Version 5.4
Homo sapiens Protein: SULT6B1
Summary
InnateDB Protein IDBP-602072.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol SULT6B1
Protein Name sulfotransferase family, cytosolic, 6B, member 1
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000444081
InnateDB Gene IDBG-45165 (SULT6B1)
Protein Structure
UniProt Annotation
Function Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of thyroxine. Involved in the metabolism of thyroxine (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}.
Disease Associations
Tissue Specificity Specifically expressed in kidney and testis. {ECO:0000269PubMed:19505954}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0008146 sulfotransferase activity
Biological Process
GO:0008152 metabolic process
Cellular Component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR000863 Sulfotransferase domain
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF00685
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q6IMI4
PhosphoSite PhosphoSite-Q6IMI4
TrEMBL
UniProt Splice Variant
Entrez Gene 391365
UniGene Hs.631892
RefSeq XP_005264364
HUGO HGNC:33433
OMIM
CCDS
HPRD
IMGT
EMBL AC007899 BC140797 BK001437
GenPept AAI40798 DAA01772

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca