SULT1C2

Sulfotransferase 1C2 is an enzyme that in humans is encoded by the SULT1C2 gene.

SULT1C2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3BFX
Identifiers
Aliases	SULT1C2, ST1C1, ST1C2, SULT1C1, humSULTC2, sulfotransferase family 1C member 2
External IDs	OMIM: 602385; MGI: 1916333; HomoloGene: 38201; GeneCards: SULT1C2; OMA:SULT1C2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q12.3 Start 108,288,639 bp End 108,309,915 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 C Start 54,136,665 bp End 54,153,367 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pylorus kidney tubule renal medulla buccal mucosa cell human kidney gastric mucosa glomerulus corpus epididymis metanephric glomerulus caput epididymis Top expressed in epithelium of stomach pyloric antrum mucous cell of stomach basilar part of occipital bone right kidney human kidney rib splanchnocranium humerus Meckel's cartilage More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity sulfotransferase activity protein binding aryl sulfotransferase activity Cellular component cytoplasm cytosol Biological process amine metabolic process 3'-phosphoadenosine 5'-phosphosulfate metabolic process sulfation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6819 69083 Ensembl ENSG00000198203 ENSMUSG00000023122 UniProt O00338 Q9D939 RefSeq (mRNA) NM_001056 NM_176825 NM_026935 RefSeq (protein) NP_001047 NP_789795 NP_081211 Location (UCSC) Chr 2: 108.29 – 108.31 Mb Chr 17: 54.14 – 54.15 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Further reading

• 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. doi:10.1096/fasebj.11.1.9034160. PMID 9034160. S2CID 12532583.
• 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. PMID 10720750.
• Glatt H (December 2000). "Sulfotransferases in the bioactivation of xenobiotics". Chemico-Biological Interactions. 129 (1–2): 141–70. Bibcode:2000CBI...129..141G. doi:10.1016/S0009-2797(00)00202-7. PMID 11154739.
• 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. PMID 11535246.
• 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. PMID 7642552.
• 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. PMID 9635888.
• 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. PMID 9852044.
• 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" (PDF). The International Journal of Biochemistry & Cell Biology. 31 (8): 869–82. doi:10.1016/S1357-2725(99)00038-2. PMID 10481272.
• 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. PMID 11077054.
• Freimuth RR, Eckloff B, Wieben ED, Weinshilboum RM (December 2001). "Human sulfotransferase SULT1C1 pharmacogenetics: gene resequencing and functional genomic studies". Pharmacogenetics. 11 (9): 747–56. doi:10.1097/00008571-200112000-00002. PMID 11740338.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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. PMID 16804942. S2CID 32647194.