SULT1B1

SULT1B1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2Z5F, 3CKL
Identifiers
Aliases	SULT1B1 , ST1B1, ST1B2, SULT1B2, sulfotransferase family 1B member 1
External IDs	OMIM: 608436; MGI: 2136282; HomoloGene: 69169; GeneCards: SULT1B1; OMA:SULT1B1 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4q13.3 Start 69,721,167 bp [1] End 69,787,961 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 E1 Start 87,661,198 bp [2] End 87,686,054 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in rectum mucosa of transverse colon jejunal mucosa duodenum monocyte epithelium of colon mucosa of sigmoid colon blood mucosa of ileum right lobe of liver Top expressed in duodenum jejunum colon left colon mucous cell of stomach ileum epithelium of stomach pyloric antrum epithelium of small intestine intestinal villus 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 steroid metabolic process phenol-containing compound metabolic process epithelial cell differentiation sulfation lipid metabolism cellular biogenic amine metabolic process flavonoid metabolic process thyroid hormone metabolic process xenobiotic metabolic process ethanol catabolic process 3'-phosphoadenosine 5'-phosphosulfate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27284 56362 Ensembl ENSG00000173597 ENSMUSG00000029269 UniProt O43704 Q9QWG7 RefSeq (mRNA) NM_014465 NM_019878 NM_001356943 NM_001382837 RefSeq (protein) NP_055280 NP_063931 NP_001343872 NP_001369766 Location (UCSC) Chr 4: 69.72 – 69.79 Mb Chr 5: 87.66 – 87.69 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Sulfotransferase family cytosolic 1B member 1 is an enzyme that in humans is encoded by the SULT1B1 gene. ^{[5] [6] [7]}

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. However, the total genomic length of this gene is greater than that of all of the other SULT1 genes. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000173597 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029269 – 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. Meinl W, Glatt H (Nov 2001). "Structure and localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene". Biochem Biophys Res Commun. 288 (4): 855–62. doi:10.1006/bbrc.2001.5829. PMID   11688987.
6. Fujita K, Nagata K, Ozawa S, Sasano H, Yamazoe Y (Feb 1998). "Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases". J Biochem. 122 (5): 1052–61. doi:10.1093/oxfordjournals.jbchem.a021846. PMID   9443824.
7. "Entrez Gene: SULT1B1 sulfotransferase family, cytosolic, 1B, member 1".

Further reading

• Weinshilboum RM, Otterness DM, Aksoy IA, et al. (1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes". FASEB J. 11 (1): 3–14. doi: 10.1096/fasebj.11.1.9034160 . PMID   9034160. S2CID   12532583.
• Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology". Toxicol. Lett. 112–113 (1–3): 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID   10720750.
• Glatt H (2001). "Sulfotransferases in the bioactivation of xenobiotics". Chem. Biol. Interact. 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, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutat. Res. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID   11535246.
• Wang J, Falany JL, Falany CN (1998). "Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver". Mol. Pharmacol. 53 (2): 274–82. doi:10.1124/mol.53.2.274. PMID   9463486.
• Tsoi C, Falany CN, Morgenstern R, Swedmark S (2001). "Molecular cloning, expression, and characterization of a canine sulfotransferase that is a human ST1B2 ortholog". Arch. Biochem. Biophys. 390 (1): 87–92. doi:10.1006/abbi.2001.2373. PMID   11368519.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Dombrovski L, Dong A, Bochkarev A, Plotnikov AN (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.
• Allali-Hassani A, Pan PW, Dombrovski L, et al. (2007). "Structural and chemical profiling of the human cytosolic sulfotransferases". PLOS Biol. 5 (5): e97. doi: 10.1371/journal.pbio.0050097 . PMC   1847840 . PMID   17425406.