Version 5.4
Homo sapiens Protein: NDST4
Summary
InnateDB Protein IDBP-35248.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol NDST4
Protein Name N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 4
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000264363
InnateDB Gene IDBG-35246 (NDST4)
Protein Structure
UniProt Annotation
Function Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity (By similarity). {ECO:0000250}.
Subcellular Localization Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
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:0008146 sulfotransferase activity
GO:0015016 [heparan sulfate]-glucosamine N-sulfotransferase activity
GO:0016787 hydrolase activity
GO:0019213 deacetylase activity
Biological Process
GO:0015012 heparan sulfate proteoglycan biosynthetic process
GO:0030210 heparin biosynthetic process
Cellular Component
GO:0000139 Golgi membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID
InterPro IPR000863 Sulfotransferase domain
IPR021930 Heparan sulphate-N-deacetylase
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF00685
PF12062
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9H3R1
PhosphoSite PhosphoSite-Q9H3R1
TrEMBL
UniProt Splice Variant
Entrez Gene 64579
UniGene Hs.591700
RefSeq NP_072091
HUGO HGNC:20779
OMIM 615039
CCDS CCDS3706
HPRD 10116
IMGT
EMBL AB036429
GenPept BAB18535

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) 

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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