Version 5.4
Mus musculus Protein: Arpc5l
Summary
InnateDB Protein IDBP-167128.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Arpc5l
Protein Name actin related protein 2/3 complex, subunit 5-like
Synonyms 2010015J01Rik; AI852867; ARC16-2; AW555592; AW742746;
Species Mus musculus
Ensembl Protein ENSMUSP00000088516
InnateDB Gene IDBG-167126 (Arpc5l)
Protein Structure
UniProt Annotation
Function May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. {ECO:0000250}.
Subcellular Localization Cytoplasm, cytoskeleton {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
They are also associated with 12 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 12 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0003779 actin binding
Biological Process
GO:0008150 biological_process
GO:0030833 regulation of actin filament polymerization
Cellular Component
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
Protein Structure and Domains
PDB ID MGI:1921442
InterPro IPR006789 ARP2/3 complex, 16kDa subunit (p16-Arc)
PFAM PF04699
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9D898
PhosphoSite PhosphoSite-Q9D898
TrEMBL
UniProt Splice Variant
Entrez Gene 74192
UniGene Mm.448914
RefSeq NP_083085
MGI ID
MGI Symbol Arpc5l
OMIM
CCDS CCDS38120
HPRD
IMGT
EMBL AK008255 BC024482
GenPept AAH24482 BAB25561

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