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Gene Review

SULT1C4  -  sulfotransferase family, cytosolic, 1C,...

Homo sapiens

Synonyms: ST1C4, SULT1C, SULT1C#2, SULT1C2, Sulfotransferase 1C2, ...
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Disease relevance of SULT1C4

  • Induction of differentiation did not generally affect SULT expression, although that of SULT1C2 was reduced after differentiation of the neuroblastoma cell line, NB-1, was induced [1].
  • 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 [2].

High impact information on SULT1C4

  • In the same model, increased relapse risk was associated with SULT1C2 heterozygosity (RR = 4.1; P = .004), FLT3-ITD (RR 3.3; P = .003), and MDR1 variant alleles (RR = 2.4; P = .02) [3].
  • Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene [2].
  • As there are no isoform-selective substrates for SULTs 1B1 and 1C2 we used immunoblot analysis to show for the first time expression of SULT1B1 at high levels in fetal small intestine, and expression of SULT1C2 in fetal liver, kidney and small intestine [4].
  • The amino acid sequence of ratSULT1C2 is 84% identical to the human SULT1C2 and 81% identical to a rabbit SULT1C2 sulfotransferase. ratSULT1C2 and ratSULT1C2A are 92% identical but differ in 22 amino acids [5].
  • Activity data showed that P-form (SULT1A1) PST displayed the highest activity toward these compounds, while SULT1C ST #2 also showed considerable activity, indicating that these enzymes may play a more important role in detoxification of environmental xenoestrogens [6].

Biological context of SULT1C4


Other interactions of SULT1C4


Analytical, diagnostic and therapeutic context of SULT1C4


  1. 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]
  2. 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]
  3. Genomic polymorphisms provide prognostic information in intermediate-risk acute myeloblastic leukemia. Monzo, M., Brunet, S., Urbano-Ispizua, A., Navarro, A., Perea, G., Esteve, J., Artells, R., Granell, M., Berlanga, J., Ribera, J.M., Bueno, J., Llorente, A., Guardia, R., Tormo, M., Torres, P., Nomdedéu, J.F., Montserrat, E., Sierra, J. Blood (2006) [Pubmed]
  4. Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification. Stanley, E.L., Hume, R., Coughtrie, M.W. Mol. Cell. Endocrinol. (2005) [Pubmed]
  5. Enzymatic properties, tissue-specific expression, and lysosomal location of two highly homologous rat SULT1C2 sulfotransferases. Xiangrong, L., Jöhnk, C., Hartmann, D., Schestag, F., Krömer, W., Gieselmann, V. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  6. Differential xenoestrogen-sulfating activities of the human cytosolic sulfotransferases: molecular cloning, expression, and purification of human SULT2B1a and SULT2B1b sulfotransferases. Pai, T.G., Sugahara, T., Suiko, M., Sakakibara, Y., Xu, F., Liu, M.C. Biochim. Biophys. Acta (2002) [Pubmed]
  7. 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]
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