Version 5.4
Mus musculus Protein: Rnf150
Summary
InnateDB Protein IDBP-171639.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rnf150
Protein Name ring finger protein 150
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000077610
InnateDB Gene IDBG-171637 (Rnf150)
Protein Structure
UniProt Annotation
Function
Subcellular Localization Membrane {ECO:0000305}; Single-pass type I 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 7 interaction(s) predicted by orthology.
Predicted by orthology
Total 7 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:2443860
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 Q5DTZ6
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 330812
UniGene Mm.66737
RefSeq NP_796352
MGI ID
MGI Symbol Rnf150
OMIM
CCDS CCDS40402
HPRD
IMGT
EMBL AC124757 AC132372 AC166939 AK041412 AK220374
GenPept BAD90433

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