ID   RD23A_MOUSE             Reviewed;         363 AA.
AC   P54726; B7ZNQ1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=UV excision repair protein RAD23 homolog A;
DE            Short=HR23A;
DE            Short=mHR23A;
GN   Name=Rad23a; Synonyms=Mhr23a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=8808275; DOI=10.1006/geno.1996.0004;
RA   van der Spek P.J., Visser C.E., Hanaoka F., Smit B., Hagemeijer A.,
RA   Bootsma D., Hoeijmakers J.H.J.;
RT   "Cloning, comparative mapping, and RNA expression of the mouse homologues
RT   of the Saccharomyces cerevisiae nucleotide excision repair gene RAD23.";
RL   Genomics 31:20-27(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12815074; DOI=10.1101/gad.260003;
RA   Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K.,
RA   Vrieling H., Hoeijmakers J.H.;
RT   "A novel regulation mechanism of DNA repair by damage-induced and RAD23-
RT   dependent stabilization of xeroderma pigmentosum group C protein.";
RL   Genes Dev. 17:1630-1645(2003).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15336624; DOI=10.1016/j.dnarep.2004.06.010;
RA   Okuda Y., Nishi R., Ng J.M., Vermeulen W., van der Horst G.T., Mori T.,
RA   Hoeijmakers J.H., Hanaoka F., Sugasawa K.;
RT   "Relative levels of the two mammalian Rad23 homologs determine composition
RT   and stability of the xeroderma pigmentosum group C protein complex.";
RL   DNA Repair 3:1285-1295(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-133; SER-136 AND
RP   SER-138, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC       proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains
CC       in a length-dependent manner and with a lower affinity to 'Lys-63'-
CC       linked polyubiquitin chains. Proposed to be capable to bind
CC       simultaneously to the 26S proteasome and to polyubiquitinated
CC       substrates and to deliver ubiquitinated proteins to the proteasome (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Involved in nucleotide excision repair and is thought to be
CC       functional equivalent for Rad23b in global genome nucleotide excision
CC       repair (GG-NER) by association with Xpc. In vitro, the XPC:RAD23A dimer
CC       has NER activity. Can stabilize Xpc. Reported differences to Rad23b in
CC       regard to NER activity and Xpc stabilization are probably due to
CC       differences in expression levels with Rad23a being much less expressed
CC       than Rad23b. {ECO:0000269|PubMed:12815074,
CC       ECO:0000269|PubMed:15336624}.
CC   -!- SUBUNIT: Interacts with XPC; the interaction is suggesting the
CC       existence of a functional equivalent variant XPC complex. Interacts
CC       with PSMD4 and PSMC5. Interacts with ATXN3. Interacts with UBQLN2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The ubiquitin-like (UBL) and the UBA (ubiquitin-associated)
CC       domains interact intramolecularly in a highly dynamic manner, as each
CC       UBA domain competes for an overlapping UBL domain surface. Binding of
CC       ubiquitin or proteasome subunit Psmd4 disrupt the UBL-UBA domain
CC       interactions and drive Rad23a in to an open conformation (By
CC       similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Rad23a and Rad23b double
CC       knockout is embryonic lethal. Cells show reduced cell survival upopn UV
CC       radiation and reduced steady-state level of Xpc indicating a reduced
CC       NER capacity. {ECO:0000269|PubMed:12815074,
CC       ECO:0000269|PubMed:15336624}.
CC   -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
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DR   EMBL; X92410; CAA63145.1; -; mRNA.
DR   EMBL; BC145372; AAI45373.1; -; mRNA.
DR   EMBL; CH466525; EDL10960.1; -; Genomic_DNA.
DR   CCDS; CCDS80908.1; -.
DR   RefSeq; NP_001284535.1; NM_001297606.1.
DR   AlphaFoldDB; P54726; -.
DR   BMRB; P54726; -.
DR   SMR; P54726; -.
DR   BioGRID; 202561; 19.
DR   IntAct; P54726; 1.
DR   STRING; 10090.ENSMUSP00000105383; -.
DR   iPTMnet; P54726; -.
DR   PhosphoSitePlus; P54726; -.
DR   CPTAC; non-CPTAC-3664; -.
DR   EPD; P54726; -.
DR   jPOST; P54726; -.
DR   MaxQB; P54726; -.
DR   PaxDb; 10090-ENSMUSP00000003911; -.
DR   PeptideAtlas; P54726; -.
DR   ProteomicsDB; 255137; -.
DR   Pumba; P54726; -.
DR   Antibodypedia; 13484; 539 antibodies from 35 providers.
DR   DNASU; 19358; -.
DR   Ensembl; ENSMUST00000109761.9; ENSMUSP00000105383.3; ENSMUSG00000003813.16.
DR   GeneID; 19358; -.
DR   KEGG; mmu:19358; -.
DR   UCSC; uc009mnm.2; mouse.
DR   AGR; MGI:105126; -.
DR   CTD; 5886; -.
DR   MGI; MGI:105126; Rad23a.
DR   VEuPathDB; HostDB:ENSMUSG00000003813; -.
DR   eggNOG; KOG0011; Eukaryota.
DR   GeneTree; ENSGT00390000012078; -.
DR   InParanoid; P54726; -.
DR   OMA; VACCVRI; -.
DR   OrthoDB; 158575at2759; -.
DR   PhylomeDB; P54726; -.
DR   Reactome; R-MMU-5689877; Josephin domain DUBs.
DR   Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR   BioGRID-ORCS; 19358; 8 hits in 115 CRISPR screens.
DR   ChiTaRS; Rad23a; mouse.
DR   PRO; PR:P54726; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P54726; Protein.
DR   Bgee; ENSMUSG00000003813; Expressed in hindlimb stylopod muscle and 262 other cell types or tissues.
DR   ExpressionAtlas; P54726; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR   GO; GO:0006974; P:DNA damage response; IGI:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   CDD; cd14377; UBA1_Rad23; 1.
DR   CDD; cd14427; UBA2_HR23A; 1.
DR   CDD; cd17126; Ubl_HR23A; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR   Gene3D; 1.10.10.540; XPC-binding domain; 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   NCBIfam; TIGR00601; rad23; 1.
DR   PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1.
DR   PANTHER; PTHR10621:SF29; UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A; 1.
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; SSF46934; UBA-like; 2.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF101238; XPC-binding domain; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   Genevisible; P54726; MM.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..363
FT                   /note="UV excision repair protein RAD23 homolog A"
FT                   /id="PRO_0000114905"
FT   DOMAIN          1..79
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          161..201
FT                   /note="UBA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          318..358
FT                   /note="UBA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          83..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..111
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54725"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54725"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54725"
FT   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   CROSSLNK        122
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P54725"
FT   CONFLICT        62..63
FT                   /note="KE -> RD (in Ref. 1; CAA63145)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="P -> S (in Ref. 1; CAA63145)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218..219
FT                   /note="AP -> RA (in Ref. 1; CAA63145)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  39706 MW;  BA129D69318BDDE7 CRC64;
     MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY AGKILSDDVP
     IKEYHIDEKN FVVVMVTKAK AGQGIPAPPE ASPTAVPEPS TPFPPVLASG MSHPPPTSRE
     DKSPSEESTT TTSPESISGS VPSSGSSGRE EDAASTLVTG SEYETMLTEI MSMGYERERV
     VAALRASYNN PHRAVEYLLT GIPGSPEPEH GSVQESQAPE QPATEAAGEN PLEFLRDQPQ
     FQNMRQVIQQ NPALLPALLQ QLGQENPQLL QQISRHQEQF IQMLNEPPGE LADISDVEGE
     VGAIGEEAPQ MNYIQVTPQE KEAIERLKAL GFPESLVIQA YFACEKNENL AANFLLSQNF
     DDE
//