ID:RD23B_HUMAN DESCRIPTION: RecName: Full=UV excision repair protein RAD23 homolog B; Short=HR23B; Short=hHR23B; AltName: Full=XP-C repair-complementing complex 58 kDa protein; Short=p58; 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. 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. SUBUNIT: Component 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). INTERACTION: P19447:ERCC3; NbExp=2; IntAct=EBI-954531, EBI-1183307; P24610:Pax3 (xeno); NbExp=4; IntAct=EBI-954531, EBI-1208116; P55036:PSMD4; NbExp=5; IntAct=EBI-954531, EBI-359318; Q01831:XPC; NbExp=5; IntAct=EBI-954531, EBI-372610; SUBCELLULAR LOCATION: 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. DOMAIN: The ubiquitin-like domain mediates interaction with ATXN3. SIMILARITY: Belongs to the RAD23 family. SIMILARITY: Contains 1 STI1 domain. SIMILARITY: Contains 2 UBA domains. SIMILARITY: Contains 1 ubiquitin-like domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rad23b/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P54727
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000715 nucleotide-excision repair, DNA damage recognition GO:0006281 DNA repair GO:0006289 nucleotide-excision repair GO:0006294 nucleotide-excision repair, preincision complex assembly GO:0006457 protein folding GO:0006974 cellular response to DNA damage stimulus GO:0007283 spermatogenesis GO:0016579 protein deubiquitination GO:0032434 regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process GO:0048568 embryonic organ development GO:0070911 global genome nucleotide-excision repair
AK293532 - Homo sapiens cDNA FLJ56531 complete cds, highly similar to UV excision repair protein RAD23 homolog B. AK125226 - Homo sapiens cDNA FLJ43236 fis, clone HCHON2004531, highly similar to UV excision repair protein RAD23 homolog B. AK223479 - Homo sapiens mRNA for UV excision repair protein RAD23 homolog B variant, clone: FCC118G10. JD376379 - Sequence 357403 from Patent EP1572962. D21090 - Homo sapiens mRNA for XP-C repair complementing protein (p58/HHR23B), complete cds. JD399260 - Sequence 380284 from Patent EP1572962. JD125409 - Sequence 106433 from Patent EP1572962. DQ890563 - Synthetic construct clone IMAGE:100003193; FLH163976.01X; RZPDo839B05162D RAD23 homolog B (S. cerevisiae) (RAD23B) gene, encodes complete protein. DQ893726 - Synthetic construct Homo sapiens clone IMAGE:100008186; FLH163972.01L; RZPDo839B05161D RAD23 homolog B (S. cerevisiae) (RAD23B) gene, encodes complete protein. AB527553 - Synthetic construct DNA, clone: pF1KB6607, Homo sapiens RAD23B gene for RAD23 homolog B, without stop codon, in Flexi system. CU676798 - Synthetic construct Homo sapiens gateway clone IMAGE:100017205 5' read RAD23B mRNA. KJ897442 - Synthetic construct Homo sapiens clone ccsbBroadEn_06836 RAD23B gene, encodes complete protein. AY313777 - Homo sapiens RAD23-like protein B mRNA, complete cds; alternatively spliced. AK297986 - Homo sapiens cDNA FLJ50817 complete cds, highly similar to UV excision repair protein RAD23 homolog B. AK316189 - Homo sapiens cDNA, FLJ79088 complete cds, highly similar to UV excision repair protein RAD23 homolog B. BC015805 - Homo sapiens RAD23 homolog B (S. cerevisiae), mRNA (cDNA clone IMAGE:3906541). JD225745 - Sequence 206769 from Patent EP1572962. JD507856 - Sequence 488880 from Patent EP1572962. JD506124 - Sequence 487148 from Patent EP1572962. JD229863 - Sequence 210887 from Patent EP1572962. JD324721 - Sequence 305745 from Patent EP1572962. JD564955 - Sequence 545979 from Patent EP1572962. JD313572 - Sequence 294596 from Patent EP1572962. JD327297 - Sequence 308321 from Patent EP1572962. JD302599 - Sequence 283623 from Patent EP1572962. JD314665 - Sequence 295689 from Patent EP1572962. JD562516 - Sequence 543540 from Patent EP1572962. JD305771 - Sequence 286795 from Patent EP1572962. JD433082 - Sequence 414106 from Patent EP1572962. JD269167 - Sequence 250191 from Patent EP1572962. JD551509 - Sequence 532533 from Patent EP1572962. JD057897 - Sequence 38921 from Patent EP1572962. JD169578 - Sequence 150602 from Patent EP1572962.
Biochemical and Signaling Pathways
Reactome (by CSHL, EBI, and GO)
Protein P54727 (Reactome details) participates in the following event(s):
R-HSA-5691004 XPC binds RAD23 and CETN2 R-HSA-5688786 ATXN3 binds RAD23 R-HSA-5691006 XPC:RAD23:CETN2 and UV-DDB bind distorted dsDNA site R-HSA-6790487 RNF111 ubiquitinates SUMOylated XPC R-HSA-8850594 Deglycosylation complex hydrolyses N-glycans from unfolded glycoproteins R-HSA-6782943 UV-DDB ubiquitinates XPC R-HSA-5696664 PARP1 or PARP2 binds DDB2 at GG-NER site R-HSA-6790454 SUMOylation of XPC R-HSA-5690996 ERCC2 and ERCC3 DNA helicases form an open bubble structure in damaged DNA R-HSA-5691000 TFIIH binds GG-NER site to form a verification complex R-HSA-5696655 PARP1 or PARP2 PARylates DDB2 and autoPARylates R-HSA-5696670 CHD1L is recruited to GG-NER site R-HSA-5689861 Recruitment of XPA and release of CAK R-HSA-5696394 DNA Damage Recognition in GG-NER R-HSA-5689877 Josephin domain DUBs R-HSA-5696395 Formation of Incision Complex in GG-NER R-HSA-5696399 Global Genome Nucleotide Excision Repair (GG-NER) R-HSA-5688426 Deubiquitination R-HSA-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle R-HSA-5696398 Nucleotide Excision Repair R-HSA-597592 Post-translational protein modification R-HSA-446203 Asparagine N-linked glycosylation R-HSA-73894 DNA Repair R-HSA-392499 Metabolism of proteins
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
