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Identification
HMDB Protein ID HMDBP12795
Secondary Accession Numbers None
Name UV excision repair protein RAD23 homolog B
Synonyms
  1. HR23B
  2. hHR23B
  3. XP-C repair-complementing complex 58 kDa protein
  4. p58
Gene Name RAD23B
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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.
Pathways
  • Nucleotide excision repair
  • Protein processing in endoplasmic reticulum
Reactions Not Available
GO Classification
Biological Process
spermatogenesis
protein deubiquitination
nucleotide-excision repair
protein folding
embryonic organ development
cellular response to interleukin-7
global genome nucleotide-excision repair
nucleotide-excision repair, DNA damage recognition
nucleotide-excision repair, preincision complex assembly
regulation of proteasomal ubiquitin-dependent protein catabolic process
nucleotide-excision repair, DNA duplex unwinding
proteasomal ubiquitin-dependent protein catabolic process
Cellular Component
cytosol
nucleus
XPC complex
nucleoplasm
proteasome complex
Molecular Function
ubiquitin binding
proteasome binding
single-stranded DNA binding
damaged DNA binding
polyubiquitin binding
RNA polymerase II core promoter proximal region sequence-specific DNA binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 409
Molecular Weight 43170.86
Theoretical pI 4.836
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P54727
UniProtKB/Swiss-Prot Entry Name RD23B_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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