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Human Metabolome Database Version 2.5

 

Showing metabocard for Adenosine 3',5'-diphosphate (HMDB00061)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:39
Accession Number HMDB00061
Secondary Accession Numbers HMDB01468
Common Name Adenosine 3',5'-diphosphate
Description Adenosine 3', 5'-diphosphate or PAP is a nucleotide that is closely related to ADP. It has two phosphate groups attached to the 5' and 3' positions of the pentose sugar ribose (instead of pyrophosphoric acid at the 5' position, as found in ADP), and the nucleobase adenine. PAP is converted to PAPS by Sulfotransferase and then back to PAP after the sulfotransferase reaction. Sulfotransferase (STs) catalyze the transfer reaction of the sulfate group from the ubiquitous donor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to an acceptor group of numerous substrates. This reaction, often referred to as sulfuryl transfer, sulfation, or sulfonation, is widely observed from bacteria to humans and plays a key role in various biological processes such as cell communication, growth and development, and defense. PAP also appears to a role in bipolar depression. Phosphatases converting 3'-phosphoadenosine 5'-phosphate (PAP) into adenosine 5'-phosphate are of fundamental importance in living cells as the accumulation of PAP is toxic to several cellular systems. These enzymes are lithium-sensitive and we have characterized a human PAP phosphatase as a potential target of lithium therapy.
Synonyms
  1. 3,5-Diphosphoadenosine
  2. 3,5-ADP
  3. 3-Phosphoadenosine 5-phosphate
  4. 3'-Phosphoryl-AMP
  5. 5-(dihydrogen phosphate) 3-Adenylate
  6. 5-(dihydrogen phosphate)3'-Adenylic acid
  7. Adenosine 3,5-bis
  8. Adenosine 3,5-bisphosphate
  9. Adenosine 3,5-diphosphic acid
  10. adenosine 3',5'-bisphosphate
Chemical IUPAC Name [5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxy-oxolan-2-yl]methoxyphosphonic acid
Chemical Formula C10H15N5O10P2
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
  • 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 427.201
Monoisotopic Molecular Weight 427.029419
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC(COP(O)(O)=O)C(OP(O)(O)=O)C1O
KEGG Compound ID C00054 Link Image
BioCyc ID 3-5-ADP Link Image
BiGG ID 33684 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00061 Link Image
Metagene Link HMDB00061 Link Image
METLIN ID Not Available
PubChem Compound 159296 Link Image
PubChem Substance 836671 Link Image
ChEBI ID 17985 Link Image
CAS Registry Number 1053-73-2
InChI Identifier InChI=1/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-6(16)7(25-27(20,21)22)4(24-10)1-23-26(17,18)19/h2-4,6-7,10,16H,1H2,(H2,11,12,13)(H2,17,18,19)(H2,20,21,22)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Tsunako, Mitsutomo; Kotone, Akira. Preparation of nucleoside-2',5'- and 3',5'-diphosphoric acids. Jpn. Kokai Tokkyo Koho (1991), 13 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility 614.5 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 3.33 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.63 [Predicted by ALOGPS]; -4.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • golgi apparatus
Biofluid Location
  • Cellular Cytoplasm
Tissue Location
Tissue References
Brain —
Liver —
Concentrations (Normal)
Biofluid Cellular Cytoplasm
Value 137 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Traut TW: Physiological concentrations of purines and pyrimidines. Mol Cell Biochem. 1994 Nov 9;140(1):1-22. [PubMed Link Image]
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. Lewis AJ, Otake Y, Walle UK, Walle T: Sulphonation of N-hydroxy-2-acetylaminofluorene by human dehydroepiandrosterone sulphotransferase. Xenobiotica. 2000 Mar;30(3):253-61. [PubMed Link Image]
  2. Gasmi L, McLennan AG: The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem J. 2001 Jul 1;357(Pt 1):33-8. [PubMed Link Image]
  3. Leonidas DD, Chavali GB, Oikonomakos NG, Chrysina ED, Kosmopoulou MN, Vlassi M, Frankling C, Acharya KR: High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors. Protein Sci. 2003 Nov;12(11):2559-74. [PubMed Link Image]
  4. Turner NA, Moake JL, McIntire LV: Blockade of adenosine diphosphate receptors P2Y(12) and P2Y(1) is required to inhibit platelet aggregation in whole blood under flow. Blood. 2001 Dec 1;98(12):3340-5. [PubMed Link Image]
  5. Traut TW: Physiological concentrations of purines and pyrimidines. Mol Cell Biochem. 1994 Nov 9;140(1):1-22. [PubMed Link Image]
  6. Russo N, Acharya KR, Vallee BL, Shapiro R: A combined kinetic and modeling study of the catalytic center subsites of human angiogenin. Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):804-8. [PubMed 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. Galactosylceramide sulfotransferase
  6. Estrogen sulfotransferase
  7. Heparan sulfate glucosamine 3-O-sulfotransferase 2
  8. Sulfotransferase family cytosolic 2B member 1
  9. Monoamine-sulfating phenol sulfotransferase
  10. Carbohydrate sulfotransferase 7
  11. N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
  12. cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
  13. Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2
  14. cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform C
  15. cDNA FLJ75927, highly similar to Homo sapiens carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11), mRNA (Carbohydrate (Chondroitin 4) sulfotransferase 11, isoform CRA_a)
  16. Carbohydrate (Chondroitin 4) sulfotransferase 12
  17. Tyrosylprotein sulfotransferase 1 (Tyrosylprotein sulfotransferase 1, isoform CRA_a)
  18. cDNA FLJ76340, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 5 (HS3ST5), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 5)
  19. cDNA FLJ77168, highly similar to Homo sapiens heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1 (HS3ST3A1), mRNA (Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3A1)
  20. cDNA FLJ90057 fis, clone HEMBA1003101, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
  21. cDNA FLJ39504 fis, clone PROST2017203, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 1 (EC 2.8.2.23)
  22. Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a
Enzyme 1 [top]
Enzyme 1 ID 5351
Enzyme 1 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 1 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. 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 104925
Enzyme 1 Theoretical pI 7.14
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 1 General Function Not Available
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
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 189650 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 >2622 bp 
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 1 GenBank Gene ID M57736 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
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/nucleotide pyrophosphatase 3
  3. Phosphodiesterase I beta
  4. PD-Ibeta
  5. CD203c antigen[Includes: Alkaline phosphodiesterase I
  6. NPPase]
Enzyme 2 Gene Name ENPP3
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Enzyme 2 Number of Residues 875
Enzyme 2 Molecular Weight 100097
Enzyme 2 Theoretical pI 6.55
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
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
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-38
Enzyme 2 Transmembrane Regions Not Available
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. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5519
Enzyme 3 Name Carbohydrate sulfotransferase 3
Enzyme 3 Synonyms
  1. Chondroitin 6- sulfotransferase
  2. Chondroitin 6-O-sulfotransferase 1
  3. C6ST-1
  4. C6ST
  5. Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O- sulfotransferase 0
  6. 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 54707
Enzyme 3 Theoretical pI 8.75
Enzyme 3 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 3 General Function Not Available
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
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-38
Enzyme 3 Transmembrane Regions Not Available
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 10
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]
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. C4ST3
  4. C4ST- 3
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 38920
Enzyme 4 Theoretical pI 11.00
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
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
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-26
Enzyme 4 Transmembrane Regions Not Available
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 5554
Enzyme 5 Name Galactosylceramide sulfotransferase
Enzyme 5 Synonyms
  1. GalCer sulfotransferase
  2. Cerebroside sulfotransferase
  3. 3'- phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
  4. 3'- phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase
Enzyme 5 Gene Name GAL3ST1
Enzyme 5 Protein Sequence >Galactosylceramide sulfotransferase 
MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPE
AVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTF
FARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPV
VPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHIL
EVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAW
NMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDE
AMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDF
LRW
Enzyme 5 Number of Residues 423
Enzyme 5 Molecular Weight 48765
Enzyme 5 Theoretical pI 8.78
Enzyme 5 GO Classification
Function
  • catalytic activity
  • galactose 3-O-sulfotransferase activity
  • galactosylceramide sulfotransferase activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
  • Golgi apparatus
  • cell
  • integral to membrane
  • intracellular membrane-bound organelle
  • intrinsic to membrane
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the nonreducing 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 5 Pathways
Enzyme 5 Reactions
  • 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + galactosylceramidesulfate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-33
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1871141 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q99999 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name G3ST1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID D88667 Link Image
Enzyme 5 GeneCard ID GAL3ST1 Link Image
Enzyme 5 GenAtlas ID GAL3ST1 Link Image
Enzyme 5 HGNC ID HGNC:24240 Link Image
Enzyme 5 Chromosome Location 22
Enzyme 5 Locus 22q12.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5582
Enzyme 6 Name Estrogen sulfotransferase
Enzyme 6 Synonyms
  1. Sulfotransferase, estrogen- preferring
  2. EST-1
Enzyme 6 Gene Name SULT1E1
Enzyme 6 Protein Sequence >Estrogen sulfotransferase 
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMI
YKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEK
DCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWE
KGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYT
TLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
Enzyme 6 Number of Residues 294
Enzyme 6 Molecular Weight 35127
Enzyme 6 Theoretical pI 6.61
Enzyme 6 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 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 6 Pathways
Enzyme 6 Reactions
  • 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 488283 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P49888 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ST1E1_HUMAN Link Image
Enzyme 6 PDB ID 1G3M Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >885 bp 
ATGAATTCTGAACTTGACTATTATGAAAAGTTTGAAGAAGTCCATGGGATTCTAATGTAT
AAAGATTTTGTCAAATATTGGGATAATGTGGAAGCGTTCCAGGCAAGACCAGATGATCTT
GTCATTGCCACCTACCCTAAATCTGGTACAACCTGGGTTAGTGAAATTGTGTATATGATC
TATAAAGAGGGTGATGTGGAAAAGTGCAAAGAAGATGTAATTTTTAATCGAATACCTTTC
CTGGAATGCAGAAAAGAAAACCTCATGAATGGAGTAAAACAATTAGATGAGATGAATTCT
CCTAGAATTGTGAAGACTCATTTGCCACCTGAACTTCTTCCTGCCTCATTTTGGGAAAAG
GATTGTAAGATAATCTATCTTTGCCGGAATGCAAAGGATGTGGCTGTTTCCTTTTATTAT
TTCTTTCTAATGGTGGCTGGTCATCCAAATCCTGGATCCTTTCCAGAGTTTGTGGAGAAA
TTCATGCAAGGACAGGTTCCTTATGGTTCCTGGTATAAACATGTAAAATCTTGGTGGGAA
AAGGGAAAGAGTCCACGTGTACTATTTCTTTTCTACGAAGACCTGAAAGAGGATATCAGA
AAAGAGGTGATAAAATTGATACATTTCCTGGAAAGGAAGCCATCAGAGGAGCTTGTGGAC
AGGATTATACATCATACTTCGTTCCAAGAGATGAAGAACAATCCATCCACAAATTACACA
ACACTGCCAGACGAAATTATGAACCAGAAATTGTCGCCCTTCATGAGAAAGGGAATTACA
GGAGACTGGAAAAATCACTTTACAGTAGCCCTGAATGAAAAATTTGATAAACATTATGAG
CAGCAAATGAAGGAATCTACACTGAAGTTTCGAACTGAGATCTAA
Enzyme 6 GenBank Gene ID U08098 Link Image
Enzyme 6 GeneCard ID SULT1E1 Link Image
Enzyme 6 GenAtlas ID SULT1E1 Link Image
Enzyme 6 HGNC ID HGNC:11377 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4q13.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5588
Enzyme 7 Name Heparan sulfate glucosamine 3-O-sulfotransferase 2
Enzyme 7 Synonyms
  1. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2
  2. Heparan sulfate 3-O-sulfotransferase 2
  3. h3-OST-2
Enzyme 7 Gene Name HS3ST2
Enzyme 7 Protein Sequence >Heparan sulfate glucosamine 3-O-sulfotransferase 2 
MAYRVLGRAGPPQPRRARRLLFAFTLSLSCTYLCYSFLCCCDDLGRSRLLGAPRCLRGPS
AGGQKLLQKSRPCDPSGPTPSEPSAPSAPAAAVPAPRLSGSNHSGSPKLGTKRLPQALIV
GVKKGGTRAVLEFIRVHPDVRALGTEPHFFDRNYGRGLDWYRSLMPRTLESQITLEKTPS
YFVTQEAPRRIFNMSRDTKLIVVVRNPVTRAISDYTQTLSKKPDIPTFEGLSFRNRTLGL
VDVSWNAIRIGMYVLHLESWLQYFPLAQIHFVSGERLITDPAGEMGRVQDFLGIKRFITD
KHFYFNKTKGFPCLKKTESSLLPRCLGKSKGRTHVQIDPEVIDQLREFYRPYNIKFYETV
GQDFRWE
Enzyme 7 Number of Residues 367
Enzyme 7 Molecular Weight 41501
Enzyme 7 Theoretical pI 10.39
Enzyme 7 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 7 General Function Not Available
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 GlcA2S-GlcNS. 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
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-36
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4835719 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y278 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name OST2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1104 bp 
ATGGCCTATAGGGTCCTGGGCCGCGCGGGGCCACCTCAGCCGCGGAGGGCGCGCAGGCTG
CTCTTCGCCTTCACGCTCTCGCTCTCCTGCACTTACCTGTGTTACAGCTTCCTGTGCTGC
TGCGACGACCTGGGTCGGAGCCGCCTCCTCGGCGCGCCTCGCTGCCTCCGCGGCCCCAGC
GCGGGCGGCCAGAAACTTCTCCAGAAGTCCCGCCCCTGTGATCCCTCCGGGCCGACGCCC
AGCGAGCCCAGCGCTCCCAGCGCGCCCGCCGCCGCCGTGCCCGCCCCTCGCCTCTCCGGT
TCCAACCACTCCGGCTCACCCAAGCTGGGTACCAAGCGGTTGCCCCAAGCCCTCATTGTG
GGCGTGAAGAAGGGGGGCACCCGGGCCGTGCTGGAGTTTATCCGAGTACACCCGGACGTG
CGGGCCTTGGGCACGGAACCCCACTTCTTTGACAGGAACTACGGCCGCGGGCTGGATTGG
TACAGGAGCCTGATGCCCAGGACCCTCGAGAGCCAGATCACGCTGGAGAAGACGCCCAGC
TACTTTGTCACTCAAGAGGCTCCTCGACGCATCTTCAACATGTCCCGAGACACCAAGCTG
ATCGTGGTTGTGCGGAACCCTGTGACCCGTGCCATCTCTGATTACACGCAGACACTCTCC
AAGAAGCCCGACATCCCGACCTTTGAGGGCCTCTCCTTCCGCAACCGCACCCTGGGCCTG
GTGGACGTGTCGTGGAACGCCATCCGCATCGGCATGTACGTGCTGCACCTGGAGAGCTGG
CTGCAGTACTTCCCGCTAGCTCAGATTCACTTCGTCAGTGGCGAGCGACTCATCACTGAC
CCGGCCGGCGAGATGGGGCGAGTCCAGGACTTCCTGGGCATTAAGAGATTCATCACGGAC
AAGCACTTCTATTTCAACAAGACCAAAGGATTCCCTTGCTTGAAAAAAACAGAATCGAGC
CTCCTGCCTCGATGCTTGGGCAAATCAAAAGGGAGAACTCATGTACAGATTGATCCTGAA
GTGATAGACCAGCTCCGAGAATTTTATAGACCGTATAATATCAAATTTTATGAAACCGTT
GGGCAGGACTTCAGGTGGGAATAA
Enzyme 7 GenBank Gene ID AF105374 Link Image
Enzyme 7 GeneCard ID HS3ST2 Link Image
Enzyme 7 GenAtlas ID HS3ST2 Link Image
Enzyme 7 HGNC ID HGNC:5195 Link Image
Enzyme 7 Chromosome Location 16
Enzyme 7 Locus 16p12
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. 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. 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 5591
Enzyme 8 Name Sulfotransferase family cytosolic 2B member 1
Enzyme 8 Synonyms
  1. Sulfotransferase 2B1
  2. Alcohol sulfotransferase
  3. Hydroxysteroid sulfotransferase 2
Enzyme 8 Gene Name SULT2B1
Enzyme 8 Protein Sequence >Sulfotransferase family cytosolic 2B member 1 
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS
Enzyme 8 Number of Residues 365
Enzyme 8 Molecular Weight 41308
Enzyme 8 Theoretical pI 5.05
Enzyme 8 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 8 General Function Not Available
Enzyme 8 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 8 Pathways
Enzyme 8 Reactions
  • 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1923291 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O00204 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ST2B1_HUMAN Link Image
Enzyme 8 PDB ID 1Q1Q Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1053 bp 
ATGGCGTCTCCCCCACCTTTCCACAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAG
GGCGTCCCCTTCCCCGTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACC
CAAGATGTGCGGGACGACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGG
ATGATCGAGATCATCTGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTG
CCCATCTGGGAGCGGGCACCCTGGTGTGAGACCATTGTGGGTGCTTTCAGCCTCCCGGAC
CAGTACAGCCCCCGCCTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTC
TTCAGCTCCAAGGCCAAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCC
CTCTATCATTACTCCAAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTC
CTGAGGGACTTCCTCAAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGC
TGGCTTCGGATGAAGGGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAG
GACTTACAGGGCTCCGTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAG
GCACTGGGCTCCGTCGTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCC
AACTACACGCTGCTGCCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAA
GGGGTCTGCGGCGACTGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGT
GCCTACCGCAAGCAGATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAG
GATGGCAGCCCAGATCCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCC
AACACCAGCCTGGAGCGTGAGCCCAGACCCAACTCCAGCCCCAACCCCAGCCCCGGCCAG
GCCTCTGAGACCCCGCACCCACGACCCTCATAA
Enzyme 8 GenBank Gene ID U92314 Link Image
Enzyme 8 GeneCard ID SULT2B1 Link Image
Enzyme 8 GenAtlas ID SULT2B1 Link Image
Enzyme 8 HGNC ID HGNC:11459 Link Image
Enzyme 8 Chromosome Location 19
Enzyme 8 Locus 19q13.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. 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]
  3. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5592
Enzyme 9 Name Monoamine-sulfating phenol sulfotransferase
Enzyme 9 Synonyms
  1. Aryl sulfotransferase 1A3
  2. Sulfotransferase, monoamine-preferring
  3. M-PST
  4. Thermolabile phenol sulfotransferase
  5. TL-PST
  6. Placental estrogen sulfotransferase
  7. Catecholamine-sulfating phenol sulfotransferase
  8. HAST3
Enzyme 9 Gene Name SULT1A3
Enzyme 9 Protein Sequence >Monoamine-sulfating phenol sulfotransferase 
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDM
IYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLD
QKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNY
TTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
Enzyme 9 Number of Residues 295
Enzyme 9 Molecular Weight 34197
Enzyme 9 Theoretical pI 5.88
Enzyme 9 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Catalyzes the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs
Enzyme 9 Pathways
Enzyme 9 Reactions
  • 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 306457 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P50224 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ST1A3_HUMAN Link Image
Enzyme 9 PDB ID 1CJM Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >888 bp 
ATGGAGCTGATCCAGGACACCTCCCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAAGCCCGACCTGATGAC
CTGCTCATCAACACCTACCCCAAGTCTGGCACCACCTGGGTGAGCCAGATACTGGACATG
ATCTACCAGGGCGGCGACCTAGAGAAGTGTAACCGGGCTCCCATCTACGTACGGGTGCCC
TTCCTTGAGGTCAATGATCCAGGGGAACCCTCAGGGCTGGAGACTCTGAAAGACACACCG
CCCCCACGGCTCATCAAGTCACACCTGCCCCTGGCTCTGCTCCCTCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGAAACCCAAAGGACGTGGCGGTCTCCTACTAC
CATTTCCACCGTATGGAAAAGGCGCACCCTGAGCCTGGGACCTGGGACAGCTTCCTGGAA
AAGTTCATGGCTGGAGAAGTGTCCTACGGGTCCTGGTACCAGCACGTGCAGGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACCATG
GACTTCATGGTTCAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCCCCAGGAGCTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Enzyme 9 GenBank Gene ID L19956 Link Image
Enzyme 9 GeneCard ID SULT1A3 Link Image
Enzyme 9 GenAtlas ID SULT1A3 Link Image
Enzyme 9 HGNC ID HGNC:11455 Link Image
Enzyme 9 Chromosome Location 16
Enzyme 9 Locus 16p11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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. 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]
  9. 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]
  10. 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5989
Enzyme 10 Name Carbohydrate sulfotransferase 7
Enzyme 10 Synonyms
  1. Chondroitin 6-sulfotransferase 2
  2. C6ST-2
  3. N-acetylglucosamine 6-O- sulfotransferase 1
  4. GlcNAc6ST-4
  5. Galactose/N-acetylglucosamine/N- acetylglucosamine 6-O-sulfotransferase 5
  6. GST-5
Enzyme 10 Gene Name CHST7
Enzyme 10 Protein Sequence >Carbohydrate sulfotransferase 7 
MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKGAEHCPGLQRSLGVWSLEAA
AAGEREQGAEARAAEEGGANQSPRFPSNLSGAVGEAVSREKQHIYVHATWRTGSSFLGEL
FNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAAR
APDTANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDTACERSCPPVAIRALEAE
CRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQ
VLRTRQRGDRFHRVLLAHGVGARPGGQSRALPAAPRADFFLTGALEVICEAWLRDLLFAR
GAPAWLRRRYLRLRYEDLVRQPRAQLRRLLRFSGLRALAALDAFALNMTRGAAYGADRPF
HLSARDAREAVHAWRERLSREQVRQVEAACAPAMRLLAYPRSGEEGDAEQPREGETPLEM
DADGAT
Enzyme 10 Number of Residues 486
Enzyme 10 Molecular Weight 54267
Enzyme 10 Theoretical pI 9.96
Enzyme 10 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 10 General Function Not Available
Enzyme 10 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 10 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 10 Reactions
  • 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-34
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 10336539 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9NS84 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name CHST7_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 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
GAGCAGGTGCGCCAGGTGGAGGCCGCCTGCGCTCCAGCCATGCGTCTGCTCGCCTACCCT
CGCAGCGGAGAGGAGGGCGACGCGGAGCAGCCCAGGGAAGGGGAGACGCCGCTGGAGATG
GATGCCGACGGCGCCACGTAG
Enzyme 10 GenBank Gene ID AB040711 Link Image
Enzyme 10 GeneCard ID CHST7 Link Image
Enzyme 10 GenAtlas ID CHST7 Link Image
Enzyme 10 HGNC ID HGNC:13817 Link Image
Enzyme 10 Chromosome Location X
Enzyme 10 Locus Xp11.23
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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]
  2. 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]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 12871
Enzyme 11 Name N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
Enzyme 11 Synonyms
  1. GalNAc4S-6ST
  2. B-cell RAG-associated gene protein
  3. hBRAG
Enzyme 11 Gene Name GALNAC4S6ST
Enzyme 11 Protein Sequence >N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase 
MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEV
RTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNP
SLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQE
LHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHL
AHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRL
RDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTF
FYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVT
EALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLED
HASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFY
RPFNARLAQVLADEAFAWKTT
Enzyme 11 Number of Residues 561
Enzyme 11 Molecular Weight 64927
Enzyme 11 Theoretical pI Not Available
Enzyme 11 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 11 General Function Not Available
Enzyme 11 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 nonreducing 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 11 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
  • Glycan structures - biosynthesis 1 (map01030 Link Image)
Enzyme 11 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] ALL_REAC R02181 R07288
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 81-101
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3169791 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q7LFX5 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ST4S6_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AF026477 Link Image
Enzyme 11 GeneCard ID Not Available
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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. 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]
  3. 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]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 13112
Enzyme 12 Name cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
Enzyme 12 Synonyms
  1. PIP gene
  2. 3'(2', 5'-bisphosphate nucleotidase 1, isoform CRA_a
Enzyme 12 Gene Name BPNT1
Enzyme 12 Protein Sequence >cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase 
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
Enzyme 12 Number of Residues 308
Enzyme 12 Molecular Weight 33393
Enzyme 12 Theoretical pI 5.41
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function Not Available
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 158257318 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID A8K7C8 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name A8K7C8_HUMAN Link Image
Enzyme 12 PDB ID 1JP4 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK291943 Link Image
Enzyme 12 GeneCard ID A8K7C8 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15180
Enzyme 13 Name Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name SULT1A2
Enzyme 13 Protein Sequence >Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2 
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNY
TTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
Enzyme 13 Number of Residues 295
Enzyme 13 Molecular Weight 34311
Enzyme 13 Theoretical pI 7.32
Enzyme 13 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 109731387 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q14CJ7 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q14CJ7_HUMAN Link Image
Enzyme 13 PDB ID 1LS6 Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >888 bp 
ATGGAGCTGATCCAGGACATCTCTCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGCGGTGACCTGGAAAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGTCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAAACACACCA
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCGGTTTCCTACTAC
CACTTCTACCACATGGCCAAAGTGTACCCTCACCCTGGGACCTGGGAAAGCTTCCTGGAG
AAGTTCATGGCTGGAGAAGTGTCCTATGGGTCCTGGTACCAGCACGTGCAAGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACTGTG
GACCTCATGGTTGAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCGCCGGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
Enzyme 13 GenBank Gene ID BC113727 Link Image
Enzyme 13 GeneCard ID Q14CJ7 Link Image
Enzyme 13 GenAtlas ID SULT1A2 Link Image
Enzyme 13 HGNC ID HGNC:11454 Link Image
Enzyme 13 Chromosome Location 16
Enzyme 13 Locus 16p12.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 15181
Enzyme 14 Name cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform C
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name SULT2A1
Enzyme 14 Protein Sequence >cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA (Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform CRA_a) 
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
Enzyme 14 Number of Residues 285
Enzyme 14 Molecular Weight 33780
Enzyme 14 Theoretical pI 5.76
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 158259783 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID A8K015 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A8K015_HUMAN Link Image
Enzyme 14 PDB ID 1OV4 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >858 bp 
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAACGGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
Enzyme 14 GenBank Gene ID AK289380 Link Image
Enzyme 14 GeneCard ID A8K015 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location 19
Enzyme 14 Locus 19q13.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 15182
Enzyme 15 Name cDNA FLJ75927, highly similar to Homo sapiens carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11), mRNA (Carbohydrate (Chondroitin 4) sulfotransferase 11, isoform CRA_a)
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name CHST11
Enzyme 15 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 15 Number of Residues 352
Enzyme 15 Molecular Weight 41555
Enzyme 15 Theoretical pI 9.07
Enzyme 15 GO Classification Not Available
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function Not Available
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 158255282 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID A8K4F8 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name A8K4F8_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1059 bp 
ATGAAGCCAGCGCTGCTGGAAGTGATGAGGATGAACAGAATCTGCCGGATGGTGCTGGCC
ACTTGCTTGGGATCCTTTATCCTGGTCATCTTCTATTTCCAAAGTATGTTGCACCCAGTC
ATGCGGAGGAATCCCTTTGGTGTGGACATCTGCTGCCGGAAGGGGTCCCGAAGCCCCCTG
CAGGAACTCTACAACCCAATCCAGCTGGAGCTCTCAAACACTGCTGTCCTGCACCAGATG
CGGCGGGACCAGGTGACAGACACGTGCCGAGCCAACAGCGCCACAAGCCGTAAGCGGAGG
GTGCTGACCCCCAACGACCTGAAGCACTTGGTGGTGGATGAGGACCACGAGCTCATCTAC
TGCTACGTGCCCAAGGTGGCCTGCACCAACTGGAAGCGGCTCATGATGGTCCTGACCGGG
CGGGGGAAGTACAGCGACCCCATGGAGATCCCGGCCAACGAGGCACACGTCTCCGCCAAC
CTGAAGACCCTGAACCAGTACAGCATCCCAGAAATCAACCACCGCTTGAAAAGCTACATG
AAGTTCCTGTTTGTCCGGGAGCCCTTCGAGAGGCTAGTGTCCGCCTACCGCAACAAGTTC
ACCCAGAAGTACAACATCTCCTTCCACAAGCGGTACGGCACCAAGATCATCAAACGCCAG
CGGAAGAACGCCACCCAGGAGGCCCTGCGCAAAGGGGACGATGTCAAATTCGAGGAGTTT
GTGGCCTATCTCATCGACCCACACACCCAGCGGGAGGAGCCTTTCAACGAACACTGGCAA
ACCGTCTACTCACTCTGCCATCCCTGCCACATCCACTATGACCTCGTGGGCAAGTACGAG
ACACTGGAAGAGGATTCTAATTACGTCCTGCAGCTGGCAGGAGTGGGCAGCTACCTGAAG
TTCCCCACCTATGCAAAGTCTACGAGAACTACTGATGAAATGACCACAGAATTCTTCCAG
AACATCAGCTCAGAGCACCAAACGCAGCTGTACGAAGTCTACAAACTCGATTTTTTAATG
TTCAATTACTCAGTGCCAAGCTACCTGAAATTGGAATAA
Enzyme 15 GenBank Gene ID AK290923 Link Image
Enzyme 15 GeneCard ID A8K4F8 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location 12
Enzyme 15 Locus 12q
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 15183
Enzyme 16 Name Carbohydrate (Chondroitin 4) sulfotransferase 12
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name CHST12
Enzyme 16 Protein Sequence >Carbohydrate (Chondroitin 4) sulfotransferase 12 
MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDREL
TADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQ
QAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKR
VMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTK
FLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSF
ANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDR
QLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
Enzyme 16 Number of Residues 414
Enzyme 16 Molecular Weight 48415
Enzyme 16 Theoretical pI 9.69
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID A4D1Z9 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name A4D1Z9_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID CH236953 Link Image
Enzyme 16 GeneCard ID A4D1Z9 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15184
Enzyme 17 Name Tyrosylprotein sulfotransferase 1 (Tyrosylprotein sulfotransferase 1, isoform CRA_a)
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name TPST1
Enzyme 17 Protein Sequence >Tyrosylprotein sulfotransferase 1 (Tyrosylprotein sulfotransferase 1, isoform CRA_a) 
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPVKLESTRTTVRTGLDLKAN
KTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKE
KIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFL
LMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYE
QLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALS
KWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKIIENTRRVYKGEFQLPDFL
KEKPQTEQVE
Enzyme 17 Number of Residues 370
Enzyme 17 Molecular Weight 42189
Enzyme 17 Theoretical pI 9.49
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function Not Available
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 A4D2M0 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name A4D2M0_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID CH236961 Link Image
Enzyme 17 GeneCard ID A4D2M0 Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15185
Enzyme 18 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 18 Synonyms Not Available
Enzyme 18 Gene Name HS3ST5
Enzyme 18 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 18 Number of Residues 346
Enzyme 18 Molecular Weight 40409
Enzyme 18 Theoretical pI 10.31
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158260837 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8K1J2 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8K1J2_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1041 bp 
ATGCTATTCAAACAGCAGGCGTGGCTGAGACAGAAGCTCCTGGTGCTGGGAAGCCTTGCC
GTTGGGAGTCTCCTGTATCTAGTCGCCAGAGTTGGGAGCTTGGATAGGCTACAACCCATT
TGCCCCATTGAAGGTCGACTGGGTGGAGCCCGCACTCAGGCTGAATTCCCACTTCGCGCC
CTGCAGTTTAAGCGTGGCCTGCTGCACGAGTTCCGGAAGGGCAACGCTTCCAAGGAGCAG
GTTCGCCTCCATGACCTGGTCCAGCAGCTCCCCAAGGCCATTATCATTGGGGTGAGGAAA
GGAGGCACAAGGGCCCTGCTTGAAATGCTGAACCTACATCCGGCAGTAGTCAAAGCCTCT
CAAGAAATCCACTTTTTTGATAATGATGAGAATTATGGTAAGGGCATTGAGTGGTATAGG
AAAAAGATGCCTTTTTCCTACCCTCAGCAAATCACAATTGAAAAGAGCCCAGCATATTTT
ATCACAGAGGAGGTTCCAGAAAGGATTTACAAAATGAACTCATCCATCAAGTTGTTGATC
ATTGTCAGGGAGCCAACCACAAGAGCTATTTCTGATTATACTCAGGTGCTAGAGGGGAAG
GAGAGGAAGAACAAAACTTATTACAAGTTTGAGAAGCTGGCCATAGACCCTAATACATGC
GAAGTGAACACAAAATACAAAGCAGTAAGAACCAGCATCTACACCAAACATCTGGAAAGG
TGGTTGAAATACTTTCCAATTGAGCAATTTCATGTCGTCGATGGAGATCGCCTCATCACG
GAACCTCTGCCAGAACTTCAGCTCGTGGAGAAGTTCCTAAATCTGCCTCCAAGGATAAGT
CAATACAATTTATACTTCAATGCTACCAGAGGGTTTTACTGCTTGCGGTTTAATATTATC
TTTAATAAGTGCCTGGCGGGCAGCAAGGGGCGCATTCATCCAGAGGTGGACCCCTCTGTC
ATTACTAAATTGCGCAAATTCTTTCATCCTTTTAATCAAAAATTTTACCAGATCACTGGG
AGGACATTGAACTGGCCCTAA
Enzyme 18 GenBank Gene ID AK289907 Link Image
Enzyme 18 GeneCard ID A8K1J2 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 15186
Enzyme 19 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 19 Synonyms Not Available
Enzyme 19 Gene Name HS3ST3A1
Enzyme 19 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 19 Number of Residues 406
Enzyme 19 Molecular Weight 44900
Enzyme 19 Theoretical pI 9.98
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function Not Available
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 158257526 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID A8K7N2 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name A8K7N2_HUMAN Link Image
Enzyme 19 PDB ID 1T8U Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 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 19 GenBank Gene ID AK292047 Link Image
Enzyme 19 GeneCard ID A8K7N2 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 17
Enzyme 19 Locus 17p12-p11.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16469
Enzyme 20 Name cDNA FLJ90057 fis, clone HEMBA1003101, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
Enzyme 20 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 20 Gene Name TPST2
Enzyme 20 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 20 Number of Residues 377
Enzyme 20 Molecular Weight 41912
Enzyme 20 Theoretical pI 9.42
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586] ALL_REAC R02586
Enzyme 20 Pfam Domain Function Not Available
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID B3KQA7 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name B3KQA7_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AK074538 Link Image
Enzyme 20 GeneCard ID B3KQA7 Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location 22
Enzyme 20 Locus 22q12.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 16470
Enzyme 21 Name cDNA FLJ39504 fis, clone PROST2017203, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 1 (EC 2.8.2.23)
Enzyme 21 Synonyms
  1. SubName: Heparan sulfate (Glucosamine) 3-O-sulfotransferase 1, isoform CRA_a
Enzyme 21 Gene Name HS3ST1
Enzyme 21 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 21 Number of Residues 307
Enzyme 21 Molecular Weight 35773
Enzyme 21 Theoretical pI 9.16
Enzyme 21 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate ALL_REAC (other) R04064
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID B3KUA6 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name B3KUA6_HUMAN Link Image
Enzyme 21 PDB ID 1VKJ Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AK096823 Link Image
Enzyme 21 GeneCard ID B3KUA6 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 16471
Enzyme 22 Name Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a
Enzyme 22 Synonyms
  1. SubName: cDNA FLJ13661 fis, clone PLACE1011635, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 3B1
Enzyme 22 Gene Name HS3ST3B1
Enzyme 22 Protein Sequence >Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a 
MGQRLSGGRSCLDVPGRLLPQPPPPPPPVRRKLALLFAMLCVWLYMFLYSCAGSCAAAPG
LLLLGSGSRAAHDPPALATAPDGTPPRLPFRAPPATPLASGKEMAEGAASPEEQSPEVPD
SPSPISSFFSGSGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKG
LAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQ
TLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERL
ISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEI
DREVVRRLREFYRPFNLKFYQMTGHDFGWD
Enzyme 22 Number of Residues 390
Enzyme 22 Molecular Weight 43325
Enzyme 22 Theoretical pI 10.14
Enzyme 22 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
—
Component
—
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID B3KN58 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name B3KN58_HUMAN Link Image
Enzyme 22 PDB ID 1T8U Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID AK023723 Link Image
Enzyme 22 GeneCard ID B3KN58 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location 17
Enzyme 22 Locus 17p12-p11.2
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available