Version 5.4
Mus musculus Protein: Cirbp
Summary
InnateDB Protein IDBP-539973.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Cirbp
Protein Name cold inducible RNA binding protein
Synonyms Cirp; R74941;
Species Mus musculus
Ensembl Protein ENSMUSP00000121214
InnateDB Gene IDBG-173083 (Cirbp)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 6 experimentally validated interaction(s) in this database.
They are also associated with 41 interaction(s) predicted by orthology.
Experimentally validated
Total 6 [view]
Protein-Protein 6 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 41 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0003730 mRNA 3'-UTR binding
GO:0070181 SSU rRNA binding
Biological Process
GO:0009409 response to cold
GO:0009411 response to UV
GO:0045727 positive regulation of translation
GO:0048255 mRNA stabilization
Cellular Component
Protein Structure and Domains
PDB ID MGI:893588
InterPro IPR000504 RNA recognition motif domain
IPR003954 RNA recognition motif domain, eukaryote
PFAM PF00076
PRINTS
PIRSF
SMART SM00360
SM00361
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL D3YU80
UniProt Splice Variant
Entrez Gene 12696
UniGene Mm.487902
RefSeq
MGI ID
MGI Symbol Cirbp
OMIM
CCDS
HPRD
IMGT
EMBL AC159999
GenPept

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