SULT1B1

Protein-coding gene in the species Homo sapiens
SULT1B1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2Z5F, 3CKL

Identifiers
AliasesSULT1B1, ST1B1, ST1B2, SULT1B2, sulfotransferase family 1B member 1
External IDsOMIM: 608436; MGI: 2136282; HomoloGene: 69169; GeneCards: SULT1B1; OMA:SULT1B1 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for SULT1B1
Genomic location for SULT1B1
Band4q13.3Start69,721,167 bp[1]
End69,787,961 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for SULT1B1
Genomic location for SULT1B1
Band5|5 E1Start87,661,198 bp[2]
End87,686,054 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 5: 87.66 – 87.69 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000173597 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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.
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