Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

UV excision repair protein RAD23 homolog A (HR23A) (hHR23A)

 RD23A_HUMAN             Reviewed;         363 AA.
P54725; K7ESE3; Q59EU8; Q5M7Z1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=UV excision repair protein RAD23 homolog A;
Short=HR23A;
Short=hHR23A;
Name=RAD23A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8168482;
Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M.,
Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D.,
Hoeijmakers J.H.J., Hanaoka F.;
"Purification and cloning of a nucleotide excision repair complex
involving the Xeroderma pigmentosum group C protein and a human
homologue of yeast RAD23.";
EMBO J. 13:1831-1843(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-131 AND MET-200.
NIEHS SNPs program;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal liver;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ALA-131.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Pancreas, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH HIV-1 VPR.
PubMed=9371639;
Withers-Ward E.S., Jowett J.B., Stewart S.A., Xie Y.M., Garfinkel A.,
Shibagaki Y., Chow S.A., Shah N., Hanaoka F., Sawitz D.G.,
Armstrong R.W., Souza L.M., Chen I.S.;
"Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a
cellular protein implicated in nucleotide excision DNA repair.";
J. Virol. 71:9732-9742(1997).
[8]
FUNCTION IN DNA REPAIR.
PubMed=9372924; DOI=10.1128/MCB.17.12.6924;
Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A.,
van der Spek P.J., Eker A.P., Rademakers S., Visser C.,
Aboussekhra A., Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H.;
"Two human homologs of Rad23 are functionally interchangeable in
complex formation and stimulation of XPC repair activity.";
Mol. Cell. Biol. 17:6924-6931(1997).
[9]
INTERACTION WITH PSMD4.
PubMed=10488153; DOI=10.1074/jbc.274.39.28019;
Hiyama H., Yokoi M., Masutani C., Sugasawa K., Maekawa T., Tanaka K.,
Hoeijmakers J.H., Hanaoka F.;
"Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23
mediates interaction with S5a subunit of 26 S proteasome.";
J. Biol. Chem. 274:28019-28025(1999).
[10]
INTERACTION WITH ATXN3.
PubMed=10915768; DOI=10.1093/hmg/9.12.1795;
Wang G., Sawai N., Kotliarova S., Kanazawa I., Nukina N.;
"Ataxin-3, the MJD1 gene product, interacts with the two human
homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B.";
Hum. Mol. Genet. 9:1795-1803(2000).
[11]
FUNCTION, AND POLYUBIQUITIN-BINDING.
PubMed=14621999; DOI=10.1021/bi035391j;
Wang Q., Goh A.M., Howley P.M., Walters K.J.;
"Ubiquitin recognition by the DNA repair protein hHR23a.";
Biochemistry 42:13529-13535(2003).
[12]
FUNCTION IN PROTEASOMAL DEGRADATION, AND POLYUBIQUITIN-BINDING.
PubMed=12643283; DOI=10.1074/jbc.M212841200;
Raasi S., Pickart C.M.;
"Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-
catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin
chains.";
J. Biol. Chem. 278:8951-8959(2003).
[13]
FUNCTION IN POLYUBIQUITIN-BINDING.
PubMed=15321727; DOI=10.1016/j.jmb.2004.06.057;
Raasi S., Orlov I., Fleming K.G., Pickart C.M.;
"Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains
of HHR23A.";
J. Mol. Biol. 341:1367-1379(2004).
[14]
INTERACTION WITH PSMD1; PSMC1 AND EEF1A1, AND MUTAGENESIS OF LYS-8 AND
THR-79.
PubMed=16712842; DOI=10.1016/j.febslet.2006.05.012;
Chen L., Madura K.;
"Evidence for distinct functions for human DNA repair factors hHR23A
and hHR23B.";
FEBS Lett. 580:3401-3408(2006).
[15]
INTERACTION WITH UBQLN2.
PubMed=17098253; DOI=10.1016/j.jmb.2006.10.056;
Kang Y., Zhang N., Koepp D.M., Walters K.J.;
"Ubiquitin receptor proteins hHR23a and hPLIC2 interact.";
J. Mol. Biol. 365:1093-1101(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
MUTAGENESIS OF LEU-10; LYS-47 AND THR-77.
PubMed=18234089; DOI=10.1186/1471-2091-9-4;
Goh A.M., Walters K.J., Elsasser S., Verma R., Deshaies R.J.,
Finley D., Howley P.M.;
"Components of the ubiquitin-proteasome pathway compete for surfaces
on Rad23 family proteins.";
BMC Biochem. 9:4-4(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-133; SER-205
AND SER-295, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
FUNCTION IN VIRAL REPLICATION.
PubMed=20614012; DOI=10.1371/journal.pone.0011371;
Li G., Elder R.T., Dubrovsky L., Liang D., Pushkarsky T., Chiu K.,
Fan T., Sire J., Bukrinsky M., Zhao R.Y.;
"HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S
proteasome.";
PLoS ONE 5:E11371-E11371(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-128; SER-133
AND SER-136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-295, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
STRUCTURE BY NMR OF 319-363.
PubMed=9846873; DOI=10.1038/4220;
Dieckmann T., Withers-Ward E.S., Jarosinski M.A., Liu C.F.,
Chen I.S.Y., Feigon J.;
"Structure of a human DNA repair protein UBA domain that interacts
with HIV-1 Vpr.";
Nat. Struct. Biol. 5:1042-1047(1998).
[27]
STRUCTURE BY NMR OF 319-363, INTERACTION WITH HIV-1 VPR, AND
MUTAGENESIS OF PRO-333.
PubMed=11087358; DOI=10.1021/bi0017071;
Withers-Ward E.S., Mueller T.D., Chen I.S.Y., Feigon J.;
"Biochemical and structural analysis of the interaction between the
UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr.";
Biochemistry 39:14103-14112(2000).
[28]
STRUCTURE BY NMR OF 156-204.
PubMed=12079361; DOI=10.1016/S0022-2836(02)00302-9;
Mueller T.D., Feigon J.;
"Solution structures of UBA domains reveal a conserved hydrophobic
surface for protein-protein interactions.";
J. Mol. Biol. 319:1243-1255(2002).
[29]
STRUCTURE BY NMR OF 1-78, INTERACTION WITH PSMD4, AND MUTAGENESIS OF
ILE-49; ILE-54; PHE-71 AND THR-77.
PubMed=12970176; DOI=10.1093/emboj/cdg467;
Mueller T.D., Feigon J.;
"Structural determinants for the binding of ubiquitin-like domains to
the proteasome.";
EMBO J. 22:4634-4645(2003).
[30]
STRUCTURE BY NMR OF 2-363, INTERACTION WITH PSMD4, AND MUTAGENESIS OF
THR-9 AND ILE-49.
PubMed=14557549; DOI=10.1073/pnas.1634989100;
Walters K.J., Lech P.J., Goh A.M., Wang Q., Howley P.M.;
"DNA-repair protein hHR23a alters its protein structure upon binding
proteasomal subunit S5a.";
Proc. Natl. Acad. Sci. U.S.A. 100:12694-12699(2003).
[31]
STRUCTURE BY NMR OF 223-317.
PubMed=15322280; DOI=10.1110/ps.04824304;
Kamionka M., Feigon J.;
"Structure of the XPC binding domain of hHR23A reveals hydrophobic
patches for protein interaction.";
Protein Sci. 13:2370-2377(2004).
[32]
3D-STRUCTURE MODELING OF 315-363.
PubMed=15949443; DOI=10.1016/j.molcel.2005.05.013;
Varadan R., Assfalg M., Raasi S., Pickart C., Fushman D.;
"Structural determinants for selective recognition of a Lys48-linked
polyubiquitin chain by a UBA domain.";
Mol. Cell 18:687-698(2005).
-!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin
chains in a length-dependent manner and with a lower affinity to
'Lys-63'-linked 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.
-!- FUNCTION: Involved in nucleotide excision repair and is thought to
be functional equivalent for RAD23B in global genome nucleotide
excision repair (GG-NER) by association with XPC. In vitro, the
XPC:RAD23A dimer has NER activity. Can stabilize XPC.
-!- FUNCTION: Involved in vpr-dependent replication of HIV-1 in non-
proliferating cells and primary macrophages. Required for the
association of HIV-1 vpr with the host proteasome.
-!- SUBUNIT: Interacts with XPC; the interaction is suggesting the
existence of a functional equivalent variant XPC complex.
Interacts with PSMD4 and PSMC5. Interacts with ATXN3. Interacts
with HIV-1 vpr. Interacts with UBQLN2.
{ECO:0000269|PubMed:10488153, ECO:0000269|PubMed:10915768,
ECO:0000269|PubMed:11087358, ECO:0000269|PubMed:12970176,
ECO:0000269|PubMed:14557549, ECO:0000269|PubMed:16712842,
ECO:0000269|PubMed:17098253, ECO:0000269|PubMed:9371639}.
-!- INTERACTION:
Q6AI12:ANKRD40; NbExp=3; IntAct=EBI-746453, EBI-2838246;
P68104:EEF1A1; NbExp=2; IntAct=EBI-746453, EBI-352162;
Q9H8M7:MINDY3; NbExp=5; IntAct=EBI-746453, EBI-724928;
Q96IV0:NGLY1; NbExp=7; IntAct=EBI-746453, EBI-6165879;
Q9JI78:Ngly1 (xeno); NbExp=2; IntAct=EBI-746453, EBI-3648128;
P55036:PSMD4; NbExp=5; IntAct=EBI-746453, EBI-359318;
Q13501:SQSTM1; NbExp=2; IntAct=EBI-746453, EBI-307104;
Q12933:TRAF2; NbExp=6; IntAct=EBI-746453, EBI-355744;
O00463:TRAF5; NbExp=3; IntAct=EBI-746453, EBI-523498;
Q86XT4:TRIM50; NbExp=4; IntAct=EBI-746453, EBI-9867283;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-746453, EBI-2130429;
Q15654:TRIP6; NbExp=3; IntAct=EBI-746453, EBI-742327;
Q9UHD9:UBQLN2; NbExp=5; IntAct=EBI-746453, EBI-947187;
Q9UHP3:USP25; NbExp=7; IntAct=EBI-746453, EBI-2513462;
Q9HCK0:ZBTB26; NbExp=4; IntAct=EBI-746453, EBI-3918996;
Q8NCP5:ZBTB44; NbExp=3; IntAct=EBI-746453, EBI-5658292;
Q96BR9:ZBTB8A; NbExp=5; IntAct=EBI-746453, EBI-742740;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P54725-1; Sequence=Displayed;
Name=2;
IsoId=P54725-2; Sequence=VSP_047565;
Note=No experimental confirmation available.;
Name=3;
IsoId=P54725-3; Sequence=VSP_054694;
Note=No experimental confirmation available.;
-!- DOMAIN: The ubiquitin-like domain mediates interaction with ATXN3.
-!- DOMAIN: The ubiquitin-like (UBL) and the UBA (ubiquitin-
associated) domains interact intramolecularly in a highly dynamic
manner, as each UBA domain competes for an overlapping UBL domain
surface. Binding of ubiquitin or proteasome subunit PSMD4 disrupt
the UBL-UBA domain interactions and drive RAD23A in to an open
conformation.
-!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92950.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BX448989; Type=Frameshift; Positions=159, 333, 339, 347; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rad23a/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D21235; BAA04767.1; -; mRNA.
EMBL; AF549209; AAN39383.1; -; Genomic_DNA.
EMBL; BX448989; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB209713; BAD92950.1; ALT_INIT; mRNA.
EMBL; AC092069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AD000092; AAB51177.1; -; Genomic_DNA.
EMBL; BC014026; AAH14026.1; -; mRNA.
EMBL; BC088364; AAH88364.1; -; mRNA.
CCDS; CCDS12289.1; -. [P54725-1]
CCDS; CCDS59357.1; -. [P54725-2]
CCDS; CCDS59358.1; -. [P54725-3]
PIR; S44443; S44443.
RefSeq; NP_001257291.1; NM_001270362.1. [P54725-3]
RefSeq; NP_001257292.1; NM_001270363.1. [P54725-2]
RefSeq; NP_005044.1; NM_005053.3. [P54725-1]
UniGene; Hs.643267; -.
PDB; 1DV0; NMR; -; A=319-363.
PDB; 1F4I; NMR; -; A=319-363.
PDB; 1IFY; NMR; -; A=156-204.
PDB; 1OQY; NMR; -; A=1-363.
PDB; 1P98; NMR; -; A=1-78.
PDB; 1P9D; NMR; -; U=1-78.
PDB; 1QZE; NMR; -; A=2-363.
PDB; 1TP4; NMR; -; A=223-317.
PDB; 1ZO6; Model; -; A=315-363.
PDB; 2WYQ; X-ray; 1.65 A; A=1-82.
PDB; 5XBO; NMR; -; B=156-204.
PDBsum; 1DV0; -.
PDBsum; 1F4I; -.
PDBsum; 1IFY; -.
PDBsum; 1OQY; -.
PDBsum; 1P98; -.
PDBsum; 1P9D; -.
PDBsum; 1QZE; -.
PDBsum; 1TP4; -.
PDBsum; 1ZO6; -.
PDBsum; 2WYQ; -.
PDBsum; 5XBO; -.
DisProt; DP00156; -.
ProteinModelPortal; P54725; -.
SMR; P54725; -.
BioGrid; 111823; 245.
DIP; DIP-34442N; -.
IntAct; P54725; 66.
MINT; MINT-105454; -.
STRING; 9606.ENSP00000467024; -.
iPTMnet; P54725; -.
PhosphoSitePlus; P54725; -.
BioMuta; RAD23A; -.
DMDM; 1709983; -.
EPD; P54725; -.
MaxQB; P54725; -.
PaxDb; P54725; -.
PeptideAtlas; P54725; -.
PRIDE; P54725; -.
DNASU; 5886; -.
Ensembl; ENST00000316856; ENSP00000321365; ENSG00000179262. [P54725-3]
Ensembl; ENST00000586534; ENSP00000467024; ENSG00000179262. [P54725-1]
Ensembl; ENST00000592268; ENSP00000468674; ENSG00000179262. [P54725-2]
GeneID; 5886; -.
KEGG; hsa:5886; -.
UCSC; uc002mvw.3; human. [P54725-1]
CTD; 5886; -.
DisGeNET; 5886; -.
EuPathDB; HostDB:ENSG00000179262.9; -.
GeneCards; RAD23A; -.
HGNC; HGNC:9812; RAD23A.
HPA; HPA053901; -.
HPA; HPA057003; -.
HPA; HPA065599; -.
MIM; 600061; gene.
neXtProt; NX_P54725; -.
OpenTargets; ENSG00000179262; -.
PharmGKB; PA34172; -.
eggNOG; KOG0011; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00390000012078; -.
HOGENOM; HOG000172162; -.
HOVERGEN; HBG055042; -.
InParanoid; P54725; -.
KO; K10839; -.
OMA; KGRDAFP; -.
OrthoDB; EOG091G0DVL; -.
PhylomeDB; P54725; -.
Reactome; R-HSA-5689877; Josephin domain DUBs.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
ChiTaRS; RAD23A; human.
EvolutionaryTrace; P54725; -.
GeneWiki; RAD23A; -.
GenomeRNAi; 5886; -.
PMAP-CutDB; P54725; -.
PRO; PR:P54725; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000179262; -.
CleanEx; HS_RAD23A; -.
ExpressionAtlas; P54725; baseline and differential.
Genevisible; P54725; HS.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0019900; F:kinase binding; IPI:CAFA.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:CAFA.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:CAFA.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
GO; GO:0031648; P:protein destabilization; IMP:CAFA.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR004806; Rad23.
InterPro; IPR006636; STI1_HS-bd.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR000626; Ubiquitin_dom.
InterPro; IPR015360; XPC-bd.
InterPro; IPR036353; XPC-bd_sf.
Pfam; PF00627; UBA; 2.
Pfam; PF00240; ubiquitin; 1.
Pfam; PF09280; XPC-binding; 1.
PRINTS; PR01839; RAD23PROTEIN.
SMART; SM00727; STI1; 1.
SMART; SM00165; UBA; 2.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF101238; SSF101238; 1.
SUPFAM; SSF46934; SSF46934; 2.
SUPFAM; SSF54236; SSF54236; 1.
TIGRFAMs; TIGR00601; rad23; 1.
PROSITE; PS50030; UBA; 2.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA repair; Host-virus interaction; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Proteasome; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 363 UV excision repair protein RAD23 homolog
A.
/FTId=PRO_0000114904.
DOMAIN 1 81 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 161 201 UBA 1. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 318 358 UBA 2. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
REGION 319 363 HIV-1 vpr binding.
MOD_RES 123 123 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000250|UniProtKB:P54726}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 226 226 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_054694.
VAR_SEQ 272 326 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_047565.
VARIANT 131 131 T -> A (in dbSNP:rs11558955).
{ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_016251.
VARIANT 179 179 R -> Q (in dbSNP:rs4987203).
/FTId=VAR_020377.
VARIANT 200 200 T -> M (in dbSNP:rs4987202).
{ECO:0000269|Ref.2}.
/FTId=VAR_016252.
MUTAGEN 8 8 K->A: No effect on interaction with
EEF1A1. {ECO:0000269|PubMed:16712842}.
MUTAGEN 9 9 T->A: Abolishes interaction with PSMD4;
when associated with T-49.
{ECO:0000269|PubMed:14557549}.
MUTAGEN 10 10 L->E: Impairs UBL-UBA domain interaction
and enhances ubiquitin-binding; when
associated with Glu-47.
{ECO:0000269|PubMed:18234089}.
MUTAGEN 47 47 K->A: No effect on UBL-UBA domain
interaction.
{ECO:0000269|PubMed:18234089}.
MUTAGEN 47 47 K->E: Impairs UBL-UBA domain interaction
and enhances ubiquitin-binding; when
associated with Glu-10.
{ECO:0000269|PubMed:18234089}.
MUTAGEN 47 47 K->E: Impairs UBL-UBA domain interaction
and enhances ubiquitin-binding; when
associated with Glu-77.
{ECO:0000269|PubMed:18234089}.
MUTAGEN 49 49 I->A: Impairs interaction with PSMD4.
{ECO:0000269|PubMed:12970176,
ECO:0000269|PubMed:14557549}.
MUTAGEN 49 49 I->T: Abolishes interaction with PSMD4;
when associated with A-9.
{ECO:0000269|PubMed:12970176,
ECO:0000269|PubMed:14557549}.
MUTAGEN 54 54 I->A: Impairs interaction with PSMD4.
{ECO:0000269|PubMed:12970176}.
MUTAGEN 71 71 F->A: Impairs interaction with PSMD4.
{ECO:0000269|PubMed:12970176}.
MUTAGEN 77 77 T->E: Impairs UBL-UBA domain interaction
and enhances ubiquitin-binding; when
associated with Glu-47.
{ECO:0000269|PubMed:12970176,
ECO:0000269|PubMed:18234089}.
MUTAGEN 77 77 T->S: No effect on interaction with
PSMD4. {ECO:0000269|PubMed:12970176,
ECO:0000269|PubMed:18234089}.
MUTAGEN 79 79 T->P: Increases interaction with PSMD1
and PSMC1. {ECO:0000269|PubMed:16712842}.
MUTAGEN 333 333 P->E: Abolishes interaction with HIV-1
vpr. {ECO:0000269|PubMed:11087358}.
STRAND 3 9 {ECO:0000244|PDB:2WYQ}.
TURN 10 12 {ECO:0000244|PDB:1OQY}.
STRAND 14 19 {ECO:0000244|PDB:2WYQ}.
STRAND 21 23 {ECO:0000244|PDB:1P98}.
HELIX 25 36 {ECO:0000244|PDB:2WYQ}.
TURN 38 40 {ECO:0000244|PDB:2WYQ}.
HELIX 43 45 {ECO:0000244|PDB:2WYQ}.
STRAND 46 50 {ECO:0000244|PDB:2WYQ}.
STRAND 53 55 {ECO:0000244|PDB:1P98}.
STRAND 57 60 {ECO:0000244|PDB:1OQY}.
HELIX 61 64 {ECO:0000244|PDB:2WYQ}.
STRAND 70 76 {ECO:0000244|PDB:2WYQ}.
STRAND 81 83 {ECO:0000244|PDB:1OQY}.
STRAND 96 98 {ECO:0000244|PDB:1OQY}.
STRAND 106 108 {ECO:0000244|PDB:1OQY}.
STRAND 116 119 {ECO:0000244|PDB:1OQY}.
HELIX 161 172 {ECO:0000244|PDB:1IFY}.
HELIX 177 185 {ECO:0000244|PDB:1IFY}.
TURN 186 188 {ECO:0000244|PDB:1IFY}.
HELIX 192 200 {ECO:0000244|PDB:1IFY}.
HELIX 233 237 {ECO:0000244|PDB:1OQY}.
HELIX 239 246 {ECO:0000244|PDB:1OQY}.
TURN 248 250 {ECO:0000244|PDB:1OQY}.
HELIX 254 259 {ECO:0000244|PDB:1OQY}.
TURN 260 265 {ECO:0000244|PDB:1OQY}.
HELIX 267 285 {ECO:0000244|PDB:1OQY}.
STRAND 298 301 {ECO:0000244|PDB:1OQY}.
TURN 318 320 {ECO:0000244|PDB:1OQY}.
HELIX 321 324 {ECO:0000244|PDB:1DV0}.
TURN 325 331 {ECO:0000244|PDB:1DV0}.
HELIX 334 341 {ECO:0000244|PDB:1DV0}.
TURN 342 345 {ECO:0000244|PDB:1DV0}.
HELIX 348 354 {ECO:0000244|PDB:1DV0}.
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


Related products :

Catalog number Product name Quantity
EIAAB34138 hHR23A,Homo sapiens,HR23A,Human,RAD23A,UV excision repair protein RAD23 homolog A
18-003-43728 UV excision repair protein RAD23 homolog A - hHR23A Polyclonal 0.1 mg Protein A
18-003-43729 UV excision repair protein RAD23 homolog A - hHR23A Polyclonal 0.1 mg Protein A
EIAAB34137 HR23A,mHR23A,Mhr23a,Mouse,Mus musculus,Rad23a,UV excision repair protein RAD23 homolog A
EIAAB34140 hHR23B,Homo sapiens,HR23B,Human,p58,RAD23B,UV excision repair protein RAD23 homolog B,XP-C repair-complementing complex 58 kDa protein
CSB-RP037744h Recombinant human UV excision repair protein RAD23 homolog A 500ug
CSB-EL019260RA Rat UV excision repair protein RAD23 homolog B(RAD23B) ELISA kit 96T
I1664 UV excision repair protein RAD23 homolog B (RAD23B), Rat, ELISA Kit 96T
CSB-EL019259MO Mouse UV excision repair protein RAD23 homolog A(RAD23A) ELISA kit 96T
EIAAB34136 Bos taurus,Bovine,RAD23A,UV excision repair protein RAD23 homolog A
EIAAB34142 Rad23b,Rat,Rattus norvegicus,UV excision repair protein RAD23 homolog B
EIAAB34139 Bos taurus,Bovine,RAD23B,UV excision repair protein RAD23 homolog B
CSB-EL019260MO Mouse UV excision repair protein RAD23 homolog B(RAD23B) ELISA kit 96T
15-1030-1 Polyclonal antibody Anti-UV excision repair protein RAD23 homolog A 100
I1663 UV excision repair protein RAD23 homolog B (RAD23B), Mouse, ELISA Kit 96T
I1662 UV excision repair protein RAD23 homolog B (RAD23B), Human, ELISA Kit 96T
abx109043 Polyclonal Rabbit UV excision repair protein RAD23 homolog A Antibody (HRP) 100 μg
CSB-EL019260RA Rat UV excision repair protein RAD23 homolog B(RAD23B) ELISA kit SpeciesRat 96T
I1658 UV excision repair protein RAD23 homolog A (RAD23A), Bovine, ELISA Kit 96T
CSB-EL019260HU Human UV excision repair protein RAD23 homolog B(RAD23B) ELISA kit 96T
I1659 UV excision repair protein RAD23 homolog A (RAD23A), Mouse, ELISA Kit 96T
I1660 UV excision repair protein RAD23 homolog A(RAD23A), Human, ELISA Kit 96T
CSB-EL019259BO Bovine UV excision repair protein RAD23 homolog A(RAD23A) ELISA kit 96T
I1661 UV excision repair protein RAD23 homolog B (RAD23B), Bovine, ELISA Kit 96T
CSB-EL019260BO Bovine UV excision repair protein RAD23 homolog B(RAD23B) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur