Version 5.4
Mus musculus Protein: Svil
Summary
InnateDB Protein IDBP-539095.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Svil
Protein Name supervillin
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000119287
InnateDB Gene IDBG-127842 (Svil)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
They are also associated with 63 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 3 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 63 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003779 actin binding
GO:0051015 actin filament binding
Biological Process
GO:0007010 cytoskeleton organization
GO:0007519 skeletal muscle tissue development
Cellular Component
GO:0005634 nucleus
GO:0005886 plasma membrane
GO:0015629 actin cytoskeleton
GO:0043034 costamere
Protein Structure and Domains
PDB ID MGI:2147319
InterPro IPR003128 Villin headpiece
IPR007122 Villin/Gelsolin
IPR007123 Gelsolin-like domain
PFAM PF02209
PF00626
PRINTS PR00597
PIRSF
SMART SM00153
SM00262
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-ENSMUSP00000119287
TrEMBL E9Q983
UniProt Splice Variant
Entrez Gene 225115
UniGene Mm.448198
RefSeq XP_006525861
MGI ID
MGI Symbol Svil
OMIM
CCDS
HPRD
IMGT
EMBL AC115928 AC124770
GenPept

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