Homo sapiens Protein: RAD23B
Summary
InnateDB Protein IDBP-79799.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol RAD23B
Protein Name RAD23 homolog B (S. cerevisiae)
Synonyms HHR23B; HR23B; P58;
Species Homo sapiens
Ensembl Protein ENSP00000350708
InnateDB Gene IDBG-79797 (RAD23B)
Protein Structure
UniProt Annotation
Function Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum- associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
Subcellular Localization Nucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S- phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 248 experimentally validated interaction(s) in this database.
They are also associated with 9 interaction(s) predicted by orthology.
Experimentally validated
Total 248 [view]
Protein-Protein 247 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 9 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003684 damaged DNA binding
GO:0003697 single-stranded DNA binding
GO:0005515 protein binding
GO:0031593 polyubiquitin binding
Biological Process
GO:0000715 nucleotide-excision repair, DNA damage recognition
GO:0000718 nucleotide-excision repair, DNA damage removal
GO:0006281 DNA repair
GO:0006289 nucleotide-excision repair
GO:0006974 cellular response to DNA damage stimulus
GO:0007283 spermatogenesis
GO:0032434 regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0071942 XPC complex
Protein Structure and Domains
PDB ID
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 P54727
PhosphoSite PhosphoSite-P54727
TrEMBL Q5W0S5
UniProt Splice Variant
Entrez Gene 5887
UniGene Hs.521640
RefSeq NP_002865
HUGO HGNC:9813
OMIM 600062
CCDS CCDS6769
HPRD 06772
IMGT
EMBL AK125226 AL137852 AY165178 AY313777 BC020973 CH471105 D21090
GenPept AAH20973 AAN47194 AAP81008 BAA04652 BAG54170 CAD13275 EAW59016 EAW59017