RD23B_BOVIN
ID RD23B_BOVIN Reviewed; 408 AA.
AC Q29RK4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UV excision repair protein RAD23 homolog B;
GN Name=RAD23B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC proteasomal degradation. Binds to polyubiquitin chains. Proposed to be
CC capable to bind simultaneously to the 26S proteasome and to
CC polyubiquitinated substrates and to deliver ubiquitinated proteins to
CC the proteasome. May play a role in endoplasmic reticulum-associated
CC degradation (ERAD) of misfolded glycoproteins by association with
CC PNGase and delivering deglycosylated proteins to the proteasome (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Involved in global genome nucleotide excision repair (GG-NER)
CC by acting as component of the XPC complex. Cooperatively with CETN2
CC appears to stabilize XPC. May protect XPC from proteasomal degradation
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The XPC complex is proposed to represent the first factor
CC bound at the sites of DNA damage and together with other core
CC recognition factors, XPA, RPA and the TFIIH complex, is part of the
CC pre-incision (or initial recognition) complex. The XPC complex
CC recognizes a wide spectrum of damaged DNA characterized by distortions
CC of the DNA helix such as single-stranded loops, mismatched bubbles or
CC single-stranded overhangs. The orientation of XPC complex binding
CC appears to be crucial for inducing a productive NER. XPC complex is
CC proposed to recognize and to interact with unpaired bases on the
CC undamaged DNA strand which is followed by recruitment of the TFIIH
CC complex and subsequent scanning for lesions in the opposite strand in a
CC 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers
CC (CPDs) which are formed upon UV-induced DNA damage esacpe detection by
CC the XPC complex due to a low degree of structural perurbation. Instead
CC they are detected by the UV-DDB complex which in turn recruits and
CC cooperates with the XPC complex in the respective DNA repair. In vitro,
CC the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially
CC binds to cisplatin and UV-damaged double-stranded DNA and also binds to
CC a variety of chemically and structurally diverse DNA adducts.
CC XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a
CC preference for the 5' side. XPC:RAD23B induces a bend in DNA upon
CC binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and
CC SMUG1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and
CC CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3. Interacts
CC with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the
CC interaction is indirect and mediated by NGLY1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The ubiquitin-like domain mediates interaction with MJD.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC114133; AAI14134.1; -; mRNA.
DR RefSeq; NP_001039775.1; NM_001046310.1.
DR AlphaFoldDB; Q29RK4; -.
DR BMRB; Q29RK4; -.
DR SMR; Q29RK4; -.
DR STRING; 9913.ENSBTAP00000002506; -.
DR PaxDb; Q29RK4; -.
DR PeptideAtlas; Q29RK4; -.
DR PRIDE; Q29RK4; -.
DR Ensembl; ENSBTAT00000002506; ENSBTAP00000002506; ENSBTAG00000001926.
DR GeneID; 530189; -.
DR KEGG; bta:530189; -.
DR CTD; 5887; -.
DR VEuPathDB; HostDB:ENSBTAG00000001926; -.
DR VGNC; VGNC:33683; RAD23B.
DR eggNOG; KOG0011; Eukaryota.
DR GeneTree; ENSGT00390000012078; -.
DR HOGENOM; CLU_040364_0_1_1; -.
DR InParanoid; Q29RK4; -.
DR OMA; MWDEQSA; -.
DR OrthoDB; 1260050at2759; -.
DR TreeFam; TF101216; -.
DR Reactome; R-BTA-5689877; Josephin domain DUBs.
DR Reactome; R-BTA-5696394; DNA Damage Recognition in GG-NER.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000001926; Expressed in semimembranosus muscle and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0071942; C:XPC complex; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd14377; UBA1_Rad23; 1.
DR Gene3D; 1.10.10.540; -; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR041811; RAD23A/B_UBA1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF101238; SSF101238; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR TIGRFAMs; TIGR00601; rad23; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..408
FT /note="UV excision repair protein RAD23 homolog B"
FT /id="PRO_0000244596"
FT DOMAIN 1..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 188..228
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 273..316
FT /note="STI1"
FT DOMAIN 363..403
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 80..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54727"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54727"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMA2"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMA2"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMA2"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMA2"
SQ SEQUENCE 408 AA; 43117 MW; AC48796AEFC0A02C CRC64;
MLVTLKTLQQ QTFKIDIDPD ETVRALKEKI ESEKGKDAFP VAGQKLIYAG KILNDDTALK
EYKIDEKNFV VVMVTKPKAV TTPAPATTQQ SNSAATTTVS SSTAPAVTQA PAPAPASAPT
PTPVSVTPAP TTASSEPAPA SAAKQEKPAE RPVETPVATT PTSTDSTSGD SSRSNLFEDA
TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD
PPPAASTGAP QSSVAAAAAT TTATTTTTSS GGHPLEFLRN QPQFQQMRQI IQQNPSLLPA
LLQQIGRENP QLLQQISQHQ EHFIQMLNEP VQEAGGQGGG GGGGSGGIAE AGGGHMNYIQ
VTPQEKEAIE RLKALGFPEG LVIQAYFACE KNENLAANFL LQQNFDED
