Version 5.4
Mus musculus Protein: Rnf133
Summary
InnateDB Protein IDBP-129903.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rnf133
Protein Name ring finger protein 133
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000066906
InnateDB Gene IDBG-129901 (Rnf133)
Protein Structure
UniProt Annotation
Function Has E3 ubiquitin-protein ligase activity. {ECO:0000269PubMed:18574499}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000305PubMed:18574499}; Single-pass membrane protein {ECO:0000305PubMed:18574499}.
Disease Associations
Tissue Specificity Testis-specific. {ECO:0000269PubMed:18574499}.
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: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:0005789 endoplasmic reticulum membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2677436
InterPro IPR001841 Zinc finger, RING-type
IPR003137 Protease-associated domain, PA
IPR018957 Zinc finger, C3HC4 RING-type
PFAM PF13639
PF14634
PF02225
PF00097
PRINTS
PIRSF
SMART SM00184
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q14B02
PhosphoSite PhosphoSite-Q14B02
TrEMBL
UniProt Splice Variant
Entrez Gene 386611
UniGene Mm.436547
RefSeq NP_937894
MGI ID
MGI Symbol Rnf133
OMIM
CCDS CCDS19938
HPRD
IMGT
EMBL AK028082 AY155441 BC116423 BC116424 CH466533
GenPept AAI16424 AAI16425 AAN75222 BAC25740 EDL13834

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