Version 5.4
Mus musculus Protein: Rnf115
Summary
InnateDB Protein IDBP-176390.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rnf115
Protein Name ring finger protein 115
Synonyms 2610028E05Rik; AU042696; Zfp364;
Species Mus musculus
Ensembl Protein ENSMUSP00000029740
InnateDB Gene IDBG-176388 (Rnf115)
Protein Structure
UniProt Annotation
Function Acts as an E2-dependent E3 ubiquitin-protein ligase. May be involved in endocytic trafficking. {ECO:0000269PubMed:17462600}.
Subcellular Localization Cytoplasm, cytosol {ECO:0000269PubMed:12972561}. Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes.
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 9 [view]
Protein-DNA 0
Protein-RNA 1 [view]
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 23 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004842 ubiquitin-protein transferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0051865 protein autoubiquitination
Cellular Component
GO:0005829 cytosol
Protein Structure and Domains
PDB ID MGI:1915095
InterPro IPR001841 Zinc finger, RING-type
IPR018957 Zinc finger, C3HC4 RING-type
PFAM PF13639
PF14634
PF00097
PRINTS
PIRSF
SMART SM00184
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9D0C1
PhosphoSite PhosphoSite-Q9D0C1
TrEMBL
UniProt Splice Variant
Entrez Gene 67845
UniGene Mm.431735
RefSeq NP_080682
MGI ID
MGI Symbol Rnf115
OMIM
CCDS CCDS17647
HPRD
IMGT
EMBL AK008329 AK011584 BC023113
GenPept AAH23113 BAB25607 BAB27716

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