Version 5.4
Mus musculus Protein: Exoc4
Summary
InnateDB Protein IDBP-134241.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Exoc4
Protein Name exocyst complex component 4
Synonyms C78892; Sec8; Sec8l1;
Species Mus musculus
Ensembl Protein ENSMUSP00000051965
InnateDB Gene IDBG-134233 (Exoc4)
Protein Structure
UniProt Annotation
Function Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
They are also associated with 23 interaction(s) predicted by orthology.
Experimentally validated
Total 10 [view]
Protein-Protein 10 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 23 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0030165 PDZ domain binding
GO:0047485 protein N-terminus binding
Biological Process
GO:0006904 vesicle docking involved in exocytosis
GO:0015031 protein transport
Cellular Component
GO:0000145 exocyst
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0032584 growth cone membrane
GO:0035748 myelin sheath abaxonal region
Protein Structure and Domains
PDB ID MGI:1096376
InterPro IPR007191 Sec8 exocyst complex component specific domain
PFAM PF04048
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O35382
PhosphoSite PhosphoSite-O35382
TrEMBL Q8CEG7
UniProt Splice Variant
Entrez Gene 20336
UniGene Mm.490746
RefSeq NP_033174
MGI ID
MGI Symbol Exoc4
OMIM
CCDS CCDS19987
HPRD
IMGT
EMBL AC132453 AC141927 AC152961 AC154020 AC155915 AF022962 AK028250 AK086603 AK173235 BC034644
GenPept AAB86537 AAH34644 BAC25841 BAC39700 BAD32513

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