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Gene Review

SULT1C2  -  sulfotransferase family, cytosolic, 1C,...

Homo sapiens

Synonyms: ST1C1, ST1C2, SULT1C#1, SULT1C1, Sulfotransferase 1C1, ...
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Disease relevance of SULT1C2

  • Recombinant human SULT1C sulfotransferases 1 and 2, expressed in Escherichia coli and purified to near electrophoretic homogeneity, were shown to cross-react with the antiserum against the rat liver SULT1C1 sulfotransferase and exhibited sulfonating activities with N-OH-2AAF as substrate [1].
  • While the increased expression of SULT1C1 in malignant tissue seems to reflect tumor dedifferentiation, our finding of unspliced SULT1A2 mRNA in non-malignant tissue offers additional aspects regarding the search for breast cancer risk factors [2].

High impact information on SULT1C2


Biological context of SULT1C2


Anatomical context of SULT1C2

  • Because SULT1C1 is present in the adult thyroid, intra-thyroidal sulfation of thyroid hormones and their metabolites might occur [8].

Associations of SULT1C2 with chemical compounds


Other interactions of SULT1C2

  • SULT1C1 and SULT1C2 were approximately 21 and 10 kb in length, respectively [6].
  • With the exception of SULT1B1, SULT1C1, and SULT4A1, all of the human SULTs studied catalyzed the sulfate conjugation of CEs [10].
  • The amino acid sequence of the protein encoded by the cDNA was 62% identical with that encoded by the rat ST1C1 cDNA and included signature sequences that are conserved in all cytosolic SULT enzymes [5].
  • Activities were markedly lower with SULT1E1, 1A1 and 2A1, and were negligible with SULT1C1, 2B1a, 2B1b and 4A1 [11].
  • The experiments using anti-rat ST1C1 antibody and nucleotide probes for human ST1C1 showed no detectable band in Western blots and an mRNA-detecting method with polymerase chain reaction, respectively, in human liver samples [12].

Analytical, diagnostic and therapeutic context of SULT1C2


  1. Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. Sakakibara, Y., Yanagisawa, K., Katafuchi, J., Ringer, D.P., Takami, Y., Nakayama, T., Suiko, M., Liu, M.C. J. Biol. Chem. (1998) [Pubmed]
  2. Altered expression of the hormone- and xenobiotic-metabolizing sulfotransferase enzymes 1A2 and 1C1 in malignant breast tissue. Aust, S., Obrist, P., Klimpfinger, M., Tucek, G., Jäger, W., Thalhammer, T. Int. J. Oncol. (2005) [Pubmed]
  3. Human sulfotransferase SULT1C1 pharmacogenetics: gene resequencing and functional genomic studies. Freimuth, R.R., Eckloff, B., Wieben, E.D., Weinshilboum, R.M. Pharmacogenetics (2001) [Pubmed]
  4. Molecular characterization of ST1C1-related human sulfotransferase. Yoshinari, K., Nagata, K., Shimada, M., Yamazoe, Y. Carcinogenesis (1998) [Pubmed]
  5. Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization. Her, C., Kaur, G.P., Athwal, R.S., Weinshilboum, R.M. Genomics (1997) [Pubmed]
  6. Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization. Freimuth, R.R., Raftogianis, R.B., Wood, T.C., Moon, E., Kim, U.J., Xu, J., Siciliano, M.J., Weinshilboum, R.M. Genomics (2000) [Pubmed]
  7. Identification of a novel zebrafish SULT1 cytosolic sulfotransferase: cloning, expression, characterization, and developmental expression study. Liu, M.Y., Yang, Y.S., Sugahara, T., Yasuda, S., Liu, M.C. Arch. Biochem. Biophys. (2005) [Pubmed]
  8. Sulfation of iodothyronines by human sulfotransferase 1C1 (SULT1C1)*. Li, X., Clemens, D.L., Anderson, R.J. Biochem. Pharmacol. (2000) [Pubmed]
  9. Expression profiling of sulfotransferases in human cell lines derived from extra-hepatic tissues. Tamura, H.O., Taniguchi, K., Hayashi, E., Hiyoshi, Y., Nagai, F. Biol. Pharm. Bull. (2001) [Pubmed]
  10. Catecholestrogen sulfation: possible role in carcinogenesis. Adjei, A.A., Weinshilboum, R.M. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  11. Sulpho-conjugation of ethanol in humans in vivo and by individual sulphotransferase forms in vitro. Schneider, H., Glatt, H. Biochem. J. (2004) [Pubmed]
  12. Arylamine activating sulfotransferase in liver. Nagata, K., Yoshinari, K., Ozawa, S., Yamazoe, Y. Mutat. Res. (1997) [Pubmed]
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