Version 5.4
Mus musculus Protein: Rnf138
Summary
InnateDB Protein IDBP-130549.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rnf138
Protein Name ring finger protein 138
Synonyms 2410015A17Rik; 2810480D20Rik; STRIN; Trif; Trif-d;
Species Mus musculus
Ensembl Protein ENSMUSP00000072626
InnateDB Gene IDBG-130545 (Rnf138)
Protein Structure
UniProt Annotation
Function E3 ubiquitin-protein ligase. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 4 experimentally validated interaction(s) in this database.
They are also associated with 12 interaction(s) predicted by orthology.
Experimentally validated
Total 4 [view]
Protein-Protein 4 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 12 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0019901 protein kinase binding
GO:0046872 metal ion binding
Biological Process
GO:0008150 biological_process
GO:0016055 Wnt signaling pathway
GO:0016567 protein ubiquitination
Cellular Component
Protein Structure and Domains
PDB ID MGI:1929211
InterPro IPR001841 Zinc finger, RING-type
IPR004181 Zinc finger, MIZ-type
IPR018957 Zinc finger, C3HC4 RING-type
PFAM PF13639
PF14634
PF02891
PF00097
PRINTS
PIRSF
SMART SM00184
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9CQE0
PhosphoSite PhosphoSite-Q9CQE0
TrEMBL
UniProt Splice Variant
Entrez Gene 56515
UniGene Mm.489970
RefSeq NP_062680
MGI ID
MGI Symbol Rnf138
OMIM
CCDS CCDS29089
HPRD
IMGT
EMBL AB025010 AB025011 AK004238 AK010486 AK136138 BC003712
GenPept AAH03712 BAA76376 BAA76377 BAB23232 BAB26977 BAE22840

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