Version 5.4
Mus musculus Protein: Ggcx
Summary
InnateDB Protein IDBP-157284.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ggcx
Protein Name gamma-glutamyl carboxylase
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000070109
InnateDB Gene IDBG-157282 (Ggcx)
Protein Structure
UniProt Annotation
Function Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass 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.
They are also associated with 3 interaction(s) predicted by orthology.
Predicted by orthology
Total 3 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0008488 gamma-glutamyl carboxylase activity
Biological Process
GO:0017187 peptidyl-glutamic acid carboxylation
Cellular Component
GO:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1927655
InterPro IPR007782 Vitamin K-dependent gamma-carboxylase
IPR011020 HTTM
IPR011051 RmlC-like cupin domain
PFAM PF05090
PRINTS
PIRSF
SMART SM00752
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9QYC7
PhosphoSite PhosphoSite-Q9QYC7
TrEMBL Q8BSR0
UniProt Splice Variant
Entrez Gene 56316
UniGene Mm.400367
RefSeq NP_062776
MGI ID
MGI Symbol Ggcx
OMIM
CCDS CCDS20242
HPRD
IMGT
EMBL AF087938 AK030779 AK033496 AK036577 AK135425 BC138763 BC138764 CH466523
GenPept AAF21291 AAI38764 AAI38765 BAC27134 BAC28319 BAC29487 BAE22528 EDK98981

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