Version 5.4
Mus musculus Protein: Rnf213
Summary
InnateDB Protein IDBP-214714.5
Last Modified 2012-02-14 [Report errors or provide feedback]
Gene Symbol Rnf213
Protein Name ring finger protein 213
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000091429
InnateDB Gene IDBG-214708 (Rnf213)
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 0 experimentally validated interaction(s) in this database.
They are also associated with 6 interaction(s) predicted by orthology.
Predicted by orthology
Total 6 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0004842 ubiquitin-protein transferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATPase activity
GO:0017111 nucleoside-triphosphatase activity
Biological Process
GO:0006200 ATP catabolic process
GO:0016567 protein ubiquitination
GO:0051865 protein autoubiquitination
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane
Protein Structure and Domains
PDB ID MGI:1289196
InterPro IPR001841 Zinc finger, RING-type
IPR003593 AAA+ ATPase domain
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF13639
PF14634
PRINTS
PIRSF
SMART SM00184
SM00382
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-ENSMUSP00000091429
TrEMBL Q3UD49
UniProt Splice Variant
Entrez Gene 672511
UniGene
RefSeq XP_006534693
MGI ID
MGI Symbol Rnf213
OMIM
CCDS
HPRD
IMGT
EMBL AK150249 AK156571 AL645911
GenPept BAE29413 BAE33759

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