Version 5.4
Mus musculus Protein: Rfwd2
Summary
InnateDB Protein IDBP-200869.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rfwd2
Protein Name ring finger and WD repeat domain 2
Synonyms AI316802; C80879; Cop1;
Species Mus musculus
Ensembl Protein ENSMUSP00000076160
InnateDB Gene IDBG-200867 (Rfwd2)
Protein Structure
UniProt Annotation
Function E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1 (By similarity). Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus speckle {ECO:0000269PubMed:10395541}. Cytoplasm {ECO:0000269PubMed:10395541}. Note=In the nucleus, it forms nuclear speckles.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 7 experimentally validated interaction(s) in this database.
They are also associated with 66 interaction(s) predicted by orthology.
Experimentally validated
Total 7 [view]
Protein-Protein 7 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 66 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0016567 protein ubiquitination
Cellular Component
GO:0000139 Golgi membrane
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005813 centrosome
GO:0005925 focal adhesion
GO:0016607 nuclear speck
Protein Structure and Domains
PDB ID MGI:1347046
InterPro IPR001680 WD40 repeat
IPR001841 Zinc finger, RING-type
IPR017986 WD40-repeat-containing domain
IPR018957 Zinc finger, C3HC4 RING-type
PFAM PF00400
PF13639
PF14634
PF00097
PRINTS
PIRSF
SMART SM00320
SM00184
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9R1A8
PhosphoSite PhosphoSite-Q9R1A8
TrEMBL
UniProt Splice Variant
Entrez Gene 26374
UniGene Mm.394355
RefSeq NP_036061
MGI ID
MGI Symbol Rfwd2
OMIM
CCDS CCDS35745
HPRD
IMGT
EMBL AF151110 BC082804
GenPept AAD51094 AAH82804

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