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Revision as of 20:25, 5 June 2016 by Boghog(talk | contribs)(removed no longer needed PBB controls and templates; consistent citation formatting; removed further reading citations not specific to this gene)
Sulfotransferase 1C2 is an enzyme that in humans is encoded by the SULT1C2gene.[5][6][7]
Function
Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a protein that belongs to the SULT1 subfamily, responsible for transferring a sulfo moiety from PAPS to phenol-containing compounds. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[7]
Weinshilboum RM, Otterness DM, Aksoy IA, Wood TC, Her C, Raftogianis RB (January 1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes". FASEB Journal. 11 (1): 3–14. PMID9034160.
Glatt H, Engelke CE, Pabel U, Teubner W, Jones AL, Coughtrie MW, Andrae U, Falany CN, Meinl W (March 2000). "Sulfotransferases: genetics and role in toxicology". Toxicology Letters. 112–113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID10720750.
Glatt H (December 2000). "Sulfotransferases in the bioactivation of xenobiotics". Chemico-Biological Interactions. 129 (1–2): 141–70. doi:10.1016/S0009-2797(00)00202-7. PMID11154739.
Glatt H, Boeing H, Engelke CE, Ma L, Kuhlow A, Pabel U, Pomplun D, Teubner W, Meinl W (October 2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutation Research. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID11535246.
Kiehlbauch CC, Lam YF, Ringer DP (August 1995). "Homodimeric and heterodimeric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene". The Journal of Biological Chemistry. 270 (32): 18941–7. doi:10.1074/jbc.270.32.18941. PMID7642552.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Yoshinari K, Nagata K, Shimada M, Yamazoe Y (May 1998). "Molecular characterization of ST1C1-related human sulfotransferase". Carcinogenesis. 19 (5): 951–3. doi:10.1093/carcin/19.5.951. PMID9635888.
Sakakibara Y, Yanagisawa K, Katafuchi J, Ringer DP, Takami Y, Nakayama T, Suiko M, Liu MC (December 1998). "Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene". The Journal of Biological Chemistry. 273 (51): 33929–35. doi:10.1074/jbc.273.51.33929. PMID9852044.{{cite journal}}: CS1 maint: unflagged free DOI (link)
Hehonah N, Zhu X, Brix L, Bolton-Grob R, Barnett A, Windmill K, McManus M (August 1999). "Molecular cloning, expression, localisation and functional characterisation of a rabbit SULT1C2 sulfotransferase". The International Journal of Biochemistry & Cell Biology. 31 (8): 869–82. doi:10.1016/S1357-2725(99)00038-2. PMID10481272.
Li X, Clemens DL, Anderson RJ (December 2000). "Sulfation of iodothyronines by human sulfotransferase 1C1 (SULT1C1)*". Biochemical Pharmacology. 60 (11): 1713–6. doi:10.1016/S0006-2952(00)00475-5. PMID11077054.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
Dombrovski L, Dong A, Bochkarev A, Plotnikov AN (September 2006). "Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP)". Proteins. 64 (4): 1091–4. doi:10.1002/prot.21048. PMID16804942.