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MGP002566

UniProt Annotations

Entry Information
Gene NameRAD23 homolog B (S. cerevisiae)
Protein EntryRD23B_HUMAN
UniProt IDP54727
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P54727-1; Sequence=Displayed; Name=2; IsoId=P54727-2; Sequence=VSP_045606; Note=Highly expressed in the testis and in ejaculated spermatozoa.;
DomainThe ubiquitin-like domain mediates interaction with ATXN3.
FunctionInvolved 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.
FunctionMultiubiquitin 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.
FunctionThe 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.
InteractionQ16186:ADRM1; NbExp=2; IntAct=EBI-954531, EBI-954387; P54252:ATXN3; NbExp=2; IntAct=EBI-954531, EBI-946046; P19447:ERCC3; NbExp=2; IntAct=EBI-954531, EBI-1183307; P24610:Pax3 (xeno); NbExp=4; IntAct=EBI-954531, EBI-1208116; P55036:PSMD4; NbExp=12; IntAct=EBI-954531, EBI-359318; P55034:RPN10 (xeno); NbExp=3; IntAct=EBI-954531, EBI-2620423; Q8TBC4:UBA3; NbExp=2; IntAct=EBI-954531, EBI-717567; P0CG48:UBC; NbExp=4; IntAct=EBI-954531, EBI-3390054; P45974:USP5; NbExp=2; IntAct=EBI-954531, EBI-741277; P08670:VIM; NbExp=2; IntAct=EBI-954531, EBI-353844; Q01831:XPC; NbExp=5; IntAct=EBI-954531, EBI-372610;
SimilarityBelongs to the RAD23 family. {ECO:0000305}.
SimilarityContains 1 STI1 domain. {ECO:0000305}.
SimilarityContains 1 ubiquitin-like domain. {ECO:0000255|PROSITE-ProRule:PRU00214}.
SimilarityContains 2 UBA domains. {ECO:0000255|PROSITE- ProRule:PRU00212}.
Subcellular LocationNucleus. 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.
SubunitComponent of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3. Interacts with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1 (By similarity). {ECO:0000250}.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rad23b/";
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