Version 5.4
Mus musculus Protein: Gcnt7
Summary
InnateDB Protein IDBP-213311.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Gcnt7
Protein Name glucosaminyl (N-acetyl) transferase family member 7
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000096659
InnateDB Gene IDBG-213309 (Gcnt7)
Protein Structure
UniProt Annotation
Function Glycosyltransferase. {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:0003674 molecular_function
GO:0008375 acetylglucosaminyltransferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0008150 biological_process
Cellular Component
GO:0000139 Golgi membrane
GO:0005575 cellular_component
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:3606143
InterPro IPR003406 Glycosyl transferase, family 14
PFAM PF02485
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3V3K7
PhosphoSite PhosphoSite-
TrEMBL F8WK01
UniProt Splice Variant
Entrez Gene 654821
UniGene Mm.389337
RefSeq NP_001034649
MGI ID
MGI Symbol Gcnt7
OMIM
CCDS CCDS17133
HPRD
IMGT
EMBL AB089317 AK039414 AK132647 AL833787 BC139073 BC139076
GenPept AAI39074 AAI39077 BAE20545 BAE21278 BAK57444 CAM18028

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