Version 5.4
Homo sapiens Protein: RNF138
Summary
InnateDB Protein IDBP-2192.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol RNF138
Protein Name ring finger protein 138
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000257190
InnateDB Gene IDBG-2188 (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. {ECO:0000269PubMed:16714285}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 14 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 14 [view]
Protein-Protein 14 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0019901 protein kinase binding
Biological Process
GO:0016055 Wnt signaling pathway
GO:0016567 protein ubiquitination
Cellular Component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID
InterPro IPR004181 Zinc finger, MIZ-type
PFAM PF02891
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8WVD3
PhosphoSite PhosphoSite-Q8WVD3
TrEMBL
UniProt Splice Variant
Entrez Gene 51444
UniGene Hs.661501
RefSeq NP_937761
HUGO HGNC:17765
OMIM
CCDS CCDS11904
HPRD 11508
IMGT
EMBL AF162680 AK023579 AK315761 AL133557 BC018107 BT006878 CH471088 CR457150
GenPept AAD46623 AAH18107 AAP35524 BAB14614 BAG38114 CAB63712 CAG33431 EAX01280

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