Version 5.4
Mus musculus Protein: Rnf217
Summary
InnateDB Protein IDBP-142730.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rnf217
Protein Name ring finger protein 217
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000080650
InnateDB Gene IDBG-142728 (Rnf217)
Protein Structure
UniProt Annotation
Function E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
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 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0008270 zinc ion binding
GO:0016874 ligase activity
Biological Process
GO:0008150 biological_process
GO:0016567 protein ubiquitination
Cellular Component
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:3610311
InterPro IPR002867 Zinc finger, C6HC-type
PFAM PF01485
PRINTS
PIRSF
SMART SM00647
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt D3YYI7
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 268291
UniGene Mm.295212
RefSeq NP_001139821
MGI ID
MGI Symbol Rnf217
OMIM
CCDS CCDS48531
HPRD
IMGT
EMBL AC116557
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