1. Sulfate (ion 2-)
2. Sulfate anion
3. Sulfate anion(2-)
4. Sulfate dianion
5. Sulfate ion
6. Sulfate ion (SO42-)
7. Sulfate(2-)
8. Sulfuric acid ion(2-)
9. Sulphate

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• Cytoplasm
• endoplasmic reticulum
• Extracellular
• lysosome
• mitochondria

• Blood
• Urine

1. Eisenhofer G, Coughtrie MW, Goldstein DS: Dopamine sulphate: an enigma resolved. Clin Exp Pharmacol Physiol Suppl. 1999 Apr;26:S41-53. [PubMed ]
2. Ho HS, Lim SH, Loo S: The use of magnesium sulphate in the intensive care management of an Asian patient with tetanus. Ann Acad Med Singapore. 1999 Jul;28(4):586-9. [PubMed ]
3. Perrimon N, Bernfield M: Specificities of heparan sulphate proteoglycans in developmental processes. Nature. 2000 Apr 13;404(6779):725-8. [PubMed ]
4. Duley L, Henderson-Smart D: Magnesium sulphate versus diazepam for eclampsia. Cochrane Database Syst Rev. 2000;(2):CD000127. [PubMed ]
5. Duley L, Henderson-Smart D: Magnesium sulphate versus phenytoin for eclampsia. Cochrane Database Syst Rev. 2000;(2):CD000128. [PubMed ]
6. Duffy PE, Fried M: Malaria during pregnancy: parasites, antibodies and chondroitin sulphate A. Biochem Soc Trans. 1999 Aug;27(4):478-82. [PubMed ]
7. Bateman KL, Delehedde M, Sergeant N, Wartelle I, Vidyasagar R, Fernig DG: Heparan sulphate. Regulation of growth factors in the mammary gland. Adv Exp Med Biol. 2000;480:65-9. [PubMed ]
8. McCormick C, Duncan G, Tufaro F: Herpes simplex virus: discovering the link between heparan sulphate and hereditary bone tumours. Rev Med Virol. 2000 Nov-Dec;10(6):373-84. [PubMed ]
9. Manyemba J: Magnesium sulphate for eclampsia: putting the evidence into clinical practice. Cent Afr J Med. 2000 Jun;46(6):166-9. [PubMed ]
10. Duley L, Gulmezoglu AM: Magnesium sulphate versus lytic cocktail for eclampsia. Cochrane Database Syst Rev. 2001;(1):CD002960. [PubMed ]
11. Kornacka MK: [Magnesium sulphate in the treatment of ischemic-hypoxic neonatal encephalopathy] Neurol Neurochir Pol. 2001 Mar-Apr;35(2):299-308. [PubMed ]
12. Karas Z: [Skin patch test with nickel sulphate--an attempt of broader interpretation of the results] Pol Merkur Lekarski. 2002 Aug;13(74):143-6. [PubMed ]
13. Morgenstern DA, Asher RA, Fawcett JW: Chondroitin sulphate proteoglycans in the CNS injury response. Prog Brain Res. 2002;137:313-32. [PubMed ]
14. Crowther CA, Hiller JE, Doyle LW: Magnesium sulphate for preventing preterm birth in threatened preterm labour. Cochrane Database Syst Rev. 2002;(4):CD001060. [PubMed ]
15. Kakuta Y, Li L, Pedersen LC, Pedersen LG, Negishi M: Heparan sulphate N-sulphotransferase activity: reaction mechanism and substrate recognition. Biochem Soc Trans. 2003 Apr;31(2):331-4. [PubMed ]
16. Properzi F, Asher RA, Fawcett JW: Chondroitin sulphate proteoglycans in the central nervous system: changes and synthesis after injury. Biochem Soc Trans. 2003 Apr;31(2):335-6. [PubMed ]
17. Kjellen L: Glucosaminyl N-deacetylase/N-sulphotransferases in heparan sulphate biosynthesis and biology. Biochem Soc Trans. 2003 Apr;31(2):340-2. [PubMed ]
18. Catlow K, Deakin JA, Delehedde M, Fernig DG, Gallagher JT, Pavao MS, Lyon M: Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate. Biochem Soc Trans. 2003 Apr;31(2):352-3. [PubMed ]
19. Smetana R, Stuhlinger HG, Kiss K, Glogar DH: Intravenous magnesium sulphate in acute myocardial infarction--is the answer "MAGIC"? Magnes Res. 2003 Mar;16(1):65-9. [PubMed ]
20. Duley L, Gulmezoglu AM, Henderson-Smart DJ: Magnesium sulphate and other anticonvulsants for women with pre-eclampsia. Cochrane Database Syst Rev. 2003;(2):CD000025. [PubMed ]
21. van Horssen J, Wesseling P, van den Heuvel LP, de Waal RM, Verbeek MM: Heparan sulphate proteoglycans in Alzheimer's disease and amyloid-related disorders. Lancet Neurol. 2003 Aug;2(8):482-92. [PubMed ]
22. Markovich D, Murer H: The SLC13 gene family of sodium sulphate/carboxylate cotransporters. Pflugers Arch. 2004 Feb;447(5):594-602. Epub 2003 Aug 12. [PubMed ]
23. Nenci GG: Dermatan sulphate as an antithrombotic drug. Pathophysiol Haemost Thromb. 2002 Sep-Dec;32(5-6):303-7. [PubMed ]
24. Duley L, Henderson-Smart D: Magnesium sulphate versus diazepam for eclampsia. Cochrane Database Syst Rev. 2003;(4):CD000127. [PubMed ]
25. Duley L, Henderson-Smart D: Magnesium sulphate versus phenytoin for eclampsia. Cochrane Database Syst Rev. 2003;(4):CD000128. [PubMed ]
26. Thijs L, Fagard R, Forette F, Nawrot T, Staessen JA: Are low dehydroepiandrosterone sulphate levels predictive for cardiovascular diseases? A review of prospective and retrospective studies. Acta Cardiol. 2003 Oct;58(5):403-10. [PubMed ]
27. Rhodes KE, Fawcett JW: Chondroitin sulphate proteoglycans: preventing plasticity or protecting the CNS? J Anat. 2004 Jan;204(1):33-48. [PubMed ]
28. Gallagher JT, Turnbull JE: Heparan sulphate in the binding and activation of basic fibroblast growth factor. Glycobiology. 1992 Dec;2(6):523-8. [PubMed ]
29. Crespo-Santiago D: [The extracellular matrix of the central nervous system: chondroitin sulphate type proteoglycans and neural repair] Rev Neurol. 2004 May 1-15;38(9):843-51. [PubMed ]
30. Gallagher JT, Turnbull JE, Lyon M: Patterns of sulphation in heparan sulphate: polymorphism based on a common structural theme. Int J Biochem. 1992 Apr;24(4):553-60. [PubMed ]
31. Cheuk DK, Chau TC, Lee SL: A meta-analysis on intravenous magnesium sulphate for treating acute asthma. Arch Dis Child. 2005 Jan;90(1):74-7. [PubMed ]
32. Mittendorf R, Pryde PG: A review of the role for magnesium sulphate in preterm labour. BJOG. 2005 Mar;112 Suppl 1:84-8. [PubMed ]
33. Duley L: Evidence and practice: the magnesium sulphate story. Best Pract Res Clin Obstet Gynaecol. 2005 Feb;19(1):57-74. [PubMed ]
34. Rusnati M, Oreste P, Zoppetti G, Presta M: Biotechnological engineering of heparin/heparan sulphate: a novel area of multi-target drug discovery. Curr Pharm Des. 2005;11(19):2489-99. [PubMed ]
35. Hacker U, Nybakken K, Perrimon N: Heparan sulphate proteoglycans: the sweet side of development. Nat Rev Mol Cell Biol. 2005 Jul;6(7):530-41. [PubMed ]
36. Rozenberg P: [Magnesium sulphate for the management of preeclampsia] Gynecol Obstet Fertil. 2006 Jan;34(1):54-9. Epub 2006 Jan 6. [PubMed ]
37. Vives RR, Lortat-Jacob H, Fender P: Heparan sulphate proteoglycans and viral vectors : ally or foe? Curr Gene Ther. 2006 Feb;6(1):35-44. [PubMed ]
38. Kemp LE, Mulloy B, Gherardi E: Signalling by HGF/SF and Met: the role of heparan sulphate co-receptors. Biochem Soc Trans. 2006 Jun;34(Pt 3):414-7. [PubMed ]
39. Gallagher JT: Multiprotein signalling complexes: regional assembly on heparan sulphate. Biochem Soc Trans. 2006 Jun;34(Pt 3):438-41. [PubMed ]
40. Harmer NJ: Insights into the role of heparan sulphate in fibroblast growth factor signalling. Biochem Soc Trans. 2006 Jun;34(Pt 3):442-5. [PubMed ]
41. Stringer SE: The role of heparan sulphate proteoglycans in angiogenesis. Biochem Soc Trans. 2006 Jun;34(Pt 3):451-3. [PubMed ]
42. Kurup S, Abramsson A, Li JP, Lindahl U, Kjellen L, Betsholtz C, Gerhardt H, Spillmann D: Heparan sulphate requirement in platelet-derived growth factor B-mediated pericyte recruitment. Biochem Soc Trans. 2006 Jun;34(Pt 3):454-5. [PubMed ]
43. Rider CC: Heparin/heparan sulphate binding in the TGF-beta cytokine superfamily. Biochem Soc Trans. 2006 Jun;34(Pt 3):458-60. [PubMed ]
44. Lortat-Jacob H: Interferon and heparan sulphate. Biochem Soc Trans. 2006 Jun;34(Pt 3):461-4. [PubMed ]
45. Parish CR: The role of heparan sulphate in inflammation. Nat Rev Immunol. 2006 Sep;6(9):633-43. Epub 2006 Aug 18. [PubMed ]
46. Campo GM, Avenoso A, Campo S, Ferlazzo AM, Calatroni A: Chondroitin sulphate: antioxidant properties and beneficial effects. Mini Rev Med Chem. 2006 Dec;6(12):1311-20. [PubMed ]
47. Bishop JR, Schuksz M, Esko JD: Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature. 2007 Apr 26;446(7139):1030-7. [PubMed ]
48. Heisel J, Forster KK: [Therapy of osteoarthritis crystalline glucosamine sulphate/a review of the clinical effcacy] Arzneimittelforschung. 2007;57(4):203-17. [PubMed ]
49. Doyle LW, Crowther CA, Middleton P, Marret S: Magnesium sulphate for women at risk of preterm birth for neuroprotection of the fetus. Cochrane Database Syst Rev. 2007 Jul 18;(3):CD004661. [PubMed ]
50. Del Rio JA, Soriano E: Overcoming chondroitin sulphate proteoglycan inhibition of axon growth in the injured brain: lessons from chondroitinase ABC. Curr Pharm Des. 2007;13(24):2485-92. [PubMed ]
51. Peng L, Ye L, Guo X, Tan H, Zhou X, Wang C, Li R: Evaluation of formocresol versus ferric sulphate primary molar pulpotomy: a systematic review and meta-analysis. Int Endod J. 2007 Oct;40(10):751-7. Epub 2007 Aug 22. [PubMed ]
52. Bianchi-Bosisio A, D'Agrosa F, Gaboardi F, Gianazza E, Righetti PG: Sodium dodecyl sulphate electrophoresis of urinary proteins. J Chromatogr. 1991 Sep 13;569(1-2):243-60. [PubMed ]
53. Sutton DN, Tremlett MR, Woodcock TE, Nielsen MS: Management of autonomic dysfunction in severe tetanus: the use of magnesium sulphate and clonidine. Intensive Care Med. 1990;16(2):75-80. [PubMed ]
54. Murer H, Markovich D, Biber J: Renal and small intestinal sodium-dependent symporters of phosphate and sulphate. J Exp Biol. 1994 Nov;196:167-81. [PubMed ]
55. Thiele B, Steinbach F: Dextran sulphate induces a PKC and actin independent internalisation of CD4. Immunol Lett. 1994 Sep;42(1-2):105-10. [PubMed ]
56. Scott JE: Keratan sulphate--a 'reserve' polysaccharide? Eur J Clin Chem Clin Biochem. 1994 Apr;32(4):217-23. [PubMed ]
57. van Heerden PV, Jenkins IR, Woods WP, Rossi E, Cameron PD: Death by tanning--a case of fatal basic chromium sulphate poisoning. Intensive Care Med. 1994;20(2):145-7. [PubMed ]
58. Rosen SD, Bertozzi CR: Two selectins converge on sulphate. Leukocyte adhesion. Curr Biol. 1996 Mar 1;6(3):261-4. [PubMed ]
59. Izzo AA, Gaginella TS, Capasso F: The osmotic and intrinsic mechanisms of the pharmacological laxative action of oral high doses of magnesium sulphate. Importance of the release of digestive polypeptides and nitric oxide. Magnes Res. 1996 Jun;9(2):133-8. [PubMed ]
60. Khaw KT: Dehydroepiandrosterone, dehydroepiandrosterone sulphate and cardiovascular disease. J Endocrinol. 1996 Sep;150 Suppl:S149-53. [PubMed ]
61. Coombe DR: The role of stromal cell heparan sulphate in regulating haemopoiesis. Leuk Lymphoma. 1996 May;21(5-6):399-406. [PubMed ]
62. Stringer SE, Gallagher JT: Heparan sulphate. Int J Biochem Cell Biol. 1997 May;29(5):709-14. [PubMed ]
63. McGrath JA, Eady RA: Heparan sulphate proteoglycan and wound healing in skin. J Pathol. 1997 Nov;183(3):251-2. [PubMed ]
64. Gallagher JT: Structure-activity relationship of heparan sulphate. Biochem Soc Trans. 1997 Nov;25(4):1206-9. [PubMed ]
65. Wikipedia

1. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
3. Arylsulfatase D precursor
4. Arylsulfatase A precursor
5. Arylsulfatase B precursor
6. Arylsulfatase E precursor
7. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
8. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
9. Steryl-sulfatase precursor
10. Glutathione S-transferase Mu 2
11. Glutathione S-transferase Mu 1
12. Glutathione S-transferase Mu 3
13. Glutathione S-transferase A1
14. Glutathione S-transferase theta-2
15. Glutathione S-transferase Mu 5
16. Microsomal glutathione S-transferase 2
17. Glutathione transferase omega-1
18. Glutathione S-transferase A5
19. Glutathione S-transferase A2
20. Glutathione transferase omega-2
21. Glutathione S-transferase theta-1
22. Glutathione S-transferase P
23. Sulfite oxidase, mitochondrial precursor
24. Iduronate 2-sulfatase precursor
25. N-acetylglucosamine-6-sulfatase precursor
26. N-acetylgalactosamine-6-sulfatase precursor
27. Sulfate transporter
28. Solute carrier family 13 member 4
29. Solute carrier family 26 member 11
30. Uncharacterized protein GSTZ1
31. Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
32. cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
33. LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
34. cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a)
35. cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
36. cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)

1. E- NPP 1
2. Phosphodiesterase I/nucleotide pyrophosphatase 1
3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
4. NPPase]

MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED

• Nicotinate and Nicotinamide Metabolism (map00760 )
• Pantothenate and CoA Biosynthesis (map00770 )
• Purine Metabolism (map00230 )
• Riboflavin Metabolism (map00740 )
• Starch and Sucrose Metabolism (map00500 )

• A dinucleotide + H2O = 2 mononucleotides

• Phosphodiest (PF01663 )
• Somatomedin_B (PF01033 )

• None

• 77-97

ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA

1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed ]
2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed ]
3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed ]
5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed ]
6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed ]
7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed ]

1. E- NPP 3
2. Phosphodiesterase I/nucleotide pyrophosphatase 3
3. Phosphodiesterase I beta
4. PD-Ibeta
5. CD203c antigen[Includes: Alkaline phosphodiesterase I
6. NPPase]

MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI

• Nicotinate and Nicotinamide Metabolism (map00760 )
• Pantothenate and CoA Biosynthesis (map00770 )
• Purine Metabolism (map00230 )
• Riboflavin Metabolism (map00740 )
• Starch and Sucrose Metabolism (map00500 )

• A dinucleotide + H2O = 2 mononucleotides

• Phosphodiest (PF01663 )
• Somatomedin_B (PF01033 )

• 1-38

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

1. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]

1. ASD

MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEERGLLTAEASAHAEWGGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP

• Sulfatase (PF00884 )

• 1-33

• 206-225
• 229-251
• 292-314

ATGCGATCCGCCGCGCGGAGGGGACGCGCCGCGCCCGCCGCCAGGGACTCTTTGCCGGTG
CTACTGTTTTTATGCTTGCTTCTGAAGACGTGTGAACCTAAAACTGCAAATGCCTTTAAA
CCAAATATCCTACTGATCATGGCGGATGATCTAGGCACTGGGGATCTCGGTTGCTACGGG
AACAATACACTGAGAACGCCGAATATTGACCAGCTTGCAGAGGAAGGTGTGAGGCTCACT
CAGCACCTGGCGGCCGCCCCGCTCTGCACCCCAAGCCGAGCTGCATTCCTCACAGGGAGA
CATTCCTTCAGATCAGGCATGGACGCCAGCAATGGATACCGGGCCCTTCAGTGGAACGCA
GGCTCAGGTGGACTCCCTGAGAACGAAACCACTTTTGCAAGAATCTTGCAGCAGCATGGC
TATGCAACCGGCCTCATAGGAAAATGGCACCAGGGTGTGAATTGTGCATCCCGCGGGGAT
CACTGCCACCACCCCCTGAACCACGGATTTGACTATTTCTACGGCATGCCCTTCACGCTC
ACAAACGACTGTGACCCAGGCAGGCCCCCCGAAGTGGACGCCGCCCTGAGGGCGCAGCTC
TGGGGTTACACCCAGTTCCTGGCGCTGGGGATTCTCACCCTGGCTGCCGGCCAGACCTGC
GGTTTCTTCTCTGTCTCCGCGAGAGCAGTCACCGGCATGGCCGGCGTGGGCTGCCTGTTT
TTCATCTCTTGGTACTCCTCCTTCGGGTTTGTGCGACGCTGGAACTGTATCCTGATGAGA
AACCATGACGTCACGGAGCAACCCATGGTTCTGGAGAAAACAGCGAGTCTTATGCTAAAG
GAAGCTGTTTCCTATATTGAAAGACACAAGCATGGGCCATTTCTCCTCTTCCTTTCTTTG
CTGCATGTGCACATTCCCCTTGTGACCACGAGTGCATTCCTGGGGAAAAGTCAGCATGGC
TTATATGGTGATAATGTGGAGGAGATGGACTGGCTCATAGGTAAGGTTCTTAATGCCATC
GAAGACAATGGTTTAAAGAACTCAACATTCACGTATTTCACCTCTGACCATGGAGGACAT
TTAGAGGCAAGAGATGGACACAGCCAGTTAGGGGGATGGAACGGAATTTACAAAGGTGGG
AAGGGCATGGGAGGATGGGAAGGTGGGATCCGAGTGCCCGGGATCTTCCACTGGCCGGGG
GTGCTCCCGGCCGGCCGAGTGATTGGAGAGCCCACGAGCCTGATGGACGTGTTCCCTACT
GTGGTCCAGCTGGTGGGTGGCGAGGTGCCCCAGGACAGGGTGATTGATGGCCACAGCCTG
GTACCCTTGCTGCAGGGAGCTGAGGCACGCTCGGCACATGAGTTCCTGTTTCATTACTGT
GGGCAGCATCTTCACGCAGCACGCTGGCACCAGAAGGACAGTGGAAGCGTCTGGAAGGTT
CATTACACGACCCCGCAGTTCCACCCCGAGGAGCGGGGCCTGCTAACGGCCGAGGCGTCT
GCCCATGCTGAATGGGGAGGCGTGACCCATCACAGACCCCCTTTGCTCTTTGACCTCTCC
AGGGACCCCTCCGAGGCACGGCCCCTGACCCCCGACTCCGAGCCCCTGTACCACGCCGTG
ATAGCAAGGGTAGGTGCCGCGGTGTCGGAGCATCGGCAGACCCTGAGTCCTGTGCCCCAG
CAGTTTTCCATGAGCAACATCCTGTGGAAGCCGTGGCTGCAGCCGTGCTGCGGACATTTC
CCGTTCTGTTCATGCCACGAGGATGGGGATGGCACCCCCTGA

1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed ]
2. Urbitsch P, Salzer MJ, Hirschmann P, Vogt PH: Arylsulfatase D gene in Xp22.3 encodes two protein isoforms. DNA Cell Biol. 2000 Dec;19(12):765-73. [PubMed ]

1. ASA
2. Cerebroside-sulfatase[Contains: Arylsulfatase A component B
3. Arylsulfatase A component C]

MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFT
DFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGM
AGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIP
LLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAE
RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRC
GKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSP
LLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSL
TAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARG
EDPALQICCHPGCTPRPACCHCPDPHA

• Sphingolipid Metabolism (map00600 )

• A cerebroside 3-sulfate + H2O = a cerebroside + sulfate

• Sulfatase (PF00884 )

• 1-18

ATGGGGGCACCGCGGTCCCTCCTCCTGGCCCTGGCTGCTGGCCTGGCCGTTGCCCGTCCG
CCCAACATCGTGCTGATCTTTGCCGACGACCTCGGCTATGGGGACCTGGGCTGCTATGGG
CACCCCAGCTCTACCACTCCCAACCTGGACCAGCTGGCGGCGGGAGGGCTGCGGTTCACA
GACTTCTACGTGCCTGTGTCTCTGTGCACACCCTCTAGGGCCGCCCTCCTGACCGGCCGG
CTCCCGGTTCGGATGGGCATGTACCCTGGCGTCCTGGTGCCCAGCTCCCGGGGGGGCCTG
CCCCTGGAGGAGGTGACCGTGGCCGAAGTCCTGGCTGCCCGAGGCTACCTCACAGGAATG
GCCGGCAAGTGGCACCTTGGGGTGGGGCCTGAGGGGGCCTTCCTGCCCCCCCATCAGGGC
TTCCATCGATTTCTAGGCATCCCGTACTCCCACGACCAGGGCCCCTGCCAGAACCTGACC
TGCTTCCCGCCGGCCACTCCTTGCGACGGTGGCTGTGACCAGGGCCTGGTCCCCATCCCA
CTGTTGGCCAACCTGTCCGTGGAGGCGCAGCCCCCCTGGCTGCCCGGACTAGAGGCCCGC
TACATGGCTTTCGCCCATGACCTCATGGCCGACGCCCAGCGCCAGGATCGCCCCTTCTTC
CTGTACTATGCCTCTCACCACACCCACTACCCTCAGTTCAGTGGGCAGAGCTTTGCAGAG
CGTTCAGGCCGCGGGCCATTTGGGGACTCCCTGATGGAGCTGGATGCAGCTGTGGGGACC
CTGATGACAGCCATAGGGGACCTGGGGCTGCTTGAAGAGACGCTGGTCATCTTCACTGCA
GACAATGGACCTGAGACCATGCGTATGTCCCGAGGCGGCTGCTCCGGTCTCTTGCGGTGT
GGAAAGGGAACGACCTACGAGGGCGGTGTCCGAGAGCCTGCCTTGGCCTTCTGGCCAGGT
CATATCGCTCCCGGCGTGACCCACGAGCTGGCCAGCTCCCTGGACCTGCTGCCTACCCTG
GCAGCCCTGGCTGGGGCCCCACTGCCCAATGTCACCTTGGATGGCTTTGACCTCAGCCCC
CTGCTGCTGGGCACAGGCAAGAGCCCTCGGCAGTCTCTCTTCTTCTACCCGTCCTACCCA
GACGAGGTCCGTGGGGTTTTTGCTGTGCGGACTGGAAAGTACAAGGCTCACTTCTTCACC
CAGGGCTCTGCCCACAGTGATACCACTGCAGACCCTGCCTGCCACGCCTCCAGCTCTCTG
ACTGCTCATGAGCCCCCGCTGCTCTATGACCTGTCCAAGGACCCTGGTGAGAACTACAAC
CTGCTGGGGGGTGTGGCCGGGGCCACCCCAGAGGTGCTGCAAGCCCTGAAACAGCTTCAG
CTGCTCAAGGCCCAGTTAGACGCAGCTGTGACCTTCGGCCCCAGCCAGGTGGCCCGGGGC
GAGGACCCCGCCCTGCAGATCTGCTGTCATCCTGGCTGCACCCCCCGCCCAGCTTGCTGC
CATTGCCCAGATCCCCATGCCTGA

1. Stein C, Gieselmann V, Kreysing J, Schmidt B, Pohlmann R, Waheed A, Meyer HE, O'Brien JS, von Figura K: Cloning and expression of human arylsulfatase A. J Biol Chem. 1989 Jan 15;264(2):1252-9. [PubMed ]
2. Kreysing J, von Figura K, Gieselmann V: Structure of the arylsulfatase A gene. Eur J Biochem. 1990 Aug 17;191(3):627-31. [PubMed ]
3. 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 ]
4. Fujii T, Kobayashi T, Honke K, Gasa S, Ishikawa M, Shimizu T, Makita A: Proteolytic processing of human lysosomal arylsulfatase A. Biochim Biophys Acta. 1992 Jul 13;1122(1):93-8. [PubMed ]
5. Schmidt B, Selmer T, Ingendoh A, von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. [PubMed ]
6. Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W: Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry. 1998 Mar 17;37(11):3654-64. [PubMed ]
7. von Bulow R, Schmidt B, Dierks T, von Figura K, Uson I: Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. J Mol Biol. 2001 Jan 12;305(2):269-77. [PubMed ]
8. Gieselmann V, Zlotogora J, Harris A, Wenger DA, Morris CP: Molecular genetics of metachromatic leukodystrophy. Hum Mutat. 1994;4(4):233-42. [PubMed ]
9. Kappler J, von Figura K, Gieselmann V: Late-onset metachromatic leukodystrophy: molecular pathology in two siblings. Ann Neurol. 1992 Mar;31(3):256-61. [PubMed ]
10. Gieselmann V, Fluharty AL, Tonnesen T, Von Figura K: Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy. Am J Hum Genet. 1991 Aug;49(2):407-13. [PubMed ]
11. Kondo R, Wakamatsu N, Yoshino H, Fukuhara N, Miyatake T, Tsuji S: Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy. Am J Hum Genet. 1991 May;48(5):971-8. [PubMed ]
12. Polten A, Fluharty AL, Fluharty CB, Kappler J, von Figura K, Gieselmann V: Molecular basis of different forms of metachromatic leukodystrophy. N Engl J Med. 1991 Jan 3;324(1):18-22. [PubMed ]
13. Honke K, Kobayashi T, Fujii T, Gasa S, Xu M, Takamaru Y, Kondo R, Tsuji S, Makita A: An adult-type metachromatic leukodystrophy caused by substitution of serine for glycine-122 in arylsulfatase A. Hum Genet. 1993 Nov;92(5):451-6. [PubMed ]
14. Kafert S, Heinisch U, Zlotogora J, Gieselmann V: A missense mutation P136L in the arylsulfatase A gene causes instability and loss of activity of the mutant enzyme. Hum Genet. 1995 Feb;95(2):201-4. [PubMed ]
15. Hasegawa Y, Kawame H, Eto Y: Mutations in the arylsulfatase A gene of Japanese patients with metachromatic leukodystrophy. DNA Cell Biol. 1993 Jul-Aug;12(6):493-8. [PubMed ]
16. Harvey JS, Nelson PV, Carey WF, Robertson EF, Morris CP: An arylsulfatase A (ARSA) missense mutation (T274M) causing late-infantile metachromatic leukodystrophy. Hum Mutat. 1993;2(4):261-7. [PubMed ]
17. Kreysing J, Bohne W, Bosenberg C, Marchesini S, Turpin JC, Baumann N, von Figura K, Gieselmann V: High residual arylsulfatase A (ARSA) activity in a patient with late-infantile metachromatic leukodystrophy. Am J Hum Genet. 1993 Aug;53(2):339-46. [PubMed ]
18. Gieselmann V, Polten A, Kreysing J, von Figura K: Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9436-40. [PubMed ]
19. Barth ML, Fensom A, Harris A: Prevalence of common mutations in the arylsulphatase A gene in metachromatic leukodystrophy patients diagnosed in Britain. Hum Genet. 1993 Mar;91(1):73-7. [PubMed ]
20. Barth ML, Fensom A, Harris A: Missense mutations in the arylsulphatase A genes of metachromatic leukodystrophy patients. Hum Mol Genet. 1993 Dec;2(12):2117-21. [PubMed ]
21. Barth ML, Fensom A, Harris A: Identification of seven novel mutations associated with metachromatic leukodystrophy. Hum Mutat. 1995;6(2):170-6. [PubMed ]
22. Hess B, Kafert S, Heinisch U, Wenger DA, Zlotogora J, Gieselmann V: Characterization of two arylsulfatase A missense mutations D335V and T274M causing late infantile metachromatic leukodystrophy. Hum Mutat. 1996;7(4):311-7. [PubMed ]
23. Draghia R, Letourneur F, Drugan C, Manicom J, Blanchot C, Kahn A, Poenaru L, Caillaud C: Metachromatic leukodystrophy: identification of the first deletion in exon 1 and of nine novel point mutations in the arylsulfatase A gene. Hum Mutat. 1997;9(3):234-42. [PubMed ]
24. Regis S, Filocamo M, Stroppiano M, Corsolini F, Caroli F, Gatti R: A 9-bp deletion (2320del9) on the background of the arylsulfatase A pseudodeficiency allele in a metachromatic leukodystrophy patient and in a patient with nonprogressive neurological symptoms. Hum Genet. 1998 Jan;102(1):50-3. [PubMed ]
25. Gomez-Lira M, Perusi C, Mottes M, Pignatti PF, Manfredi M, Rizzuto N, Salviati A: Molecular genetic characterization of two metachromatic leukodystrophy patients who carry the T799G mutation and show different phenotypes; description of a novel null-type mutation. Hum Genet. 1998 Apr;102(4):459-63. [PubMed ]
26. Coulter-Mackie MB, Gagnier L: Two novel mutations in the arylsulfatase A gene associated with juvenile (R390Q) and adult onset (H397Y) metachromatic leukodystrophy. Hum Mutat. 1998;Suppl 1:S254-6. [PubMed ]
27. Ricketts MH, Poretz RD, Manowitz P: The R496H mutation of arylsulfatase A does not cause metachromatic leukodystrophy. Hum Mutat. 1998;12(4):238-9. [PubMed ]
28. Berger J, Gmach M, Mayr U, Molzer B, Bernheimer H: Coincidence of two novel arylsulfatase A alleles and mutation 459+1G>A within a family with metachromatic leukodystrophy: molecular basis of phenotypic heterogeneity. Hum Mutat. 1999;13(1):61-8. [PubMed ]
29. Marcao A, Amaral O, Pinto E, Pinto R, Sa Miranda MC: Metachromatic leucodystrophy in Portugal-finding of four new molecular lesions: C300F, P425T, g.1190-1191insC, and g.2408delC. Mutations in brief no. 232. Online. Hum Mutat. 1999;13(4):337-8. [PubMed ]

1. ASB
2. N-acetylgalactosamine- 4-sulfatase
3. G4S

MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDV
GFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPS
CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHER
CTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQS
VHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTD
NGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKL
ARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLP
EYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRD
PEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM

• Glycosaminoglycan degradation (map00531 )

• Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate

• Sulfatase (PF00884 )

• 1-36

ATGGGTCCGCGCGGCGCGGCGAGCTTGCCCCGAGGCCCCGGACCTCGGCGGCTGCTCCTC
CCCGTCGTCCTCCCGCTGCTGCTGCTGCTGTTGTTGGCGCCGCCGGGCTCGGGCGCCGGG
GCCAGCCGGCCGCCCCACCTGGTCTTCTTGCTGGCAGACGACCTAGGCTGGAACGACGTC
GGCTTCCACGGCTCCCGCATCCGCACGCCGCACCTGGACGCGCTGGCGGCCGGCGGGGTG
CTCCTGGACAACTACTACACGCAGCCGCTGTGCACGCCGTCGCGGAGCCAGCTGCTCACT
GGCCGCTACCAGATCCGTACAGGTTTACAGCACCAAATAATCTGGCCCTGTCAGCCCAGC
TGTGTTCCTCTGGATGAAAAACTCCTGCCCCAGCTCCTAAAAGAAGCAGGTTATACTACC
CATATGGTCGGAAAATGGCACCTGGGAATGTACCGGAAAGAATGCCTTCCAACCCGCCGA
GGATTTGATACCTACTTTGGATATCTCCTGGGTAGTGAAGATTATTATTCCCATGAACGC
TGTACATTAATTGACGCTCTGAATGTCACACGATGTGCTCTTGATTTTCGAGATGGCGAA
GAAGTTGCAACAGGATATAAAAATATGTATTCAACAAACATATTCACCAAAAGGGCTATA
GCCCTCATAACTAACCATCCACCAGAGAAGCCTCTGTTTCTCTACCTTGCTCTCCAGTCT
GTGCATGAGCCCCTTCAGGTCCCTGAGGAATACTTGAAGCCATATGACTTTATCCAAGAC
AAGAACAGGCATCACTATGCAGGAATGGTGTCCCTTATGGATGAAGCAGTAGGAAATGTC
ACTGCAGCTTTAAAAAGCAGTGGGCTCTGGAACAACACGGTGTTCATCTTTTCTACAGAT
AACGGAGGGCAGACTTTGGCAGGGGGTAATAACTGGCCCCTTCGAGGAAGAAAATGGAGC
CTGTGGGAAGGAGGCGTCCGAGGGGTGGGCTTTGTGGCAAGCCCCTTGCTGAAGCAGAAG
GGCGTGAAGAACCGGGAGCTCATCCACATCTCTGACTGGCTGCCAACACTCGTGAAGCTG
GCCAGGGGACACACCAATGGCACAAAGCCTCTGGATGGCTTCGACGTGTGGAAAACCATC
AGTGAAGGAAGCCCATCCCCCAGAATTGAGCTGCTGCATAATATTGACCCAAACTTCGTG
GACTCTTCACCGTGTCCCAGGAACAGCATGGCTCCAGCAAAGGATGACTCTTCTCTTCCA
GAATATTCAGCCTTTAACACATCTGTCCATGCTGCAATTAGACATGGAAATTGGAAACTC
CTCACGGGCTACCCAGGCTGTGGTTACTGGTTCCCTCCACCGTCTCAATACAATGTTTCT
GAGATACCCTCATCAGACCCACCAACCAAGACCCTCTGGCTCTTTGATATTGATCGGGAC
CCTGAAGAAAGACATGACCTGTCCAGAGAATATCCTCACATCGTCACAAAGCTCCTGTCC
CGCCTACAGTTCTACCATAAACACTCAGTCCCCGTGTACTTCCCTGCACAGGACCCCCGC
TGTGATCCCAAGGCCACTGGGGTGTGGGGCCCTTGGATGTAG

1. Peters C, Schmidt B, Rommerskirch W, Rupp K, Zuhlsdorf M, Vingron M, Meyer HE, Pohlmann R, von Figura K: Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B. J Biol Chem. 1990 Feb 25;265(6):3374-81. [PubMed ]
2. Schuchman EH, Jackson CE, Desnick RJ: Human arylsulfatase B: MOPAC cloning, nucleotide sequence of a full-length cDNA, and regions of amino acid identity with arylsulfatases A and C. Genomics. 1990 Jan;6(1):149-58. [PubMed ]
3. Modaressi S, Rupp K, von Figura K, Peters C: Structure of the human arylsulfatase B gene. Biol Chem Hoppe Seyler. 1993 May;374(5):327-35. [PubMed ]
4. Litjens T, Morris CP, Gibson GJ, Beckmann KR, Hopwood JJ: Human N-acetylgalactosamine-4-sulphatase: protein maturation and isolation of genomic clones. Biochem Int. 1991 May;24(2):209-15. [PubMed ]
5. Kobayashi T, Honke K, Jin T, Gasa S, Miyazaki T, Makita A: Components and proteolytic processing sites of arylsulfatase B from human placenta. Biochim Biophys Acta. 1992 Oct 20;1159(3):243-7. [PubMed ]
6. Schmidt B, Selmer T, Ingendoh A, von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. [PubMed ]
7. Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM: Structure of a human lysosomal sulfatase. Structure. 1997 Feb 15;5(2):277-89. [PubMed ]
8. Wicker G, Prill V, Brooks D, Gibson G, Hopwood J, von Figura K, Peters C: Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B. J Biol Chem. 1991 Nov 15;266(32):21386-91. [PubMed ]
9. Jin WD, Jackson CE, Desnick RJ, Schuchman EH: Mucopolysaccharidosis type VI: identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity. Am J Hum Genet. 1992 Apr;50(4):795-800. [PubMed ]
10. Isbrandt D, Arlt G, Brooks DA, Hopwood JJ, von Figura K, Peters C: Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique arylsulfatase B gene alleles causing variable disease phenotypes. Am J Hum Genet. 1994 Mar;54(3):454-63. [PubMed ]
11. Voskoboeva E, Isbrandt D, von Figura K, Krasnopolskaya X, Peters C: Four novel mutant alleles of the arylsulfatase B gene in two patients with intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). Hum Genet. 1994 Mar;93(3):259-64. [PubMed ]
12. Simonaro CM, Schuchman EH: N-acetylgalactosamine-4-sulfatase: identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI. Biochim Biophys Acta. 1995 Dec 12;1272(3):129-32. [PubMed ]
13. Litjens T, Brooks DA, Peters C, Gibson GJ, Hopwood JJ: Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS-VI patients. Am J Hum Genet. 1996 Jun;58(6):1127-34. [PubMed ]
14. Wang DG, Fan JB, Siao CJ, Berno A, Young P, Sapolsky R, Ghandour G, Perkins N, Winchester E, Spencer J, Kruglyak L, Stein L, Hsie L, Topaloglou T, Hubbell E, Robinson E, Mittmann M, Morris MS, Shen N, Kilburn D, Rioux J, Nusbaum C, Rozen S, Hudson TJ, Lipshutz R, Chee M, Lander ES: Large-scale identification, mapping, and genotyping of single-nucleotide polymorphisms in the human genome. Science. 1998 May 15;280(5366):1077-82. [PubMed ]
15. Villani GR, Balzano N, Vitale D, Saviano M, Pavone V, Di Natale P: Maroteaux-lamy syndrome: five novel mutations and their structural localization. Biochim Biophys Acta. 1999 Feb 24;1453(2):185-92. [PubMed ]
16. Yang CF, Wu JY, Lin SP, Tsai FJ: Mucopolysaccharidosis type VI: Report of two Taiwanese patients and identification of one novel mutation. J Formos Med Assoc. 2001 Dec;100(12):820-3. [PubMed ]

1. ASE

MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ

• Sulfatase (PF00884 )

• 1-31

• 200-222
• 227-249
• 289-311

ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCATGGCTTTGAGCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCGGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAACATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA

1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed ]
2. Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G: Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. [PubMed ]
3. Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G: X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. [PubMed ]

1. PAPS synthetase 1
2. PAPSS 1
3. Sulfurylase kinase 1
4. SK1
5. SK 1[Includes: Sulfate adenylyltransferase
6. Sulfate adenylate transferase
7. SAT
8. ATP-sulfurylase
9. Adenylyl-sulfate kinase
10. Adenylylsulfate 3'-phosphotransferase
11. APS kinase
12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]

MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA

• Purine Metabolism (map00230 )
• Selenoamino Acid Metabolism (map00450 )
• Sulfate and Sulfite Metabolism (map00920 )

• ATP + sulfate = diphosphate + adenylylsulfate

• APS_kinase (PF01583 )
• ATP-sulfurylase (PF01747 )

• None

• None

ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG

1. Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed ]
2. Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed ]
3. Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed ]
4. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed ]
5. Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed ]

1. PAPS synthetase 2
2. PAPSS 2
3. Sulfurylase kinase 2
4. SK2
5. SK 2[Includes: Sulfate adenylyltransferase
6. Sulfate adenylate transferase
7. SAT
8. ATP-sulfurylase
9. Adenylyl-sulfate kinase
10. Adenylylsulfate 3'-phosphotransferase
11. APS kinase
12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]

MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN

• Purine Metabolism (map00230 )
• Selenoamino Acid Metabolism (map00450 )
• Sulfate and Sulfite Metabolism (map00920 )

• ATP + sulfate = diphosphate + adenylylsulfate

• APS_kinase (PF01583 )
• ATP-sulfurylase (PF01747 )

• None

• None

ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAGGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACCTGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCCAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA

1. ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed ]
2. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed ]
3. Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [PubMed ]
4. Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed ]

1. Steroid sulfatase
2. Steryl- sulfate sulfohydrolase
3. Arylsulfatase C
4. ASC

MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLAS
GGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAK
LLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTT
GFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPL
NCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFA
GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGS
NGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI
IDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNG
CFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQT
LPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR

• Androgen and Estrogen Metabolism (map00150 )

• 3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate

• Sulfatase (PF00884 )

• 1-21

• 185-208 213-234

ATGCCTTTAAGGAAGATGAAGATCCCTTTCCTCCTACTGTTCTTTCTGTGGGAAGCCGAG
AGCCACGCAGCATCAAGGCCGAACATCATCCTGGTGATGGCTGACGACCTCGGCATTGGA
GATCCTGGGTGCTATGGGAACAAAACTATCAGGACTCCCAATATCGACCGGTTGGCCAGT
GGGGGAGTGAAACTCACTCAGCACCTGGCAGCATCACCGCTGTGCACACCAAGCAGGGCA
GCCTTCATGACTGGCCGGTACCCTGTCCGATCAGGAATGGCATCTTGGTCCCGCACTGGA
GTTTTCCTCTTCACAGCCTCTTCGGGAGGACTTCCCACCGATGAGATTACCTTTGCTAAG
CTTCTGAAGGATCAAGGTTATTCAACAGCACTGATAGGGAAATGGCACCTTGGGATGAGC
TGTCACAGCAAGACTGACTTCTGTCACCACCCTTTACATCACGGCTTCAATTATTTCTAT
GGGATCTCTTTGACCAATCTGAGAGACTGCAAGCCCGGAGAGGGCAGTGTCTTCACCACG
GGCTTCAAGAGGCTGGTCTTCCTCCCCCTGCAGATCGTCGGGGTCACCCTCCTTACCCTT
GCTGCACTCAATTGTCTGGGGCTACTCCACGTGCCTCTAGGCGTTTTTTTCAGCCTTCTC
TTCCTAGCAGCCCTAATCCTGACCCTTTTCTTGGGCTTCCTTCATTACTTCCGGCCCCTG
AACTGCTTCATGATGAGGAACTACGAGATCATTCAGCAGCCCATGTCCTATGACAATCTC
ACCCAGAGGCTAACGGTGGAGGCGGCCCAGTTCATACAGCGGAACACTGAGACTCCGTTC
CTGCTTGTCTTGTCCTACCTCCACGTGCACACAGCCCTGTTCTCCAGCAAAGACTTTGCT
GGCAAAAGTCAACACGGAGTCTACGGGGATGCTGTTGAGGAAATGGACTGGAGTGTGGGG
CAGATCTTGAACCTTCTGGATGAGCTGAGATTGGCTAATGATACCCTCATCTACTTCACA
TCGGACCAGGGAGCACATGTAGAGGAGGTGTCTTCCAAAGGAGAAATTCATGGCGGAAGT
AATGGGATCTATAAAGGAGGAAAAGCAAACAACTGGGAAGGAGGTATCCGGGTTCCAGGC
ATCCTTCGTTGGCCCAGGGTGATACAGGCTGGCCAGAAGATTGATGAGCCCACTAGCAAC
ATGGACATATTTCCTACAGTAGCCAAGCTGGCTGGAGCTCCCTTGCCTGAGGACAGGATC
ATTGATGGACGTGATCTGATGCCCCTGCTTGAAGGAAAAAGCCAACGCTCCGATCATGAG
TTTCTCTTCCATTACTGCAACGCCTACTTAAATGCTGTGCGCTGGCACCCTCAGAACAGC
ACATCCATCTGGAAGGCCTTTTTCTTCACCCCCAACTTCAACCCCGTGGGTTCCAACGGA
TGCTTTGCCACACACGTGTGCTTCTGTTTCGGGAGTTATGTCACCCATCACGACCCACCT
TTACTCTTTGATATTTCCAAAGATCCCAGAGAGAGAAACCCACTAACTCCAGCATCCGAG
CCCCGGTTTTATGAAATCCTCAAAGTCATGCAGGAAGCTGCGGACAGACACACCCAGACC
CTGCCAGAGGTGCCCGATCAGTTTTCATGGAACAACTTTCTTTGGAAGCCCTGGCTTCAG
CTGTGCTGTCCTTCCACCGGCCTGTCTTGCCAGTGTGATAGAGAAAAACAGGATAAGAGA
CTGAGCCGCTAG

1. Stein C, Hille A, Seidel J, Rijnbout S, Waheed A, Schmidt B, Geuze H, von Figura K: Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. J Biol Chem. 1989 Aug 15;264(23):13865-72. [PubMed ]
2. Yen PH, Allen E, Marsh B, Mohandas T, Wang N, Taggart RT, Shapiro LJ: Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. Cell. 1987 May 22;49(4):443-54. [PubMed ]
3. Yen PH, Marsh B, Allen E, Tsai SP, Ellison J, Connolly L, Neiswanger K, Shapiro LJ: The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. Cell. 1988 Dec 23;55(6):1123-35. [PubMed ]
4. Kawano J, Kotani T, Ohtaki S, Minamino N, Matsuo H, Oinuma T, Aikawa E: Characterization of rat and human steroid sulfatases. Biochim Biophys Acta. 1989 Aug 31;997(3):199-205. [PubMed ]
5. Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D: Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. [PubMed ]
6. Basler E, Grompe M, Parenti G, Yates J, Ballabio A: Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am J Hum Genet. 1992 Mar;50(3):483-91. [PubMed ]
7. Alperin ES, Shapiro LJ: Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J Biol Chem. 1997 Aug 15;272(33):20756-63. [PubMed ]
8. Sugawara T, Shimizu H, Hoshi N, Fujimoto Y, Nakajima A, Fujimoto S: PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum Mutat. 2000 Mar;15(3):296. [PubMed ]
9. Oyama N, Satoh M, Iwatsuki K, Kaneko F: Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. J Invest Dermatol. 2000 Jun;114(6):1195-9. [PubMed ]

1. GSTM2-2
2. GST class-mu 2

MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDF
EKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• 1-16

ATGCCCATGACACTGGGGTACTGGAACATCCGCGGGCTGGCCCATTCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGACTCACAAGATCACCCAGAGCAATGCCATCCTGCGGTACATT
GCCCGCAAGCACAACCTGTGCGGGGAATCAGAAAAGGAGCAGATTCGCGAAGACATTTTG
GAGAACCAGTTTATGGACAGCCGTATGCAGCTGGCCAAACTCTGCTATGACCCAGATTTT
GAGAAACTGAAACCAGAATACCTGCAGGCACTCCCTGAAATGCTGAAGCTCTACTCACAG
TTTCTGGGGAAGCAGCCATGGTTTCTTGGGGACAAGATCACCTTTGTGGATTTCATCGCT
TATGATGTCCTTGAGAGAAACCAAGTATTTGAGCCCAGCTGCCTGGATGCCTTCCCAAAC
CTGAAGGACTTCATCTCCCGATTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCACAAAGATGGCTGTCTGGGGCAACAAGTAG

1. Vorachek WR, Pearson WR, Rule GS: Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4443-7. [PubMed ]
2. Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed ]
3. Raghunathan S, Chandross RJ, Kretsinger RH, Allison TJ, Penington CJ, Rule GS: Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J Mol Biol. 1994 May 20;238(5):815-32. [PubMed ]

1. GSTM1-1
2. GST class-mu 1
3. GSTM1a-1a
4. GSTM1b-1b
5. HB subunit 4
6. GTH4

MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• 1-16

ATGCCCATGATACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTATGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCTTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGACCATGGACAACCATATGCAGCTGGGCATGATCTGCTACAATCCAGAATTT
GAGAAACTGAAGCCAAAGTACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAAACAAGATCACTTTTGTAGATTTTCTCGTC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCTCAAAGATGGCTGTCTGGGGCAACAAGTAG

1. DeJong JL, Chang CM, Whang-Peng J, Knutsen T, Tu CP: The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hb subunit cDNA. Nucleic Acids Res. 1988 Sep 12;16(17):8541-54. [PubMed ]
2. Seidegard J, Vorachek WR, Pero RW, Pearson WR: Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7293-7. [PubMed ]
3. Zhong S, Spurr NK, Hayes JD, Wolf CR: Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4. Biochem J. 1993 Apr 1;291 ( Pt 1):41-50. [PubMed ]
4. Comstock KE, Sanderson BJ, Claflin G, Henner WD: GST1 gene deletion determined by polymerase chain reaction. Nucleic Acids Res. 1990 Jun 25;18(12):3670. [PubMed ]
5. Pearson WR, Vorachek WR, Xu SJ, Berger R, Hart I, Vannais D, Patterson D: Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Am J Hum Genet. 1993 Jul;53(1):220-33. [PubMed ]
6. Tsuchida S, Maki T, Sato K: Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart. Multiplicity of the human class Mu forms. J Biol Chem. 1990 May 5;265(13):7150-7. [PubMed ]
7. Mannervik B, Alin P, Guthenberg C, Jensson H, Tahir MK, Warholm M, Jornvall H: Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7202-6. [PubMed ]
8. Alin P, Mannervik B, Jornvall H: Structural evidence for three different types of glutathione transferase in human tissues. FEBS Lett. 1985 Mar 25;182(2):319-22. [PubMed ]
9. Singhal SS, Ahmad H, Sharma R, Gupta S, Haque AK, Awasthi YC: Purification and characterization of human muscle glutathione S-transferases: evidence that glutathione S-transferase zeta corresponds to a locus distinct from GST1, GST2, and GST3. Arch Biochem Biophys. 1991 Feb 15;285(1):64-73. [PubMed ]
10. Singhal SS, Saxena M, Awasthi S, Ahmad H, Sharma R, Awasthi YC: Gender related differences in the expression and characteristics of glutathione S-transferases of human colon. Biochim Biophys Acta. 1992 Nov 15;1171(1):19-26. [PubMed ]
11. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed ]
12. Patskovsky YV, Patskovska LN, Listowsky I: Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a. Biochemistry. 1999 Jan 26;38(4):1193-202. [PubMed ]

1. GSTM3-3
2. GST class-mu 3
3. hGSTM3-3

MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLD
FPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCY
SSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLD
EFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

ATGTCGTGCGAGTCGTCTATGGTTCTCGGGTACTGGGATATTCGTGGGCTGGCGCACGCC
ATCCGCCTGCTCCTGGAGTTCACGGATACCTCTTATGAGGAGAAACGGTACACGTGCGGG
GAAGCTCCTGACTATGATCGAAGCCAATGGCTGGATGTGAAATTCAAGCTAGACCTGGAC
TTTCCTAATCTGCCCTACCTCCTGGATGGGAAGAACAAGATCACCCAGAGCAATGCCATC
TTGCGCTACATCGCTCGCAAGCACAACATGTGTGGTGAGACTGAAGAAGAAAAGATTCGA
GTGGACATCATAGAGAACCAAGTAATGGATTTCCGCACACAACTGATAAGGCTCTGTTAC
AGCTCTGACCACGAAAAACTGAAGCCTCAGTACTTGGAAGAGCTACCTGGACAACTGAAA
CAATTCTCCATGTTTCTGTGGAAATTCTCATGGTTTGCCGGGGAAAAGCTCACCTTTGTG
GATTTTCTCACCTATGATATCTTGGATCAGAACCGTATATTTGACCCCAAGTGCCTGGAT
GAGTTCCCAAACCTGAAGGCTTTCATGTGCCGTTTTGAGGCTTTGGAGAAAATCGCTGCC
TACTTACAGTCTGATCAGTTCTGCAAGATGCCCATCAACAACAAGATGGCCCAGTGGGGC
AACAAGCCTGTATGCTGA

1. Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I: A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes. J Biol Chem. 1990 Jun 5;265(16):9188-93. [PubMed ]
2. Patskovsky YV, Huang MQ, Takayama T, Listowsky I, Pearson WR: Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster. Arch Biochem Biophys. 1999 Jan 1;361(1):85-93. [PubMed ]
3. Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed ]
4. Hussey AJ, Hayes JD: Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue. Biochim Biophys Acta. 1993 Nov 10;1203(1):131-41. [PubMed ]
5. Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. [PubMed ]

1. GTH1
2. HA subunit 1
3. GST- epsilon
4. GSTA1-1
5. GST class-alpha member 1

MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAK
LALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

ATGGCAGAGAAGCCCAAGCTCCACTACTTCAATGCACGGGGCAGAATGGAGTCCACCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAGAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTCCTTCTGCCCGTATGTCCACCTGAGGAAAAAGATGCCAAG
CTTGCCTTGATCAAGGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCATCTG
GTGGAACTTCTCTACTACGTCGAGGAGCTTGACTCCAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA

1. Tu CP, Qian B: Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA. Biochem Biophys Res Commun. 1986 Nov 26;141(1):229-37. [PubMed ]
2. Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed ]
3. Tu CP, Qian B: Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA. Biochem Soc Trans. 1987 Aug;15(4):734-6. [PubMed ]
4. Board PG, Webb GC: Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. Proc Natl Acad Sci U S A. 1987 Apr;84(8):2377-81. [PubMed ]
5. Rozen F, Nguyen T, Pickett CB: Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene. Arch Biochem Biophys. 1992 Feb 1;292(2):589-93. [PubMed ]
6. Chow NW, Whang-Peng J, Kao-Shan CS, Tam MF, Lai HC, Tu CP: Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities. J Biol Chem. 1988 Sep 15;263(26):12797-800. [PubMed ]
7. Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed ]
8. Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed ]
9. Board PG, Mannervik B: The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase. Biochem J. 1991 Apr 1;275 ( Pt 1):171-4. [PubMed ]
10. Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG, et al.: Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J Mol Biol. 1993 Jul 5;232(1):192-212. [PubMed ]
11. Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA: Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure. 1995 Jul 15;3(7):717-27. [PubMed ]

1. GST class-theta-2

MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDG
DFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLG
PLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALG
YELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRI
ARIP

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• 1-16

ATGGGCCTAGAGCTGTTTCTTGACCTGGTGTCCCAGCCCAGCCGCGCCGTCTACATCTTC
GCCAAGAAGAATGGCATCCCCTTAGAGCTGCGCACCGTGGATTTGGTCAAAGGGCAGCAC
AAGAGCAAGGAGTTCTTGCAGATCAACAGCCTGGGGAAACTGCCGACGCTCAAGGATGGT
GATTTCATCTTGACCGAAAGCTCGGCCATCCTGATTTACCTGAGCTGTAAGTACCAGACG
CCGGACCACTGGTATCCATCTGACCTGCAGGCTCGTGCCCGTGTTCATGAGTACCTGGGC
TGGCATGCCGACTGCATCCGTGGCACCTTTGGTATACCCCTGTGGGTCCAGGTGTTGGGG
CCACTCATTGGGGTCCAGGTGCCCGAGGAGAAGGTGGAACGCAACAGGACTGCCATGGAC
CAGGCCCTGCAATGGCTGGAGGACAAGTTCCTGGGGGACAGGCCCTTCCTCGCTGGCCAG
CAGGTGACACTGGCTGATCTCATGGCCCTGGAGGAGCTGATGCAGCCGGTGGCTCTCGGC
TACGAACTGTTTGAGGGACGGCCACGACTGGCAGCATGGCGTGGACGAGTGGAGGCTTTC
CTGGGTGCTGAGCTATGCCAGGAGGCCCACAGCATCATCTTGAGCATCCTGGAACAGGCG
GCCAAGAAAACCCTCCCAACACCCTCACCAGAGGCCTATCAGGCTATGCTGCTTCGAATC
GCCAGGATCCCCTGA

1. Tan KL, Webb GC, Baker RT, Board PG: Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathione S-transferase gene (GSTT2) to chromosome 22. Genomics. 1995 Jan 20;25(2):381-7. [PubMed ]
2. Sprenger R, Schlagenhaufer R, Kerb R, Bruhn C, Brockmoller J, Roots I, Brinkmann U: Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics. 2000 Aug;10(6):557-65. [PubMed ]
3. 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 ]
4. Hussey AJ, Hayes JD: Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate. Biochem J. 1992 Sep 15;286 ( Pt 3):929-35. [PubMed ]
5. Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T: The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochem J. 1996 Aug 15;318 ( Pt 1):297-303. [PubMed ]
6. Rossjohn J, McKinstry WJ, Oakley AJ, Verger D, Flanagan J, Chelvanayagam G, Tan KL, Board PG, Parker MW: Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure. 1998 Mar 15;6(3):309-22. [PubMed ]

1. GSTM5-5
2. GST class-mu 5

MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLN
LKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• 1-16

ATGCCCATGACTCTGGGGTACTGGGACATCCGTGGGCTGGCCCACGCCATCCGCTTGCTC
CTGGAATACACAGACTCAAGCTATGTGGAAAAGAAGTACACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAATGCCATCCTGCGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGTTATGGATAACCACATGGAGCTGGTCAGACTGTGCTATGACCCAGATTTT
GAGAAACTGAAGCCAAAATACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAGACAAGATCACCTTTGTGGATTTCCTTGCC
TATGATGTCCTTGACATGAAGCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCTAAAC
TTGAAGGACTTCATCTCCCGCTTTGAGGGTTTGAAGAAGATCTCTGCCTACATGAAGTCC
AGCCAATTCCTCCGAGGTCTTTTGTTTGGAAAGTCAGCTACATGGAACAGCAAATAG

1. Takahashi Y, Campbell EA, Hirata Y, Takayama T, Listowsky I: A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5. J Biol Chem. 1993 Apr 25;268(12):8893-8. [PubMed ]

1. Microsomal GST- 2
2. Microsomal GST-II

MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFY
PIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTL
LGALGIANSFLDEYLDLNIAKKLRRQF

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• MAPEG (PF01124 )

• 1-23

ATGGCCGGGAACTCGATCCTGCTGGCTGCTGTCTCTATTCTCTCGGCCTGTCAGCAAAGT
TATTTTGCTTTGCAAGTTGGAAAGGCAAGATTAAAATACAAAGTTACGCCCCCAGCAGTC
ACTGGGTCACCAGAGTTTGAGAGAGTATTTCGGGCACAACAAAACTGTGTGGAGTTTTAT
CCTATATTCATAATTACATTGTGGATGGCTGGGTGGTATTTCAACCAAGTTTTTGCTACT
TGTCTGGGTCTGGTGTACATATATGGCCGTCACCTATACTTCTGGGGATATTCAGAAGCT
GCTAAAAAACGGATCACCGGTTTCCGACTGAGTCTGGGGATTTTGGCCTTGTTGACCCTC
CTAGGTGCCCTGGGAATTGCAAACAGCTTTCTGGATGAATATCTGGACCTCAATATTGCC
AAGAAACTGAGGCGGCAATTCTAA

1. Jakobsson PJ, Mancini JA, Ford-Hutchinson AW: Identification and characterization of a novel human microsomal glutathione S-transferase with leukotriene C4 synthase activity and significant sequence identity to 5-lipoxygenase-activating protein and leukotriene C4 synthase. J Biol Chem. 1996 Sep 6;271(36):22203-10. [PubMed ]

1. GSTO 1-1

MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTGCCATCCTTGGTAGGAAGCTTTATTAGAAGCCAAAATAAAGAAGACTATGCT
GGCCTAAAAGAAGAATTTCGTAAAGAATTTACCAAGCTAGAGGAGGTTCTGACTAATAAG
AAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATTGATTACCTCATCTGGCCCTGG
TTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTAGACCACACTCCAAAACTGAAA
CTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCAGCCCTGCTTACTAGTGAGAAA
GACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGCCCTGAGGCCTGTGACTATGGG
CTCTGA

1. Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J: Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem. 2000 Aug 11;275(32):24798-806. [PubMed ]
2. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed ]
3. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed ]
4. Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed ]

1. Glutathione S-transferase A5-5
2. GST class-alpha member 5

MAEKPKLHYSNARGSMESIRWLLAAAGVELEEKFLESAEDLDKLRNDGSLLFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDMKERALIDMYTEGIVDLTEMILLLLICQPEERDAK
TALVKEKIKNRYFPAFEKVLKSHRQDYLVGNKLSWADIHLVELFYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSQRKPPMDEKSLEEARKIFRF

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATGCACGGGGCAGTATGGAGTCCATTCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTGGAAGAGAAATTTCTAGAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGGAGTTTGCTGTTCCAGCAAGTACCAATGGTTGAGATT
GACGGGATGAAGCTGGTGCAGACCAGAGCCATTCTTAACTACATTGCCAGCAAATACAAC
CTTTATGGGAAAGACATGAAGGAGAGAGCCCTGATTGATATGTACACAGAAGGTATAGTA
GATTTGACTGAAATGATCCTTCTTCTGCTCATATGTCAACCAGAGGAAAGAGATGCCAAG
ACTGCCTTGGTCAAAGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACAGACAAGACTACCTTGTTGGCAACAAGCTGAGCTGGGCTGACATTCACCTG
GTGGAACTTTTCTACTACGTGGAAGAGCTTGACTCGAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTGCAGCCT
GGCAGCCAGAGAAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA

1. 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 ]
2. Morel F, Rauch C, Coles B, Le Ferrec E, Guillouzo A: The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter. Pharmacogenetics. 2002 Jun;12(4):277-86. [PubMed ]

1. GTH2
2. HA subunit 2
3. GST- gamma
4. GSTA2-2
5. GST class-alpha member 2

MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK
LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTACTCAACCTGAGGAACAAGATGCCAAG
CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG
GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC
AGGTTTTAA

1. Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed ]
2. Rohrdanz E, Nguyen T, Pickett CB: Isolation and characterization of the human glutathione S-transferase A2 subunit gene. Arch Biochem Biophys. 1992 Nov 1;298(2):747-52. [PubMed ]
3. Klone A, Hussnatter R, Sies H: Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. Biochem J. 1992 Aug 1;285 ( Pt 3):925-8. [PubMed ]
4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
5. Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed ]
6. Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed ]
7. Tetlow N, Liu D, Board P: Polymorphism of human Alpha class glutathione transferases. Pharmacogenetics. 2001 Oct;11(7):609-17. [PubMed ]

1. GSTO-2

MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKP
EWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELF
CKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWP
WFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDF
GLC

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_N (PF02798 )

• None

• None

ATGTCTGGGGATGCGACCAGGACCCTGGGGAAAGGAAGCCAGCCCCCAGGGCCAGTCCCG
GAGGGGCTGATCCGCATCTACAGCATGAGGTTCTGCCCCTATTCTCACAGGACCCGCCTC
GTCCTCAAGGCCAAAGACATCAGACATGAAGTGGTCAACATTAACCTGAGAAACAAGCCT
GAATGGTACTATACAAAGCACCCTTTTGGCCACATTCCTGTCCTGGAGACCAGCCAATGT
CAACTGATCTATGAATCTGTTATTGCTTGTGAGTACCTGGATGATGCTTATCCAGGAAGG
AAGCTGTTTCCATATGACCCTTATGAACGAGCTCGCCAAAAGATGTTATTGGAGCTATTT
TGTAAGGTCCCACATTTGACCAAGGAGTGCCTGGTAGCGTTGAGATGTGGGAGAGAATGC
ACTAATCTGAAGGCAGCCCTGCGTCAGGAATTCAGCAACCTGGAAGAGATTCTTGAGTAT
CAGAACACCACCTTCTTTGGTGGAACCTGTATATCCATGATTGATTACCTCCTCTGGCCC
TGGTTTGAGCGGCTGGATGTGTATGGGATACTGGACTGTGTGAGCCACACGCCAGCCCTG
CGGCTCTGGATATCAGCCATGAAGTGGGACCCCACAGTCTGTGCTCTTCTCATGGATAAG
AGCATTTTCCAGGGCTTCTTGAATCTCTATTTTCAGAACAACCCTAATGCCTTTGACTTT
GGGCTGTGCTGA

1. Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed ]

1. GST class-theta-1
2. Glutathione transferase T1-1

MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDG
DFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMF
PVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGA
GCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• 1-16

ATGGGTCTGGAGCTCTACCTGGACCTGCTGTCCCAGCCCTGCCGCGCTGTTTACATCTTT
GCCAAGAAGAACGACATTCCCTTCGAGCTGCGCATCGTGGATCTGATTAAAGGTCAGCAC
TTAAGCGATGCCTTTGCCCAGGTGAACCCCCTCAAGAAGGTGCCGGCCTTGAAGGACGGG
GACTTCACCTTGACGGAGAGTGTGGCCATCCTGCTCTACCTGACGCGCAAATATAAGGTC
CCTGACTACTGGTACCCTCAGGACCTGCAGGCCCGTGCCCGTGTGGATGAGTACCTGGCA
TGGCAGCACACGACTCTGCGGAGAAGCTGCCTCCGGGCCTTGTGGCATAAGGTGATGTTC
CCTGTGTTCCTGGGTGGGCCAGTATCTCCCCAGACACTGGCAGCCACCCTGGCAGAGTTG
GATGTGACCCTGCAGTTGCTCGAGGACAAGTTCCTCCAGAACAAGGCCTTCCTTACTGGT
CCTCACATCTCCTTAGCTGACCTCGTAGCCATCACGGAGCTGATGCATCCCGTGGGTGCT
GGCTGCCAAGTCTTCGAAGGCCGACCCAAGCTGGCCACATGGCGGCAGCGCGTGGAGGCA
GCAGTGGGGGAGGACCTCTTCCAGGAGGCCCATGAGGTCATTCTGAAGGCCAAGGACTTC
CCACCTGCAGACCCCACCATAAAGCAGAAGCTGATGCCCTGGGTGCTGGCCATGATCCGG
TGA

1. Pemble S, Schroeder KR, Spencer SR, Meyer DJ, Hallier E, Bolt HM, Ketterer B, Taylor JB: Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem J. 1994 May 15;300 ( Pt 1):271-6. [PubMed ]
2. Jemth P, Mannervik B: Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Arch Biochem Biophys. 1997 Dec 15;348(2):247-54. [PubMed ]
3. Sprenger R, Schlagenhaufer R, Kerb R, Bruhn C, Brockmoller J, Roots I, Brinkmann U: Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics. 2000 Aug;10(6):557-65. [PubMed ]
4. 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 ]
5. Meyer DJ, Coles B, Pemble SE, Gilmore KS, Fraser GM, Ketterer B: Theta, a new class of glutathione transferases purified from rat and man. Biochem J. 1991 Mar 1;274 ( Pt 2):409-14. [PubMed ]
6. Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T: The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochem J. 1996 Aug 15;318 ( Pt 1):297-303. [PubMed ]

1. GST class-pi
2. GSTP1-1

MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGD
LTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAY
VGRLSARPKLKAFLASPEYVNLPINGNGKQ

• Glutathione Metabolism (map00480 )

• RX + glutathione = HX + R-S-glutathione

• GST_C (PF00043 )
• GST_N (PF02798 )

• 1-17

ATGCCGCCCTACACCGTGGTCTATTTCCCAGTTCGAGGCCGCTGCGCGGCCCTGCGCATG
CTGCTGGCAGATCAGGGCCAGAGCTGGAAGGAGGAGGTGGTGACCGTGGAGACGTGGCAG
GAGGGCTCACTCAAAGCCTCCTGCCTATACGGGCAGCTCCCCAAGTTCCAGGACGGAGAC
CTCACCCTGTACCAGTCCAATACCATCCTGCGTCACCTGGGCCGCACCCTTGGGCTCTAT
GGGAAGGACCAGCAGGAGGCAGCCCTGGTGGACATGGTGAATGACGGCGTGGAGGACCTC
CGCTGCAAATACATCTCCCTCATCTACACCAACTATGAGGCGGGCAAGGATGACTATGTG
AAGGCACTGCCCGGGCAACTGAAGCCTTTTGAGACCCTGCTGTCCCAGAACCAGGGAGGC
AAGACCTTCATTGTGGGAGACCAGATCTCCTTCGCTGACTACAACCTGCTGGACTTGCTG
CTGATCCATGAGGTCCTAGCCCCTGGCTGCCTGGATGCGTTCCCCCTGCTCTCAGCATAT
GTGGGGCGCCTCAGCGCCCGGCCCAAGCTCAAGGCCTTCCTGGCCTCCCCTGAGTACGTG
AACCTCCCCATCAATGGCAACGGGAAACAGTGA

1. Kano T, Sakai M, Muramatsu M: Structure and expression of a human class pi glutathione S-transferase messenger RNA. Cancer Res. 1987 Nov 1;47(21):5626-30. [PubMed ]
2. Cowell IG, Dixon KH, Pemble SE, Ketterer B, Taylor JB: The structure of the human glutathione S-transferase pi gene. Biochem J. 1988 Oct 1;255(1):79-83. [PubMed ]
3. Morrow CS, Cowan KH, Goldsmith ME: Structure of the human genomic glutathione S-transferase-pi gene. Gene. 1989 Jan 30;75(1):3-11. [PubMed ]
4. Moscow JA, Fairchild CR, Madden MJ, Ransom DT, Wieand HS, O'Brien EE, Poplack DG, Cossman J, Myers CE, Cowan KH: Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors. Cancer Res. 1989 Mar 15;49(6):1422-8. [PubMed ]
5. Ali-Osman F, Akande O, Antoun G, Mao JX, Buolamwini J: Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. J Biol Chem. 1997 Apr 11;272(15):10004-12. [PubMed ]
6. Alin P, Mannervik B, Jornvall H: Structural evidence for three different types of glutathione transferase in human tissues. FEBS Lett. 1985 Mar 25;182(2):319-22. [PubMed ]
7. Mannervik B, Alin P, Guthenberg C, Jensson H, Tahir MK, Warholm M, Jornvall H: Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7202-6. [PubMed ]
8. Singh SV, Ahmad H, Kurosky A, Awasthi YC: Purification and characterization of unique glutathione S-transferases from human muscle. Arch Biochem Biophys. 1988 Jul;264(1):13-22. [PubMed ]
9. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
10. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed ]
11. Ahmad H, Wilson DE, Fritz RR, Singh SV, Medh RD, Nagle GT, Awasthi YC, Kurosky A: Primary and secondary structural analyses of glutathione S-transferase pi from human placenta. Arch Biochem Biophys. 1990 May 1;278(2):398-408. [PubMed ]
12. Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW: Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol. 1992 Sep 5;227(1):214-26. [PubMed ]
13. Oakley AJ, Rossjohn J, Lo Bello M, Caccuri AM, Federici G, Parker MW: The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry. 1997 Jan 21;36(3):576-85. [PubMed ]
14. Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P: Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry. 1997 Aug 12;36(32):9690-702. [PubMed ]
15. Oakley AJ, Lo Bello M, Battistoni A, Ricci G, Rossjohn J, Villar HO, Parker MW: The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J Mol Biol. 1997 Nov 21;274(1):84-100. [PubMed ]
16. Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W: Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor. Structure. 1997 Oct 15;5(10):1287-95. [PubMed ]
17. Ji X, Blaszczyk J, Xiao B, O'Donnell R, Hu X, Herzog C, Singh SV, Zimniak P: Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry. 1999 Aug 10;38(32):10231-8. [PubMed ]
18. Nicotra M, Paci M, Sette M, Oakley AJ, Parker MW, Lo Bello M, Caccuri AM, Federici G, Ricci G: Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure. Biochemistry. 1998 Mar 3;37(9):3020-7. [PubMed ]
19. Kong KH, Inoue H, Takahashi K: Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1. Protein Eng. 1993 Jan;6(1):93-9. [PubMed ]

MGTLLGLGAVLAYQDHRCRAAQESTHIYTKEEVSSHTSPETGIWVTLGSEVFDVTEFVDL
HPGGPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYKIGELNPEDKVAPTVETSDPYA
DDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGA
PGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGAR
LCDVLAQAGHQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPL
PRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSA
PSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDG
EEQRPRKAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWH
RVHVYVSP

• Sulfate and Sulfite Metabolism (map00920 )

• sulfite + O2 + H2O = sulfate + H2O2

• Cyt-b5 (PF00173 )
• Mo-co_dimer (PF03404 )
• Oxidored_molyb (PF00174 )

• None

• None

ATGGGGACCCTATTAGGTCTCGGTGCAGTGTTGGCCTATCAGGACCATCGGTGTAGGGCT
GCTCAGGAGTCAACACACATATACACTAAGGAGGAAGTGAGTTCCCACACCAGCCCTGAG
ACTGGGATCTGGGTGACTCTGGGCTCTGAGGTCTTTGATGTCACAGAATTTGTGGACCTA
CATCCAGGGGGGCCTTCAAAGCTGATGCTAGCAGCTGGGGGTCCCCTAGAGCCCTTCTGG
GCCCTCTATGCTGTTCACAACCAGTCCCATGTGCGTGAGTTACTGGCTCAGTACAAGATT
GGGGAGCTGAATCCTGAAGACAAGGTAGCCCCCACCGTGGAGACCTCTGACCCTTATGCT
GATGATCCTGTACGTCACCCAGCCCTGAAGGTCAACAGCCAGCGGCCCTTTAATGCAGAG
CCTCCCCCTGAGCTGCTGACAGAAAACTACATCACACCCAACCCTATCTTCTTCACCCGG
AACCATCTGCCTGTACCTAACCTGGATCCAGACACCTATCGCTTACACGTAGTAGGAGCA
CCTGGGGGTCAGTCACTGTCTCTTTCCCTGGATGACTTGCACAACTTTCCCAGGTACGAG
ATCACAGTCACTCTGCAGTGTGCCGGCAACCGACGCTCTGAGATGACTCAGGTCAAAGAA
GTAAAAGGTCTGGAGTGGAGAACAGGAGCCATCAGCACTGCACGCTGGGCTGGGGCACGG
CTCTGTGATGTGTTAGCCCAGGCTGGCCACCAACTCTGTGAAACTGAGGCCCACGTCTGC
TTTGAGGGACTGGACTCAGACCCTACTGGGACTGCCTATGGAGCATCCATCCCTCTGGCT
CGGGCCATGGACCCTGAAGCTGAGGTCCTGCTGGCATATGAGATGAATGGGCAGCCTCTG
CCACGTGACCACGGCTTCCCTGTGCGTGTGGTGGTTCCTGGAGTGGTGGGTGCCCGCCAT
GTCAAATGGCTGGGCAGAGTGAGTGTGCAGCCAGAGGAAAGTTACAGCCACTGGCAACGG
CGGGATTACAAAGGCTTCTCTCCATCTGTGGACTGGGAGACTGTAGATTTTGACTCTGCT
CCATCCATTCAGGAACTTCCTGTCCAGTCCGCCATCACAGAGCCCCGGGATGGAGAGACT
GTAGAATCAGGGGAGGTGACCATCAAGGGCTATGCATGGAGTGGTGGTGGCAGGGCTGTG
ATCCGGGTGGATGTGTCTCTGGATGGGGGCCTAACCTGGCAGGTGGCTAAGCTGGATGGA
GAGGAACAGCGCCCCAGGAAGGCCTGGGCATGGCGTCTGTGGCAGTTGAAAGCCCCTGTG
CCAGCTGGACAAAAGGAACTGAACATTGTTTGTAAGGCTGTGGATGATGGTTACAATGTG
CAGCCAGACACCGTGGCCCCAATCTGGAACCTGCGAGGTGTTCTCAGCAATGCCTGGCAT
CGTGTCCATGTCTATGTCTCCCCATGA

1. Garrett RM, Bellissimo DB, Rajagopalan KV: Molecular cloning of human liver sulfite oxidase. Biochim Biophys Acta. 1995 Jun 9;1262(2-3):147-9. [PubMed ]
2. Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC: Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 1997 Dec 26;91(7):973-83. [PubMed ]
3. Garrett RM, Johnson JL, Graf TN, Feigenbaum A, Rajagopalan KV: Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Proc Natl Acad Sci U S A. 1998 May 26;95(11):6394-8. [PubMed ]
4. Edwards MC, Johnson JL, Marriage B, Graf TN, Coyne KE, Rajagopalan KV, MacDonald IM: Isolated sulfite oxidase deficiency: review of two cases in one family. Ophthalmology. 1999 Oct;106(10):1957-61. [PubMed ]
5. Johnson JL, Coyne KE, Garrett RM, Zabot MT, Dorche C, Kisker C, Rajagopalan KV: Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients. Hum Mutat. 2002 Jul;20(1):74. [PubMed ]
6. Lee HF, Mak BS, Chi CS, Tsai CR, Chen CH, Shu SG: A novel mutation in neonatal isolated sulphite oxidase deficiency. Neuropediatrics. 2002 Aug;33(4):174-9. [PubMed ]

1. Alpha-L-iduronate sulfate sulfatase
2. Idursulfase[Contains: Iduronate 2-sulfatase 42 kDa chain
3. Iduronate 2-sulfatase 14 kDa chain]

MPPPRTGRGLLWLGLVLSSVCVALGSETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVR
SPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIP
QYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHA
NLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQK
LYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSY
FASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLI
FYVPGRTASLPEAGEKLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPP
RCPVPSFHVELCREGKNLLKHFRFRDLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSDKP
SLKDIKIMGYSIRTIDYRYTVWVGFNPDEFLANFSDIHAGELYFVDSDPLQDHNMYNDSQ
GGDLFQLLMP

• Glycosaminoglycan degradation (map00531 )

• Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin

• Sulfatase (PF00884 )

• 1-25

ATGCCGCCACCCCGGACCGGCCGAGGCCTTCTCTGGCTGGGTCTGGTTCTGAGCTCCGTC
TGCGTCGCCCTCGGATCCGAAACGCAGGCCAACTCGACCACAGATGCTCTGAACGTTCTT
CTCATCATCGTGGATGACCTGCGCCCCTCCCTGGGCTGTTATGGGGATAAGCTGGTGAGG
TCCCCAAATATTGACCAACTGGCATCCCACAGCCTCCTCTTCCAGAATGCCTTTGCGCAG
CAAGCAGTGTGCGCCCCGAGCCGCGTTTCTTTCCTCACTGGCAGGAGACCTGACACCACC
CGCCTGTACGACTTCAACTCCTACTGGAGGGTGCACGCTGGAAACTTCTCCACCATCCCC
CAGTACTTCAAGGAGAATGGCTATGTGACCATGTCGGTGGGAAAAGTCTTTCACCCTGGG
ATATCTTCTAACCATACCGATGATTCTCCGTATAGCTGGTCTTTTCCACCTTATCATCCT
TCCTCTGAGAAGTATGAAAACACTAAGACATGTCGAGGGCCAGATGGAGAACTCCATGCC
AACCTGCTTTGCCCTGTGGATGTGCTGGATGTTCCCGAGGGCACCTTGCCTGACAAACAG
AGCACTGAGCAAGCCATACAGTTGTTGGAAAAGATGAAAACGTCAGCCAGTCCTTTCTTC
CTGGCCGTTGGGTATCATAAGCCACACATCCCCTTCAGATACCCCAAGGAATTTCAGAAG
TTGTATCCCTTGGAGAACATCACCCTGGCCCCCGATCCCGAGGTCCCTGATGGCCTACCC
CCTGTGGCCTACAACCCCTGGATGGACATCAGGCAACGGGAAGACGTCCAAGCCTTAAAC
ATCAGTGTGCCGTATGGTCCAATTCCTGTGGACTTTCAGCGGAAAATCCGCCAGAGCTAC
TTTGCCTCTGTGTCATATTTGGATACACAGGTCGGCCGCCTCTTGAGTGCTTTGGACGAT
CTTCAGCTGGCCAACAGCACCATCATTGCATTTACCTCGGATCATGGGTGGGCTCTAGGT
GAACATGGAGAATGGGCCAAATACAGCAATTTTGATGTTGCTACCCATGTTCCCCTGATA
TTCTATGTTCCTGGAAGGACGGCTTCACTTCCGGAGGCAGGCGAGAAGCTTTTCCCTTAC
CTCGACCCTTTTGATTCCGCCTCACAGTTGATGGAGCCAGGCAGGCAATCCATGGACCTT
GTGGAACTTGTGTCTCTTTTTCCCACGCTGGCTGGACTTGCAGGACTGCAGGTTCCACCT
CGCTGCCCCGTTCCTTCATTTCACGTTGAGCTGTGCAGAGAAGGCAAGAACCTTCTGAAG
CATTTTCGATTCCGTGACTTGGAAGAGGATCCGTACCTCCCTGGTAATCCCCGTGAACTG
ATTGCCTATAGCCAGTATCCCCGGCCTTCAGACATCCCTCAGTGGAATTCTGACAAGCCG
AGTTTAAAAGATATAAAGATCATGGGCTATTCCATACGCACCATAGACTATAGGTATACT
GTGTGGGTTGGCTTCAATCCTGATGAATTTCTAGCTAACTTTTCTGACATCCATGCAGGG
GAACTGTATTTTGTGGATTCTGACCCATTGCAGGATCACAATATGTATAATGATTCCCAA
GGTGGAGATCTTTTCCAGTTGTTGATGCCTTGA

1. Wilson PJ, Morris CP, Anson DS, Occhiodoro T, Bielicki J, Clements PR, Hopwood JJ: Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8531-5. [PubMed ]
2. Wilson PJ, Meaney CA, Hopwood JJ, Morris CP: Sequence of the human iduronate 2-sulfatase (IDS) gene. Genomics. 1993 Sep;17(3):773-5. [PubMed ]
3. Timms KM, Lu F, Shen Y, Pierson CA, Muzny DM, Gu Y, Nelson DL, Gibbs RA: 130 kb of DNA sequence reveals two new genes and a regional duplication distal to the human iduronate-2-sulfate sulfatase locus. Genome Res. 1995 Aug;5(1):71-8. [PubMed ]
4. Malmgren H, Carlberg BM, Pettersson U, Bondeson ML: Identification of an alternative transcript from the human iduronate-2-sulfatase (IDS) gene. Genomics. 1995 Sep 1;29(1):291-3. [PubMed ]
5. Flomen RH, Green EP, Green PM, Bentley DR, Giannelli F: Determination of the organisation of coding sequences within the iduronate sulphate sulphatase (IDS) gene. Hum Mol Genet. 1993 Jan;2(1):5-10. [PubMed ]
6. Hopwood JJ, Bunge S, Morris CP, Wilson PJ, Steglich C, Beck M, Schwinger E, Gal A: Molecular basis of mucopolysaccharidosis type II: mutations in the iduronate-2-sulphatase gene. Hum Mutat. 1993;2(6):435-42. [PubMed ]
7. Bunge S, Steglich C, Beck M, Rosenkranz W, Schwinger E, Hopwood JJ, Gal A: Mutation analysis of the iduronate-2-sulfatase gene in patients with mucopolysaccharidosis type II (Hunter syndrome). Hum Mol Genet. 1992 Aug;1(5):335-9. [PubMed ]
8. Crotty PL, Braun SE, Anderson RA, Whitley CB: Mutation R468W of the iduronate-2-sulfatase gene in mild Hunter syndrome (mucopolysaccharidosis type II) confirmed by in vitro mutagenesis and expression. Hum Mol Genet. 1992 Dec;1(9):755-7. [PubMed ]
9. Bunge S, Steglich C, Zuther C, Beck M, Morris CP, Schwinger E, Schinzel A, Hopwood JJ, Gal A: Iduronate-2-sulfatase gene mutations in 16 patients with mucopolysaccharidosis type II (Hunter syndrome). Hum Mol Genet. 1993 Nov;2(11):1871-5. [PubMed ]
10. Schroder W, Wulff K, Wehnert M, Seidlitz G, Herrmann FH: Mutations of the iduronate-2-sulfatase (IDS) gene in patients with Hunter syndrome (mucopolysaccharidosis II). Hum Mutat. 1994;4(2):128-31. [PubMed ]
11. Jonsson JJ, Aronovich EL, Braun SE, Whitley CB: Molecular diagnosis of mucopolysaccharidosis type II (Hunter syndrome) by automated sequencing and computer-assisted interpretation: toward mutation mapping of the iduronate-2-sulfatase gene. Am J Hum Genet. 1995 Mar;56(3):597-607. [PubMed ]
12. Popowska E, Rathmann M, Tylki-Szymanska A, Bunge S, Steglich C, Schwinger E, Gal A: Mutations of the iduronate-2-sulfatase gene in 12 Polish patients with mucopolysaccharidosis type II (Hunter syndrome). Hum Mutat. 1995;5(1):97-100. [PubMed ]
13. Li P, Huffman P, Thompson JN: Mutations of the iduronate-2-sulfatase gene on a T146T background in three patients with Hunter syndrome. Hum Mutat. 1995;5(3):272-4. [PubMed ]
14. Rathmann M, Bunge S, Beck M, Kresse H, Tylki-Szymanska A, Gal A: Mucopolysaccharidosis type II (Hunter syndrome): mutation "hot spots" in the iduronate-2-sulfatase gene. Am J Hum Genet. 1996 Dec;59(6):1202-9. [PubMed ]
15. Olsen TC, Eiken HG, Knappskog PM, Kase BF, Mansson JE, Boman H, Apold J: Mutations in the iduronate-2-sulfatase gene in five Norwegians with Hunter syndrome. Hum Genet. 1996 Feb;97(2):198-203. [PubMed ]
16. Li P, Thompson JN: Detection of four novel mutations in the iduronate-2-sulphatase gene by single-strand conformation polymorphism analysis of genomic amplicons. J Inherit Metab Dis. 1996;19(1):93-4. [PubMed ]
17. Villani GR, Balzano N, Grosso M, Salvatore F, Izzo P, Di Natale P: Mucopolysaccharidosis type II: identification of six novel mutations in Italian patients. Hum Mutat. 1997;10(1):71-5. [PubMed ]
18. Sukegawa K, Song XQ, Masuno M, Fukao T, Shimozawa N, Fukuda S, Isogai K, Nishio H, Matsuo M, Tomatsu S, Kondo N, Orii T: Hunter disease in a girl caused by R468Q mutation in the iduronate-2-sulfatase gene and skewed inactivation of the X chromosome carrying the normal allele. Hum Mutat. 1997;10(5):361-7. [PubMed ]
19. Vafiadaki E, Cooper A, Heptinstall LE, Hatton CE, Thornley M, Wraith JE: Mutation analysis in 57 unrelated patients with MPS II (Hunter's disease). Arch Dis Child. 1998 Sep;79(3):237-41. [PubMed ]
20. Karsten S, Voskoboeva E, Tishkanina S, Pettersson U, Krasnopolskaja X, Bondeson ML: Mutational spectrum of the iduronate-2-sulfatase (IDS) gene in 36 unrelated Russian MPS II patients. Hum Genet. 1998 Dec;103(6):732-5. [PubMed ]
21. Gort L, Coll MJ, Chabas A: Mutations in the iduronate-2-sulfatase gene in 12 Spanish patients with Hunter disease. Hum Mutat. 1998;Suppl 1:S66-8. [PubMed ]
22. Vallance HD, Bernard L, Rashed M, Chiu D, Le G, Toone J, Applegarth DA, Coulter-Mackie M: Identification of 6 new mutations in the iduronate sulfatase gene. Mutation in brief no. 233. Online. Hum Mutat. 1999;13(4):338. [PubMed ]
23. Hartog C, Fryer A, Upadhyaya M: Mutation analysis of iduronate-2-sulphatase gene in 24 patients with Hunter syndrome: characterisation of 6 novel mutations. Mutation in brief no. 249. Online. Hum Mutat. 1999;14(1):87. [PubMed ]
24. Li P, Bellows AB, Thompson JN: Molecular basis of iduronate-2-sulphatase gene mutations in patients with mucopolysaccharidosis type II (Hunter syndrome). J Med Genet. 1999 Jan;36(1):21-7. [PubMed ]

1. G6S
2. Glucosamine-6-sulfatase

MRLLPLAPGRLRRGSPRHLPSCSPALLLLVLGGCLGVFGVAAGTRRPNVVLLLTDDQDEV
LGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSS
KSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSK
YYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHSPWTA
APQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRKRWQTLLSVD
DLVEKLVKRLEFTGELNNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIK
PNQTSKMLVANIDLGPTILDIAGYDLNKTQMDGMSLLPILRGASNLTWRSDVLVEYQGEG
RNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTMSALWNLQYCEFDDQEVFVEVYN
LTADPDQITNIAKTIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDPRLMFSNRG
SVRTRRFSKHLL

• Glycosaminoglycan degradation (map00531 )

• Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate

• Sulfatase (PF00884 )

• 1-36

ATGCGGCTCCTGCCTCTAGCCCCAGGTCGGCTCCGGCGGGGCAGCCCCCGCCACCTGCCC
TCCTGCAGCCCAGCGCTGCTACTGCTGGTGCTGGGCGGCTGCCTGGGGGTCTTCGGGGTG
GCTGCGGGAACCCGGAGGCCCAACGTGGTGCTGCTCCTCACGGACGACCAGGACGAAGTG
CTCGGCGGCATGACACCACTAAAGAAAACCAAAGCTCTCATCGGAGAGATGGGGATGACT
TTTTCCAGTGCTTATGTGCCAAGTGCTCTCTGCTGCCCCAGCAGAGCCAGTATCCTGACA
GGAAAGTACCCACATAATCATCACGTTGTGAACAACACTCTGGAGGGGAACTGCAGTAGT
AAGTCCTGGCAGAAGATCCAAGAACCAAATACTTTCCCAGCAATTCTCAGATCAATGTGT
GGTTATCAGACCTTTTTTGCAGGGAAATATTTAAATGAGTACGGAGCCCCAGATGCAGGT
GGACTAGAACACGTTCCTCTGGGTTGGAGTTACTGGTATGCCTTGGAAAAGAATTCTAAG
TATTATAATTACACCCTGTCTATCAATGGGAAGGCACGGAAGCATGGTGAAAACTATAGT
GTGGACTACCTGACAGATGTTTTGGCTAATGTCTCCTTGGACTTTCTGGACTACAAGTCC
AACTTTGAGCCCTTCTTCATGATGATCGCCACTCCAGCGCCTCATTCGCCTTGGACAGCT
GCACCTCAGTACCAGAAGGCTTTCCAGAATGTCTTTGCACCAAGAAACAAGAACTTCAAC
ATCCATGGAACGAACAAGCACTGGTTAATTAGGCAAGCCAAGACTCCAATGACTAATTCT
TCAATACAGTTTTTAGATAATGCATTTAGGAAAAGGTGGCAAACTCTCCTCTCAGTTGAT
GACCTTGTGGAGAAACTGGTCAAGAGGCTGGAGTTCACTGGGGAGCTCAACAACACTTAC
ATCTTCTATACCTCAGACAATGGCTATCACACAGGACAGTTTTCCTTGCCAATAGACAAG
AGACAGCTGTATGAGTTTGATATCAAAGTTCCACTGTTGGTTCGAGGACCTGGGATCAAA
CCAAATCAGACAAGCAAGATGCTGGTTGCCAACATTGACTTGGGTCCTACTATTTTGGAC
ATTGCTGGCTACGACCTAAATAAGACACAGATGGATGGGATGTCCTTATTGCCCATTTTG
AGAGGTGCCAGTAACTTGACCTGGCGATCAGATGTCCTGGTGGAATACCAAGGAGAAGGC
CGTAACGTCACTGACCCAACATGCCCTTCCCTGAGTCCTGGCGTATCTCAATGCTTCCCA
GACTGTGTATGTGAAGATGCTTATAACAATACCTATGCCTGTGTGAGGACAATGTCAGCA
TTGTGGAATTTGCAGTATTGCGAGTTTGATGACCAGGAGGTGTTTGTAGAAGTCTATAAT
CTGACTGCAGACCCAGACCAGATCACTAACATTGCTAAAACCATAGACCCAGAGCTTTTA
GGAAAGATGAACTATCGGTTAATGATGTTACAGTCCTGTTCTGGGCCAACCTGTCGCACT
CCAGGGGTTTTTGACCCCGGATACAGGTTTGACCCCCGTCTCATGTTCAGCAATCGCGGC
AGTGTCAGGACTCGAAGATTTTCCAAACATCTTCTGTAG

1. Robertson DA, Freeman C, Morris CP, Hopwood JJ: A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases. Biochem J. 1992 Dec 1;288 ( Pt 2):539-44. [PubMed ]
2. Robertson DA, Freeman C, Nelson PV, Morris CP, Hopwood JJ: Human glucosamine-6-sulfatase cDNA reveals homology with steroid sulfatase. Biochem Biophys Res Commun. 1988 Nov 30;157(1):218-24. [PubMed ]
3. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed ]

1. N- acetylgalactosamine-6-sulfate sulfatase
2. Galactose-6-sulfate sulfatase
3. GalNAc6S sulfatase
4. Chondroitinsulfatase
5. Chondroitinase

MAAVVAATRWWQLLLVLSAAGMGASGAPQPPNILLLLMDDMGWGDLGVYGEPSRETPNLD
RMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIVGGIPDS
EQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPV
YRDWEMVGRYYEEFPINLKTGEANLTQIYLQEALDFIKRQARHHPFFLYWAVDATHAPVY
ASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPEQG
GSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSD
RAIDGLNLLPTLLQGRLMDRPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFRQGIDFCP
GQNVSGVTTHNLEDHTKLPLIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALV
PAQPQLNVCNWAVMNWAPPGCEKLGKCLTPPESIPKKCLWSH

• Glycosaminoglycan degradation (map00531 )

• Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate

• Sulfatase (PF00884 )

• 1-26

ATGGCGGCGGTTGTCGCGGCGACGAGGTGGTGGCAGCTGTTGCTGGTGCTCAGCGCCGCG
GGGATGGGGGCCTCGGGCGCCCCGCAGCCCCCCAACATCCTGCTCCTGCTCATGGACGAC
ATGGGATGGGGTGACCTCGGGGTGTATGGAGAGCCCTCCAGAGAGACCCCGAATTTGGAC
CGGATGGCTGCAGAAGGGCTGCTTTTCCCAAACTTCTATTCTGCCAACCCTCTGTGCTCG
CCATCGAGGGCGGCACTGCTCACAGGACGGCTACCCATCCGCAATGGCTTCTACACCACC
AACGCCCATGCCAGAAACGCCTACACACCGCAGGAGATTGTGGGCGGCATCCCAGACTCG
GAGCAGCTCCTGCCGGAGCTTCTGAAGAAGGCCGGCTACGTCAGCAAGATTGTCGGCAAG
TGGCATCTGGGTCACAGGCCCCAGTTCCACCCCCTGAAGCACGGATTTGATGAGTGGTTT
GGATCCCCCAACTGCCACTTTGGACCTTATGACAACAAGGCCAGGCCCAACATCCCTGTG
TACAGGGACTGGGAGATGGTTGGCAGATATTATGAAGAATTTCCTATTAATCTGAAGACG
GGGGAAGCCAACCTCACCCAGATCTACCTGCAGGAAGCCCTGGACTTCATTAAGAGACAG
GCACGGCACCACCCCTTTTTCCTCTACTGGGCTGTCGACGCCACGCATGCACCCGTCTAT
GCCTCCAAACCCTTCTTGGGCACCAGTCAGCGAGGGCGGTATGGAGACGCCGTCCGGGAG
ATTGATGACAGCATTGGGAAGATACTGGAGCTCCTCCAAGACCTGCACGTCGCGGACAAC
ACCTTCGTCTTCTTCACGTCGGACAACGGCGCTGCCCTCATTTCCGCCCCCGAACAAGGT
GGCAGCAACGGCCCCTTTCTGTGTGGGAAGCAGACCACGTTTGAAGGAGGGATGAGGGAG
CCTGCCCTCGCATGGTGGCCAGGGCACGTCACTGCAGGCCAGGTGAGCCACCAGCTGGGC
AGCATCATGGACCTCTTCACCACCAGCCTGGCCCTTGCGGGCCTGACGCCGCCCAGCGAC
AGGGCCATTGATGGCCTCAACCTCCTCCCCACCCTCCTGCAGGGCCGGCTGATGGACAGG
CCTATCTTCTATTACCGTGGCGACACGCTGATGGCGGCCACCCTCGGGCAGCACAAGGCT
CACTTCTGGACCTGGACCAACTCCTGGGAGAACTTCAGACAGGGCATTGATTTCTGCCCT
GGGCAGAACGTTTCAGGGGTCACAACTCACAATCTGGAAGACCACACGAAGCTGCCCCTG
ATCTTCCACCTGGGACGGGACCCAGGGGAGAGGTTCCCCCTCAGCTTTGCCAGCGCCGAG
TACCAGGAGGCCCTCAGCAGGATCACCTCGGTCGTCCAGCAGCACCAGGAAGCCTTGGTC
CCCGCGCAGCCCCAGCTCAACGTGTGCAACTGGGCGGTCATGAACTGGGCACCTCCGGGC
TGTGAAAAGTTAGGGAAGTGTCTGACACCTCCAGAATCCATTCCCAAGAAGTGCCTCTGG
TCCCACTAG

1. Tomatsu S, Fukuda S, Masue M, Sukegawa K, Fukao T, Yamagishi A, Hori T, Iwata H, Ogawa T, Nakashima Y, et al.: Morquio disease: isolation, characterization and expression of full-length cDNA for human N-acetylgalactosamine-6-sulfate sulfatase. Biochem Biophys Res Commun. 1991 Dec 16;181(2):677-83. [PubMed ]
2. Morris CP, Guo XH, Apostolou S, Hopwood JJ, Scott HS: Morquio A syndrome: cloning, sequence, and structure of the human N-acetylgalactosamine 6-sulfatase (GALNS) gene. Genomics. 1994 Aug;22(3):652-4. [PubMed ]
3. Fukuda S, Tomatsu S, Masue M, Sukegawa K, Iwata H, Ogawa T, Nakashima Y, Hori T, Yamagishi A, Hanyu Y, et al.: Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases. J Clin Invest. 1992 Sep;90(3):1049-53. [PubMed ]
4. Tomatsu S, Fukuda S, Cooper A, Wraith JE, Rezvi GM, Yamagishi A, Yamada N, Kato Z, Isogai K, Sukegawa K, et al.: Mucopolysaccharidosis IVA: identification of a common missense mutation I113F in the N-Acetylgalactosamine-6-sulfate sulfatase gene. Am J Hum Genet. 1995 Sep;57(3):556-63. [PubMed ]
5. Ogawa T, Tomatsu S, Fukuda S, Yamagishi A, Rezvi GM, Sukegawa K, Kondo N, Suzuki Y, Shimozawa N, Oru T: Mucopolysaccharidosis IVA: screening and identification of mutations of the N-acetylgalactosamine-6-sulfate sulfatase gene. Hum Mol Genet. 1995 Mar;4(3):341-9. [PubMed ]
6. Tomatsu S, Fukuda S, Cooper A, Wraith JE, Rezvi GM, Yamagishi A, Yamada N, Kato Z, Isogai K, Sukegawa K, et al.: Mucopolysaccharidosis type IVA: identification of six novel mutations among non-Japanese patients. Hum Mol Genet. 1995 Apr;4(4):741-3. [PubMed ]
7. Tomatsu S, Fukuda S, Cooper A, Wraith JE, Yamada N, Isogai K, Kato Z, Sukegawa K, Kondo N, Suzuki Y, et al.: Two new mutations, Q473X and N487S, in a Caucasian patient with mucopolysaccharidosis IVA (Morquio disease). Hum Mutat. 1995;6(2):195-6. [PubMed ]
8. Tomatsu S, Fukuda S, Yamagishi A, Cooper A, Wraith JF, Hori T, Kato Z, Yamada N, Isogai K, Sukegawa K, Kondo N, Suzuki Y, Shimozawa N, Orii T: Mucopolysaccharidosis IVA: four new exonic mutations in patients with N-acetylgalactosamine-6-sulfate sulfatase deficiency. Am J Hum Genet. 1996 May;58(5):950-62. [PubMed ]
9. Cole DE, Fukuda S, Gordon BA, Rip JW, LeCouteur AN, Rupar CA, Tomatsu S, Ogawa T, Sukegawa K, Orii T: Heteroallelic missense mutations of the galactosamine-6-sulfate sulfatase (GALNS) gene in a mild form of Morquio disease (MPS IVA). Am J Med Genet. 1996 Jun 28;63(4):558-65. [PubMed ]
10. Bunge S, Kleijer WJ, Tylki-Szymanska A, Steglich C, Beck M, Tomatsu S, Fukuda S, Poorthuis BJ, Czartoryska B, Orii T, Gal A: Identification of 31 novel mutations in the N-acetylgalactosamine-6-sulfatase gene reveals excessive allelic heterogeneity among patients with Morquio A syndrome. Hum Mutat. 1997;10(3):223-32. [PubMed ]
11. Tomatsu S, Fukuda S, Cooper A, Wraith JE, Ferreira P, Di Natale P, Tortora P, Fujimoto A, Kato Z, Yamada N, Isogai K, Yamagishi A, Sukegawa K, Suzuki Y, Shimozawa N, Kondo N, Sly WS, Orii T: Fourteen novel mucopolysaccharidosis IVA producing mutations in GALNS gene. Hum Mutat. 1997;10(5):368-75. [PubMed ]
12. Yamada N, Fukuda S, Tomatsu S, Muller V, Hopwood JJ, Nelson J, Kato Z, Yamagishi A, Sukegawa K, Kondo N, Orii T: Molecular heterogeneity in mucopolysaccharidosis IVA in Australia and Northern Ireland: nine novel mutations including T312S, a common allele that confers a mild phenotype. Hum Mutat. 1998;11(3):202-8. [PubMed ]
13. Tomatsu S, Fukuda S, Cooper A, Wraith JE, Yamagishi A, Kato Z, Yamada N, Isogai K, Sukegawa K, Suzuki Y, Shimozawa N, Kondo N, Orii T: Fifteen polymorphisms in the N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene: diagnostic implications in Morquio disease. Hum Mutat. 1998;Suppl 1:S42-6. [PubMed ]

1. Diastrophic dysplasia protein
2. Solute carrier family 26 member 2

MSSESKEQHNVSPRDSAEGNDSYPSGIHLELQRESSTDFKQFETNDQCRPYHRILIERQE
KSDTNFKEFVIKKLQKNCQCSPAKAKNMILGFLPVLQWLPKYDLKKNILGDVMSGLIVGI
LLVPQSIAYSLLAGQEPVYGLYTSFFASIIYFLLGTSRHISVGIFGVLCLMIGETVDREL
QKAGYDNAHSAPSLGMVSNGSTLLNHTSDRICDKSCYAIMVGSTVTFIAGVYQVAMGFFQ
VGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLNLPRTNGVGSLITTWIHVFRNIHKT
NLCDLITSLLCLLVLLPTKELNEHFKSKLKAPIPIELVVVVAATLASHFGKLHENYNSSI
AGHIPTGFMPPKVPEWNLIPSVAVDAIAISIIGFAITVSLSEMFAKKHGYTVKANQEMYA
IGFCNIIPSFFHCFTTSAALAKTLVKESTGCHTQLSGVVTALVLLLVLLVIAPLFYSLQK
SVLGVITIVNLRGALRKFRDLPKMWSISRMDTVIWFVTMLSSALLSTEIGLLVGVCFSIF
CVILRTQKPKSSLLGLVEESEVFESVSAYKNLQTKPGIKIFRFVAPLYYINKECFKSALY
KQTVNPILIKVAWKKAAKRKIKEKVVTLGGIQDEMSVQLSHDPLELHTIVIDCSAIQFLD
TAGIHTLKEVRRDYEAIGIQVLLAQCNPTVRDSLTNGEYCKKEEENLLFYSVYEAMAFAE
VSKNQKGVCVPNGLSLSSD

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• None

• 112-132 137-157 160-180 219-239 242-262 297-317 329-349 378-398 421-441 455-475 524-544 644-664

ATGTCTTCAGAAAGTAAAGAGCAACATAACGTTTCACCCAGAGACTCAGCTGAAGGAAAT
GACAGTTATCCATCTGGGATCCATCTGGAACTTCAAAGGGAATCAAGTACTGACTTCAAG
CAATTTGAGACCAATGATCAATGCAGACCTTATCATAGGATCCTTATTGAGCGTCAAGAG
AAATCAGATACAAACTTCAAGGAGTTTGTTATTAAAAAGCTGCAGAAGAATTGCCAGTGC
AGTCCAGCCAAAGCCAAAAATATGATTTTAGGTTTCCTTCCTGTTTTGCAGTGGCTCCCA
AAATACGACCTAAAGAAAAACATTTTAGGGGATGTGATGTCAGGCTTGATTGTGGGCATA
TTATTGGTGCCCCAGTCCATTGCTTATTCCCTGCTGGCTGGCCAAGAACCTGTCTATGGT
CTGTACACATCTTTTTTTGCCAGCATCATTTATTTTCTCTTGGGTACCTCCCGTCACATC
TCTGTGGGCATTTTTGGAGTACTGTGCCTTATGATTGGTGAGACAGTTGACCGAGAACTA
CAGAAAGCTGGCTATGACAATGCCCATAGTGCTCCTTCCTTAGGAATGGTTTCAAATGGG
AGCACATTATTAAATCATACATCAGACAGGATATGTGACAAAAGTTGCTATGCAATTATG
GTTGGCAGCACTGTAACCTTTATAGCTGGAGTTTATCAGGTAGCGATGGGCTTCTTTCAA
GTGGGTTTTGTTTCTGTCTACCTCTCAGATGCCTTGCTGAGTGGATTTGTCACTGGTGCC
TCCTTCACTATTCTTACATCTCAGGCCAAGTATCTTCTTGGGCTCAACCTTCCTCGGACT
AATGGTGTGGGCTCACTCATCACTACCTGGATACATGTCTTCAGAAACATCCATAAGACC
AATCTCTGTGATCTTATCACCAGCCTTTTGTGCCTTTTGGTTCTTTTGCCAACCAAAGAA
CTCAATGAACACTTCAAATCCAAGCTTAAGGCACCGATTCCTATTGAACTTGTTGTTGTT
GTAGCAGCCACATTAGCCTCTCATTTTGGAAAACTACATGAAAATTATAATTCTAGTATT
GCTGGACATATTCCCACTGGGTTTATGCCACCCAAAGTACCAGAATGGAACCTAATTCCT
AGTGTGGCTGTAGATGCAATAGCTATTTCCATCATTGGTTTTGCTATCACTGTATCACTT
TCTGAGATGTTTGCCAAGAAACATGGTTACACAGTCAAAGCAAACCAGGAAATGTATGCC
ATTGGCTTTTGTAATATCATCCCTTCCTTCTTCCACTGTTTTACTACTAGTGCAGCTCTT
GCAAAGACATTGGTTAAAGAATCAACAGGCTGCCATACTCAGCTTTCTGGTGTGGTAACA
GCCCTGGTTCTTTTGTTGGTCCTCCTAGTAATAGCTCCTTTGTTCTATTCCCTTCAAAAA
AGTGTCCTTGGTGTGATCACAATTGTAAATCTACGGGGAGCCCTTCGTAAATTTAGGGAT
CTTCCCAAAATGTGGAGTATTAGTAGAATGGATACAGTTATCTGGTTTGTTACTATGCTG
TCCTCTGCACTGCTAAGTACTGAAATAGGCCTACTTGTTGGGGTTTGTTTTTCTATATTT
TGTGTCATCCTCCGCACTCAGAAGCCAAAGAGTTCACTGCTTGGCTTGGTGGAAGAGTCT
GAGGTCTTTGAATCTGTGTCTGCTTACAAGAACCTTCAGACTAAGCCAGGCATCAAGATT
TTCCGCTTTGTAGCCCCTCTCTACTACATAAACAAAGAATGCTTTAAATCTGCTTTATAC
AAACAAACTGTCAACCCAATCTTAATAAAGGTGGCTTGGAAGAAGGCAGCAAAGAGAAAG
ATCAAAGAAAAAGTAGTGACTCTTGGTGGAATCCAGGATGAAATGTCAGTGCAACTTTCC
CATGATCCCTTGGAGCTGCATACTATAGTGATTGACTGCAGTGCAATTCAATTTTTAGAT
ACAGCAGGGATCCACACACTGAAAGAAGTTCGCAGAGATTATGAAGCCATTGGAATCCAG
GTTCTGCTGGCTCAGTGCAATCCCACTGTGAGGGATTCCCTAACCAACGGAGAATATTGC
AAAAAGGAAGAAGAAAACCTTCTCTTCTATAGTGTGTATGAAGCGATGGCTTTTGCAGAA
GTATCTAAAAATCAGAAAGGAGTATGTGTTCCCAATGGTCTGAGTCTTAGTAGTGATTAA

1. Hastbacka J, de la Chapelle A, Mahtani MM, Clines G, Reeve-Daly MP, Daly M, Hamilton BA, Kusumi K, Trivedi B, Weaver A, et al.: The diastrophic dysplasia gene encodes a novel sulfate transporter: positional cloning by fine-structure linkage disequilibrium mapping. Cell. 1994 Sep 23;78(6):1073-87. [PubMed ]
2. Superti-Furga A, Hastbacka J, Wilcox WR, Cohn DH, van der Harten HJ, Rossi A, Blau N, Rimoin DL, Steinmann B, Lander ES, Gitzelmann R: Achondrogenesis type IB is caused by mutations in the diastrophic dysplasia sulphate transporter gene. Nat Genet. 1996 Jan;12(1):100-2. [PubMed ]
3. Hastbacka J, Superti-Furga A, Wilcox WR, Rimoin DL, Cohn DH, Lander ES: Atelosteogenesis type II is caused by mutations in the diastrophic dysplasia sulfate-transporter gene (DTDST): evidence for a phenotypic series involving three chondrodysplasias. Am J Hum Genet. 1996 Feb;58(2):255-62. [PubMed ]

1. Na(+/sulfate cotransporter SUT-1

MGLLQGLLRVRKLLLVVCVPLLLLPLPVLHPSSEASCAYVLIVTAVYWVSEAVPLGAAAL
VPAFLYPFFGVLRSNEVAAEYFKNTTLLLVGVICVAAAVEKWNLHKRIALRMVLMAGAKP
GMLLLCFMCCTTLLSMWLSNTSTTAMVMPIVEAVLQELVSAEDEQLVAGNSNTEEAEPIS
LDVKNSQPSLELIFVNEDRSNADLTTLMHNENLNGVPSITNPIKTANQHQGKKQHPSQEK
PQVLTPSPRKQKLNRKYRSHHDQMICKCLSLSISYSATIGGLTTIIGTSTSLIFLEHFNN
QYPAAEVVNFGTWFLFSFPISLIMLVVSWFWMHWLFLGCNFKETCSLSKKKKTKREQLSE
KRIQEEYEKLGDISYPEMVTGFFFILMTVLWFTREPGFVPGWDSFFEKKGYRTDATVSVF
LGFLLFLIPAKKPCFGKKNDGENQEHSLGTEPIITWKDFQKTMPWEIVILVGGGYALASG
SKSSGLSTWIGNQMLSLSSLPPWAVTLLACILVSIVTEFVSNPATITIFLPILCSLSETM
HINPLYTLIPVTMCISFAVMLPVGNPPNAIVFSYGHCQIKDMVKAGLGVNVIGLVIVMVA
INTWGVSLFHLDTYPAWARVSNITDQA

• Na_sulph_symp (PF00939 )

• 1-25

• 13-33 52-72 79-99 113-133 275-295 310-330 373-393 415-435 467-487 500-520 544-564 591-611

ATGGGCCTGCTGCAGGGCCTGCTCCGAGTCCGGAAGCTGCTGCTGGTCGTCTGCGTCCCG
CTCCTGCTGCTGCCTCTGCCCGTCCTCCACCCCAGCAGCGAGGCCTCGTGTGCTTACGTG
CTGATCGTGACTGCTGTGTACTGGGTGTCGGAGGCAGTGCCTCTGGGAGCTGCAGCCCTG
GTGCCGGCCTTCCTCTACCCGTTCTTCGGAGTCCTCCGGTCCAATGAGGTGGCGGCGGAG
TACTTCAAGAACACCACGCTGCTGCTGGTGGGGGTCATCTGCGTGGCGGCTGCCGTGGAG
AAGTGGAACCTGCATAAGCGCATTGCTCTGCGCATGGTCTTGATGGCCGGGGCCAAGCCG
GGCATGCTGCTGCTCTGCTTCATGTGCTGTACCACGTTGCTGTCCATGTGGCTGTCCAAC
ACCTCCACCACCGCCATGGTGATGCCCATCGTGGAGGCCGTGCTGCAGGAGCTGGTCAGT
GCTGAGGACGAGCAGCTCGTGGCGGGCAACTCCAACACCGAAGAGGCCGAACCCATCAGT
CTGGATGTAAAGAACAGCCAACCTTCTCTGGAACTCATCTTTGTCAATGAAGACAGGTCC
AACGCAGACCTCACCACTCTGATGCACAACGAGAACCTGAATGGTGTGCCCTCGATCACC
AACCCCATCAAAACTGCAAACCAACACCAGGGCAAGAAGCAACACCCATCCCAGGAAAAG
CCACAAGTCCTGACCCCCAGCCCCAGGAAGCAGAAGCTGAACAGAAAGTACAGGTCCCAC
CATGACCAGATGATCTGCAAGTGCCTCTCCCTGAGCATATCCTACTCCGCTACCATTGGC
GGCCTGACCACCATCATCGGCACCTCCACCAGCCTCATCTTCCTGGAACACTTCAACAAC
CAGTATCCAGCCGCAGAGGTGGTGAACTTTGGCACCTGGTTCCTCTTCAGCTTCCCCATA
TCCCTCATCATGCTGGTGGTCAGCTGGTTCTGGATGCACTGGCTGTTCCTGGGCTGCAAT
TTTAAAGAGACCTGCTCTCTGAGCAAGAAGAAGAAGACCAAAAGGGAACAGTTGTCAGAG
AAGAGGATCCAAGAAGAATATGAAAAACTGGGAGACATTAGCTACCCAGAAATGGTGACT
GGATTTTTCTTCATCCTGATGACCGTACTGTGGTTTACCCGGGAGCCTGGCTTTGTCCCT
GGCTGGGATTCTTTCTTTGAAAAGAAAGGCTACCGTACTGATGCCACAGTCTCTGTCTTC
CTTGGCTTCCTCCTCTTCCTCATTCCAGCGAAGAAGCCCTGCTTTGGGAAAAAGAATGAT
GGAGAGAACCAGGAGCACTCACTGGGGACCGAGCCCATCATCACGTGGAAGGACTTCCAG
AAGACCATGCCCTGGGAGATTGTCATTCTGGTTGGGGGAGGCTATGCTCTGGCTTCTGGT
AGCAAGAGCTCTGGCCTCTCTACATGGATTGGGAACCAGATGTTGTCCCTGAGCAGCCTC
CCACCGTGGGCTGTCACCCTGCTGGCATGCATCCTCGTGTCCATTGTCACTGAGTTTGTG
AGCAACCCAGCAACCATCACCATCTTCCTGCCCATCCTGTGCAGCCTGTCTGAAACGATG
CACATTAACCCCCTCTACACCCTGATCCCAGTCACCATGTGCATCTCCTTTGCAGTGATG
CTGCCTGTGGGCAATCCCCCTAATGCCATCGTCTTCAGCTATGGGCACTGCCAGATCAAA
GATATGGTGAAAGCTGGCCTGGGAGTCAACGTTATTGGACTGGTGATAGTAATGGTGGCC
ATCAACACCTGGGGAGTTAGCCTCTTCCACCTGGACACTTACCCAGCATGGGCGAGGGTC
AGCAACATCACTGATCAAGCCTAA

1. Girard JP, Baekkevold ES, Feliu J, Brandtzaeg P, Amalric F: Molecular cloning and functional analysis of SUT-1, a sulfate transporter from human high endothelial venules. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12772-7. [PubMed ]

MPSSVTALGQARSYGPGMAPSACCCSPAALQRRLPILAWLPSYSLQWLKMDFVAGLSVGL
TAIPQALAYAEVAGLPPQYGLYSAFMGCFVYFFLGTSRDVTLGPTAIMSLLVSFYTFHEP
AYAVLLAFLSGCIQLAMGVLRLGFLLDFISYPVIKGFTSAAAVTIGFGQIKNLLGLQNIP
RPFFLQVYHTFLRIAETRVGDAVLGLVCMLLLLVLKLMRDHVPPVHPEMPPGVRLSRGLV
WAATTARNALVVSFAALVAYSFEVTGYQPFILTGETAEGLPPVRIPPFSVTTANGTISFT
EMVQDMGAGLAVVPLMGLMESIAVAKAFASQDNYRIDANQELLAIGLTNMLGSLVSSYPV
TGSFGRTAVNAQSGVCTPAGGLVTGVLVLLSLDYLTSLFYYIPKSALAAVIIMAVAPLFD
TKIFRTLWRVKRLDLLPLCVTFLLCFWEVQYGILAGALVSLLMLLHSAARPETKVSEGPV
LVLQPASGLSFPAMEALREEILSRALEVSPPRCLVLECTHVCSIDYTVVLGLGELLQDFQ
KQGVALAFVGLQVPVLRVLLSADLKGFQYFSTLEEAEKHLRQEPGTQPYNIREDSILDQK
VALLKA

• (2)Bicarbonate[c] + Sulfate[e] --> (2)Bicarbonate[e] + Sulfate[c]

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• None

• None

1. Vincourt JB, Jullien D, Amalric F, Girard JP: Molecular and functional characterization of SLC26A11, a sodium-independent sulfate transporter from high endothelial venules. FASEB J. 2003 May;17(8):890-2. Epub 2003 Mar 5. [PubMed ]

1. Glutathione transferase zeta 1
2. Maleylacetoacetate isomerase, isoform CRA_a

MKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQN
LSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAER
FKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]

MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

ATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGGCAGAATGGAGCCCATCCGG
TGGCTCTTGGCTGCAGCTGGAGTGGAGTTTGAAGAGAAATTTATAGGATCTGCAGAAGAT
TTGGGAAAGTTAAGAAATGATGGGAGTTTGATGTTCCAGCAAGTACCAATGGTTGAGATT
GATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTACGGGAAAGACATAAAGGAGAGAGCCCTAATTGATATGTATACAGAAGGTATGGCA
GATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCGACCTGAGGAAAAAGATGCCAAG
ATTGCCTTGATCAAAGAGAAAACAAAAAGTCGCTATTTCCCTGCCTTCGAAAAAGTGTTA
CAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTAGCCTG
GTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCTTATCTCCAACTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGAAGAAGCCAGAAAGATTTTC
AGGTTTTAA

MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF
EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK

• None

• None

ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA

MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL

• DSBA (PF01323 )

• None

• None

ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA

1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]

MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAK
KYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIA
YLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL

• None

• None

ATGGTTGACCTCACCCAGGTAATGGATGATGAAGTATTCATGGCTTTTGCATCCTATGCA
ACAATTATTCTTTCAAAAATGATGCTTATGAGTACTGCAACTGCATTCTATAGATTGACA
AGAAAGGTTTTTGCCAATCCAGAAGACTGTGTAGCATTTGGCAAAGGTGAAAATGCCAAG
AAGTATCTTCGAACAGATGACAGAGTAGAACGTGTACGCAGAGCCCACCTGAATGACCTT
GAAAATATTATTCCATTTCTTGGAATTGGCCTCCTGTATTCCTTGAGTGGTCCCGACCCC
TCTACAGCCATCCTGCACTTCAGACTATTTGTCGGAGCACGGATCTACCACACCATTGCA
TATTTGACACCCCTTCCCCAGCCAAATAGAGCTTTGAGTTTTTTTGTTGGATATGGAGTT
ACTCTTTCCATGGCTTACAGGTTGCTGAAAAGTAAATTGTACCTGTAA

MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP

• GST_C (PF00043 )
• GST_N (PF02798 )

• None

• None

MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRA
HQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSI
ALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH

• MAPEG (PF01124 )

• None

• None