RD23B_RAT
ID RD23B_RAT Reviewed; 415 AA.
AC Q4KMA2; Q0D2G8; Q5CZZ8; Q6IRD5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=UV excision repair protein RAD23 homolog B;
GN Name=Rad23b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Heart, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 7-14; 37-45; 52-60 AND 205-212, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; THR-186; SER-199 AND
RP TYR-202, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:Rad22b 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 AMFR. Interacts with VCP; the interaction is indirect and mediated
CC by NGLY1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
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DR EMBL; BC070960; AAH70960.1; -; mRNA.
DR EMBL; BC090351; AAH90351.1; -; mRNA.
DR EMBL; BC098674; AAH98674.1; -; mRNA.
DR EMBL; BC111406; AAI11407.1; -; mRNA.
DR RefSeq; NP_001020446.1; NM_001025275.1.
DR AlphaFoldDB; Q4KMA2; -.
DR BMRB; Q4KMA2; -.
DR SMR; Q4KMA2; -.
DR BioGRID; 255730; 63.
DR IntAct; Q4KMA2; 53.
DR STRING; 10116.ENSRNOP00000021629; -.
DR iPTMnet; Q4KMA2; -.
DR PhosphoSitePlus; Q4KMA2; -.
DR jPOST; Q4KMA2; -.
DR PaxDb; Q4KMA2; -.
DR PRIDE; Q4KMA2; -.
DR Ensembl; ENSRNOT00000021629; ENSRNOP00000021629; ENSRNOG00000016137.
DR GeneID; 298012; -.
DR KEGG; rno:298012; -.
DR UCSC; RGD:1562958; rat.
DR CTD; 5887; -.
DR RGD; 1562958; Rad23b.
DR eggNOG; KOG0011; Eukaryota.
DR GeneTree; ENSGT00390000012078; -.
DR HOGENOM; CLU_040364_0_1_1; -.
DR InParanoid; Q4KMA2; -.
DR OMA; MWDEQSA; -.
DR OrthoDB; 1260050at2759; -.
DR PhylomeDB; Q4KMA2; -.
DR TreeFam; TF101216; -.
DR Reactome; R-RNO-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-RNO-5689877; Josephin domain DUBs.
DR Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR PRO; PR:Q4KMA2; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016137; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q4KMA2; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:0140612; F:DNA damage sensor activity; ISO:RGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0098761; P:cellular response to interleukin-7; ISO:RGD.
DR GO; GO:0048568; P:embryonic organ development; IEP:RGD.
DR GO; GO:0006289; P:nucleotide-excision repair; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..415
FT /note="UV excision repair protein RAD23 homolog B"
FT /id="PRO_0000287582"
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 274..317
FT /note="STI1"
FT DOMAIN 370..410
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 80..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
SQ SEQUENCE 415 AA; 43497 MW; 221022C803418390 CRC64;
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILSDDTALK
EYKIDEKNFV VVMVTKPKAV TSAVPATTQQ SSSPSTTTVS SSPAAAVAQA PAPTPALAPT
STPASTTPAS TTASSEPAPT GATQPEKPAE KPAQTPVLTS PAPADSTPGD SSRSNLFEDA
TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD
PPPQAVSTGT PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGGGGGG GGGGIAEAGS
GHMNYIQVTP QEKEAIERLK ALGFPEGLVI QAYFACEKNE NLAANFLLQQ NFDED
