Chem. 1998 Apr 10;273(15):9208-13. [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. 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8609
Enzyme 20 Name Heparan-sulfate 6-O-sulfotransferase 2
Enzyme 20 Synonyms
  1. HS6ST-2
Enzyme 20 Gene Name HS6ST2
Enzyme 20 Protein Sequence >Heparan-sulfate 6-O-sulfotransferase 2
MALPACAVREFEPPRQPERGAPVRTTCPRRHSRVEAELAASRPGSVAASVRAGPPRGVSH
GFHTRPLLDKPRKASSSLAGAACAPLFALLSRGRRRRMHVLRRRWDLGSLCRALLTRGLA
ALGHSLKHVLGAIFSKIFGPMASVGNMDEKSNKLLLALVMLFLFAVIVLQYVCPGTECQL
LRLQAFSSPVPDPYRSEDESSARFVPRYNFTRGDLLRKVDFDIKGDDLIVFLHIQKTGGT
TFGRHLVRNIQLEQPCECRVGQKKCTCHRPGKRETWLFSRFSTGWSCGLHADWTELTSCV
PSVVDGKRDARLRPSRNFHYITILRDPVSRYLSEWRHVQRGATWKASLHVCDGRPPTSEE
LPSCYTGDDWSGCPLKEFMDCPYNLANNRQVRMLSDLTLVGCYNLSVMPEKQRNKVLLES
AKSNLKHMAFFGLTEFQRKTQYLFEKTFNMNFISPFTQYNTTRASSVEINEEIQKRIEGL
NFLDMELYSYAKDLFLQRYQFMRQKEHQEARRKRQEQRKFLKGRLLQTHFQSQGQGQSQN
PNQNQSQNPNPNANQNLTQNLMQNLTQSLSQKENRESPKQNSGKEQNDNTSNGTNDYIGS
VEKWR
Enzyme 20 Number of Residues 605
Enzyme 20 Molecular Weight 69129.3
Enzyme 20 Theoretical pI 10.25
Enzyme 20 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate biosynthetic process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 20 General Function Involved in sulfotransferase activity
Enzyme 20 Specific Function 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 5-27
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 116295254 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q96MM7 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name H6ST2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1818 bp
ATGGCACTGCCTGCGTGTGCAGTCCGGGAGTTCGAGCCGCCGCGGCAACCGGAGCGAGGA
GCGCCCGTCCGCACCACCTGTCCCCGCCGGCATTCCAGAGTAGAGGCCGAATTGGCAGCG
AGCCGGCCCGGGTCGGTCGCCGCCTCAGTTCGCGCGGGCCCTCCTAGGGGTGTGTCTCAC
GGATTCCACACCCGGCCGCTCCTGGACAAGCCCCGAAAGGCGTCTTCTTCCCTGGCGGGA
GCCGCGTGCGCCCCGCTTTTCGCGCTGCTGTCCCGGGGCCGCCGCAGGCGGATGCACGTC
CTCAGGCGACGCTGGGACCTGGGCTCCCTCTGCCGGGCCCTGCTCACTCGGGGCCTGGCC
GCCCTGGGCCACTCGCTGAAGCACGTGCTCGGTGCGATCTTCTCCAAGATTTTCGGCCCC
ATGGCCAGCGTCGGGAACATGGATGAGAAATCCAACAAGCTGCTGCTAGCTTTGGTGATG
CTCTTCCTATTTGCCGTGATCGTCCTCCAATACGTGTGCCCCGGCACAGAATGCCAGCTC
CTCCGCCTGCAGGCGTTCAGCTCCCCGGTGCCGGACCCGTACCGCTCGGAGGATGAGAGC
TCCGCCAGGTTCGTGCCCCGCTACAATTTCACCCGCGGCGACCTCCTGCGCAAGGTAGAC
TTCGACATCAAGGGCGATGACCTGATCGTGTTCCTGCACATCCAGAAGACCGGGGGCACC
ACTTTCGGCCGCCACTTGGTGCGTAACATCCAGCTGGAGCAGCCGTGCGAGTGCCGCGTG
GGTCAGAAGAAATGCACTTGCCACCGGCCGGGTAAGCGGGAAACCTGGCTCTTCTCCAGG
TTCTCCACGGGCTGGAGCTGCGGGTTGCACGCCGACTGGACCGAGCTCACCAGCTGTGTG
CCCTCCGTGGTGGACGGCAAGCGCGACGCCAGGCTGAGACCGTCCAGGAACTTCCACTAC
ATCACCATCCTCCGAGACCCAGTGTCCCGGTACTTGAGTGAGTGGAGGCATGTCCAGAGA
GGGGCAACATGGAAAGCATCCCTGCATGTCTGCGATGGAAGGCCTCCAACCTCCGAAGAG
CTGCCCAGCTGCTACACTGGCGATGACTGGTCTGGCTGCCCCCTCAAAGAGTTTATGGAC
TGTCCCTACAATCTAGCCAACAACCGCCAGGTGCGCATGCTCTCCGACCTGACCCTGGTA
GGCTGCTACAACCTCTCTGTCATGCCTGAAAAGCAAAGAAACAAGGTCCTTCTGGAAAGT
GCCAAGTCAAATCTGAAGCACATGGCGTTCTTCGGCCTCACTGAGTTTCAGCGGAAGACC
CAATATCTGTTTGAGAAAACCTTCAACATGAACTTTATTTCGCCATTTACCCAGTATAAT
ACCACTAGGGCCTCTAGTGTAGAGATCAATGAGGAAATTCAAAAGCGTATTGAGGGACTG
AATTTTCTGGATATGGAGTTGTACAGCTATGCCAAAGACCTTTTTTTGCAGAGGTATCAG
TTTATGAGGCAGAAAGAGCATCAGGAGGCCAGGCGAAAGCGTCAGGAACAACGCAAATTT
CTGAAGGGAAGGCTCCTTCAGACCCATTTCCAGAGCCAGGGTCAGGGCCAGAGCCAGAAT
CCGAATCAGAATCAGAGTCAGAACCCAAATCCGAATGCCAATCAGAACCTGACTCAGAAT
CTGATGCAGAATCTGACTCAGAGTTTGAGCCAGAAGGAGAACCGGGAAAGCCCGAAGCAG
AACTCAGGCAAGGAGCAGAATGATAACACCAGCAATGGCACCAACGACTACATAGGCAGT
GTAGAGAAATGGCGTTAA
Enzyme 20 GenBank Gene ID NM_147175.3 Link Image
Enzyme 20 GeneCard ID HS6ST2 Link Image
Enzyme 20 GenAtlas ID HS6ST2 Link Image
Enzyme 20 HGNC ID HGNC:19133 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Habuchi H, Miyake G, Nogami K, Kuroiwa A, Matsuda Y, Kusche-Gullberg M, Habuchi O, Tanaka M, Kimata K: Biosynthesis of heparan sulphate with diverse structures and functions: two alternatively spliced forms of human heparan sulphate 6-O-sulphotransferase-2 having different expression patterns and properties. Biochem J. 2003 Apr 1;371(Pt 1):131-42. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  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. 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]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 8826
Enzyme 21 Name Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Enzyme 21 Synonyms
  1. PAPS transporter 1
  2. Putative MAPK-activating protein PM15
  3. Putative NF-kappa-B-activating protein 48
  4. Solute carrier family 35 member B2
Enzyme 21 Gene Name SLC35B2
Enzyme 21 Protein Sequence >Adenosine 3'-phospho 5'-phosphosulfate transporter 1
MDARWWAVVVLAAFPSLGAGGETPEAPPESWTQLWFFRFVVNAAGYASFMVPGYLLVQYF
RRKNYLETGRGLCFPLVKACVFGNEPKASDEVPLAPRTEAAETTPMWQALKLLFCATGLQ
VSYLTWGVLQERVMTRSYGATATSPGERFTDSQFLVLMNRVLALIVAGLSCVLCKQPRHG
APMYRYSFASLSNVLSSWCQYEALKFVSFPTQVLAKASKVIPVMLMGKLVSRRSYEHWEY
LTATLISIGVSMFLLSSGPEPRSSPATTLSGLILLAGYIAFDSFTSNWQDALFAYKMSSV
QMMFGVNFFSCLFTVGSLLEQGALLEGTRFMGRHSEFAAHALLLSICSACGQLFIFYTIG
QFGAAVFTIIMTLRQAFAILLSCLLYGHTVTVVGGLGVAVVFAALLLRVYARGRLKQRGK
KAVPVESPVQKV
Enzyme 21 Number of Residues 432
Enzyme 21 Molecular Weight 47514.3
Enzyme 21 Theoretical pI 9.40
Enzyme 21 GO Classification
Function
Process
  • establishment of localization
  • transmembrane transport
  • transport
Component
Enzyme 21 General Function Involved in transmembrane transport
Enzyme 21 Specific Function Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF- kappa-B and MAPK pathways
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 5-25 40-60 109-129 154-174 238-258 265-285 299-319 353-373 387-407
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 30026034 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8TB61 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name S35B2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1299 bp
ATGGACGCCAGATGGTGGGCAGTGGTGGTGCTGGCTGCGTTCCCCTCCCTAGGGGCAGGT
GGGGAGACTCCCGAAGCCCCTCCGGAGTCATGGACCCAGCTATGGTTCTTCCGATTTGTG
GTGAATGCTGCTGGCTATGCCAGCTTTATGGTACCTGGCTACCTCCTGGTGCAGTACTTC
AGGCGGAAGAACTACCTGGAGACCGGTAGGGGCCTCTGCTTTCCCCTGGTGAAAGCTTGT
GTGTTTGGCAATGAGCCCAAGGCCTCTGATGAGGTTCCCCTGGCGCCCCGAACAGAGGCG
GCAGAGACCACCCCGATGTGGCAGGCCCTGAAGCTGCTCTTCTGTGCCACAGGGCTCCAG
GTGTCTTATCTGACTTGGGGTGTGCTGCAGGAAAGAGTGATGACCCGCAGCTATGGGGCC
ACAGCCACATCACCGGGTGAGCGCTTTACGGACTCGCAGTTCCTGGTGCTAATGAACCGA
GTGCTGGCACTGATTGTGGCTGGCCTCTCCTGTGTTCTCTGCAAGCAGCCCCGGCATGGG
GCACCCATGTACCGGTACTCCTTTGCCAGCCTGTCCAATGTGCTTAGCAGCTGGTGCCAA
TACGAAGCTCTTAAGTTCGTCAGCTTCCCCACCCAGGTGCTGGCCAAGGCCTCTAAGGTG
ATCCCTGTCATGCTGATGGGAAAGCTTGTGTCTCGGCGCAGCTACGAACACTGGGAGTAC
CTGACAGCCACCCTCATCTCCATTGGGGTCAGCATGTTTCTGCTATCCAGCGGACCAGAG
CCCCGCAGCTCCCCAGCCACCACACTCTCAGGCCTCATCTTACTGGCAGGTTATATTGCT
TTTGACAGCTTCACCTCAAACTGGCAGGATGCCCTGTTTGCCTATAAGATGTCATCGGTG
CAGATGATGTTTGGGGTCAATTTCTTCTCCTGCCTCTTCACAGTGGGCTCACTGCTAGAA
CAGGGGGCCCTACTGGAGGGAACCCGCTTCATGGGGCGACACAGTGAGTTTGCTGCCCAT
GCCCTGCTACTCTCCATCTGCTCCGCATGTGGCCAGCTCTTCATCTTTTACACCATTGGG
CAGTTTGGGGCTGCCGTCTTCACCATCATCATGACCCTCCGCCAGGCCTTTGCCATCCTT
CTTTCCTGCCTTCTCTATGGCCACACTGTCACTGTGGTGGGAGGGCTGGGGGTGGCTGTG
GTCTTTGCTGCCCTCCTGCTCAGAGTCTACGCGCGGGGCCGTCTAAAGCAACGGGGAAAG
AAGGCTGTGCCTGTTGAGTCTCCTGTGCAGAAGGTTTGA
Enzyme 21 GenBank Gene ID NM_178148.2 Link Image
Enzyme 21 GeneCard ID SLC35B2 Link Image
Enzyme 21 GenAtlas ID SLC35B2 Link Image
Enzyme 21 HGNC ID HGNC:16872 Link Image
Enzyme 21 Chromosome Location 6
Enzyme 21 Locus 6p12.1-p11.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Kamiyama S, Suda T, Ueda R, Suzuki M, Okubo R, Kikuchi N, Chiba Y, Goto S, Toyoda H, Saigo K, Watanabe M, Narimatsu H, Jigami Y, Nishihara S: Molecular cloning and identification of 3'-phosphoadenosine 5'-phosphosulfate transporter. J Biol Chem. 2003 Jul 11;278(28):25958-63. Epub 2003 Apr 25. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [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. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. 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]
  11. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 8880
Enzyme 22 Name Heparan-sulfate 6-O-sulfotransferase 3
Enzyme 22 Synonyms
  1. HS6ST-3
Enzyme 22 Gene Name HS6ST3
Enzyme 22 Protein Sequence >Heparan-sulfate 6-O-sulfotransferase 3
MDERFNKWLLTPVLTLLFVVIMYQYVSPSCTSSCTNFGEQPRAGEAGPPAVPGPARRAQA
PPEEWERRPQLPPPPRGPPEGPRGAAAPEEEDEEPGDPREGEEEEEEDEPDPEAPENGSL
PRFVPRFNFSLKDLTRFVDFNIKGRDVIVFLHIQKTGGTTFGRHLVKNIRLEQPCSCKAG
QKKCTCHRPGKKETWLFSRFSTGWSCGLHADWTELTNCVPAIMEKKDCPRNHSHTRNFYY
ITMLRDPVSRYLSEWKHVQRGATWKTSLHMCDGRSPTPDELPTCYPGDDWSGVSLREFMD
CTYNLANNRQVRMLADLSLVGCYNLTFMNESERNTILLQSAKNNLKNMAFFGLTEFQRKT
QFLFERTFNLKFISPFTQFNITRASNVEINEGARQRIEDLNFLDMQLYEYAKDLFQQRYH
HTKQLEHQRDRQKRREERRLQREHRDHQWPKEDGAAEGTVTEDYNSQVVRW
Enzyme 22 Number of Residues 471
Enzyme 22 Molecular Weight 54843.3
Enzyme 22 Theoretical pI 6.82
Enzyme 22 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • carbohydrate biosynthetic process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 22 General Function Involved in sulfotransferase activity
Enzyme 22 Specific Function 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 5-27
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 23452527 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q8IZP7 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name H6ST3_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1416 bp
ATGGATGAAAGGTTCAACAAGTGGCTGCTGACGCCGGTGCTCACTCTCCTCTTCGTGGTC
ATCATGTACCAGTACGTGTCCCCCTCCTGCACCAGCTCCTGCACCAACTTGGGGGAGCAG
CCCCGCGCGGGGGAGGCCGGCCCGCCCGCCGTCCCGGGTCCCGCCCGCCGGGCTCAGGCG
CCGCCGGAGGAGTGGGAGCGGCGGCCCCAGTTGCCCCCGCCGCCCCGGGGGCCCCCCGAG
GGACCTCGGGGGGCCSCGGCGCCGGAGGAGGAGGACGAGGAGCCCGGAGACCCCCGGGAG
GGGGAGGAAGAGGAGGAGGAAGACGAGCCGGACCCCGAGGCCCCGGAAAACGGCTCCCTG
CCCCGATTCGTGCCGCGCTTCAACTTCAGCCTGAAGGACCTGACCCGCTTCGTGGATTTC
AACATCAAAGGGCGCGACGTGATCGTGTTCCTCCACATCCAGAAGACGGGGGGCACCACT
TTCGGCCGGCACCTGGTGAAGAACATCCGGCTGGAGCAGCCTTGTAGCTGCAAAGCGGGT
CAGAAGAAGTGCACCTGCCACCGGCCTGGCAAGAAGGAGACGTGGCTCTTCTCCCGCTTC
TCCACCGGCTGGAGCTGCGGGCTGCACGCCGACTGGACGGAGCTCACCAACTGCGTGCCG
GCCATCATGGAGAAGAAGGACTGTCCCCGCAACCACAGCCACACCAGGAATTTCTATTAC
ATCACAATGTTACGGGATCCAGTGTCACGTTACCTGAGCGAGTGGAAACATGTCCAGAGA
GGGGCCACTTGGAAAACCTCTCTTCATATGTGTGATGGAAGAAGCCCCACCCCAGATGAG
CTGCCTACCTGCTACCCTGGGGATGACTGGTCTGGGGTCAGCTTGCGGGAGTTTATGGAT
TGCACCTACAACCTGGCTAACAATCGCCAGGTGCGCATGCTGGCTGACCTCAGCCTGGTG
GGCTGCTATAACTTGACTTTCATGAACGAGAGTGAAAGAAACACCATCCTGTTGCAGAGT
GCAAAGAACAACCTGAAGAACATGGCCTTCTTTGGGCTCACTGAGTTCCAGAGGAAGACA
CAGTTTCTCTTTGAGAGAACATTCAACCTCAAGTTCATCTCCCCCTTCACACAGTTCAAC
ATCACGCGGGCTTCTAACGTGGAGATCAACGAGGGTGCCCGCCAACGCATTGAGGATCTA
AACTTCCTGGACATGCAGCTTTACGAGTATGCAAAAGATCTCTTCCAGCAGCGCTACCAC
CACACCAAGCAGCTAGAGCACCAGAGGGACCGCCAGAAGCGGCGGGAGGAGCGGAGGCTG
CAGCGAGAGCACAGGGACCACCAGTGGCCCAAAGAAGATGGGGCTGCAGAAGGGACTGTC
ACCGAGGACTACAACAGCCAGGTGGTGAGATGGTGA
Enzyme 22 GenBank Gene ID AF539426 Link Image
Enzyme 22 GeneCard ID HS6ST3 Link Image
Enzyme 22 GenAtlas ID HS6ST3 Link Image
Enzyme 22 HGNC ID HGNC:19134 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 13q32.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 12871
Enzyme 23 Name Carbohydrate sulfotransferase 15
Enzyme 23 Synonyms
  1. B-cell RAG-associated gene protein
  2. hBRAG
  3. N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
  4. GalNAc4S-6ST
Enzyme 23 Gene Name CHST15
Enzyme 23 Protein Sequence >Carbohydrate sulfotransferase 15
MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEV
RTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNP
SLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQE
LHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHL
AHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRL
RDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTF
FYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVT
EALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLED
HASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFY
RPFNARLAQVLADEAFAWKTT
Enzyme 23 Number of Residues 561
Enzyme 23 Molecular Weight 64925.7
Enzyme 23 Theoretical pI 8.40
Enzyme 23 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 23 General Function Involved in sulfotransferase activity
Enzyme 23 Specific Function Sulfotransferase that transfers sulfate from 3'- phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non- reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B- cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo
Enzyme 23 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
  • Glycan structures - biosynthesis 1 (map01030 Link Image)
Enzyme 23 Reactions
  • (1) 3'-phosphoadenylyl sulfate + dermatan = adenosine 3',5'-bisphosphate + dermatan 6'-sulfate [RN:R07288]
  • (2) 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 81-101
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 45505173 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q7LFX5 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name CHSTF_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1686 bp
ATGAGGCACTGCATTAATTGCTGCATACAGCTGTTACCCGACGGCGCACACAAGCAGCAG
GTCAACTGCCAAGGGGGCCCCCATCACGGTCACCAGGCGTGCCCCACGTGCAAAGGAGAA
AACAAAATTCTGTTTCGTGTGGACAGTAAGCAGATGAACTTGCTTGCTGTTCTCGAAGTG
AGGACTGAAGGGAACGAAAACTGGGGTGGGTTTTTGCGCTTCAAAAAGGGGAAGCGATGT
AGCCTCGTTTTTGGACTGATAATAATGACCTTGGTAATGGCTTCTTACATCCTTTCTGGG
GCCCACCAAGAGCTTCTGATCTCATCACCTTTCCATTACGGAGGCTTCCCCAGCAACCCC
AGCTTGATGGACAGCGAAAACCCAAGTGACACAAAGGAGCATCACCACCAATCCTCTGTA
AATAATATTTCATACATGAAGGACTATCCAAGCATTAAATTAATTATCAACAGCATCACA
ACTAGGATTGAGTTCACGACCAGACAGCTCCCAGACTTAGAAGACCTTAAGAAGCAGGAG
TTGCATATGTTTTCAGTCATCCCCAACAAATTCCTTCCAAACAGTAAGAGCCCCTGTTGG
TACGAGGAGTTCTCGGGGCAGAACACCACCGACCCCTACCTCACCAACTCCTACGTGCTC
TACTCCAAGCGCTTCCGCTCCACCTTCGACGCCCTGCGCAAGGCCTTCTGGGGCCACCTG
GCGCACGCGCACGGGAAGCACTTCCGCCTGCGCTGCCTGCCGCACTTCTACATCATAGGG
CAGCCCAAGTGCGGGACCACAGACCTCTATGACCGCCTGCGGCTGCACCCTGAGGTCAAG
TTCTCCGCCATCAAGGAGCCACACTGGTGGACCCGGAAGCGCTTTGGAATCGTCCGCCTA
AGAGATGGGCTGCGAGACCGCTATCCCGTGGAAGATTATCTGGACCTCTTTGACCTGGCC
GCACACCAGATCCATCAAGGACTGCAGGCCAGCTCTGCAAAGGAGCAGAGCAAGATGAAT
ACAATCATTATCGGGGAGGCCAGTGCCTCCACGATGTGGGATAATAATGCCTGGACGTTC
TTCTACGACAACAGCACGGATGGCGAGCCACCGTTTCTGACGCAGGACTTCATCCACGCC
TTTCAGCCAAATGCCAGACTGATTGTCATGCTCAGGGACCCTGTGGAGAGGTTGTACTCA
GACTATCTCTACTTTGCAAGTTCGAATAAATCCGCGGACGACTTCCATGAGAAAGTGACA
GAAGCACTGCAGCTGTTTGAAAATTGCATGCTTGATTATTCACTGCGCGCCTGCGTCTAC
AACAACACCCTCAACAACGCCATGCCTGTGAGGCTCCAGGTTGGGCTCTATGCTGTGTAC
CTTCTGGACTGGCTCAGCGTTTTTGACAAGCAACAGTTTCTCATTCTTCGCCTGGAAGAT
CATGCATCCAACGTCAAGTACACCATGCACAAGGTCTTCCAGTTTCTGAACCTAGGGCCC
TTAAGTGAGAAGCAGGAGGCTTTGATGACCAAGAGCCCCGCATCCAATGCACGGCGTCCC
GAGGACCGGAACCTGGGGCCCATGTGGCCCATCACACAGAAGATTCTGCGGGATTTCTAC
AGGCCCTTCAACGCTAGGCTGGCGCAGGTCCTCGCGGATGAGGCGTTTGCGTGGAAGACG
ACGTGA
Enzyme 23 GenBank Gene ID NM_015892.3 Link Image
Enzyme 23 GeneCard ID CHST15 Link Image
Enzyme 23 GenAtlas ID CHST15 Link Image
Enzyme 23 HGNC ID HGNC:18137 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 10q26
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Verkoczy LK, Marsden PA, Berinstein NL: hBRAG, a novel B cell lineage cDNA encoding a type II transmembrane glycoprotein potentially involved in the regulation of recombination activating gene 1 (RAG1). Eur J Immunol. 1998 Sep;28(9):2839-53. [PubMed Link Image]
  2. Yuki M, Yoshinaga K, Yamakawa H, Sakurada K, Sato S, Yajima A, Horii A: Structure, expression and mutational analysis of the hBRAG gene on 10q in the frequently deleted region in human endometrial cancer. Oncol Rep. 2000 Nov-Dec;7(6):1339-42. [PubMed Link Image]
  3. Ohtake S, Ito Y, Fukuta M, Habuchi O: Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to human B cell recombination activating gene-associated gene. J Biol Chem. 2001 Nov 23;276(47):43894-900. Epub 2001 Sep 25. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. 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]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Verkoczy LK, Guinn B, Berinstein NL: Characterization of the human B cell RAG-associated gene, hBRAG, as a B cell receptor signal-enhancing glycoprotein dimer that associates with phosphorylated proteins in resting B cells. J Biol Chem. 2000 Jul 14;275(28):20967-79. [PubMed Link Image]
  9. Ohtake S, Kimata K, Habuchi O: A unique nonreducing terminal modification of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase. J Biol Chem. 2003 Oct 3;278(40):38443-52. Epub 2003 Jul 21. [PubMed Link Image]
  10. Sawada T, Fujii S, Nakano H, Ohtake S, Kimata K, Habuchi O: Synthesis of sulfated phenyl 2-acetamido-2-deoxy-D-galactopyranosides. 4-O-Sulfated phenyl 2-acetamido-2-deoxy-beta-D-galactopyranoside is a competitive acceptor that decreases sulfation of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase. Carbohydr Res. 2005 Sep 5;340(12):1983-96. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 13112
Enzyme 24 Name cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
Enzyme 24 Synonyms
  1. PIP gene
  2. 3'(2', 5'-bisphosphate nucleotidase 1, isoform CRA_a
Enzyme 24 Gene Name BPNT1
Enzyme 24 Protein Sequence >cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
Enzyme 24 Number of Residues 308
Enzyme 24 Molecular Weight 33393
Enzyme 24 Theoretical pI 5.41
Enzyme 24 GO Classification Not Available
Enzyme 24 General Function Carbohydrate transport and metabolism
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function Not Available
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 158257318 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID A8K7C8 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name A8K7C8_HUMAN Link Image
Enzyme 24 PDB ID 1JP4 Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AK291943 Link Image
Enzyme 24 GeneCard ID A8K7C8 Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15180
Enzyme 25 Name Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name SULT1A2
Enzyme 25 Protein Sequence >Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNY
TTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
Enzyme 25 Number of Residues 295
Enzyme 25 Molecular Weight 34311
Enzyme 25 Theoretical pI 7.32
Enzyme 25 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 109731387 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q14CJ7 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name Q14CJ7_HUMAN Link Image
Enzyme 25 PDB ID 1LS6 Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >888 bp
ATGGAGCTGATCCAGGACATCTCTCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGCGGTGACCTGGAAAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGTCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAAACACACCA
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCGGTTTCCTACTAC
CACTTCTACCACATGGCCAAAGTGTACCCTCACCCTGGGACCTGGGAAAGCTTCCTGGAG
AAGTTCATGGCTGGAGAAGTGTCCTATGGGTCCTGGTACCAGCACGTGCAAGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACTGTG
GACCTCATGGTTGAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCGCCGGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Enzyme 25 GenBank Gene ID BC113727 Link Image
Enzyme 25 GeneCard ID Q14CJ7 Link Image
Enzyme 25 GenAtlas ID SULT1A2 Link Image
Enzyme 25 HGNC ID HGNC:11454 Link Image
Enzyme 25 Chromosome Location 16
Enzyme 25 Locus 16p12.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15181
Enzyme 26 Name Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
Enzyme 26 Synonyms
  1. SubName: Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform CRA_a
  2. SubName: cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA
  3. SubName: cDNA, FLJ93953, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA) -preferring, member 1 (SULT2A1), mRNA
Enzyme 26 Gene Name SULT2A1
Enzyme 26 Protein Sequence >Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Enzyme 26 Number of Residues 285
Enzyme 26 Molecular Weight 33779.6
Enzyme 26 Theoretical pI 5.76
Enzyme 26 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 26 General Function Involved in sulfotransferase activity
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 158259783 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID A8K015 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name A8K015_HUMAN Link Image
Enzyme 26 PDB ID 1OV4 Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >858 bp
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAACGGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
Enzyme 26 GenBank Gene ID AK289380 Link Image
Enzyme 26 GeneCard ID SULT2A1 Link Image
Enzyme 26 GenAtlas ID SULT2A1 Link Image
Enzyme 26 HGNC ID HGNC:11458 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 19q13.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15182
Enzyme 27 Name cDNA FLJ75927, highly similar to Homo sapiens carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11), mRNA (Carbohydrate (Chondroitin 4) sulfotransferase 11, isoform CRA_a)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name CHST11
Enzyme 27 Protein Sequence >cDNA FLJ75927, highly similar to Homo sapiens carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11), mRNA (Carbohydrate (Chondroitin 4) sulfotransferase 11, isoform CRA_a)
MKPALLEVMRMNRICRMVLATCLGSFILVIFYFQSMLHPVMRRNPFGVDICCRKGSRSPL
QELYNPIQLELSNTAVLHQMRRDQVTDTCRANSATSRKRRVLTPNDLKHLVVDEDHELIY
CYVPKVACTNWKRLMMVLTGRGKYSDPMEIPANEAHVSANLKTLNQYSIPEINHRLKSYM
KFLFVREPFERLVSAYRNKFTQKYNISFHKRYGTKIIKRQRKNATQEALRKGDDVKFEEF
VAYLIDPHTQREEPFNEHWQTVYSLCHPCHIHYDLVGKYETLEEDSNYVLQLAGVGSYLK
FPTYAKSTRTTDEMTTEFFQNISSEHQTQLYEVYKLDFLMFNYSVPSYLKLE
Enzyme 27 Number of Residues 352
Enzyme 27 Molecular Weight 41555
Enzyme 27 Theoretical pI 9.07
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function Not Available
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 158255282 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID A8K4F8 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name A8K4F8_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1059 bp
ATGAAGCCAGCGCTGCTGGAAGTGATGAGGATGAACAGAATCTGCCGGATGGTGCTGGCC
ACTTGCTTGGGATCCTTTATCCTGGTCATCTTCTATTTCCAAAGTATGTTGCACCCAGTC
ATGCGGAGGAATCCCTTTGGTGTGGACATCTGCTGCCGGAAGGGGTCCCGAAGCCCCCTG
CAGGAACTCTACAACCCAATCCAGCTGGAGCTCTCAAACACTGCTGTCCTGCACCAGATG
CGGCGGGACCAGGTGACAGACACGTGCCGAGCCAACAGCGCCACAAGCCGTAAGCGGAGG
GTGCTGACCCCCAACGACCTGAAGCACTTGGTGGTGGATGAGGACCACGAGCTCATCTAC
TGCTACGTGCCCAAGGTGGCCTGCACCAACTGGAAGCGGCTCATGATGGTCCTGACCGGG
CGGGGGAAGTACAGCGACCCCATGGAGATCCCGGCCAACGAGGCACACGTCTCCGCCAAC
CTGAAGACCCTGAACCAGTACAGCATCCCAGAAATCAACCACCGCTTGAAAAGCTACATG
AAGTTCCTGTTTGTCCGGGAGCCCTTCGAGAGGCTAGTGTCCGCCTACCGCAACAAGTTC
ACCCAGAAGTACAACATCTCCTTCCACAAGCGGTACGGCACCAAGATCATCAAACGCCAG
CGGAAGAACGCCACCCAGGAGGCCCTGCGCAAAGGGGACGATGTCAAATTCGAGGAGTTT
GTGGCCTATCTCATCGACCCACACACCCAGCGGGAGGAGCCTTTCAACGAACACTGGCAA
ACCGTCTACTCACTCTGCCATCCCTGCCACATCCACTATGACCTCGTGGGCAAGTACGAG
ACACTGGAAGAGGATTCTAATTACGTCCTGCAGCTGGCAGGAGTGGGCAGCTACCTGAAG
TTCCCCACCTATGCAAAGTCTACGAGAACTACTGATGAAATGACCACAGAATTCTTCCAG
AACATCAGCTCAGAGCACCAAACGCAGCTGTACGAAGTCTACAAACTCGATTTTTTAATG
TTCAATTACTCAGTGCCAAGCTACCTGAAATTGGAATAA
Enzyme 27 GenBank Gene ID AK290923 Link Image
Enzyme 27 GeneCard ID A8K4F8 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location 12
Enzyme 27 Locus 12q
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 15183
Enzyme 28 Name Carbohydrate (Chondroitin 4) sulfotransferase 12
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name CHST12
Enzyme 28 Protein Sequence >Carbohydrate (Chondroitin 4) sulfotransferase 12
MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDREL
TADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQ
QAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKR
VMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTK
FLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSF
ANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDR
QLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
Enzyme 28 Number of Residues 414
Enzyme 28 Molecular Weight 48415
Enzyme 28 Theoretical pI 9.69
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID A4D1Z9 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name A4D1Z9_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID CH236953 Link Image
Enzyme 28 GeneCard ID A4D1Z9 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 15184
Enzyme 29 Name Tyrosylprotein sulfotransferase 1
Enzyme 29 Synonyms
  1. SubName: Tyrosylprotein sulfotransferase 1, isoform CRA_a
  2. SubName: cDNA, FLJ93583, Homo sapiens tyrosylprotein sulfotransferase 1 (TPST1), mRNA
Enzyme 29 Gene Name TPST1
Enzyme 29 Protein Sequence >Tyrosylprotein sulfotransferase 1
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPVKLESTRTTVRTGLDLKAN
KTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKE
KIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFL
LMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYE
QLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALS
KWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKIIENTRRVYKGEFQLPDFL
KEKPQTEQVE
Enzyme 29 Number of Residues 370
Enzyme 29 Molecular Weight 42188.1
Enzyme 29 Theoretical pI 9.49
Enzyme 29 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 29 General Function Involved in sulfotransferase activity
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 189053670 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID A4D2M0 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name A4D2M0_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1113 bp
ATGGTTGGAAAGCTGAAGCAGAACTTACTATTGGCATGTCTGGTGATTAGTTCTGTGACT
GTGTTTTACCTGGGCCAGCATGCCATGGAATGCCATCACCGGATAGAGGAACGTAGCCAG
CCAGTCAAATTGGAGAGCACAAGGACCACTGTGAGAACTGGCCTGGACCTCAAAGCCAAC
AAAACCTTTGCCTATCACAAAGATATGCCTTTAATATTTATTGGAGGTGTGCCTCGGAGT
GGAACCACACTCATGAGGGCCATGCTGGACGCACATCCTGACATTCGCTGTGGAGAGGAA
ACCAGGGTCATTCCCCGAATCCTGGCCCTGAAGCAGATGTGGTCACGGTCAAGTAAAGAG
AAGATCCGCCTGGATGAGGCTGGTGTTACTGATGAAGTGCTGGATTCTGCCATGCAAGCC
TTCTTACTAGAAATTATCGTTAAGCATGGGGAGCCAGCCCCTTATTTATGTAATAAAGAT
CCTTTTGCCCTGAAATCTTTAACTTACCTTTCTAGGTTATTCCCCAATGCCAAATTTCTC
CTGATGGTCCGAGATGGCCGGGCATCAGTACATTCAATGATTTCTCGAAAAGTTACTATA
GCTGGATTTGATCTGAACAGCTATAGGGACTGTTTGACAAAGTGGAATCGTGCTATAGAG
ACCATGTATAACCAGTGTATGGAGGTTGGTTATAAAAAGTGCATGTTGGTTCACTATGAA
CAACTTGTCTTACATCCTGAACGGTGGATGAGAACACTCTTAAAGTTCCTCCAGATTCCA
TGGAACCACTCAGTATTGCACCATGAAGAGATGATTGGGAAAGCTGGGGGAGTGTCTCTG
TCAAAAGTGGAGAGATCTACAGACCAAGTAATCAAGCCAGTCAATGTAGGAGCTCTATCA
AAATGGGTTGGGAAGATACCGCCAGATGTTTTACAAGACATGGCAGTGATTGCTCCTATG
CTTGCCAAGCTTGGATATGACCCATATGCCAACCCACCTAACTACGGAAAACCTGATCCC
AAAATTATTGAAAACACTCGAAGGGTCTATAAGGGAGAATTCCAACTACCTGACTTTCTT
AAAGAAAAACCACAGACTGAGCAAGTGGAGTAG
Enzyme 29 GenBank Gene ID AK313098 Link Image
Enzyme 29 GeneCard ID TPST1 Link Image
Enzyme 29 GenAtlas ID TPST1 Link Image
Enzyme 29 HGNC ID HGNC:12020 Link Image
Enzyme 29 Chromosome Location 7
Enzyme 29 Locus 7q11.21
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 15185
Enzyme 30 Name cDNA FLJ76340, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 5 (HS3ST5), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 5)
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name HS3ST5
Enzyme 30 Protein Sequence >cDNA FLJ76340, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 5 (HS3ST5), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 5)
MLFKQQAWLRQKLLVLGSLAVGSLLYLVARVGSLDRLQPICPIEGRLGGARTQAEFPLRA
LQFKRGLLHEFRKGNASKEQVRLHDLVQQLPKAIIIGVRKGGTRALLEMLNLHPAVVKAS
QEIHFFDNDENYGKGIEWYRKKMPFSYPQQITIEKSPAYFITEEVPERIYKMNSSIKLLI
IVREPTTRAISDYTQVLEGKERKNKTYYKFEKLAIDPNTCEVNTKYKAVRTSIYTKHLER
WLKYFPIEQFHVVDGDRLITEPLPELQLVEKFLNLPPRISQYNLYFNATRGFYCLRFNII
FNKCLAGSKGRIHPEVDPSVITKLRKFFHPFNQKFYQITGRTLNWP
Enzyme 30 Number of Residues 346
Enzyme 30 Molecular Weight 40409
Enzyme 30 Theoretical pI 10.31
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function Not Available
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 158260837 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID A8K1J2 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name A8K1J2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1041 bp
ATGCTATTCAAACAGCAGGCGTGGCTGAGACAGAAGCTCCTGGTGCTGGGAAGCCTTGCC
GTTGGGAGTCTCCTGTATCTAGTCGCCAGAGTTGGGAGCTTGGATAGGCTACAACCCATT
TGCCCCATTGAAGGTCGACTGGGTGGAGCCCGCACTCAGGCTGAATTCCCACTTCGCGCC
CTGCAGTTTAAGCGTGGCCTGCTGCACGAGTTCCGGAAGGGCAACGCTTCCAAGGAGCAG
GTTCGCCTCCATGACCTGGTCCAGCAGCTCCCCAAGGCCATTATCATTGGGGTGAGGAAA
GGAGGCACAAGGGCCCTGCTTGAAATGCTGAACCTACATCCGGCAGTAGTCAAAGCCTCT
CAAGAAATCCACTTTTTTGATAATGATGAGAATTATGGTAAGGGCATTGAGTGGTATAGG
AAAAAGATGCCTTTTTCCTACCCTCAGCAAATCACAATTGAAAAGAGCCCAGCATATTTT
ATCACAGAGGAGGTTCCAGAAAGGATTTACAAAATGAACTCATCCATCAAGTTGTTGATC
ATTGTCAGGGAGCCAACCACAAGAGCTATTTCTGATTATACTCAGGTGCTAGAGGGGAAG
GAGAGGAAGAACAAAACTTATTACAAGTTTGAGAAGCTGGCCATAGACCCTAATACATGC
GAAGTGAACACAAAATACAAAGCAGTAAGAACCAGCATCTACACCAAACATCTGGAAAGG
TGGTTGAAATACTTTCCAATTGAGCAATTTCATGTCGTCGATGGAGATCGCCTCATCACG
GAACCTCTGCCAGAACTTCAGCTCGTGGAGAAGTTCCTAAATCTGCCTCCAAGGATAAGT
CAATACAATTTATACTTCAATGCTACCAGAGGGTTTTACTGCTTGCGGTTTAATATTATC
TTTAATAAGTGCCTGGCGGGCAGCAAGGGGCGCATTCATCCAGAGGTGGACCCCTCTGTC
ATTACTAAATTGCGCAAATTCTTTCATCCTTTTAATCAAAAATTTTACCAGATCACTGGG
AGGACATTGAACTGGCCCTAA
Enzyme 30 GenBank Gene ID AK289907 Link Image
Enzyme 30 GeneCard ID A8K1J2 Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 15186
Enzyme 31 Name cDNA FLJ77168, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1 (HS3ST3A1), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3A1)
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name HS3ST3A1
Enzyme 31 Protein Sequence >cDNA FLJ77168, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1 (HS3ST3A1), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3A1)
MAPPGPASALSTSAEPLSRSIFRKFLLMLCSLLTSLYVFYCLAERCQTLSGPVVGLSGGG
EEAGAPGGGVLAGGPRELAVWPAAAQRKRLLQLPQWRRRRPPAPRDDGEEAAWEEESPGL
SGGPGGSGAGSTVAEAPPGTLALLLDEGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRA
VGAEPHFFDRSYDKGLAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIV
VVRDPVTRAISDYTQTLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLR
HFPIRQMLFVSGERLISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSR
PHCLGKTKGRTHPEIDREVVRRLREFYRPFNLKFYQMTGHDFGWDG
Enzyme 31 Number of Residues 406
Enzyme 31 Molecular Weight 44900
Enzyme 31 Theoretical pI 9.98
Enzyme 31 GO Classification Not Available
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Not Available
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function Not Available
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 158257526 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID A8K7N2 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name A8K7N2_HUMAN Link Image
Enzyme 31 PDB ID 1T8U Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1221 bp
ATGGCCCCTCCGGGCCCGGCCAGTGCCCTCTCCACCTCGGCCGAGCCGCTGTCCCGCAGC
ATCTTCCGGAAGTTCTTGCTGATGCTCTGCTCCCTGCTCACGTCCCTTTACGTCTTCTAC
TGCCTGGCCGAGCGCTGCCAGACCCTGTCCGGCCCCGTCGTGGGGCTGTCCGGCGGCGGC
GAGGAGGCGGGGGCCCCTGGTGGCGGCGTCCTGGCCGGAGGCCCGAGGGAGCTGGCGGTG
TGGCCGGCGGCGGCACAGAGAAAGCGCCTCCTGCAACTGCCGCAGTGGCGGAGGCGCCGG
CCGCCCGCGCCCCGCGACGACGGCGAGGAGGCGGCCTGGGAAGAAGAGTCCCCTGGCCTG
TCAGGGGGTCCGGGCGGCTCCGGGGCCGGAAGCACCGTGGCCGAGGCCCCGCCGGGGACC
CTGGCGCTGCTCCTGGACGAAGGCAGCAAGCAGCTGCCGCAGGCCATCATCATCGGAGTG
AAGAAGGGCGGCACGCGGGCGCTGCTGGAGTTCCTGCGCGTGCACCCCGACGTGCGCGCC
GTGGGCGCCGAGCCCCACTTCTTCGACCGCAGCTACGACAAGGGCCTCGCCTGGTACCGG
GACCTGATGCCCAGAACCCTGGACGGGCAGATCACCATGGAGAAGACGCCCAGTTACTTC
GTCACGCGGGAGGCCCCCGCGCGCATCTCGGCCATGTCCAAGGACACCAAGCTCATCGTG
GTGGTGCGGGACCCGGTGACCAGGGCCATCTCGGACTACACGCAGACGCTGTCCAAGCGG
CCCGACATCCCCACCTTCGAGAGCTTGACGTTCAAAAACAGGACAGCGGGCCTCATCGAC
ACGTCGTGGAGCGCCATCCAGATCGGCATCTACGCCAAGCACCTGGAGCACTGGCTGCGC
CACTTCCCCATCCGCCAGATGCTCTTCGTGAGCGGCGAGCGGCTCATCAGCGACCCGGCC
GGGGAGCTGGGCCGCGTGCAAGACTTCCTGGGCCTCAAGAGGATCATCACGGACAAGCAC
TTCTACTTCAACAAGACCAAGGGCTTCCCCTGCCTGAAGAAGGCGGAGGGCAGCAGCCGG
CCCCATTGCCTGGGCAAGACCAAGGGCAGGACCCATCCTGAGATCGACCGCGAGGTGGTG
CGCAGGCTGCGCGAGTTCTACCGGCCTTTCAACCTCAAGTTCTACCAGATGACCGGGCAC
GACTTTGGCTGGGATGGATAA
Enzyme 31 GenBank Gene ID AK292047 Link Image
Enzyme 31 GeneCard ID A8K7N2 Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location 17
Enzyme 31 Locus 17p12-p11.2
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References Not Available
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 16469
Enzyme 32 Name cDNA FLJ90057 fis, clone HEMBA1003101, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
Enzyme 32 Synonyms
  1. SubName: cDNA FLJ90658 fis, clone PLACE1004775, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
  2. SubName: Tyrosylprotein sulfotransferase 2, isoform CRA_a
Enzyme 32 Gene Name TPST2
Enzyme 32 Protein Sequence >cDNA FLJ90057 fis, clone HEMBA1003101, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHV
EYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREK
LRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLL
MVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQ
LVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSK
WTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLK
GYFQVNQNSTSSHLGSS
Enzyme 32 Number of Residues 377
Enzyme 32 Molecular Weight 41912
Enzyme 32 Theoretical pI 9.42
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Not Available
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions
  • 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586] ALL_REAC R02586
Enzyme 32 Pfam Domain Function Not Available
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID B3KQA7 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name B3KQA7_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence Not Available
Enzyme 32 GenBank Gene ID AK074538 Link Image
Enzyme 32 GeneCard ID B3KQA7 Link Image
Enzyme 32 GenAtlas ID Not Available
Enzyme 32 HGNC ID Not Available
Enzyme 32 Chromosome Location 22
Enzyme 32 Locus 22q12.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References Not Available
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 16470
Enzyme 33 Name cDNA FLJ39504 fis, clone PROST2017203, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 1 (EC 2.8.2.23)
Enzyme 33 Synonyms
  1. SubName: Heparan sulfate (Glucosamine) 3-O-sulfotransferase 1, isoform CRA_a
Enzyme 33 Gene Name HS3ST1
Enzyme 33 Protein Sequence >cDNA FLJ39504 fis, clone PROST2017203, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 1 (EC 2.8.2.23)
MAALLLGAVLLVAQPQLVPSRPAELGQQELLRKAGTLQDDVRDGVAPNGSAQQLPQTIII
GVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSHGLGWYLSQMPFSWPHQLTVEKT
PAYFTSPKVPERVYSMNPSIRLLLILRDPSERVLSDYTQVFYNHMQKHKPYPSIEEFLVR
DGRLNVDYKALNRSLYHVHMQNWLRFFPLRHIHIVDGDRLIRDPFPEIQKVERFLKLSPQ
INASNFYFNKTKGFYCLRDSGRDRCLHESKGRAHPQVDPKLLNKLHEYFHEPNKKFFELV
GRTFDWH
Enzyme 33 Number of Residues 307
Enzyme 33 Molecular Weight 35773
Enzyme 33 Theoretical pI 9.16
Enzyme 33 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Not Available
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions
  • 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate ALL_REAC (other) R04064
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID B3KUA6 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name B3KUA6_HUMAN Link Image
Enzyme 33 PDB ID 1VKJ Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence Not Available
Enzyme 33 GenBank Gene ID AK096823 Link Image
Enzyme 33 GeneCard ID B3KUA6 Link Image
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID Not Available
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References Not Available
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 16471
Enzyme 34 Name Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a
Enzyme 34 Synonyms
  1. SubName: cDNA FLJ13661 fis, clone PLACE1011635, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 3B1
Enzyme 34 Gene Name HS3ST3B1
Enzyme 34 Protein Sequence >Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a
MGQRLSGGRSCLDVPGRLLPQPPPPPPPVRRKLALLFAMLCVWLYMFLYSCAGSCAAAPG
LLLLGSGSRAAHDPPALATAPDGTPPRLPFRAPPATPLASGKEMAEGAASPEEQSPEVPD
SPSPISSFFSGSGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKG
LAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQ
TLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERL
ISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEI
DREVVRRLREFYRPFNLKFYQMTGHDFGWD
Enzyme 34 Number of Residues 390
Enzyme 34 Molecular Weight 43325
Enzyme 34 Theoretical pI 10.14
Enzyme 34 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 34 General Function Not Available
Enzyme 34 Specific Function Not Available
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID B3KN58 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name B3KN58_HUMAN Link Image
Enzyme 34 PDB ID 1T8U Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence Not Available
Enzyme 34 GenBank Gene ID AK023723 Link Image
Enzyme 34 GeneCard ID B3KN58 Link Image
Enzyme 34 GenAtlas ID Not Available
Enzyme 34 HGNC ID Not Available
Enzyme 34 Chromosome Location 17
Enzyme 34 Locus 17p12-p11.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References Not Available
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 17072
Enzyme 35 Name Adenosine 3'-phospho 5'-phosphosulfate transporter 2
Enzyme 35 Synonyms
  1. 3'-phosphoadenosine 5'-phosphosulfate transporter
  2. PAPS transporter 2
  3. Solute carrier family 35 member B3
Enzyme 35 Gene Name SLC35B3
Enzyme 35 Protein Sequence >Adenosine 3'-phospho 5'-phosphosulfate transporter 2
MDLTQQAKDIQNITVQETNKNNSESIECSKITMDLKFNNSRKYISITVPSKTQTMSPHIK
SVDDVVVLGMNLSKFNKLTQFFICVAGVFVFYLIYGYLQELIFSVEGFKSCGWYLTLVQF
AFYSIFGLIELQLIQDKRRRIPGKTYMIIAFLTVGTMGLSNTSLGYLNYPTQVIFKCCKL
IPVMLGGVFIQGKRYNVADVSAAICMSLGLIWFTLADSTTAPNFNLTGVVLISLALCADA
VIGNVQEKAMKLHNASNSEMVLYSYSIGFVYILLGLTCTSGLGPAVTFCAKNPVRTYGYA
FLFSLTGYFGISFVLALIKIFGALIAVTVTTGRKAMTIVLSFIFFAKPFTFQYVWSGLLV
VLGIFLNVYSKNMDKIRLPSLYDLINKSVEARKSRTLAQTV
Enzyme 35 Number of Residues 401
Enzyme 35 Molecular Weight 44592.3
Enzyme 35 Theoretical pI 9.58
Enzyme 35 GO Classification
Function
Process
  • establishment of localization
  • transmembrane transport
  • transport
Component
Enzyme 35 General Function Involved in transmembrane transport
Enzyme 35 Specific Function Mediates the transport of adenosine 3'-phospho 5'- phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Compensates for the insufficient expression of SLC35B2/PAPST1 during the synthesis of sulfated glycoconjugates in the colon
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 78-98 114-134 147-167 170-190 196-216 223-243 267-287 298-317 324-346 349-369
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 90991129 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9H1N7 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name S35B3_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1206 bp
ATGGACTTGACACAGCAAGCAAAAGACATACAGAACATAACAGTCCAGGAAACCAACAAA
AATAACTCTGAAAGCATTGAATGCAGCAAAATAACAATGGATCTCAAGTTCAACAATTCC
AGGAAATATATTTCTATCACTGTGCCATCCAAAACCCAAACAATGTCACCACACATCAAG
TCAGTTGACGACGTTGTGGTACTTGGCATGAATCTCAGCAAGTTTAACAAACTTACTCAG
TTTTTCATATGTGTTGCTGGAGTTTTTGTATTTTACCTAATTTATGGGTATTTACAGGAA
TTAATATTTTCAGTGGAGGGTTTTAAGTCCTGTGGCTGGTACCTTACCTTAGTGCAGTTT
GCCTTTTACTCCATATTTGGCCTAATAGAACTTCAGCTTATTCAGGACAAAAGGAGGAGA
ATACCAGGAAAAACCTACATGATAATAGCTTTTCTAACTGTGGGTACTATGGGGTTATCA
AACACTTCCTTGGGCTACCTGAATTACCCTACCCAAGTCATCTTCAAGTGCTGCAAATTG
ATTCCTGTTATGCTAGGAGGAGTTTTTATTCAAGGAAAGCGTTATAATGTTGCAGATGTG
TCTGCTGCCATATGTATGAGCCTTGGCCTGATATGGTTTACCCTCGCTGACAGCACAACT
GCACCAAATTTCAACCTGACGGGTGTGGTGCTTATTTCCCTGGCACTATGTGCAGATGCC
GTCATTGGAAATGTTCAAGAGAAAGCTATGAAACTTCATAATGCTTCTAATTCTGAAATG
GTATTGTATTCGTATTCAATTGGTTTTGTATACATTTTACTGGGATTGACATGCACTAGT
GGATTAGGCCCTGCAGTAACATTTTGTGCAAAGAATCCAGTTCGGACCTATGGTTATGCG
TTCCTTTTTTCCCTCACTGGATATTTTGGAATCTCCTTTGTTCTGGCTTTGATTAAAATT
TTTGGTGCACTTATTGCTGTAACAGTGACAACAGGAAGAAAAGCAATGACCATTGTACTT
TCGTTTATATTCTTTGCTAAACCATTCACGTTTCAGTATGTATGGTCTGGTTTGTTAGTT
GTCCTTGGTATATTTCTTAATGTTTACAGCAAAAATATGGATAAAATAAGACTACCATCA
CTGTATGATTTGATAAACAAATCAGTGGAAGCAAGAAAGTCAAGGACGCTGGCACAGACT
GTATAG
Enzyme 35 GenBank Gene ID AB231931 Link Image
Enzyme 35 GeneCard ID SLC35B3 Link Image
Enzyme 35 GenAtlas ID SLC35B3 Link Image
Enzyme 35 HGNC ID HGNC:21601 Link Image
Enzyme 35 Chromosome Location 6
Enzyme 35 Locus 6p24.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Kamiyama S, Sasaki N, Goda E, Ui-Tei K, Saigo K, Narimatsu H, Jigami Y, Kannagi R, Irimura T, Nishihara S: Molecular cloning and characterization of a novel 3'-phosphoadenosine 5'-phosphosulfate transporter, PAPST2. J Biol Chem. 2006 Apr 21;281(16):10945-53. Epub 2006 Feb 21. [PubMed Link Image]
  2. 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]
  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. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available