RAD23B report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0032434Biological processregulation of proteasomal ubiquitin-dependent protein catabolic process
GO_0007283Biological processspermatogenesis
GO_0048568Biological processembryonic organ development
GO_0098761Biological processcellular response to interleukin-7
GO_0006289Biological processnucleotide-excision repair
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0000502Cellular componentproteasome complex
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0071942Cellular componentXPC complex
GO_0005634Cellular componentnucleus
GO_0000978Molecular functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
GO_0070628Molecular functionproteasome binding
GO_0003697Molecular functionsingle-stranded DNA binding
GO_0061629Molecular functionRNA polymerase II-specific DNA-binding transcription factor binding
GO_0031593Molecular functionpolyubiquitin modification-dependent protein binding
GO_0140612Molecular functionDNA damage sensor activity
GO_0005515Molecular functionprotein binding
GO_0043130Molecular functionubiquitin binding
GO_0003684Molecular functiondamaged DNA binding

IV. Literature review

[source]
Gene nameRAD23B
Protein nameAlternative protein RAD23B
RAD23 homolog B, nucleotide excision repair protein
UV excision repair protein RAD23 homolog B (HR23B) (hHR23B) (XP-C repair-complementing complex 58 kDa protein) (p58)
Synonyms
DescriptionFUNCTION: 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.; FUNCTION: 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.; FUNCTION: 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.

AccessionsL8EA19
Q5W0S5
H0Y579
P54727
ENST00000416373.6 [P54727-2]
ENST00000442587.1
ENST00000419616.5
ENST00000358015.8 [P54727-1]
Q5W0S4
ENST00000457811.1