|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5351 |
| Enzyme 1 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 |
| Enzyme 1 Synonyms |
- E-NPP 1
- Membrane component chromosome 6 surface marker 1
- Phosphodiesterase I/nucleotide pyrophosphatase 1
- Plasma-cell membrane glycoprotein PC-1
- Alkaline phosphodiesterase I
- Nucleotide pyrophosphatase
- NPPase
|
| Enzyme 1 Gene Name |
ENPP1 |
| Enzyme 1 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
|
| Enzyme 1 Number of Residues |
925 |
| Enzyme 1 Molecular Weight |
104923.6 |
| Enzyme 1 Theoretical pI |
7.14 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- ion binding
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- pattern binding
- polysaccharide binding
- receptor activity
- scavenger receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- immune response
- immune system process
- metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in catalytic activity |
| Enzyme 1 Specific Function |
Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity |
| Enzyme 1 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760
)
- Pantothenate and CoA Biosynthesis (map00770
)
- Purine Metabolism (map00230
)
- Riboflavin Metabolism (map00740
)
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 1 Reactions |
- a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
170650661  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P22413  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ENPP1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2778 bp
ATGGAGCGCGACGGCTGCGCGGGGGGCGGGAGCCGCGGCGGCGAGGGCGGGCGCGCTCCC
CGGGAGGGCCCGGCGGGGAACGGCCGCGATCGGGGCCGCAGCCACGCTGCCGAGGCGCCC
GGGGACCCGCAGGCGGCCGCGTCCTTGCTGGCCCCTATGGACGTGGGGGAGGAGCCGCTG
GAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCCAACACCTATAAAGTACTCTCGCTG
GTATTGTCAGTATGTGTGTTAACAACAATACTTGGTTGTATATTTGGGTTGAAACCAAGC
TGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGTTTCGAGAGAACATTTGGGAACTGT
CGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGCTGTTTAGATTACCAGGAGACGTGC
ATAGAACCAGAACATATATGGACTTGCAACAAATTCAGGTGTGGTGAGAAAAGGTTGACC
AGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGACAAGGGCGACTGCTGCATCAACTAC
AGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAAGAACCATGTGAGAGCATTAATGAG
CCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACCCTCTTATTTTCTTTGGATGGATTC
AGGGCAGAATATTTACACACTTGGGGTGGACTTCTTCCTGTTATTAGCAAACTAAAAAAA
TGTGGAACATATACTAAAAACATGAGACCGGTATATCCAACAAAAACTTTCCCCAATCAC
TACAGCATTGTCACCGGATTGTATCCAGAATCTCATGGCATAATCGACAATAAAATGTAT
GATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGTAAAGAGAAATTTAATCCTGAGTGG
TACAAAGGAGAACCAATTTGGGTCACAGCTAAGTATCAAGGCCTCAAGTCTGGCACATTT
TTCTGGCCAGGATCAGATGTGGAAATTAACGGAATTTTCCCAGACATCTATAAAATGTAT
AATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCTGTTCTTCAGTGGCTACAGCTTCCT
AAAGATGAAAGACCACACTTTTACACTCTGTATTTAGAAGAACCAGATTCTTCAGGTCAT
TCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCCTTGCAGAGGGTTGATGGTATGGTT
GGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTGCACAGATGCCTGAACCTCATCCTT
ATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAGAAATACATATATCTGAATAAATAT
TTGGGGGATGTTAAAAATATTAAAGTTATCTATGGACCTGCAGCTCGATTGAGACCCTCT
GATGTCCCAGATAAATACTATTCATTTAACTATGAAGGCATTGCCCGAAATCTTTCTTGC
CGGGAACCAAACCAGCACTTCAAACCTTACCTGAAACATTTCTTACCTAAGCGTTTGCAC
TTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTCTATTTGGACCCTCAGTGGCAACTT
GCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGTGGATTTCATGGCTCTGACAATGTA
TTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGACCTGGATTCAAGCATGGCATTGAG
GCTGACACCTTTGAAAACATTGAAGTCTATAACTTAATGTGTGATTTACTGAATTTGACA
CCGGCTCCTAATAACGGAACTCATGGAAGTCTTAACCACCTTCTAAAGAATCCTGTTTAT
ACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTACAGTGCCCCTTCACAAGAAACCCC
AGAGATAACCTTGGCTGCTCATGTAACCCTTCGATTTTGCCGATTGAGGATTTTCAAACA
CAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATTAAGCATGAAACTTTACCCTATGGA
AGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGTCTTCTTTCCCAGCACCAGTTTATG
AGTGGATACAGCCAAGACATCTTAATGCCCCTTTGGACATCCTATACCGTGGACAGAAAT
GACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTGTACCAGGACTTTAGAATTCCTCTT
AGTCCTGTCCATAAATGTTCATTTTATAAAAATAACACCAAAGTGAGTTACGGGTTCCTC
TCCCCACCACAACTAAATAAAAATTCAAGTGGAATATATTCTGAAGCTTTGCTTACTACA
AATATAGTGCCAATGTACCAGAGTTTTCAAGTTATATGGCGCTACTTTCATGACACCCTA
CTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAATGTCGTCAGTGGTCCTGTGTTTGAC
TTTGATTATGATGGACGTTGTGATTCCTTAGAGAATCTGAGGCAAAAAAGAAGAGTCATC
CGTAACCAAGAAATTTTGATTCCAACTCACTTCTTTATTGTGCTAACAAGCTGTAAAGAT
ACATCTCAGACGCCTTTGCACTGTGAAAACCTAGACACCTTAGCTTTCATTTTGCCTCAC
AGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAGCATGACTCCTCATGGGTTGAAGAA
TTGTTAATGTTACACAGAGCACGGATCACAGATGTTGAGCACATCACTGGACTCAGCTTC
TATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTAAAGTTGAAAACACATTTGCCAACC
TTTAGCCAAGAAGACTGA
|
| Enzyme 1 GenBank Gene ID |
NM_006208.2  |
| Enzyme 1 GeneCard ID |
ENPP1  |
| Enzyme 1 GenAtlas ID |
ENPP1  |
| Enzyme 1 HGNC ID |
HGNC:3356  |
| Enzyme 1 Chromosome Location |
6 |
| Enzyme 1 Locus |
6q22-q23 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- Bello V, Goding JW, Greengrass V, Sali A, Dubljevic V, Lenoir C, Trugnan G, Maurice M: Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Mol Biol Cell. 2001 Oct;12(10):3004-15. [PubMed
]
- Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
- 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
]
- Rutsch F, Ruf N, Vaingankar S, Toliat MR, Suk A, Hohne W, Schauer G, Lehmann M, Roscioli T, Schnabel D, Epplen JT, Knisely A, Superti-Furga A, McGill J, Filippone M, Sinaiko AR, Vallance H, Hinrichs B, Smith W, Ferre M, Terkeltaub R, Nurnberg P: Mutations in ENPP1 are associated with 'idiopathic' infantile arterial calcification. Nat Genet. 2003 Aug;34(4):379-81. [PubMed
]
- Cheng KS, Chen MR, Ruf N, Lin SP, Rutsch F: Generalized arterial calcification of infancy: different clinical courses in two affected siblings. Am J Med Genet A. 2005 Jul 15;136(2):210-3. [PubMed
]
- Bacci S, Ludovico O, Prudente S, Zhang YY, Di Paola R, Mangiacotti D, Rauseo A, Nolan D, Duffy J, Fini G, Salvemini L, Amico C, Vigna C, Pellegrini F, Menzaghi C, Doria A, Trischitta V: The K121Q polymorphism of the ENPP1/PC-1 gene is associated with insulin resistance/atherogenic phenotypes, including earlier onset of type 2 diabetes and myocardial infarction. Diabetes. 2005 Oct;54(10):3021-5. [PubMed
]
|
| 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 |
- E-NPP 3
- Phosphodiesterase I beta
- PD-Ibeta
- Phosphodiesterase I/nucleotide pyrophosphatase 3
- CD203c antigen
- Alkaline phosphodiesterase I
- Nucleotide pyrophosphatase
- NPPase
|
| Enzyme 2 Gene Name |
ENPP3 |
| Enzyme 2 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
|
| Enzyme 2 Number of Residues |
875 |
| Enzyme 2 Molecular Weight |
100123.5 |
| Enzyme 2 Theoretical pI |
6.55 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- ion binding
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- pattern binding
- polysaccharide binding
- receptor activity
- scavenger receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- immune response
- immune system process
- metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in catalytic activity |
| Enzyme 2 Specific Function |
Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD |
| Enzyme 2 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760
)
- Pantothenate and CoA Biosynthesis (map00770
)
- Purine Metabolism (map00230
)
- Riboflavin Metabolism (map00740
)
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 2 Reactions |
- a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
2465540  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O14638  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ENPP3_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
ENPP3  |
| Enzyme 2 GenAtlas ID |
ENPP3  |
| Enzyme 2 HGNC ID |
HGNC:3358  |
| Enzyme 2 Chromosome Location |
6 |
| Enzyme 2 Locus |
6q22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- Buhring HJ, Seiffert M, Giesert C, Marxer A, Kanz L, Valent P, Sano K: The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3. Blood. 2001 May 15;97(10):3303-5. [PubMed
]
- Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed
]
- Buhring HJ, Streble A, Valent P: The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell activation and allergy diagnosis. Int Arch Allergy Immunol. 2004 Apr;133(4):317-29. Epub 2004 Mar 17. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5519 |
| Enzyme 3 Name |
Carbohydrate sulfotransferase 3 |
| Enzyme 3 Synonyms |
- Chondroitin 6-O-sulfotransferase 1
- C6ST-1
- Chondroitin 6-sulfotransferase
- Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0
- GST-0
|
| Enzyme 3 Gene Name |
CHST3 |
| Enzyme 3 Protein Sequence |
>Carbohydrate sulfotransferase 3
MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALA
DANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKE
EEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGAN
AAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKK
VFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLV
RDPRAVLASRMVAFAGKYKTWKKWLDDEGQDGLREEEVQRLRGNCESIRLSAELGLRQPA
WLRGRYMLVRYEDVARGPLQKAREMYRFAGIPLTPQVEDWIQKNTQAAHDGSGIYSTQKN
SSEQFEKWRFSMPFKLAQVVQAACGPAMRLFGYKLARDAAALTNRSVSLLEERGTFWVT
|
| Enzyme 3 Number of Residues |
479 |
| Enzyme 3 Molecular Weight |
54705.5 |
| Enzyme 3 Theoretical pI |
8.75 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- Golgi membrane
- cell part
- membrane
- organelle membrane
|
|
| Enzyme 3 General Function |
Involved in sulfotransferase activity |
| Enzyme 3 Specific Function |
Catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen |
| Enzyme 3 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 3 Reactions |
- 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
3510308  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q7LGC8  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
CHST3_HUMAN  |
| 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  |
| Enzyme 3 GeneCard ID |
CHST3  |
| Enzyme 3 GenAtlas ID |
CHST3  |
| Enzyme 3 HGNC ID |
HGNC:1971  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
10q22.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Thiele H, Sakano M, Kitagawa H, Sugahara K, Rajab A, Hohne W, Ritter H, Leschik G, Nurnberg P, Mundlos S: Loss of chondroitin 6-O-sulfotransferase-1 function results in severe human chondrodysplasia with progressive spinal involvement. Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):10155-60. Epub 2004 Jun 23. [PubMed
]
- Hermanns P, Unger S, Rossi A, Perez-Aytes A, Cortina H, Bonafe L, Boccone L, Setzu V, Dutoit M, Sangiorgi L, Pecora F, Reicherter K, Nishimura G, Spranger J, Zabel B, Superti-Furga A: Congenital joint dislocations caused by carbohydrate sulfotransferase 3 deficiency in recessive Larsen syndrome and humero-spinal dysostosis. Am J Hum Genet. 2008 Jun;82(6):1368-74. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5520 |
| Enzyme 4 Name |
Carbohydrate sulfotransferase 13 |
| Enzyme 4 Synonyms |
- Chondroitin 4-O-sulfotransferase 3
- Chondroitin 4-sulfotransferase 3
- C4ST-3
- C4ST3
|
| Enzyme 4 Gene Name |
CHST13 |
| Enzyme 4 Protein Sequence |
>Carbohydrate sulfotransferase 13
MGRRCCRRRVLAAACLGAALLLLCAAPRSLRPAFGNRALGSSWLGGEKRSPLQKLYDLDQ
DPRSTLAKVHRQRRDLLNSACSRHSRRQRLLQPEDLRHVLVDDAHGLLYCYVPKVACTNW
KRVLLALSGQARGDPRAISAQEAHAPGRLPSLADFSPAEINRRLRAYLAFLFVREPFERL
ASAYRNKLARPYSAAFQRRYGARIVQRLRPRALPDARARGHDVRFAEFLAYLLDPRTRRE
EPFNEHWERAHALCHPCRLRYDVVGKFETLAEDAAFVLGLAGASDLSFPGPPRPRGAAAS
RDLAARLFRDISPFYQRRLFDLYKMDFLLFNYSAPSYLRLL
|
| Enzyme 4 Number of Residues |
341 |
| Enzyme 4 Molecular Weight |
38919.3 |
| Enzyme 4 Theoretical pI |
11.00 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- carbohydrate biosynthetic process
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 4 General Function |
Involved in sulfotransferase activity |
| Enzyme 4 Specific Function |
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan |
| Enzyme 4 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 4 Reactions |
- 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate [RN:R02180]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
22651777  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q8NET6  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
CHSTD_HUMAN  |
| 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  |
| Enzyme 4 GeneCard ID |
CHST13  |
| Enzyme 4 GenAtlas ID |
CHST13  |
| Enzyme 4 HGNC ID |
HGNC:21755  |
| Enzyme 4 Chromosome Location |
3 |
| Enzyme 4 Locus |
3q21.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5521 |
| Enzyme 5 Name |
Carbohydrate sulfotransferase 12 |
| Enzyme 5 Synonyms |
- Chondroitin 4-O-sulfotransferase 2
- Chondroitin 4-sulfotransferase 2
- C4ST-2
- C4ST2
- Sulfotransferase Hlo
|
| Enzyme 5 Gene Name |
CHST12 |
| Enzyme 5 Protein Sequence |
>Carbohydrate sulfotransferase 12
MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDREL
TADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQ
QAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKR
VMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTK
FLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSF
ANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDR
QLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
|
| Enzyme 5 Number of Residues |
414 |
| Enzyme 5 Molecular Weight |
48413.9 |
| Enzyme 5 Theoretical pI |
9.69 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- carbohydrate biosynthetic process
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 5 General Function |
Involved in sulfotransferase activity |
| Enzyme 5 Specific Function |
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor |
| Enzyme 5 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 5 Reactions |
- 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate [RN:R02180]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
8925968  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9NRB3  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
CHSTC_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1245 bp
ATGACCAAGGCCCGGCTGTTCCGGCTGTGGCTGGTGCTGGGGTCGGTGTTCATGATCCTG
CTGATCATCGTGTACTGGGACAGCGCAAGCGCCGCGCACTTCTACTTGCACACGTCCTTC
TCTAAGCCGCACACAGGGCCGCCGCTGCCCACGCCCGGGCCGGACAGGGACAGGGAGCTC
ACGGCCGACTCCGATGTCGACGAGTTTCTGGACAAGTTTCTCAGTGCTGGCGTGAAGCAG
AGCGACCTTCCCAGAAAGGAGACGGAGCAGCCGCTTGCGCCGGGGAGCATGGAGGAGAGC
GTGAGAGGCTACGACTGGTCCCCGCGCGACGCCCGGCGCAGCCCAGACCAGGGCCGGCAG
CAGGCGGAGCGGAGGAGCGTGCTGCGGGGCTTCTGCGCCAACTCCAGCCTGGCCTTCCCC
ACCAAGGAGCGCGCATTCGACGACATCCCCAACTCGGAGCTGAGCCACCTGATCGTGGAC
GACCGGCACGGGGCCATCTACTGCTACGTGCCCAAGGTGGCCTGCACCAACTGGAAGCGC
GTGATGATCGTGCTGAGCGGAAGCCTGCTGCACCGCGGTGCGCCCTACCGCGACCCGCTG
CGCATCCCGCGCGAGCACGTGCACAACGCCAGCGCGCACCTGACCTTCAACAAGTTCTGG
CGCCGCTACGGGAAGCTCTCCCGCCACCTCATGAAGGTCAAGCTCAAGAAGTACACCAAG
TTCCTCTTCGTGCGCGACCCCTTCGTGCGCCTGATCTCCGCCTTCCGCAGCAAGTTCGAG
CTGGAGAACGAGGAGTTCTACCGCAAGTTCGCCGTGCCCATGCTGCGGCTGTACGCCAAC
CACACAAGCCTGCCCGCCTCGGCGCGCGAGGCCTTCCGCGCTGGCCTCAAGGTGTCCTTC
GCCAACTTCATCCAGTACCTGCTGGACCCGCACACGGAGAAGCTGGCGCCCTTCAACGAG
CACTGGCGGCAGGTGTACCGCCTCTGCCACCCGTGCCAGATCGACTACGACTTCGTGGGG
AAGCTGGAGACTCTGGACGAGGACGCCGCGCAGCTGCTGCAGCTACTCCAGGTGGACCGG
CAGCTCCGCTTCCCCCCGAGCTACCGGAACAGGACCGCCAGCAGCTGGGAGGAGGACTGT
TTCGCCAAGATCCCCCTGGCCTGGAGGCAGCAGCTGTATAAACTCTACGAGGCCGACTTT
GTTCTCTTCGGCTACCCCAAGCCCGAAAACCTCCTCCGAGACTGA
|
| Enzyme 5 GenBank Gene ID |
AF239822  |
| Enzyme 5 GeneCard ID |
CHST12  |
| Enzyme 5 GenAtlas ID |
CHST12  |
| Enzyme 5 HGNC ID |
HGNC:17423  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7p22 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Hiraoka N, Nakagawa H, Ong E, Akama TO, Fukuda MN, Fukuda M: Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family. J Biol Chem. 2000 Jun 30;275(26):20188-96. [PubMed
]
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mikami T, Mizumoto S, Kago N, Kitagawa H, Sugahara K: Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor: implication of differential roles in dermatan sulfate biosynthesis. J Biol Chem. 2003 Sep 19;278(38):36115-27. Epub 2003 Jul 7. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5554 |
| Enzyme 6 Name |
Galactosylceramide sulfotransferase |
| Enzyme 6 Synonyms |
- GalCer sulfotransferase
- 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase
- 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
- Cerebroside sulfotransferase
|
| Enzyme 6 Gene Name |
GAL3ST1 |
| Enzyme 6 Protein Sequence |
>Galactosylceramide sulfotransferase
MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPE
AVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTF
FARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPV
VPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHIL
EVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAW
NMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDE
AMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDF
LRW
|
| Enzyme 6 Number of Residues |
423 |
| Enzyme 6 Molecular Weight |
48763.6 |
| Enzyme 6 Theoretical pI |
8.78 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- galactose 3-O-sulfotransferase activity
- galactosylceramide sulfotransferase activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
- Golgi apparatus
- cell part
- integral to membrane
- intracellular membrane-bounded organelle
- intrinsic to membrane
- membrane part
- membrane-bounded organelle
- organelle
|
|
| Enzyme 6 General Function |
Involved in galactosylceramide sulfotransferase activity |
| Enzyme 6 Specific Function |
Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro) |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate [RN:R04017 R06279]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
6714628  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q99999  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
G3ST1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1272 bp
ATGCTGCCACCGCAGAAGAAGCCCTGGGAGTCCATGGCTAAGGGGCTGGTGCTGGGCGCG
CTCTTCACTAGTTTCCTGCTGCTGGTGTACTCCTATGCCGTGCCCCCGCTGCATGCCGGC
CTGGCCTCCACGACCCCGGAGGCCGCAGCGTCCTGCTCTCCACCTGCACTCGAGCCAGAG
GCAGTGATCCGGGCCAACGGCTCGGCGGGGGAGTGCCAGCCGCGGCGCAACATCGTGTTC
TTGAAGACGCACAAGACGGCCAGCAGCACCCTGCTCAACATCCTGTTCCGCTTCGGCCAG
AAGCACCGGCTCAAGTTCGCCTTCCCTAACGGCCGCAATGACTTCGACTACCCGACCTTC
TTCGCCCGCAGCCTGGTGCAGGACTATCGGCCCGGGGCCTGCTTCAACATCATCTGCAAC
CACATGCGCTTCCACTACGACGAGGTGCGCGGCCTGGTGCCGACCAACGCCATCTTCATC
ACGGTGCTCCGCGACCCCGCCCGCTTGTTCGAGTCCTCCTTCCACTACTTCGGGCCGGTG
GTGCCCCTCACGTGGAAGCTCTCGGCCGGCGACAAGCTGACCGAGTTCCTGCAAGACCCG
GATCGCTACTACGACCCCAACGGCTTCAATGCCCACTACCTCCGAAACCTGCTCTTCTTC
GACCTGGGCTATGACAACAGCCTGGACCCCAGCAGCCCGCAGGTGCAGGAGCACATCCTG
GAGGTGGAGCGTCGCTTCCACCTGGTGCTCCTTCAAGAGTACTTCGACGAGTCGCTGGTG
CTGCTGAAGGACCTGCTGTGCTGGGAGCTGGAGGACGTGCTCTACTTCAAGCTCAACGCC
CGCCGCGACTCGCCCGTGCCGCGGCTCTCGGGGGAGCTGTATGGGCGCGCCACCGCCTGG
AACATGCTGGACTCCCACCTCTACCGCCACTTCAACGCCAGCTTCTGGCGCAAGGTGGAG
GCCTTCGGGCGGGAGCGCATGGCCCGCGAGGTGGCCGCCCTGCGCCATGCCAACGAGCGC
ATGCGGACCATCTGCATCGACGGGGGCCACGCCGTGGACGCCGCCGCCATCCAGGACGAG
GCCATGCAGCCCTGGCAGCCGCTGGGCACCAAGTCCATCCTGGGCTACAACCTCAAGAAG
AGCATCGGGCAGCGGCACGCGCAGCTCTGCCGGCGCATGCTCACGCCCGAGATCCAGTAC
CTGATGGACCTCGGCGCCAACCTGTGGGTCACCAAGCTCTGGAAGTTCATTCGCGATTTC
CTGCGGTGGTGA
|
| Enzyme 6 GenBank Gene ID |
AB029901  |
| Enzyme 6 GeneCard ID |
GAL3ST1  |
| Enzyme 6 GenAtlas ID |
GAL3ST1  |
| Enzyme 6 HGNC ID |
HGNC:24240  |
| Enzyme 6 Chromosome Location |
2 |
| Enzyme 6 Locus |
22q12.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- 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
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5575 |
| Enzyme 7 Name |
Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 |
| Enzyme 7 Synonyms |
- Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1
- 3-OST-3B
- Heparan sulfate 3-O-sulfotransferase 3B1
- h3-OST-3B
|
| Enzyme 7 Gene Name |
HS3ST3B1 |
| Enzyme 7 Protein Sequence |
>Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
MGQRLSGGRSCLDVPGRLLPQPPPPPPPVRRKLALLFAMLCVWLYMFLYSCAGSCAAAPG
LLLLGSGSRAAHDPPALATAPDGTPPRLPFRAPPATPLASGKEMAEGAASPEEQSPEVPD
SPSPISSFFSGSGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKG
LAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQ
TLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERL
ISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEI
DREVVRRLREFYRPFNLKFYQMTGHDFGWD
|
| Enzyme 7 Number of Residues |
390 |
| Enzyme 7 Molecular Weight |
43323.6 |
| Enzyme 7 Theoretical pI |
10.14 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in sulfotransferase activity |
| Enzyme 7 Specific Function |
Transfers a sulfuryl group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
4835725  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9Y662  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
HS3SB_HUMAN  |
| Enzyme 7 PDB ID |
1T8U  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1173 bp
ATGGGGCAGCGCCTGAGTGGCGGCAGATCTTGCCTCGATGTCCCCGGCCGGCTCCTACCG
CAGCCGCCGCCGCCCCCGCCGCCGGTGAGGAGGAAGCTCGCGCTGCTCTTCGCCATGCTC
TGCGTCTGGCTCTATATGTTCCTGTACTCGTGCGCCGGCTCCTGCGCCGCCGCGCCGGGG
CTGCTGCTCCTGGGCTCTGGGTCCCGCGCCGCACACGACCCGCCAGCCCTGGCCACAGCT
CCGGACGGGACGCCCCCCAGGCTGCCGTTCCGGGCGCCGCCAGCCACCCCACTGGCTTCA
GGCAAGGAGATGGCCGAGGGCGCTGCGAGCCCGGAGGAGCAGAGTCCCGAGGTGCCGGAC
TCCCCAAGCCCCATCTCCAGCTTTTTCAGTGGGTCTGGGAGCAAGCAGCTGCCGCAGGCC
ATCATCATCGGCGTGAAGAAGGGCGGCACGCGGGCGCTGCTGGAGTTTCTGCGCGTGCAC
CCCGACGTGCGCGCCGTGGGCGCCGAGCCCCATTTCTTCGATCGCAGCTACGACAAGGGC
CTCGCTTGGTACCGGGACCTGATGCCCAGAACCCTGGACGGGCAGATCACCATGGAGAAG
ACGCCCAGTTACTTCGTCACGCGGGAGGCCCCCGCGCGCATCTCGGCCATGTCCAAGGAC
ACCAAGCTCATCGTGGTGGTGCGGGACCCGGTGACCAGGGCCATCTCGGACTACACGCAG
ACGCTGTCCAAGCGGCCCGACATCCCCACCTTCGAGAGCTTGACGTTCAAAAACAGGACA
GCGGGCCTCATCGACACGTCGTGGAGCGCCATCCAGATCGGCATCTACGCCAAGCACCTG
GAGCACTGGCTGCGCCACTTCCCCATCCGCCAGATGCTCTTCGTGAGCGGCGAGCGGCTC
ATCAGCGACCCGGCCGGGGAGCTGGGCCGCGTGCAAGACTTCCTGGGCCTCAAGAGGATC
ATCACGGACAAGCACTTCTACTTCAACAAGACCAAGGGCTTCCCCTGCCTGAAGAAGGCG
GAGGGCAGCAGCCGGCCCCATTGCCTGGGCAAGACCAAGGGCAGGACCCATCCTGAGATC
GACCGCGAGGTGGTGCGCAGGCTGCGCGAGTTCTACCGGCCTTTCAACCTCAAGTTCTAC
CAGATGACCGGGCACGACTTTGGCTGGGATTGA
|
| Enzyme 7 GenBank Gene ID |
AF105377  |
| Enzyme 7 GeneCard ID |
HS3ST3B1  |
| Enzyme 7 GenAtlas ID |
HS3ST3B1  |
| Enzyme 7 HGNC ID |
HGNC:5198  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
17p12 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, Cohen GH, Eisenberg RJ, Rosenberg RD, Spear PG: A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell. 1999 Oct 1;99(1):13-22. [PubMed
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5578 |
| Enzyme 8 Name |
3'(2'),5'-bisphosphate nucleotidase 1 |
| Enzyme 8 Synonyms |
- Bisphosphate 3'-nucleotidase 1
- PAP-inositol-1,4-phosphatase
- PIP
|
| Enzyme 8 Gene Name |
BPNT1 |
| Enzyme 8 Protein Sequence |
>3'(2'),5'-bisphosphate nucleotidase 1
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
|
| Enzyme 8 Number of Residues |
308 |
| Enzyme 8 Molecular Weight |
33392.0 |
| Enzyme 8 Theoretical pI |
5.41 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 8 Specific Function |
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4- trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6 |
| Enzyme 8 Pathways |
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 8 Reactions |
- adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate [RN:R00188]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O95861  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
BPNT1_HUMAN  |
| Enzyme 8 PDB ID |
1JP4  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>927 bp
ATGGCTTCCAGTAACACTGTGTTGATGCGGTTGGTAGCCTCCGCATATTCTATTGCTCAA
AAGGCAGGAATGATAGTCAGACGTGTTATTGCTGAAGGAGACCTGGGTATTGTGGAGAAG
ACCTGTGCAACAGACCTGCAGACCAAAGCTGACCGATTGGCACAGATGAGCATATGTTCT
TCATTGGCCCGGAAATTCCCCAAACTCACAATTATAGGGGAAGAGGATCTGCCTTCTGAG
GAAGTGGATCAAGAGCTGATTGAAGACAGTCAGTGGGAAGAAATACTGAAGCAACCATGC
CCATCGCAGTACAGTGCTATTAAAGAAGAAGATCTCGTGGTCTGGGTTGATCCTCTGGAT
GGAACCAAGGAATATACCGAAGGTCTTCTTGACAATGTAACAGTTCTTATTGGAATTGCT
TATGAAGGAAAAGCCATAGCAGGAGTTATTAACCAGCCATATTACAACTATGAGGCAGGA
CCAGATGCTGTGTTGGGGAGGACAATCTGGGGAGTTTTAGGTTTAGGCGCCTTTGGGTTT
CAGCTGAAAGAAGTCCCTGCTGGGAAACACATTATCACAACTACTCGATCCCATAGCAAC
AAGTTGGTTACTGACTGTGTTGCTGCTATGAACCCCGATGCTGTGCTGCGAGTAGGAGGA
GCAGGAAATAAGATTATTCAGCTGATTGAAGGCAAAGCCTCTGCTTATGTATTTGCAAGT
CCTGGTTGTAAGAAGTGGGATACTTGTGCTCCAGAAGTTATTTTACATGCTGTGGGAGGC
AAGTTAACCGATATCCATGGGAATGTTCTTCAGTACCACAAGGATGTGAAGCATATGAAC
TCTGCAGGAGTCCTGGCCACACTGAGGAATTATGACTACTATGCAAGCCGAGTTCCAGAA
TCTATTAAAAATGCACTTGTTCCTTAA
|
| Enzyme 8 GenBank Gene ID |
AF125042  |
| Enzyme 8 GeneCard ID |
BPNT1  |
| Enzyme 8 GenAtlas ID |
BPNT1  |
| Enzyme 8 HGNC ID |
HGNC:1096  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1q41 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Spiegelberg BD, Xiong JP, Smith JJ, Gu RF, York JD: Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate. J Biol Chem. 1999 May 7;274(19):13619-28. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5579 |
| Enzyme 9 Name |
Heparan sulfate glucosamine 3-O-sulfotransferase 1 |
| Enzyme 9 Synonyms |
- Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1
- 3-OST-1
- Heparan sulfate 3-O-sulfotransferase 1
- h3-OST-1
|
| Enzyme 9 Gene Name |
HS3ST1 |
| Enzyme 9 Protein Sequence |
>Heparan sulfate glucosamine 3-O-sulfotransferase 1
MAALLLGAVLLVAQPQLVPSRPAELGQQELLRKAGTLQDDVRDGVAPNGSAQQLPQTIII
GVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSHGLGWYLSQMPFSWPHQLTVEKT
PAYFTSPKVPERVYSMNPSIRLLLILRDPSERVLSDYTQVFYNHMQKHKPYPSIEEFLVR
DGRLNVDYKALNRSLYHVHMQNWLRFFPLRHIHIVDGDRLIRDPFPEIQKVERFLKLSPQ
INASNFYFNKTKGFYCLRDSGRDRCLHESKGRAHPQVDPKLLNKLHEYFHEPNKKFFELV
GRTFDWH
|
| Enzyme 9 Number of Residues |
307 |
| Enzyme 9 Molecular Weight |
35772.8 |
| Enzyme 9 Theoretical pI |
9.16 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in sulfotransferase activity |
| Enzyme 9 Specific Function |
Rate limiting enzyme for synthesis of HSact. Performs the crucial step modification in the biosynthesis of anticoagulant heparan sulfate (HSact) that is to complete the structure of the antithrombin pentasaccharide binding site |
| Enzyme 9 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 9 Reactions |
- 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
2618973  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O14792  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
HS3S1_HUMAN  |
| Enzyme 9 PDB ID |
1VKJ  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>924 bp
ATGGCCGCGCTGCTCCTGGGCGCGGTGCTGCTGGTGGCCCAGCCCCAGCTAGTGCCTTCC
CGCCCCGCCGAGCTAGGCCAGCAGGAGCTTCTGCGGAAAGCGGGGACCCTCCAGGATGAC
GTCCGCGATGGCGTGGCCCCAAACGGCTCTGCCCAGCAGTTGCCGCAGACCATCATCATC
GGCGTGCGCAAGGGCGGCACGCGCGCACTGCTGGAGATGCTCAGCCTGCACCCCGACGTG
GCGGCCGCGGAGAACGAGGTCCACTTCTTCGACTGGGAGGAGCATTACAGCCACGGCTTG
GGCTGGTACCTCAGCCAGATGCCCTTCTCCTGGCCACACCAGCTCACAGTGGAGAAGACC
CCCGCGTATTTCACGTCGCCCAAAGTGCCTGAGCGAGTCTACAGCATGAACCCGTCCATC
CGGCTGCTGCTCATCCTGCGAGACCCGTCGGAGCGCGTGCTATCTGACTACACCCAAGTG
TTCTACAACCACATGCAGAAGCACAAGCCCTACCCGTCCATCGAGGAGTTCCTGGTGCGC
GATGGCAGGCTCAATGTGGACTACAAGGCCCTCAACCGCAGCCTCTACCACGTGCACATG
CAGAACTGGCTGCGCTTTTTCCCGCTGCGCCACATCCACATTGTGGACGGCGACCGCCTC
ATCAGGGACCCCTTCCCTGAGATCCAAAAGGTCGAGAGGTTCCTAAAGCTGTCGCCGCAG
ATCAATGCTTCGAACTTCTACTTTAACAAAACCAAGGGCTTTTACTGCCTGCGGGACAGC
GGCCGGGACCGCTGCTTACATGAGTCCAAAGGCCGGGCGCACCCCCAAGTCGATCCCAAA
CTACTCAATAAACTGCACGAATATTTTCATGAGCCAAATAAGAAGTTCTTCGAGCTTGTT
GGCAGAACATTTGACTGGCACTGA
|
| Enzyme 9 GenBank Gene ID |
AF019386  |
| Enzyme 9 GeneCard ID |
HS3ST1  |
| Enzyme 9 GenAtlas ID |
HS3ST1  |
| Enzyme 9 HGNC ID |
HGNC:5194  |
| Enzyme 9 Chromosome Location |
4 |
| Enzyme 9 Locus |
4p16 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Shworak NW, Liu J, Fritze LM, Schwartz JJ, Zhang L, Logeart D, Rosenberg RD: Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J Biol Chem. 1997 Oct 31;272(44):28008-19. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD: Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J Biol Chem. 1996 Oct 25;271(43):27072-82. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5582 |
| Enzyme 10 Name |
Estrogen sulfotransferase |
| Enzyme 10 Synonyms |
- EST-1
- Sulfotransferase 1E1
- ST1E1
- Sulfotransferase, estrogen-preferring
|
| Enzyme 10 Gene Name |
SULT1E1 |
| Enzyme 10 Protein Sequence |
>Estrogen sulfotransferase
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMI
YKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEK
DCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWE
KGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYT
TLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
|
| Enzyme 10 Number of Residues |
294 |
| Enzyme 10 Molecular Weight |
35126.2 |
| Enzyme 10 Theoretical pI |
6.61 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in sulfotransferase activity |
| Enzyme 10 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 10 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 10 Reactions |
- 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate [RN:R02350]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
Not Available |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P49888  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
ST1E1_HUMAN  |
| Enzyme 10 PDB ID |
1G3M  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>885 bp
ATGAATTCTGAACTTGACTATTATGAAAAGTTTGAAGAAGTCCATGGGATTCTAATGTAT
AAAGATTTTGTCAAATATTGGGATAATGTGGAAGCGTTCCAGGCAAGACCAGATGATCTT
GTCATTGCCACCTACCCTAAATCTGGTACAACCTGGGTTAGTGAAATTGTGTATATGATC
TATAAAGAGGGTGATGTGGAAAAGTGCAAAGAAGATGTAATTTTTAATCGAATACCTTTC
CTGGAATGCAGAAAAGAAAACCTCATGAATGGAGTAAAACAATTAGATGAGATGAATTCT
CCTAGAATTGTGAAGACTCATTTGCCACCTGAACTTCTTCCTGCCTCATTTTGGGAAAAG
GATTGTAAGATAATCTATCTTTGCCGGAATGCAAAGGATGTGGCTGTTTCCTTTTATTAT
TTCTTTCTAATGGTGGCTGGTCATCCAAATCCTGGATCCTTTCCAGAGTTTGTGGAGAAA
TTCATGCAAGGACAGGTTCCTTATGGTTCCTGGTATAAACATGTAAAATCTTGGTGGGAA
AAGGGAAAGAGTCCACGTGTACTATTTCTTTTCTACGAAGACCTGAAAGAGGATATCAGA
AAAGAGGTGATAAAATTGATACATTTCCTGGAAAGGAAGCCATCAGAGGAGCTTGTGGAC
AGGATTATACATCATACTTCGTTCCAAGAGATGAAGAACAATCCATCCACAAATTACACA
ACACTGCCAGACGAAATTATGAACCAGAAATTGTCGCCCTTCATGAGAAAGGGAATTACA
GGAGACTGGAAAAATCACTTTACAGTAGCCCTGAATGAAAAATTTGATAAACATTATGAG
CAGCAAATGAAGGAATCTACACTGAAGTTTCGAACTGAGATCTAA
|
| Enzyme 10 GenBank Gene ID |
U08098  |
| Enzyme 10 GeneCard ID |
SULT1E1  |
| Enzyme 10 GenAtlas ID |
SULT1E1  |
| Enzyme 10 HGNC ID |
HGNC:11377  |
| Enzyme 10 Chromosome Location |
4 |
| Enzyme 10 Locus |
4q13.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M: Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. [PubMed
]
- Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M: Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect. 2003 Jun;111(7):884-8. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5588 |
| Enzyme 11 Name |
Heparan sulfate glucosamine 3-O-sulfotransferase 2 |
| Enzyme 11 Synonyms |
- Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2
- 3-OST-2
- Heparan sulfate 3-O-sulfotransferase 2
- h3-OST-2
|
| Enzyme 11 Gene Name |
HS3ST2 |
| Enzyme 11 Protein Sequence |
>Heparan sulfate glucosamine 3-O-sulfotransferase 2
MAYRVLGRAGPPQPRRARRLLFAFTLSLSCTYLCYSFLCCCDDLGRSRLLGAPRCLRGPS
AGGQKLLQKSRPCDPSGPTPSEPSAPSAPAAAVPAPRLSGSNHSGSPKLGTKRLPQALIV
GVKKGGTRAVLEFIRVHPDVRALGTEPHFFDRNYGRGLDWYRSLMPRTLESQITLEKTPS
YFVTQEAPRRIFNMSRDTKLIVVVRNPVTRAISDYTQTLSKKPDIPTFEGLSFRNRTLGL
VDVSWNAIRIGMYVLHLESWLQYFPLAQIHFVSGERLITDPAGEMGRVQDFLGIKRFITD
KHFYFNKTKGFPCLKKTESSLLPRCLGKSKGRTHVQIDPEVIDQLREFYRPYNIKFYETV
GQDFRWE
|
| Enzyme 11 Number of Residues |
367 |
| Enzyme 11 Molecular Weight |
41500.6 |
| Enzyme 11 Theoretical pI |
10.39 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in sulfotransferase activity |
| Enzyme 11 Specific Function |
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 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
- 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate [RN:R05798]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
4835719  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9Y278  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
HS3S2_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1104 bp
ATGGCCTATAGGGTCCTGGGCCGCGCGGGGCCACCTCAGCCGCGGAGGGCGCGCAGGCTG
CTCTTCGCCTTCACGCTCTCGCTCTCCTGCACTTACCTGTGTTACAGCTTCCTGTGCTGC
TGCGACGACCTGGGTCGGAGCCGCCTCCTCGGCGCGCCTCGCTGCCTCCGCGGCCCCAGC
GCGGGCGGCCAGAAACTTCTCCAGAAGTCCCGCCCCTGTGATCCCTCCGGGCCGACGCCC
AGCGAGCCCAGCGCTCCCAGCGCGCCCGCCGCCGCCGTGCCCGCCCCTCGCCTCTCCGGT
TCCAACCACTCCGGCTCACCCAAGCTGGGTACCAAGCGGTTGCCCCAAGCCCTCATTGTG
GGCGTGAAGAAGGGGGGCACCCGGGCCGTGCTGGAGTTTATCCGAGTACACCCGGACGTG
CGGGCCTTGGGCACGGAACCCCACTTCTTTGACAGGAACTACGGCCGCGGGCTGGATTGG
TACAGGAGCCTGATGCCCAGGACCCTCGAGAGCCAGATCACGCTGGAGAAGACGCCCAGC
TACTTTGTCACTCAAGAGGCTCCTCGACGCATCTTCAACATGTCCCGAGACACCAAGCTG
ATCGTGGTTGTGCGGAACCCTGTGACCCGTGCCATCTCTGATTACACGCAGACACTCTCC
AAGAAGCCCGACATCCCGACCTTTGAGGGCCTCTCCTTCCGCAACCGCACCCTGGGCCTG
GTGGACGTGTCGTGGAACGCCATCCGCATCGGCATGTACGTGCTGCACCTGGAGAGCTGG
CTGCAGTACTTCCCGCTAGCTCAGATTCACTTCGTCAGTGGCGAGCGACTCATCACTGAC
CCGGCCGGCGAGATGGGGCGAGTCCAGGACTTCCTGGGCATTAAGAGATTCATCACGGAC
AAGCACTTCTATTTCAACAAGACCAAAGGATTCCCTTGCTTGAAAAAAACAGAATCGAGC
CTCCTGCCTCGATGCTTGGGCAAATCAAAAGGGAGAACTCATGTACAGATTGATCCTGAA
GTGATAGACCAGCTCCGAGAATTTTATAGACCGTATAATATCAAATTTTATGAAACCGTT
GGGCAGGACTTCAGGTGGGAATAA
|
| Enzyme 11 GenBank Gene ID |
AF105374  |
| Enzyme 11 GeneCard ID |
HS3ST2  |
| Enzyme 11 GenAtlas ID |
HS3ST2  |
| Enzyme 11 HGNC ID |
HGNC:5195  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
16p12 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
- 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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5590 |
| Enzyme 12 Name |
Protein-tyrosine sulfotransferase 2 |
| Enzyme 12 Synonyms |
- Tyrosylprotein sulfotransferase 2
- TPST-2
|
| Enzyme 12 Gene Name |
TPST2 |
| Enzyme 12 Protein Sequence |
>Protein-tyrosine sulfotransferase 2
MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHV
EYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREK
LRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLL
MVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQ
LVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSK
WTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLK
GYFQVNQNSTSSHLGSS
|
| Enzyme 12 Number of Residues |
377 |
| Enzyme 12 Molecular Weight |
41911.5 |
| Enzyme 12 Theoretical pI |
9.42 |
| Enzyme 12 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in sulfotransferase activity |
| Enzyme 12 Specific Function |
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
3617846  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
O60704  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
TPST2_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1134 bp
ATGCGCCTGTCGGTGCGGAGGGTGCTGCTGGCAGCCGGCTGCGCCCTGGTCCTGGTGCTG
GCGGTTCAGCTGGGACAGCAGGTGCTAGAGTGCCGGGCGGTGCTGGCGGGCCTGCGGAGC
CCCCGGGGGGCCATGCGGCCTGAGCAGGAGGAGCTGGTGATGGTGGGCACCAACCACGTG
GAATACCGCTATGGCAAGGCCATGCCGCTCATCTTCGTGGGTGGCGTGCCTCGCAGTGGC
ACCACGTTGATGCGCGCCATGCTGGACGCCCACCCCGAGGTGCGCTGCGGCGAGGAGACC
CGCATCATCCCGCGCGTGCTGGCCATGCGCCAGGCCTGGTCCAAGTCTGGCCGTGAGAAG
CTGCGGCTGGATGAGGCGGGGGTGACGGATGAGGTGCTGGACGCCGCCATGCAGGCCTTC
ATCCTGGAGGTGATTGCCAAGCACGGAGAGCCGGCCCGCGTGCTCTGCAACAAGGACCCA
TTTACGCTCAAGTCCTCGGTCTACCTGTCGCGCCTGTTCCCCAACTCCAAGTTCCTGCTG
ATGGTGCGGGACGGCCGGGCCTCCGTGCACTCCATGATCACGCGCAAAGTCACCATTGCG
GGCTTTGACCTCAGCAGCTACCGTGACTGCCTCACCAAGTGGAACAAGGCCATCGAGGTG
ATGTACGCCCAGTGCATGGAGGTAGGCAAGGAGAAGTGCTTGCCTGTGTACTACGAGCAG
CTGGTGCTGCACCCCAGGCGCTCACTCAAGCTCATCCTCGACTTCCTCGGCATCGCCTGG
AGCGACGCTGTCCTCCACCATGAAGACCTCATTGGCAAGCCCGGTGGTGTCTCCCTGTCC
AAGATCGAGCGGTCCACGGACCAGGTCATCAAGCCTGTTAACCTGGAAGCGCTCTCCAAG
TGGACTGGCCACATCCCTGGGGATGTGGTGCGGGACATGGCCCAGATCGCCCCCATGCTG
GCTCAGCTCGGCTATGACCCTTATGCAAACCCCCCCAACTATGGCAACCCTGACCCCTTC
GTCATCAACAACACACAGCGGGTCTTGAAAGGGGACTATAAAACACCAGCCAATCTGAAA
GGATATTTTCAGGTGAACCAGAACAGCACCTCCTCCCACTTAGGAAGCTCGTGA
|
| Enzyme 12 GenBank Gene ID |
AF049891  |
| Enzyme 12 GeneCard ID |
TPST2  |
| Enzyme 12 GenAtlas ID |
TPST2  |
| Enzyme 12 HGNC ID |
HGNC:12021  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
22q12.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Beisswanger R, Corbeil D, Vannier C, Thiele C, Dohrmann U, Kellner R, Ashman K, Niehrs C, Huttner WB: Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11134-9. [PubMed
]
- Ouyang YB, Moore KL: Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans. J Biol Chem. 1998 Sep 18;273(38):24770-4. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5591 |
| Enzyme 13 Name |
Sulfotransferase family cytosolic 2B member 1 |
| Enzyme 13 Synonyms |
- ST2B1
- Sulfotransferase 2B1
- Alcohol sulfotransferase
- Hydroxysteroid sulfotransferase 2
|
| Enzyme 13 Gene Name |
SULT2B1 |
| Enzyme 13 Protein Sequence |
>Sulfotransferase family cytosolic 2B member 1
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS
|
| Enzyme 13 Number of Residues |
365 |
| Enzyme 13 Molecular Weight |
41307.3 |
| Enzyme 13 Theoretical pI |
5.05 |
| Enzyme 13 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 13 General Function |
Involved in sulfotransferase activity |
| Enzyme 13 Specific Function |
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 13 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 13 Reactions |
- 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate [RN:R00629]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
31563386  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O00204  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
ST2B1_HUMAN  |
| Enzyme 13 PDB ID |
1Q1Q  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1098 bp
ATGGACGGGCCCGCCGAGCCCCAGATCCCGGGCTTGTGGGACACCTATGAAGATGACATC
TCGGAAATCAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAGGGCGTCCCCTTCCCC
GTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACCCAAGATGTGCGGGAC
GACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGGATGATCGAGATCATC
TGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTGCCCATCTGGGAGCGG
GCACCCTGGTGTGAGACCATTGTGGGTGCCTTCAGCCTCCCGGACCAGTACAGCCCCCGC
CTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTCTTCAGCTCCAAGGCC
AAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCCCTCTATCATTACTCC
AAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTCCTGAGGGACTTCCTC
AAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGCTGGCTTCGGATGAAG
GGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAGGACTTACAGGGCTCC
GTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAGGCACTGGGCTCCGTC
GTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCCAACTACACGCTGCTG
CCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAAGGGGTCTGCGGCGAC
TGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGTGCCTACCGCAAGCAG
ATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAGGACGGCAGCCCAGAT
CCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCCAACACCAGCCTGGAG
CGTGAGCCCAGACCCAACTCCAGCCCCAGCCCCAGCCCCGGCCAGGCCTCTGAGACCCCG
CACCCACGACCCTCATAA
|
| Enzyme 13 GenBank Gene ID |
NM_177973.1  |
| Enzyme 13 GeneCard ID |
SULT2B1  |
| Enzyme 13 GenAtlas ID |
SULT2B1  |
| Enzyme 13 HGNC ID |
HGNC:11459  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
19q13.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5592 |
| Enzyme 14 Name |
Sulfotransferase 1A3/1A4 |
| Enzyme 14 Synonyms |
- ST1A3/ST1A4
- Aryl sulfotransferase 1A3/1A4
- Catecholamine-sulfating phenol sulfotransferase
- HAST3
- M-PST
- Monoamine-sulfating phenol sulfotransferase
- Placental estrogen sulfotransferase
- Sulfotransferase, monoamine-preferring
- Thermolabile phenol sulfotransferase
- TL-PST
|
| Enzyme 14 Gene Name |
SULT1A3 |
| Enzyme 14 Protein Sequence |
>Sulfotransferase 1A3/1A4
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDM
IYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLD
QKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNY
TTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
|
| Enzyme 14 Number of Residues |
295 |
| Enzyme 14 Molecular Weight |
34196.0 |
| Enzyme 14 Theoretical pI |
5.88 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in sulfotransferase activity |
| Enzyme 14 Specific Function |
Catalyzes the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs |
| Enzyme 14 Pathways |
- Sulfate and Sulfite Metabolism (map00920
)
|
| Enzyme 14 Reactions |
- 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate [RN:R01242]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P50224  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
ST1A3_HUMAN  |
| Enzyme 14 PDB ID |
1CJM  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>888 bp
ATGGAGCTGATCCAGGACACCTCCCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAAGCCCGACCTGATGAC
CTGCTCATCAACACCTACCCCAAGTCTGGCACCACCTGGGTGAGCCAGATACTGGACATG
ATCTACCAGGGCGGCGACCTAGAGAAGTGTAACCGGGCTCCCATCTACGTACGGGTGCCC
TTCCTTGAGGTCAATGATCCAGGGGAACCCTCAGGGCTGGAGACTCTGAAAGACACACCG
CCCCCACGGCTCATCAAGTCACACCTGCCCCTGGCTCTGCTCCCTCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGAAACCCAAAGGACGTGGCGGTCTCCTACTAC
CATTTCCACCGTATGGAAAAGGCGCACCCTGAGCCTGGGACCTGGGACAGCTTCCTGGAA
AAGTTCATGGCTGGAGAAGTGTCCTACGGGTCCTGGTACCAGCACGTGCAGGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACCATG
GACTTCATGGTTCAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCCCCAGGAGCTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
|
| Enzyme 14 GenBank Gene ID |
L19956  |
| Enzyme 14 GeneCard ID |
SULT1A3  |
| Enzyme 14 GenAtlas ID |
SULT1A3  |
| Enzyme 14 HGNC ID |
HGNC:11455  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
16p11.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5989 |
| Enzyme 15 Name |
Carbohydrate sulfotransferase 7 |
| Enzyme 15 Synonyms |
- Chondroitin 6-sulfotransferase 2
- C6ST-2
- Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5
- GST-5
- N-acetylglucosamine 6-O-sulfotransferase 4
- GlcNAc6ST-4
- Gn6st-4
|
| Enzyme 15 Gene Name |
CHST7 |
| Enzyme 15 Protein Sequence |
>Carbohydrate sulfotransferase 7
MKGRRRRRREYCKFALLLVLYTLVLLLVPSVLDGGRDGDKGAEHCPGLQRSLGVWSLEAA
AAGEREQGAEARAAEEGGANQSPRFPSNLSGAVGEAVSREKQHIYVHATWRTGSSFLGEL
FNQHPDVFYLYEPMWHLWQALYPGDAESLQGALRDMLRSLFRCDFSVLRLYAPPGDPAAR
APDTANLTTAALFRWRTNKVICSPPLCPGAPRARAEVGLVEDTACERSCPPVAIRALEAE
CRKYPVVVIKDVRLLDLGVLVPLLRDPGLNLKVVQLFRDPRAVHNSRLKSRQGLLRESIQ
VLRTRQRGDRFHRVLLAHGVGARPGGQSRALPAAPRADFFLTGALEVICEAWLRDLLFAR
GAPAWLRRRYLRLRYEDLVRQPRAQLRRLLRFSGLRALAALDAFALNMTRGAAYGADRPF
HLSARDAREAVHAWRERLSREQVRQVEAACAPAMRLLAYPRSGEEGDAEQPREGETPLEM
DADGAT
|
| Enzyme 15 Number of Residues |
486 |
| Enzyme 15 Molecular Weight |
54265.6 |
| Enzyme 15 Theoretical pI |
9.96 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- Golgi membrane
- cell part
- membrane
- organelle membrane
|
|
| Enzyme 15 General Function |
Involved in sulfotransferase activity |
| Enzyme 15 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 15 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 15 Reactions |
- 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
9309344  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9NS84  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
CHST7_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1461 bp
ATGAAGGGCCGGCGGCGGCGACGCCGAGAGTACTGCAAGTTCGCGCTGCTGTTGGTGCTG
TACACGCTGGTGCTGTTGCTCGTCCCCTCCGTATTGGACGGCGGCCGCGACGGGGACAAG
GGCGCCGAGCACTGCCCCGGCCTGCAGCGCAGCCTGGGAGTGTGGAGCCTGGAGGCGGCG
GCGGCCGGCGAACGCGAGCAGGGAGCGGAGGCGCGGGCCGCCGAGGAAGGGGGCGCGAAC
CAGTCTCCTCGGTTCCCAAGCAACCTCAGCGGCGCTGTCGGGGAGGCAGTGTCTCGCGAG
AAGCAGCACATCTACGTGCATGCCACCTGGCGCACCGGCTCGTCCTTCCTGGGCGAACTC
TTTAACCAGCACCCGGACGTTTTCTACTTGTATGAGCCCATGTGGCATCTATGGCAGGCG
CTGTATCCGGGCGACGCCGAGAGCTTGCAGGGCGCGCTGCGCGACATGCTGCGTTCGCTC
TTCCGCTGCGACTTCTCCGTGCTGCGGCTGTACGCGCCGCCGGGGGACCCCGCTGCGCGC
GCCCCGGACACGGCCAATCTTACCACGGCCGCCCTCTTCCGCTGGCGGACTAACAAGGTC
ATCTGCTCGCCGCCACTGTGTCCTGGCGCACCCCGTGCCCGGGCCGAGGTGGGCCTCGTC
GAGGACACCGCCTGCGAGCGCAGCTGCCCACCCGTGGCGATACGCGCCCTGGAGGCCGAG
TGCCGAAAGTACCCGGTGGTGGTCATCAAGGACGTGCGCCTGCTCGATCTGGGCGTGCTG
GTGCCCCTGTTGCGTGATCCAGGCCTCAACCTGAAGGTGGTGCAGCTTTTCCGCGACCCG
AGGGCGGTGCACAACTCGCGCCTCAAGTCTAGGCAGGGACTGCTGCGCGAGAGCATCCAG
GTGCTGCGCACCCGCCAGAGGGGCGACCGCTTCCACCGTGTGCTGCTGGCGCACGGCGTG
GGTGCTCGCCCCGGGGGCCAGTCTCGCGCGCTGCCCGCCGCGCCGCGCGCCGATTTCTTC
CTGACCGGTGCGCTCGAGGTGATCTGCGAAGCCTGGCTGCGCGATCTGCTTTTCGCGCGC
GGCGCGCCCGCCTGGCTGCGGCGCCGCTACCTGAGGCTGCGCTATGAGGACCTGGTGCGG
CAGCCACGCGCCCAGCTGCGCCGCCTGCTGCGCTTCTCCGGGCTACGCGCGCTCGCAGCG
CTCGATGCCTTCGCGCTCAACATGACTCGCGGCGCGGCCTACGGCGCCGACCGGCCCTTC
CACCTGTCAGCGCGCGACGCCCGGGAGGCGGTGCACGCCTGGCGCGAGCGCCTGAGCCGA
GAGCAGGTGCGCCAGGTGGAGGTCGCCTGCGCTCCAGCCATGCGTCTGCTCGCCTACCCT
CGCAGCGGAGAGGAGGGCGACGCGGAGCAGCCCAGGGAAGGGGAGACGCCGCTGGAGATG
GATGCCGACGGCGCCACGTAG
|
| Enzyme 15 GenBank Gene ID |
AB037187  |
| Enzyme 15 GeneCard ID |
CHST7  |
| Enzyme 15 GenAtlas ID |
CHST7  |
| Enzyme 15 HGNC ID |
HGNC:13817  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Uchimura K, Fasakhany F, Kadomatsu K, Matsukawa T, Yamakawa T, Kurosawa N, Muramatsu T: Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities. Biochem Biophys Res Commun. 2000 Aug 2;274(2):291-6. [PubMed
]
- 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
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
12871 |
| Enzyme 16 Name |
Carbohydrate sulfotransferase 15 |
| Enzyme 16 Synonyms |
- B-cell RAG-associated gene protein
- hBRAG
- N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
- GalNAc4S-6ST
|
| Enzyme 16 Gene Name |
CHST15 |
| Enzyme 16 Protein Sequence |
>Carbohydrate sulfotransferase 15
MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEV
RTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNP
SLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQE
LHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHL
AHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRL
RDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTF
FYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVT
EALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLED
HASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFY
RPFNARLAQVLADEAFAWKTT
|
| Enzyme 16 Number of Residues |
561 |
| Enzyme 16 Molecular Weight |
64925.7 |
| Enzyme 16 Theoretical pI |
8.40 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in sulfotransferase activity |
| Enzyme 16 Specific Function |
Sulfotransferase that transfers sulfate from 3'- phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non- reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B- cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo |
| Enzyme 16 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
- Glycan structures - biosynthesis 1 (map01030
)
|
| Enzyme 16 Reactions |
- (1) 3'-phosphoadenylyl sulfate + dermatan = adenosine 3',5'-bisphosphate + dermatan 6'-sulfate [RN:R07288]
- (2) 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate [RN:R02181]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
45505173  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q7LFX5  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
CHSTF_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1686 bp
ATGAGGCACTGCATTAATTGCTGCATACAGCTGTTACCCGACGGCGCACACAAGCAGCAG
GTCAACTGCCAAGGGGGCCCCCATCACGGTCACCAGGCGTGCCCCACGTGCAAAGGAGAA
AACAAAATTCTGTTTCGTGTGGACAGTAAGCAGATGAACTTGCTTGCTGTTCTCGAAGTG
AGGACTGAAGGGAACGAAAACTGGGGTGGGTTTTTGCGCTTCAAAAAGGGGAAGCGATGT
AGCCTCGTTTTTGGACTGATAATAATGACCTTGGTAATGGCTTCTTACATCCTTTCTGGG
GCCCACCAAGAGCTTCTGATCTCATCACCTTTCCATTACGGAGGCTTCCCCAGCAACCCC
AGCTTGATGGACAGCGAAAACCCAAGTGACACAAAGGAGCATCACCACCAATCCTCTGTA
AATAATATTTCATACATGAAGGACTATCCAAGCATTAAATTAATTATCAACAGCATCACA
ACTAGGATTGAGTTCACGACCAGACAGCTCCCAGACTTAGAAGACCTTAAGAAGCAGGAG
TTGCATATGTTTTCAGTCATCCCCAACAAATTCCTTCCAAACAGTAAGAGCCCCTGTTGG
TACGAGGAGTTCTCGGGGCAGAACACCACCGACCCCTACCTCACCAACTCCTACGTGCTC
TACTCCAAGCGCTTCCGCTCCACCTTCGACGCCCTGCGCAAGGCCTTCTGGGGCCACCTG
GCGCACGCGCACGGGAAGCACTTCCGCCTGCGCTGCCTGCCGCACTTCTACATCATAGGG
CAGCCCAAGTGCGGGACCACAGACCTCTATGACCGCCTGCGGCTGCACCCTGAGGTCAAG
TTCTCCGCCATCAAGGAGCCACACTGGTGGACCCGGAAGCGCTTTGGAATCGTCCGCCTA
AGAGATGGGCTGCGAGACCGCTATCCCGTGGAAGATTATCTGGACCTCTTTGACCTGGCC
GCACACCAGATCCATCAAGGACTGCAGGCCAGCTCTGCAAAGGAGCAGAGCAAGATGAAT
ACAATCATTATCGGGGAGGCCAGTGCCTCCACGATGTGGGATAATAATGCCTGGACGTTC
TTCTACGACAACAGCACGGATGGCGAGCCACCGTTTCTGACGCAGGACTTCATCCACGCC
TTTCAGCCAAATGCCAGACTGATTGTCATGCTCAGGGACCCTGTGGAGAGGTTGTACTCA
GACTATCTCTACTTTGCAAGTTCGAATAAATCCGCGGACGACTTCCATGAGAAAGTGACA
GAAGCACTGCAGCTGTTTGAAAATTGCATGCTTGATTATTCACTGCGCGCCTGCGTCTAC
AACAACACCCTCAACAACGCCATGCCTGTGAGGCTCCAGGTTGGGCTCTATGCTGTGTAC
CTTCTGGACTGGCTCAGCGTTTTTGACAAGCAACAGTTTCTCATTCTTCGCCTGGAAGAT
CATGCATCCAACGTCAAGTACACCATGCACAAGGTCTTCCAGTTTCTGAACCTAGGGCCC
TTAAGTGAGAAGCAGGAGGCTTTGATGACCAAGAGCCCCGCATCCAATGCACGGCGTCCC
GAGGACCGGAACCTGGGGCCCATGTGGCCCATCACACAGAAGATTCTGCGGGATTTCTAC
AGGCCCTTCAACGCTAGGCTGGCGCAGGTCCTCGCGGATGAGGCGTTTGCGTGGAAGACG
ACGTGA
|
| Enzyme 16 GenBank Gene ID |
NM_015892.3  |
| Enzyme 16 GeneCard ID |
CHST15  |
| Enzyme 16 GenAtlas ID |
CHST15  |
| Enzyme 16 HGNC ID |
HGNC:18137  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
10q26 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- 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
]
- Yuki M, Yoshinaga K, Yamakawa H, Sakurada K, Sato S, Yajima A, Horii A: Structure, expression and mutational analysis of the hBRAG gene on 10q in the frequently deleted region in human endometrial cancer. Oncol Rep. 2000 Nov-Dec;7(6):1339-42. [PubMed
]
- 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
]
- 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
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Verkoczy LK, Guinn B, Berinstein NL: Characterization of the human B cell RAG-associated gene, hBRAG, as a B cell receptor signal-enhancing glycoprotein dimer that associates with phosphorylated proteins in resting B cells. J Biol Chem. 2000 Jul 14;275(28):20967-79. [PubMed
]
- Ohtake S, Kimata K, Habuchi O: A unique nonreducing terminal modification of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase. J Biol Chem. 2003 Oct 3;278(40):38443-52. Epub 2003 Jul 21. [PubMed
]
- Sawada T, Fujii S, Nakano H, Ohtake S, Kimata K, Habuchi O: Synthesis of sulfated phenyl 2-acetamido-2-deoxy-D-galactopyranosides. 4-O-Sulfated phenyl 2-acetamido-2-deoxy-beta-D-galactopyranoside is a competitive acceptor that decreases sulfation of chondroitin sulfate by N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase. Carbohydr Res. 2005 Sep 5;340(12):1983-96. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
13112 |
| Enzyme 17 Name |
cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase |
| Enzyme 17 Synonyms |
- PIP gene
- 3'(2', 5'-bisphosphate nucleotidase 1, isoform CRA_a
|
| Enzyme 17 Gene Name |
BPNT1 |
| Enzyme 17 Protein Sequence |
>cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
|
| Enzyme 17 Number of Residues |
308 |
| Enzyme 17 Molecular Weight |
33393 |
| Enzyme 17 Theoretical pI |
5.41 |
| Enzyme 17 GO Classification |
Not Available |
| Enzyme 17 General Function |
Carbohydrate transport and metabolism |
| 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 |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
158257318  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
A8K7C8  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
A8K7C8_HUMAN  |
| Enzyme 17 PDB ID |
1JP4  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
AK291943  |
| Enzyme 17 GeneCard ID |
A8K7C8  |
| 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  |
| Enzyme 17 General References |
Not Available |
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
15180 |
| Enzyme 18 Name |
Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2 |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
SULT1A2 |
| Enzyme 18 Protein Sequence |
>Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 2
MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDM
IYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLD
QKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW
ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNY
TTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
|
| Enzyme 18 Number of Residues |
295 |
| Enzyme 18 Molecular Weight |
34311 |
| Enzyme 18 Theoretical pI |
7.32 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| 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 |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
109731387  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q14CJ7  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
Q14CJ7_HUMAN  |
| Enzyme 18 PDB ID |
1LS6  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>888 bp
ATGGAGCTGATCCAGGACATCTCTCGCCCGCCACTGGAGTACGTGAAGGGGGTCCCGCTC
ATCAAGTACTTTGCAGAGGCACTGGGGCCCCTGCAGAGCTTCCAGGCCCGGCCTGATGAC
CTGCTCATCAGCACCTACCCCAAGTCCGGCACCACCTGGGTGAGCCAGATTCTGGACATG
ATCTACCAGGGCGGTGACCTGGAAAAGTGTCACCGAGCTCCCATCTTCATGCGGGTGCCC
TTCCTTGAGTTCAAAGTCCCAGGGATTCCCTCAGGGATGGAGACTCTGAAAAACACACCA
GCCCCACGACTCCTGAAGACACACCTGCCCCTGGCTCTGCTCCCCCAGACTCTGTTGGAT
CAGAAGGTCAAGGTGGTCTATGTTGCCCGCAACGCAAAGGATGTGGCGGTTTCCTACTAC
CACTTCTACCACATGGCCAAAGTGTACCCTCACCCTGGGACCTGGGAAAGCTTCCTGGAG
AAGTTCATGGCTGGAGAAGTGTCCTATGGGTCCTGGTACCAGCACGTGCAAGAGTGGTGG
GAGCTGAGCCGCACCCACCCTGTTCTCTACCTCTTCTATGAAGACATGAAGGAGAACCCC
AAAAGGGAGATTCAAAAGATCCTGGAGTTTGTGGGGCGCTCCCTGCCAGAGGAGACTGTG
GACCTCATGGTTGAGCACACGTCGTTCAAGGAGATGAAGAAGAACCCTATGACCAACTAC
ACCACCGTCCGCCGGGAGTTCATGGACCACAGCATCTCCCCCTTCATGAGGAAAGGCATG
GCTGGGGACTGGAAGACCACCTTCACCGTGGCGCAGAATGAGCGCTTCGATGCGGACTAT
GCGGAGAAGATGGCAGGCTGCAGCCTCAGCTTCCGCTCTGAGCTGTGA
|
| Enzyme 18 GenBank Gene ID |
BC113727  |
| Enzyme 18 GeneCard ID |
Q14CJ7  |
| Enzyme 18 GenAtlas ID |
SULT1A2  |
| Enzyme 18 HGNC ID |
HGNC:11454  |
| Enzyme 18 Chromosome Location |
16 |
| Enzyme 18 Locus |
16p12.1 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- 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
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
15181 |
| Enzyme 19 Name |
Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 |
| Enzyme 19 Synonyms |
- SubName: Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1, isoform CRA_a
- SubName: cDNA FLJ77905, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1 (SULT2A1), mRNA
- SubName: cDNA, FLJ93953, highly similar to Homo sapiens sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA) -preferring, member 1 (SULT2A1), mRNA
|
| Enzyme 19 Gene Name |
SULT2A1 |
| Enzyme 19 Protein Sequence |
>Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
|
| Enzyme 19 Number of Residues |
285 |
| Enzyme 19 Molecular Weight |
33779.6 |
| Enzyme 19 Theoretical pI |
5.76 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in sulfotransferase activity |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
158259783  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
A8K015  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
A8K015_HUMAN  |
| Enzyme 19 PDB ID |
1OV4  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>858 bp
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAACGGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
|
| Enzyme 19 GenBank Gene ID |
AK289380  |
| Enzyme 19 GeneCard ID |
SULT2A1  |
| Enzyme 19 GenAtlas ID |
SULT2A1  |
| Enzyme 19 HGNC ID |
HGNC:11458  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
19q13.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
15182 |
| Enzyme 20 Name |
cDNA FLJ75927, highly similar to Homo sapiens carbohydrate (chondroitin 4) sulfotransferase 11 (CHST11), mRNA (Carbohydrate (Chondroitin 4) sulfotransferase 11, isoform CRA_a) |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
CHST11 |
| Enzyme 20 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 20 Number of Residues |
352 |
| Enzyme 20 Molecular Weight |
41555 |
| Enzyme 20 Theoretical pI |
9.07 |
| 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 |
Not Available |
| Enzyme 20 Pfam Domain Function |
Not Available |
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
158255282  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
A8K4F8  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
A8K4F8_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1059 bp
ATGAAGCCAGCGCTGCTGGAAGTGATGAGGATGAACAGAATCTGCCGGATGGTGCTGGCC
ACTTGCTTGGGATCCTTTATCCTGGTCATCTTCTATTTCCAAAGTATGTTGCACCCAGTC
ATGCGGAGGAATCCCTTTGGTGTGGACATCTGCTGCCGGAAGGGGTCCCGAAGCCCCCTG
CAGGAACTCTACAACCCAATCCAGCTGGAGCTCTCAAACACTGCTGTCCTGCACCAGATG
CGGCGGGACCAGGTGACAGACACGTGCCGAGCCAACAGCGCCACAAGCCGTAAGCGGAGG
GTGCTGACCCCCAACGACCTGAAGCACTTGGTGGTGGATGAGGACCACGAGCTCATCTAC
TGCTACGTGCCCAAGGTGGCCTGCACCAACTGGAAGCGGCTCATGATGGTCCTGACCGGG
CGGGGGAAGTACAGCGACCCCATGGAGATCCCGGCCAACGAGGCACACGTCTCCGCCAAC
CTGAAGACCCTGAACCAGTACAGCATCCCAGAAATCAACCACCGCTTGAAAAGCTACATG
AAGTTCCTGTTTGTCCGGGAGCCCTTCGAGAGGCTAGTGTCCGCCTACCGCAACAAGTTC
ACCCAGAAGTACAACATCTCCTTCCACAAGCGGTACGGCACCAAGATCATCAAACGCCAG
CGGAAGAACGCCACCCAGGAGGCCCTGCGCAAAGGGGACGATGTCAAATTCGAGGAGTTT
GTGGCCTATCTCATCGACCCACACACCCAGCGGGAGGAGCCTTTCAACGAACACTGGCAA
ACCGTCTACTCACTCTGCCATCCCTGCCACATCCACTATGACCTCGTGGGCAAGTACGAG
ACACTGGAAGAGGATTCTAATTACGTCCTGCAGCTGGCAGGAGTGGGCAGCTACCTGAAG
TTCCCCACCTATGCAAAGTCTACGAGAACTACTGATGAAATGACCACAGAATTCTTCCAG
AACATCAGCTCAGAGCACCAAACGCAGCTGTACGAAGTCTACAAACTCGATTTTTTAATG
TTCAATTACTCAGTGCCAAGCTACCTGAAATTGGAATAA
|
| Enzyme 20 GenBank Gene ID |
AK290923  |
| Enzyme 20 GeneCard ID |
A8K4F8  |
| Enzyme 20 GenAtlas ID |
Not Available |
| Enzyme 20 HGNC ID |
Not Available |
| Enzyme 20 Chromosome Location |
12 |
| Enzyme 20 Locus |
12q |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
Not Available |
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
15183 |
| Enzyme 21 Name |
Carbohydrate (Chondroitin 4) sulfotransferase 12 |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
CHST12 |
| Enzyme 21 Protein Sequence |
>Carbohydrate (Chondroitin 4) sulfotransferase 12
MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDREL
TADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQ
QAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKR
VMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTK
FLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSF
ANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDR
QLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
|
| Enzyme 21 Number of Residues |
414 |
| Enzyme 21 Molecular Weight |
48415 |
| Enzyme 21 Theoretical pI |
9.69 |
| Enzyme 21 GO Classification |
Not Available |
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Not Available |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
A4D1Z9  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
A4D1Z9_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
CH236953  |
| Enzyme 21 GeneCard ID |
A4D1Z9  |
| 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  |
| Enzyme 21 General References |
- 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
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
15184 |
| Enzyme 22 Name |
Tyrosylprotein sulfotransferase 1 |
| Enzyme 22 Synonyms |
- SubName: Tyrosylprotein sulfotransferase 1, isoform CRA_a
- SubName: cDNA, FLJ93583, Homo sapiens tyrosylprotein sulfotransferase 1 (TPST1), mRNA
|
| Enzyme 22 Gene Name |
TPST1 |
| Enzyme 22 Protein Sequence |
>Tyrosylprotein sulfotransferase 1
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPVKLESTRTTVRTGLDLKAN
KTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKE
KIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFL
LMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYE
QLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALS
KWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKIIENTRRVYKGEFQLPDFL
KEKPQTEQVE
|
| Enzyme 22 Number of Residues |
370 |
| Enzyme 22 Molecular Weight |
42188.1 |
| Enzyme 22 Theoretical pI |
9.49 |
| Enzyme 22 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in sulfotransferase activity |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
189053670  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
A4D2M0  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
A4D2M0_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1113 bp
ATGGTTGGAAAGCTGAAGCAGAACTTACTATTGGCATGTCTGGTGATTAGTTCTGTGACT
GTGTTTTACCTGGGCCAGCATGCCATGGAATGCCATCACCGGATAGAGGAACGTAGCCAG
CCAGTCAAATTGGAGAGCACAAGGACCACTGTGAGAACTGGCCTGGACCTCAAAGCCAAC
AAAACCTTTGCCTATCACAAAGATATGCCTTTAATATTTATTGGAGGTGTGCCTCGGAGT
GGAACCACACTCATGAGGGCCATGCTGGACGCACATCCTGACATTCGCTGTGGAGAGGAA
ACCAGGGTCATTCCCCGAATCCTGGCCCTGAAGCAGATGTGGTCACGGTCAAGTAAAGAG
AAGATCCGCCTGGATGAGGCTGGTGTTACTGATGAAGTGCTGGATTCTGCCATGCAAGCC
TTCTTACTAGAAATTATCGTTAAGCATGGGGAGCCAGCCCCTTATTTATGTAATAAAGAT
CCTTTTGCCCTGAAATCTTTAACTTACCTTTCTAGGTTATTCCCCAATGCCAAATTTCTC
CTGATGGTCCGAGATGGCCGGGCATCAGTACATTCAATGATTTCTCGAAAAGTTACTATA
GCTGGATTTGATCTGAACAGCTATAGGGACTGTTTGACAAAGTGGAATCGTGCTATAGAG
ACCATGTATAACCAGTGTATGGAGGTTGGTTATAAAAAGTGCATGTTGGTTCACTATGAA
CAACTTGTCTTACATCCTGAACGGTGGATGAGAACACTCTTAAAGTTCCTCCAGATTCCA
TGGAACCACTCAGTATTGCACCATGAAGAGATGATTGGGAAAGCTGGGGGAGTGTCTCTG
TCAAAAGTGGAGAGATCTACAGACCAAGTAATCAAGCCAGTCAATGTAGGAGCTCTATCA
AAATGGGTTGGGAAGATACCGCCAGATGTTTTACAAGACATGGCAGTGATTGCTCCTATG
CTTGCCAAGCTTGGATATGACCCATATGCCAACCCACCTAACTACGGAAAACCTGATCCC
AAAATTATTGAAAACACTCGAAGGGTCTATAAGGGAGAATTCCAACTACCTGACTTTCTT
AAAGAAAAACCACAGACTGAGCAAGTGGAGTAG
|
| Enzyme 22 GenBank Gene ID |
AK313098  |
| Enzyme 22 GeneCard ID |
TPST1  |
| Enzyme 22 GenAtlas ID |
TPST1  |
| Enzyme 22 HGNC ID |
HGNC:12020  |
| Enzyme 22 Chromosome Location |
7 |
| Enzyme 22 Locus |
7q11.21 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- 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
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
15185 |
| Enzyme 23 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 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
HS3ST5 |
| Enzyme 23 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 23 Number of Residues |
346 |
| Enzyme 23 Molecular Weight |
40409 |
| Enzyme 23 Theoretical pI |
10.31 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
Not Available |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
Not Available |
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
158260837  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
A8K1J2  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
A8K1J2_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1041 bp
ATGCTATTCAAACAGCAGGCGTGGCTGAGACAGAAGCTCCTGGTGCTGGGAAGCCTTGCC
GTTGGGAGTCTCCTGTATCTAGTCGCCAGAGTTGGGAGCTTGGATAGGCTACAACCCATT
TGCCCCATTGAAGGTCGACTGGGTGGAGCCCGCACTCAGGCTGAATTCCCACTTCGCGCC
CTGCAGTTTAAGCGTGGCCTGCTGCACGAGTTCCGGAAGGGCAACGCTTCCAAGGAGCAG
GTTCGCCTCCATGACCTGGTCCAGCAGCTCCCCAAGGCCATTATCATTGGGGTGAGGAAA
GGAGGCACAAGGGCCCTGCTTGAAATGCTGAACCTACATCCGGCAGTAGTCAAAGCCTCT
CAAGAAATCCACTTTTTTGATAATGATGAGAATTATGGTAAGGGCATTGAGTGGTATAGG
AAAAAGATGCCTTTTTCCTACCCTCAGCAAATCACAATTGAAAAGAGCCCAGCATATTTT
ATCACAGAGGAGGTTCCAGAAAGGATTTACAAAATGAACTCATCCATCAAGTTGTTGATC
ATTGTCAGGGAGCCAACCACAAGAGCTATTTCTGATTATACTCAGGTGCTAGAGGGGAAG
GAGAGGAAGAACAAAACTTATTACAAGTTTGAGAAGCTGGCCATAGACCCTAATACATGC
GAAGTGAACACAAAATACAAAGCAGTAAGAACCAGCATCTACACCAAACATCTGGAAAGG
TGGTTGAAATACTTTCCAATTGAGCAATTTCATGTCGTCGATGGAGATCGCCTCATCACG
GAACCTCTGCCAGAACTTCAGCTCGTGGAGAAGTTCCTAAATCTGCCTCCAAGGATAAGT
CAATACAATTTATACTTCAATGCTACCAGAGGGTTTTACTGCTTGCGGTTTAATATTATC
TTTAATAAGTGCCTGGCGGGCAGCAAGGGGCGCATTCATCCAGAGGTGGACCCCTCTGTC
ATTACTAAATTGCGCAAATTCTTTCATCCTTTTAATCAAAAATTTTACCAGATCACTGGG
AGGACATTGAACTGGCCCTAA
|
| Enzyme 23 GenBank Gene ID |
AK289907  |
| Enzyme 23 GeneCard ID |
A8K1J2  |
| Enzyme 23 GenAtlas ID |
Not Available |
| Enzyme 23 HGNC ID |
Not Available |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
Not Available |
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
15186 |
| Enzyme 24 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 24 Synonyms |
Not Available |
| Enzyme 24 Gene Name |
HS3ST3A1 |
| Enzyme 24 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 24 Number of Residues |
406 |
| Enzyme 24 Molecular Weight |
44900 |
| Enzyme 24 Theoretical pI |
9.98 |
| Enzyme 24 GO Classification |
Not Available |
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Not Available |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
Not Available |
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
158257526  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
A8K7N2  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
A8K7N2_HUMAN  |
| Enzyme 24 PDB ID |
1T8U  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 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 24 GenBank Gene ID |
AK292047  |
| Enzyme 24 GeneCard ID |
A8K7N2  |
| Enzyme 24 GenAtlas ID |
Not Available |
| Enzyme 24 HGNC ID |
Not Available |
| Enzyme 24 Chromosome Location |
17 |
| Enzyme 24 Locus |
17p12-p11.2 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
Not Available |
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
16469 |
| Enzyme 25 Name |
cDNA FLJ90057 fis, clone HEMBA1003101, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20) |
| Enzyme 25 Synonyms |
- SubName: cDNA FLJ90658 fis, clone PLACE1004775, highly similar to Protein-tyrosine sulfotransferase 2 (EC 2.8.2.20)
- SubName: Tyrosylprotein sulfotransferase 2, isoform CRA_a
|
| Enzyme 25 Gene Name |
TPST2 |
| Enzyme 25 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 25 Number of Residues |
377 |
| Enzyme 25 Molecular Weight |
41912 |
| Enzyme 25 Theoretical pI |
9.42 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
- 3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate [RN:R02586] ALL_REAC R02586
|
| Enzyme 25 Pfam Domain Function |
Not Available |
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
B3KQA7  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
B3KQA7_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
AK074538  |
| Enzyme 25 GeneCard ID |
B3KQA7  |
| Enzyme 25 GenAtlas ID |
Not Available |
| Enzyme 25 HGNC ID |
Not Available |
| Enzyme 25 Chromosome Location |
22 |
| Enzyme 25 Locus |
22q12.1 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
16470 |
| Enzyme 26 Name |
cDNA FLJ39504 fis, clone PROST2017203, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 1 (EC 2.8.2.23) |
| Enzyme 26 Synonyms |
- SubName: Heparan sulfate (Glucosamine) 3-O-sulfotransferase 1, isoform CRA_a
|
| Enzyme 26 Gene Name |
HS3ST1 |
| Enzyme 26 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 26 Number of Residues |
307 |
| Enzyme 26 Molecular Weight |
35773 |
| Enzyme 26 Theoretical pI |
9.16 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- 3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate ALL_REAC (other) R04064
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
Not Available |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
B3KUA6  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
B3KUA6_HUMAN  |
| Enzyme 26 PDB ID |
1VKJ  |
| Enzyme 26 PDB File |
Show |
| Enzyme 26 3D Structure |
|
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
Not Available |
| Enzyme 26 GenBank Gene ID |
AK096823  |
| Enzyme 26 GeneCard ID |
B3KUA6  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
16471 |
| Enzyme 27 Name |
Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a |
| Enzyme 27 Synonyms |
- SubName: cDNA FLJ13661 fis, clone PLACE1011635, highly similar to Heparan sulfate glucosamine3-O-sulfotransferase 3B1
|
| Enzyme 27 Gene Name |
HS3ST3B1 |
| Enzyme 27 Protein Sequence |
>Heparan sulfate (Glucosamine) 3-O-sulfotransferase 3B1, isoform CRA_a
MGQRLSGGRSCLDVPGRLLPQPPPPPPPVRRKLALLFAMLCVWLYMFLYSCAGSCAAAPG
LLLLGSGSRAAHDPPALATAPDGTPPRLPFRAPPATPLASGKEMAEGAASPEEQSPEVPD
SPSPISSFFSGSGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKG
LAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQ
TLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERL
ISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEI
DREVVRRLREFYRPFNLKFYQMTGHDFGWD
|
| Enzyme 27 Number of Residues |
390 |
| Enzyme 27 Molecular Weight |
43325 |
| Enzyme 27 Theoretical pI |
10.14 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
B3KN58  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
B3KN58_HUMAN  |
| Enzyme 27 PDB ID |
1T8U  |
| Enzyme 27 PDB File |
Show |
| Enzyme 27 3D Structure |
|
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AK023723  |
| Enzyme 27 GeneCard ID |
B3KN58  |
| Enzyme 27 GenAtlas ID |
Not Available |
| Enzyme 27 HGNC ID |
Not Available |
| Enzyme 27 Chromosome Location |
17 |
| Enzyme 27 Locus |
17p12-p11.2 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |