SULT1C2

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)
End	108,309,915 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	54,153,367 bp
RNA expression pattern
	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
	; ; ; ;
	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
	6819
	69083
	ENSG00000198203
	ENSMUSG00000023122
	O00338
	Q9D939
	NM_001056 ; NM_176825
	NM_026935
	NP_001047 ; NP_789795
	NP_081211
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 25, 2024

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]

Related Research Articles

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Sulfotransferase 1A3/1A4 is an enzyme that in humans is encoded by the SULT1A3 gene.

Estrogen sulfotransferase is an enzyme that in humans is encoded by the SULT1E1 gene.

Sulfotransferase family cytosolic 2B member 1 is an enzyme that in humans is encoded by the SULT2B1 gene.

Sulfotransferase 1A2 is an enzyme that in humans is encoded by the SULT1A2 gene.

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.

Sulfotransferase 4A1 is an enzyme that in humans is encoded by the SULT4A1 gene.

Galactosylceramide sulfotransferase is an enzyme that in humans is encoded by the GAL3ST1 gene.

Sulfotransferase family cytosolic 1B member 1 is an enzyme that in humans is encoded by the SULT1B1 gene.

Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.

Sulfotransferase 1C4 is an enzyme that in humans is encoded by the SULT1C4 gene.

Carbohydrate sulfotransferase 12 is an enzyme that in humans is encoded by the CHST12 gene.

Galactose-3-O-sulfotransferase 4 is an enzyme that in humans is encoded by the GAL3ST4 gene.

Galactose-3-O-sulfotransferase 3 is an enzyme that in humans is encoded by the GAL3ST3 gene.

Bile salt sulfotransferase also known as hydroxysteroid sulfotransferase (HST) or sulfotransferase 2A1 (ST2A1) is an enzyme that in humans is encoded by the SULT2A1 gene.

Sulfotransferase 1C3, also known as ST1C3, is an enzyme that in humans is encoded by the SULT1C3 gene.

<span class="mw-page-title-main">Carbohydrate sulfotransferase</span> Class of enzymes which transfer an –SO3 group to glycoproteins and lipids

In biochemistry, carbohydrate sulfotransferases are enzymes within the class of sulfotransferases which catalyze the transfer of the sulfate functional group to carbohydrate groups in glycoproteins and glycolipids. Carbohydrates are used by cells for a wide range of functions from structural purposes to extracellular communication. Carbohydrates are suitable for such a wide variety of functions due to the diversity in structure generated from monosaccharide composition, glycosidic linkage positions, chain branching, and covalent modification. Possible covalent modifications include acetylation, methylation, phosphorylation, and sulfation. Sulfation, performed by carbohydrate sulfotransferases, generates carbohydrate sulfate esters. These sulfate esters are only located extracellularly, whether through excretion into the extracellular matrix (ECM) or by presentation on the cell surface. As extracellular compounds, sulfated carbohydrates are mediators of intercellular communication, cellular adhesion, and ECM maintenance.

Carbohydrate sulfotransferase 13 is a protein that is encoded in humans by the CHST13 gene.

Phenol sulfur transferase deficiency, in short PST deficiency, is the lack or the reduced activity of the functional enzyme phenol sulfur transferase, which is crucial in the detoxification of mainly phenolic compounds by catalysing the sulfate conjugation of the hydroxyl groups in the toxic phenolic compounds to result in more hydrophilic forms for more efficient excretion. This metabolic disorder was first discovered in the late 1990s by Dr. Rosemary Waring during her researches with autistic children, which also made this deficiency commonly associated to the topics of autism. Mutations in the PST genes account for the genetic causes of the deficiency, of which single nucleotide polymorphism and methylation of promoters are two examples of mutations that respectively cause conformational abnormalities and diminished expressions to the enzyme, resulting in the reduced detoxification of phenolic compounds and regulation of phenolic neurotransmitter. The deficiency may cause symptoms like flushing, tachycardia, and depression, and be a risk factor for disorders like autism, migraine, and cancer, while it also limits the use of phenolic drugs in PST deficient patients. There is currently no drug available for treating PST deficiency. However, some people suffering from PST deficiency have found taking a digestive enzyme supplement containing Xylanase 10 minutes before eating to greatly reduce symptoms.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000198203 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023122 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: SULT1C1 sulfotransferase family, cytosolic, 1C, member 1".

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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000198203 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid9169148-5] 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.

[pmid10783263-6] 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.

[entrez-7] 1 2 "Entrez Gene: SULT1C1 sulfotransferase family, cytosolic, 1C, member 1".

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SULT1C2

Contents

Function

Related Research Articles

References

Further reading