Version 5.4
Mus musculus Protein: Rad23a
Summary
InnateDB Protein IDBP-533386.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Rad23a
Protein Name RAD23a homolog (S. cerevisiae)
Synonyms 2310040P19Rik; AL024030; HR23A; mHR23A;
Species Mus musculus
Ensembl Protein ENSMUSP00000115664
InnateDB Gene IDBG-174863 (Rad23a)
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 4 experimentally validated interaction(s) in this database.
They are also associated with 111 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 111 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003684 damaged DNA binding
GO:0005515 protein binding
Biological Process
GO:0006289 nucleotide-excision repair
GO:0006974 cellular response to DNA damage stimulus
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045087 innate immune response (InnateDB)
Cellular Component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID MGI:105126
InterPro IPR000449 Ubiquitin-associated domain/translation elongation factor EF-Ts, N-terminal
IPR000626 Ubiquitin-like
IPR004806 UV excision repair protein Rad23
IPR006636 Heat shock chaperonin-binding
IPR009060 UBA-like
IPR015360 XPC-binding domain
IPR015940 Ubiquitin-associated/translation elongation factor EF1B, N-terminal, eukaryote
IPR022617 Rad60/SUMO-like domain
IPR029071 Ubiquitin-related domain
PFAM PF00627
PF00240
PF14560
PF09280
PF11976
PRINTS PR01839
PIRSF
SMART SM00213
SM00727
SM00165
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL Q3TN85
UniProt Splice Variant
Entrez Gene 19358
UniGene
RefSeq
MGI ID
MGI Symbol Rad23a
OMIM
CCDS
HPRD
IMGT
EMBL AC155163 AK165467
GenPept BAE38204

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