RD23A_HUMAN
ID RD23A_HUMAN Reviewed; 363 AA.
AC P54725; K7ESE3; Q59EU8; Q5M7Z1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=UV excision repair protein RAD23 homolog A;
DE Short=HR23A;
DE Short=hHR23A;
GN Name=RAD23A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8168482; DOI=10.1002/j.1460-2075.1994.tb06452.x;
RA Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T.,
RA Takio K., Tanaka K., van der Spek P.J., Bootsma D., Hoeijmakers J.H.J.,
RA Hanaoka F.;
RT "Purification and cloning of a nucleotide excision repair complex involving
RT the Xeroderma pigmentosum group C protein and a human homologue of yeast
RT RAD23.";
RL EMBO J. 13:1831-1843(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-131 AND MET-200.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-131.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Pancreas, and Testis;
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 [7]
RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
RX PubMed=9371639; DOI=10.1128/jvi.71.12.9732-9742.1997;
RA Withers-Ward E.S., Jowett J.B., Stewart S.A., Xie Y.M., Garfinkel A.,
RA Shibagaki Y., Chow S.A., Shah N., Hanaoka F., Sawitz D.G., Armstrong R.W.,
RA Souza L.M., Chen I.S.;
RT "Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular
RT protein implicated in nucleotide excision DNA repair.";
RL J. Virol. 71:9732-9742(1997).
RN [8]
RP FUNCTION IN DNA REPAIR.
RX PubMed=9372924; DOI=10.1128/mcb.17.12.6924;
RA Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A.,
RA van der Spek P.J., Eker A.P., Rademakers S., Visser C., Aboussekhra A.,
RA Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H.;
RT "Two human homologs of Rad23 are functionally interchangeable in complex
RT formation and stimulation of XPC repair activity.";
RL Mol. Cell. Biol. 17:6924-6931(1997).
RN [9]
RP INTERACTION WITH PSMD4.
RX PubMed=10488153; DOI=10.1074/jbc.274.39.28019;
RA Hiyama H., Yokoi M., Masutani C., Sugasawa K., Maekawa T., Tanaka K.,
RA Hoeijmakers J.H., Hanaoka F.;
RT "Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates
RT interaction with S5a subunit of 26 S proteasome.";
RL J. Biol. Chem. 274:28019-28025(1999).
RN [10]
RP INTERACTION WITH ATXN3.
RX PubMed=10915768; DOI=10.1093/hmg/9.12.1795;
RA Wang G., Sawai N., Kotliarova S., Kanazawa I., Nukina N.;
RT "Ataxin-3, the MJD1 gene product, interacts with the two human homologs of
RT yeast DNA repair protein RAD23, HHR23A and HHR23B.";
RL Hum. Mol. Genet. 9:1795-1803(2000).
RN [11]
RP FUNCTION, AND POLYUBIQUITIN-BINDING.
RX PubMed=14621999; DOI=10.1021/bi035391j;
RA Wang Q., Goh A.M., Howley P.M., Walters K.J.;
RT "Ubiquitin recognition by the DNA repair protein hHR23a.";
RL Biochemistry 42:13529-13535(2003).
RN [12]
RP FUNCTION IN PROTEASOMAL DEGRADATION, AND POLYUBIQUITIN-BINDING.
RX PubMed=12643283; DOI=10.1074/jbc.m212841200;
RA Raasi S., Pickart C.M.;
RT "Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed
RT proteolysis by sequestering lysine 48-linked polyubiquitin chains.";
RL J. Biol. Chem. 278:8951-8959(2003).
RN [13]
RP FUNCTION IN POLYUBIQUITIN-BINDING.
RX PubMed=15321727; DOI=10.1016/j.jmb.2004.06.057;
RA Raasi S., Orlov I., Fleming K.G., Pickart C.M.;
RT "Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of
RT HHR23A.";
RL J. Mol. Biol. 341:1367-1379(2004).
RN [14]
RP INTERACTION WITH PSMD1; PSMC1 AND EEF1A1, AND MUTAGENESIS OF LYS-8 AND
RP THR-79.
RX PubMed=16712842; DOI=10.1016/j.febslet.2006.05.012;
RA Chen L., Madura K.;
RT "Evidence for distinct functions for human DNA repair factors hHR23A and
RT hHR23B.";
RL FEBS Lett. 580:3401-3408(2006).
RN [15]
RP INTERACTION WITH UBQLN2.
RX PubMed=17098253; DOI=10.1016/j.jmb.2006.10.056;
RA Kang Y., Zhang N., Koepp D.M., Walters K.J.;
RT "Ubiquitin receptor proteins hHR23a and hPLIC2 interact.";
RL J. Mol. Biol. 365:1093-1101(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [17]
RP MUTAGENESIS OF LEU-10; LYS-47 AND THR-77.
RX PubMed=18234089; DOI=10.1186/1471-2091-9-4;
RA Goh A.M., Walters K.J., Elsasser S., Verma R., Deshaies R.J., Finley D.,
RA Howley P.M.;
RT "Components of the ubiquitin-proteasome pathway compete for surfaces on
RT Rad23 family proteins.";
RL BMC Biochem. 9:4-4(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-133; SER-205 AND
RP SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=20614012; DOI=10.1371/journal.pone.0011371;
RA Li G., Elder R.T., Dubrovsky L., Liang D., Pushkarsky T., Chiu K., Fan T.,
RA Sire J., Bukrinsky M., Zhao R.Y.;
RT "HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S
RT proteasome.";
RL PLoS ONE 5:E11371-E11371(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-128; SER-133 AND
RP SER-136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP INTERACTION WITH ATXN3.
RX PubMed=30455355; DOI=10.1074/jbc.ra118.005801;
RA Weishaeupl D., Schneider J., Peixoto Pinheiro B., Ruess C., Dold S.M.,
RA von Zweydorf F., Gloeckner C.J., Schmidt J., Riess O., Schmidt T.;
RT "Physiological and pathophysiological characteristics of ataxin-3
RT isoforms.";
RL J. Biol. Chem. 294:644-661(2019).
RN [27]
RP STRUCTURE BY NMR OF 319-363.
RX PubMed=9846873; DOI=10.1038/4220;
RA Dieckmann T., Withers-Ward E.S., Jarosinski M.A., Liu C.F., Chen I.S.Y.,
RA Feigon J.;
RT "Structure of a human DNA repair protein UBA domain that interacts with
RT HIV-1 Vpr.";
RL Nat. Struct. Biol. 5:1042-1047(1998).
RN [28]
RP STRUCTURE BY NMR OF 319-363, INTERACTION WITH HIV-1 VPR (MICROBIAL
RP INFECTION), AND MUTAGENESIS OF PRO-333.
RX PubMed=11087358; DOI=10.1021/bi0017071;
RA Withers-Ward E.S., Mueller T.D., Chen I.S.Y., Feigon J.;
RT "Biochemical and structural analysis of the interaction between the UBA(2)
RT domain of the DNA repair protein HHR23A and HIV-1 Vpr.";
RL Biochemistry 39:14103-14112(2000).
RN [29]
RP STRUCTURE BY NMR OF 156-204.
RX PubMed=12079361; DOI=10.1016/s0022-2836(02)00302-9;
RA Mueller T.D., Feigon J.;
RT "Solution structures of UBA domains reveal a conserved hydrophobic surface
RT for protein-protein interactions.";
RL J. Mol. Biol. 319:1243-1255(2002).
RN [30]
RP STRUCTURE BY NMR OF 1-78, INTERACTION WITH PSMD4, AND MUTAGENESIS OF
RP ILE-49; ILE-54; PHE-71 AND THR-77.
RX PubMed=12970176; DOI=10.1093/emboj/cdg467;
RA Mueller T.D., Feigon J.;
RT "Structural determinants for the binding of ubiquitin-like domains to the
RT proteasome.";
RL EMBO J. 22:4634-4645(2003).
RN [31]
RP STRUCTURE BY NMR OF 2-363, INTERACTION WITH PSMD4, AND MUTAGENESIS OF THR-9
RP AND ILE-49.
RX PubMed=14557549; DOI=10.1073/pnas.1634989100;
RA Walters K.J., Lech P.J., Goh A.M., Wang Q., Howley P.M.;
RT "DNA-repair protein hHR23a alters its protein structure upon binding
RT proteasomal subunit S5a.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12694-12699(2003).
RN [32]
RP STRUCTURE BY NMR OF 223-317.
RX PubMed=15322280; DOI=10.1110/ps.04824304;
RA Kamionka M., Feigon J.;
RT "Structure of the XPC binding domain of hHR23A reveals hydrophobic patches
RT for protein interaction.";
RL Protein Sci. 13:2370-2377(2004).
RN [33]
RP 3D-STRUCTURE MODELING OF 315-363.
RX PubMed=15949443; DOI=10.1016/j.molcel.2005.05.013;
RA Varadan R., Assfalg M., Raasi S., Pickart C., Fushman D.;
RT "Structural determinants for selective recognition of a Lys48-linked
RT polyubiquitin chain by a UBA domain.";
RL Mol. Cell 18:687-698(2005).
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.
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.
CC -!- FUNCTION: (Microbial infection) Involved in Vpr-dependent replication
CC of HIV-1 in non-proliferating cells and primary macrophages. Required
CC for the association of HIV-1 Vpr with the host proteasome.
CC {ECO:0000269|PubMed:20614012}.
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 (PubMed:30455355). Interacts
CC with UBQLN2. {ECO:0000269|PubMed:10488153, ECO:0000269|PubMed:10915768,
CC ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:14557549,
CC ECO:0000269|PubMed:16712842, ECO:0000269|PubMed:17098253,
CC ECO:0000269|PubMed:30455355}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr.
CC {ECO:0000269|PubMed:11087358, ECO:0000269|PubMed:9371639}.
CC -!- INTERACTION:
CC P54725; Q6AI12: ANKRD40; NbExp=3; IntAct=EBI-746453, EBI-2838246;
CC P54725; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-746453, EBI-2875816;
CC P54725; P54253: ATXN1; NbExp=3; IntAct=EBI-746453, EBI-930964;
CC P54725; P54252: ATXN3; NbExp=9; IntAct=EBI-746453, EBI-946046;
CC P54725; Q4VBR4: ATXN3; NbExp=6; IntAct=EBI-746453, EBI-12928880;
CC P54725; Q8N137: CNTROB; NbExp=3; IntAct=EBI-746453, EBI-947360;
CC P54725; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-746453, EBI-9087876;
CC P54725; Q15038: DAZAP2; NbExp=3; IntAct=EBI-746453, EBI-724310;
CC P54725; P68104: EEF1A1; NbExp=2; IntAct=EBI-746453, EBI-352162;
CC P54725; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-746453, EBI-21603100;
CC P54725; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-746453, EBI-10220102;
CC P54725; P42858: HTT; NbExp=3; IntAct=EBI-746453, EBI-466029;
CC P54725; P06756: ITGAV; NbExp=3; IntAct=EBI-746453, EBI-298282;
CC P54725; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-746453, EBI-10176379;
CC P54725; Q9H8M7: MINDY3; NbExp=7; IntAct=EBI-746453, EBI-724928;
CC P54725; Q9UHC7: MKRN1; NbExp=5; IntAct=EBI-746453, EBI-373524;
CC P54725; Q15843: NEDD8; NbExp=2; IntAct=EBI-746453, EBI-716247;
CC P54725; Q96IV0: NGLY1; NbExp=13; IntAct=EBI-746453, EBI-6165879;
CC P54725; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-746453, EBI-18063495;
CC P54725; Q07869: PPARA; NbExp=3; IntAct=EBI-746453, EBI-78615;
CC P54725; Q13200: PSMD2; NbExp=3; IntAct=EBI-746453, EBI-357648;
CC P54725; P55036: PSMD4; NbExp=15; IntAct=EBI-746453, EBI-359318;
CC P54725; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-746453, EBI-14093916;
CC P54725; Q04864-2: REL; NbExp=3; IntAct=EBI-746453, EBI-10829018;
CC P54725; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-746453, EBI-17589229;
CC P54725; Q9H4P4: RNF41; NbExp=3; IntAct=EBI-746453, EBI-2130266;
CC P54725; P62979: RPS27A; NbExp=3; IntAct=EBI-746453, EBI-357375;
CC P54725; Q16586: SGCA; NbExp=3; IntAct=EBI-746453, EBI-5663553;
CC P54725; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-746453, EBI-21504521;
CC P54725; Q13501: SQSTM1; NbExp=3; IntAct=EBI-746453, EBI-307104;
CC P54725; O43463: SUV39H1; NbExp=3; IntAct=EBI-746453, EBI-349968;
CC P54725; P21580: TNFAIP3; NbExp=3; IntAct=EBI-746453, EBI-527670;
CC P54725; Q12933: TRAF2; NbExp=8; IntAct=EBI-746453, EBI-355744;
CC P54725; Q13114: TRAF3; NbExp=3; IntAct=EBI-746453, EBI-357631;
CC P54725; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-746453, EBI-765817;
CC P54725; O00463: TRAF5; NbExp=3; IntAct=EBI-746453, EBI-523498;
CC P54725; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-746453, EBI-359276;
CC P54725; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-746453, EBI-11523450;
CC P54725; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-746453, EBI-9867283;
CC P54725; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-746453, EBI-2130429;
CC P54725; Q9BYV6-2: TRIM55; NbExp=3; IntAct=EBI-746453, EBI-11522718;
CC P54725; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-746453, EBI-2340370;
CC P54725; Q15654: TRIP6; NbExp=3; IntAct=EBI-746453, EBI-742327;
CC P54725; P62987: UBA52; NbExp=3; IntAct=EBI-746453, EBI-357304;
CC P54725; Q9UHD9: UBQLN2; NbExp=6; IntAct=EBI-746453, EBI-947187;
CC P54725; Q04323-2: UBXN1; NbExp=3; IntAct=EBI-746453, EBI-11530712;
CC P54725; Q96RL1-2: UIMC1; NbExp=3; IntAct=EBI-746453, EBI-17761788;
CC P54725; Q9UHP3: USP25; NbExp=12; IntAct=EBI-746453, EBI-2513462;
CC P54725; P25490: YY1; NbExp=3; IntAct=EBI-746453, EBI-765538;
CC P54725; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-746453, EBI-3918996;
CC P54725; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-746453, EBI-5658292;
CC P54725; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-746453, EBI-742740;
CC P54725; Q6FIF0: ZFAND6; NbExp=3; IntAct=EBI-746453, EBI-724630;
CC P54725; Q9JI78: Ngly1; Xeno; NbExp=2; IntAct=EBI-746453, EBI-3648128;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P54725-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54725-2; Sequence=VSP_047565;
CC Name=3;
CC IsoId=P54725-3; Sequence=VSP_054694;
CC -!- DOMAIN: The ubiquitin-like domain mediates interaction with ATXN3.
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.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BX448989; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad23a/";
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DR EMBL; D21235; BAA04767.1; -; mRNA.
DR EMBL; AF549209; AAN39383.1; -; Genomic_DNA.
DR EMBL; BX448989; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB209713; BAD92950.1; ALT_INIT; mRNA.
DR EMBL; AC092069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AD000092; AAB51177.1; -; Genomic_DNA.
DR EMBL; BC014026; AAH14026.1; -; mRNA.
DR EMBL; BC088364; AAH88364.1; -; mRNA.
DR CCDS; CCDS12289.1; -. [P54725-1]
DR CCDS; CCDS59357.1; -. [P54725-2]
DR CCDS; CCDS59358.1; -. [P54725-3]
DR PIR; S44443; S44443.
DR RefSeq; NP_001257291.1; NM_001270362.1. [P54725-3]
DR RefSeq; NP_001257292.1; NM_001270363.1. [P54725-2]
DR RefSeq; NP_005044.1; NM_005053.3. [P54725-1]
DR PDB; 1DV0; NMR; -; A=319-363.
DR PDB; 1F4I; NMR; -; A=319-363.
DR PDB; 1IFY; NMR; -; A=156-204.
DR PDB; 1OQY; NMR; -; A=1-363.
DR PDB; 1P98; NMR; -; A=1-78.
DR PDB; 1P9D; NMR; -; U=1-78.
DR PDB; 1QZE; NMR; -; A=2-363.
DR PDB; 1TP4; NMR; -; A=223-317.
DR PDB; 2WYQ; X-ray; 1.65 A; A=1-82.
DR PDB; 5XBO; NMR; -; B=156-204.
DR PDB; 6W2G; X-ray; 1.10 A; A/B=155-204.
DR PDB; 6W2H; X-ray; 1.60 A; A=155-204.
DR PDB; 6W2I; X-ray; 1.45 A; A=155-204.
DR PDB; 6XQI; X-ray; 2.34 A; F/G=319-358.
DR PDB; 6XQJ; NMR; -; A=223-363.
DR PDBsum; 1DV0; -.
DR PDBsum; 1F4I; -.
DR PDBsum; 1IFY; -.
DR PDBsum; 1OQY; -.
DR PDBsum; 1P98; -.
DR PDBsum; 1P9D; -.
DR PDBsum; 1QZE; -.
DR PDBsum; 1TP4; -.
DR PDBsum; 2WYQ; -.
DR PDBsum; 5XBO; -.
DR PDBsum; 6W2G; -.
DR PDBsum; 6W2H; -.
DR PDBsum; 6W2I; -.
DR PDBsum; 6XQI; -.
DR PDBsum; 6XQJ; -.
DR AlphaFoldDB; P54725; -.
DR BMRB; P54725; -.
DR SMR; P54725; -.
DR BioGRID; 111823; 305.
DR DIP; DIP-34442N; -.
DR IntAct; P54725; 94.
DR MINT; P54725; -.
DR STRING; 9606.ENSP00000467024; -.
DR GlyGen; P54725; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54725; -.
DR MetOSite; P54725; -.
DR PhosphoSitePlus; P54725; -.
DR BioMuta; RAD23A; -.
DR DMDM; 1709983; -.
DR EPD; P54725; -.
DR jPOST; P54725; -.
DR MassIVE; P54725; -.
DR MaxQB; P54725; -.
DR PaxDb; P54725; -.
DR PeptideAtlas; P54725; -.
DR PRIDE; P54725; -.
DR ProteomicsDB; 56700; -. [P54725-1]
DR Antibodypedia; 13484; 484 antibodies from 35 providers.
DR DNASU; 5886; -.
DR Ensembl; ENST00000316856.7; ENSP00000321365.3; ENSG00000179262.10. [P54725-3]
DR Ensembl; ENST00000586534.6; ENSP00000467024.1; ENSG00000179262.10. [P54725-1]
DR Ensembl; ENST00000592268.5; ENSP00000468674.1; ENSG00000179262.10. [P54725-2]
DR GeneID; 5886; -.
DR KEGG; hsa:5886; -.
DR MANE-Select; ENST00000586534.6; ENSP00000467024.1; NM_005053.4; NP_005044.1.
DR UCSC; uc002mvw.3; human. [P54725-1]
DR CTD; 5886; -.
DR DisGeNET; 5886; -.
DR GeneCards; RAD23A; -.
DR HGNC; HGNC:9812; RAD23A.
DR HPA; ENSG00000179262; Group enriched (skeletal muscle, tongue).
DR MIM; 600061; gene.
DR neXtProt; NX_P54725; -.
DR OpenTargets; ENSG00000179262; -.
DR PharmGKB; PA34172; -.
DR VEuPathDB; HostDB:ENSG00000179262; -.
DR eggNOG; KOG0011; Eukaryota.
DR GeneTree; ENSGT00390000012078; -.
DR HOGENOM; CLU_040364_0_1_1; -.
DR InParanoid; P54725; -.
DR OMA; ANTVESY; -.
DR OrthoDB; 1260050at2759; -.
DR PhylomeDB; P54725; -.
DR PathwayCommons; P54725; -.
DR Reactome; R-HSA-5689877; Josephin domain DUBs.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR SignaLink; P54725; -.
DR BioGRID-ORCS; 5886; 21 hits in 1084 CRISPR screens.
DR ChiTaRS; RAD23A; human.
DR EvolutionaryTrace; P54725; -.
DR GeneWiki; RAD23A; -.
DR GenomeRNAi; 5886; -.
DR Pharos; P54725; Tbio.
DR PRO; PR:P54725; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P54725; protein.
DR Bgee; ENSG00000179262; Expressed in hindlimb stylopod muscle and 202 other tissues.
DR ExpressionAtlas; P54725; baseline and differential.
DR Genevisible; P54725; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; IPI:CAFA.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:CAFA.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:CAFA.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0031648; P:protein destabilization; IMP:CAFA.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR CDD; cd14377; UBA1_Rad23; 1.
DR DisProt; DP00156; -.
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 3D-structure; Alternative splicing; DNA damage; DNA repair;
KW Host-virus interaction; 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_0000114904"
FT DOMAIN 1..81
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 81..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..363
FT /note="HIV-1 vpr binding"
FT COMPBIAS 81..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54726"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 226
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_054694"
FT VAR_SEQ 272..326
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_047565"
FT VARIANT 131
FT /note="T -> A (in dbSNP:rs11558955)"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT /id="VAR_016251"
FT VARIANT 179
FT /note="R -> Q (in dbSNP:rs4987203)"
FT /id="VAR_020377"
FT VARIANT 200
FT /note="T -> M (in dbSNP:rs4987202)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016252"
FT MUTAGEN 8
FT /note="K->A: No effect on interaction with EEF1A1."
FT /evidence="ECO:0000269|PubMed:16712842"
FT MUTAGEN 9
FT /note="T->A: Abolishes interaction with PSMD4; when
FT associated with T-49."
FT /evidence="ECO:0000269|PubMed:14557549"
FT MUTAGEN 10
FT /note="L->E: Impairs UBL-UBA domain interaction and
FT enhances ubiquitin-binding; when associated with Glu-47."
FT /evidence="ECO:0000269|PubMed:18234089"
FT MUTAGEN 47
FT /note="K->A: No effect on UBL-UBA domain interaction."
FT /evidence="ECO:0000269|PubMed:18234089"
FT MUTAGEN 47
FT /note="K->E: Impairs UBL-UBA domain interaction and
FT enhances ubiquitin-binding; when associated with Glu-10."
FT /evidence="ECO:0000269|PubMed:18234089"
FT MUTAGEN 47
FT /note="K->E: Impairs UBL-UBA domain interaction and
FT enhances ubiquitin-binding; when associated with Glu-77."
FT /evidence="ECO:0000269|PubMed:18234089"
FT MUTAGEN 49
FT /note="I->A: Impairs interaction with PSMD4."
FT /evidence="ECO:0000269|PubMed:12970176,
FT ECO:0000269|PubMed:14557549"
FT MUTAGEN 49
FT /note="I->T: Abolishes interaction with PSMD4; when
FT associated with A-9."
FT /evidence="ECO:0000269|PubMed:12970176,
FT ECO:0000269|PubMed:14557549"
FT MUTAGEN 54
FT /note="I->A: Impairs interaction with PSMD4."
FT /evidence="ECO:0000269|PubMed:12970176"
FT MUTAGEN 71
FT /note="F->A: Impairs interaction with PSMD4."
FT /evidence="ECO:0000269|PubMed:12970176"
FT MUTAGEN 77
FT /note="T->E: Impairs UBL-UBA domain interaction and
FT enhances ubiquitin-binding; when associated with Glu-47."
FT /evidence="ECO:0000269|PubMed:12970176,
FT ECO:0000269|PubMed:18234089"
FT MUTAGEN 77
FT /note="T->S: No effect on interaction with PSMD4."
FT /evidence="ECO:0000269|PubMed:12970176,
FT ECO:0000269|PubMed:18234089"
FT MUTAGEN 79
FT /note="T->P: Increases interaction with PSMD1 and PSMC1."
FT /evidence="ECO:0000269|PubMed:16712842"
FT MUTAGEN 333
FT /note="P->E: Abolishes interaction with HIV-1 vpr."
FT /evidence="ECO:0000269|PubMed:11087358"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2WYQ"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1OQY"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2WYQ"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1P98"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:2WYQ"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2WYQ"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2WYQ"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2WYQ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1P98"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1OQY"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2WYQ"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2WYQ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1OQY"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1OQY"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1OQY"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1OQY"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:6W2G"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6W2G"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:6W2G"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6W2G"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:6W2G"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:1OQY"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:1OQY"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1OQY"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:1OQY"
FT TURN 260..265
FT /evidence="ECO:0007829|PDB:1OQY"
FT HELIX 267..285
FT /evidence="ECO:0007829|PDB:1OQY"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1OQY"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:1OQY"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:6XQI"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:6XQI"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:6XQI"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:6XQI"
SQ SEQUENCE 363 AA; 39609 MW; C4E47E9313BB47B5 CRC64;
MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY AGKILSDDVP
IRDYRIDEKN FVVVMVTKTK AGQGTSAPPE ASPTAAPESS TSFPPAPTSG MSHPPPAARE
DKSPSEESAP TTSPESVSGS VPSSGSSGRE EDAASTLVTG SEYETMLTEI MSMGYERERV
VAALRASYNN PHRAVEYLLT GIPGSPEPEH GSVQESQVSE QPATEAAGEN PLEFLRDQPQ
FQNMRQVIQQ NPALLPALLQ QLGQENPQLL QQISRHQEQF IQMLNEPPGE LADISDVEGE
VGAIGEEAPQ MNYIQVTPQE KEAIERLKAL GFPESLVIQA YFACEKNENL AANFLLSQNF
DDE
