SULT1C2

Protein-coding gene in the species Homo sapiens
SULT1C2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3BFX

Identifiers
AliasesSULT1C2, ST1C1, ST1C2, SULT1C1, humSULTC2, sulfotransferase family 1C member 2
External IDsOMIM: 602385; MGI: 1916333; HomoloGene: 38201; GeneCards: SULT1C2; OMA:SULT1C2 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for SULT1C2
Genomic location for SULT1C2
Band2q12.3Start108,288,639 bp[1]
End108,309,915 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for SULT1C2
Genomic location for SULT1C2
Band17|17 CStart54,136,665 bp[2]
End54,153,367 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 17: 54.14 – 54.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198203 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023122 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Her C, Kaur GP, Athwal RS, Weinshilboum RM (May 1997). "Human sulfotransferase SULT1C1: cDNA cloning, tissue-specific expression, and chromosomal localization". Genomics. 41 (3): 467–70. doi:10.1006/geno.1997.4683. PMID 9169148.
  6. ^ Freimuth RR, Raftogianis RB, Wood TC, Moon E, Kim UJ, Xu J, Siciliano MJ, Weinshilboum RM (April 2000). "Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization". Genomics. 65 (2): 157–65. doi:10.1006/geno.2000.6150. PMID 10783263.
  7. ^ a b "Entrez Gene: SULT1C1 sulfotransferase family, cytosolic, 1C, member 1".

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.
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