Version 5.4
Mus musculus Protein: Hs3st2
Summary
InnateDB Protein IDBP-208731.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Hs3st2
Protein Name heparan sulfate (glucosamine) 3-O-sulfotransferase 2
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000081678
InnateDB Gene IDBG-208729 (Hs3st2)
Protein Structure
UniProt Annotation
Function Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N- unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). {ECO:0000250}.
Subcellular Localization Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
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:0003674 molecular_function
GO:0008146 sulfotransferase activity
GO:0033871 [heparan sulfate]-glucosamine 3-sulfotransferase 2 activity
Biological Process
GO:0007623 circadian rhythm
GO:0008152 metabolic process
Cellular Component
GO:0000139 Golgi membrane
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1333802
InterPro IPR000863 Sulfotransferase domain
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF00685
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q673U1
PhosphoSite PhosphoSite-Q673U1
TrEMBL
UniProt Splice Variant
Entrez Gene 195646
UniGene Mm.247449
RefSeq NP_001074796
MGI ID
MGI Symbol Hs3st2
OMIM
CCDS CCDS40115
HPRD
IMGT
EMBL AC098715 AC125331 AK032292 AK043969 AY533705
GenPept AAT01565 BAC27796 BAC31718

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