RD23B_HUMAN
ID RD23B_HUMAN Reviewed; 409 AA.
AC P54727; B3KWK8; G5E9P0; Q7Z5K8; Q8WUB0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=UV excision repair protein RAD23 homolog B;
DE Short=HR23B;
DE Short=hHR23B;
DE AltName: Full=XP-C repair-complementing complex 58 kDa protein;
DE Short=p58;
GN Name=RAD23B;
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), AND PARTIAL PROTEIN SEQUENCE.
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 [MRNA] (ISOFORM 2), VARIANT VAL-249, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15064313; DOI=10.1002/j.1939-4640.2004.tb02801.x;
RA Huang X., Wang H., Xu M., Lu L., Xu Z., Li J., Zhou Z., Sha J.;
RT "Expression of a novel RAD23B mRNA splice variant in the human testis.";
RL J. Androl. 25:363-368(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-249.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-249.
RC TISSUE=Uterus;
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 [8]
RP FUNCTION.
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 FUNCTION OF THE XPC COMPLEX.
RX PubMed=9734359; DOI=10.1016/s1097-2765(00)80132-x;
RA Sugasawa K., Ng J.M., Masutani C., Iwai S., van der Spek P.J., Eker A.P.,
RA Hanaoka F., Bootsma D., Hoeijmakers J.H.;
RT "Xeroderma pigmentosum group C protein complex is the initiator of global
RT genome nucleotide excision repair.";
RL Mol. Cell 2:223-232(1998).
RN [10]
RP INTERACTION WITH PSMD4 AND PSMC5.
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 [11]
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 [12]
RP FUNCTION, AND FUNCTION OF THE XPC COMPLEX.
RX PubMed=10873465; DOI=10.1006/jmbi.2000.3857;
RA Batty D., Rapic'-Otrin V., Levine A.S., Wood R.D.;
RT "Stable binding of human XPC complex to irradiated DNA confers strong
RT discrimination for damaged sites.";
RL J. Mol. Biol. 300:275-290(2000).
RN [13]
RP INTERACTION WITH CETN2, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF THE
RP XPC COMPLEX.
RX PubMed=11279143; DOI=10.1074/jbc.m100855200;
RA Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J.,
RA Ohkuma Y., Hanaoka F.;
RT "Centrosome protein centrin 2/caltractin 1 is part of the xeroderma
RT pigmentosum group C complex that initiates global genome nucleotide
RT excision repair.";
RL J. Biol. Chem. 276:18665-18672(2001).
RN [14]
RP FUNCTION OF THE XPC COMPLEX.
RX PubMed=12509299; DOI=10.1016/s1568-7864(01)00008-8;
RA Sugasawa K., Shimizu Y., Iwai S., Hanaoka F.;
RT "A molecular mechanism for DNA damage recognition by the xeroderma
RT pigmentosum group C protein complex.";
RL DNA Repair 1:95-107(2002).
RN [15]
RP INTERACTION WITH XPC.
RX PubMed=12509233; DOI=10.1016/s1568-7864(02)00031-9;
RA Uchida A., Sugasawa K., Masutani C., Dohmae N., Araki M., Yokoi M.,
RA Ohkuma Y., Hanaoka F.;
RT "The carboxy-terminal domain of the XPC protein plays a crucial role in
RT nucleotide excision repair through interactions with transcription factor
RT IIH.";
RL DNA Repair 1:449-461(2002).
RN [16]
RP FUNCTION OF THE XPC COMPLEX.
RX PubMed=12547395; DOI=10.1016/s1568-7864(02)00222-7;
RA Janicijevic A., Sugasawa K., Shimizu Y., Hanaoka F., Wijgers N.,
RA Djurica M., Hoeijmakers J.H., Wyman C.;
RT "DNA bending by the human damage recognition complex XPC-HR23B.";
RL DNA Repair 2:325-336(2003).
RN [17]
RP FUNCTION.
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 [18]
RP INTERACTION WITH NGLY1 AND PSMC1.
RX PubMed=15358861; DOI=10.1073/pnas.0405663101;
RA Katiyar S., Li G., Lennarz W.J.;
RT "A complex between peptide:N-glycanase and two proteasome-linked proteins
RT suggests a mechanism for the degradation of misfolded glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=16253613; DOI=10.1016/j.bbrc.2005.09.192;
RA Katiyar S., Lennarz W.J.;
RT "Studies on the intracellular localization of hHR23B.";
RL Biochem. Biophys. Res. Commun. 337:1296-1300(2005).
RN [20]
RP INTERACTION WITH XPC.
RX PubMed=15964821; DOI=10.1128/mcb.25.13.5664-5674.2005;
RA Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C.,
RA Sugasawa K., Hanaoka F.;
RT "Centrin 2 stimulates nucleotide excision repair by interacting with
RT xeroderma pigmentosum group C protein.";
RL Mol. Cell. Biol. 25:5664-5674(2005).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [22]
RP INTERACTION WITH EEF1A1, AND MUTAGENESIS OF LYS-6.
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP FUNCTION IN PROTEASOMAL DEGRADATION, AND POLYUBIQUITIN-BINDING.
RX PubMed=19435460; DOI=10.1042/bj20090528;
RA Li X., Demartino G.N.;
RT "Variably modulated gating of the 26S proteasome by ATP and
RT polyubiquitin.";
RL Biochem. J. 421:397-404(2009).
RN [28]
RP FUNCTION OF THE XPC COMPLEX.
RX PubMed=19941824; DOI=10.1016/j.molcel.2009.09.035;
RA Sugasawa K., Akagi J., Nishi R., Iwai S., Hanaoka F.;
RT "Two-step recognition of DNA damage for mammalian nucleotide excision
RT repair: Directional binding of the XPC complex and DNA strand scanning.";
RL Mol. Cell 36:642-653(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, 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 [30]
RP FUNCTION OF THE XPC COMPLEX.
RX PubMed=20028083; DOI=10.1021/bi901575h;
RA Neher T.M., Rechkunova N.I., Lavrik O.I., Turchi J.J.;
RT "Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals
RT contacts with both strands of the DNA duplex and spans the DNA adduct.";
RL Biochemistry 49:669-678(2010).
RN [31]
RP FUNCTION OF THE XPC COMPLEX.
RX PubMed=20798892; DOI=10.4061/2010/805698;
RA Shimizu Y., Uchimura Y., Dohmae N., Saitoh H., Hanaoka F., Sugasawa K.;
RT "Stimulation of DNA glycosylase activities by XPC Protein Complex: Roles of
RT protein-protein interactions.";
RL J. Nucleic Acids 2010:455-459(2010).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, 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 [33]
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP 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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP 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 [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND THR-164, 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 [37]
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 [38]
RP STRUCTURE BY NMR OF 1-82.
RX PubMed=12832454; DOI=10.1074/jbc.m304628200;
RA Ryu K.-S., Lee K.-J., Bae S.-H., Kim B.-K., Kim K.-A., Choi B.-S.;
RT "Binding surface mapping of intra- and interdomain interactions among
RT hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a.";
RL J. Biol. Chem. 278:36621-36627(2003).
RN [39]
RP STRUCTURE BY NMR OF 1-87 IN COMPLEX WITH PSMD4.
RX PubMed=14585839; DOI=10.1074/jbc.m309448200;
RA Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C.,
RA Tochio H., Hiroaki H., Hanaoka F., Shirakawa M.;
RT "Structure of the ubiquitin-interacting motif of S5a bound to the
RT ubiquitin-like domain of HR23B.";
RL J. Biol. Chem. 279:4760-4767(2004).
RN [40]
RP STRUCTURE BY NMR OF 275-342, AND FUNCTION.
RX PubMed=15885096; DOI=10.1111/j.1742-4658.2005.04667.x;
RA Kim B., Ryu K.-S., Kim H.-J., Cho S.-J., Choi B.-S.;
RT "Solution structure and backbone dynamics of the XPC-binding domain of the
RT human DNA repair protein hHR23B.";
RL FEBS J. 272:2467-2476(2005).
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.
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 -!- 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.
CC -!- SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and
CC CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3
CC (PubMed:30455355). Interacts with PSMD4 and PSMC5. Interacts with AMFR.
CC Interacts with VCP; the interaction is indirect and mediated by NGLY1
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:30455355}.
CC -!- INTERACTION:
CC P54727; Q16186: ADRM1; NbExp=2; IntAct=EBI-954531, EBI-954387;
CC P54727; P19447: ERCC3; NbExp=2; IntAct=EBI-954531, EBI-1183307;
CC P54727; O00291: HIP1; NbExp=3; IntAct=EBI-954531, EBI-473886;
CC P54727; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-954531, EBI-373524;
CC P54727; Q96IV0: NGLY1; NbExp=12; IntAct=EBI-954531, EBI-6165879;
CC P54727; Q96PV4: PNMA5; NbExp=6; IntAct=EBI-954531, EBI-10171633;
CC P54727; P78424: POU6F2; NbExp=3; IntAct=EBI-954531, EBI-12029004;
CC P54727; P55036: PSMD4; NbExp=11; IntAct=EBI-954531, EBI-359318;
CC P54727; Q9UHX1: PUF60; NbExp=3; IntAct=EBI-954531, EBI-1053259;
CC P54727; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-954531, EBI-11529177;
CC P54727; Q92681: RSC1A1; NbExp=3; IntAct=EBI-954531, EBI-3940171;
CC P54727; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-954531, EBI-529518;
CC P54727; Q8TBC4: UBA3; NbExp=2; IntAct=EBI-954531, EBI-717567;
CC P54727; P0CG47: UBB; NbExp=5; IntAct=EBI-954531, EBI-413034;
CC P54727; P0CG48: UBC; NbExp=5; IntAct=EBI-954531, EBI-3390054;
CC P54727; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-954531, EBI-947187;
CC P54727; Q9UHP3: USP25; NbExp=4; IntAct=EBI-954531, EBI-2513462;
CC P54727; P45974: USP5; NbExp=2; IntAct=EBI-954531, EBI-741277;
CC P54727; P08670: VIM; NbExp=2; IntAct=EBI-954531, EBI-353844;
CC P54727; Q01831: XPC; NbExp=6; IntAct=EBI-954531, EBI-372610;
CC P54727; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-954531, EBI-25475856;
CC P54727; P24610: Pax3; Xeno; NbExp=4; IntAct=EBI-954531, EBI-1208116;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The intracellular
CC distribution is cell cycle dependent. Localized to the nucleus and the
CC cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon
CC entering mitosis, relocalizes in the cytoplasm without association with
CC chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P54727-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54727-2; Sequence=VSP_045606;
CC -!- DOMAIN: The ubiquitin-like domain mediates interaction with ATXN3.
CC -!- MISCELLANEOUS: [Isoform 2]: Highly expressed in the testis and in
CC ejaculated spermatozoa. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rad23b/";
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DR EMBL; D21090; BAA04652.1; -; mRNA.
DR EMBL; AY313777; AAP81008.1; -; mRNA.
DR EMBL; AY165178; AAN47194.1; -; Genomic_DNA.
DR EMBL; AK125226; BAG54170.1; -; mRNA.
DR EMBL; AL137852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW59016.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW59017.1; -; Genomic_DNA.
DR EMBL; BC020973; AAH20973.1; -; mRNA.
DR CCDS; CCDS59138.1; -. [P54727-2]
DR CCDS; CCDS6769.1; -. [P54727-1]
DR PIR; S44346; S44346.
DR RefSeq; NP_001231653.1; NM_001244724.1. [P54727-2]
DR RefSeq; NP_002865.1; NM_002874.4. [P54727-1]
DR PDB; 1P1A; NMR; -; A=1-82.
DR PDB; 1PVE; NMR; -; A=275-342.
DR PDB; 1UEL; NMR; -; A=1-87.
DR PDBsum; 1P1A; -.
DR PDBsum; 1PVE; -.
DR PDBsum; 1UEL; -.
DR AlphaFoldDB; P54727; -.
DR BMRB; P54727; -.
DR SMR; P54727; -.
DR BioGRID; 111824; 186.
DR DIP; DIP-39944N; -.
DR IntAct; P54727; 80.
DR MINT; P54727; -.
DR STRING; 9606.ENSP00000350708; -.
DR GlyGen; P54727; 25 sites, 2 O-linked glycans (25 sites).
DR iPTMnet; P54727; -.
DR MetOSite; P54727; -.
DR PhosphoSitePlus; P54727; -.
DR SwissPalm; P54727; -.
DR BioMuta; RAD23B; -.
DR DMDM; 1709985; -.
DR OGP; P54727; -.
DR CPTAC; CPTAC-1456; -.
DR CPTAC; CPTAC-1457; -.
DR CPTAC; CPTAC-1458; -.
DR CPTAC; CPTAC-3248; -.
DR CPTAC; CPTAC-3249; -.
DR CPTAC; CPTAC-707; -.
DR CPTAC; CPTAC-723; -.
DR EPD; P54727; -.
DR jPOST; P54727; -.
DR MassIVE; P54727; -.
DR MaxQB; P54727; -.
DR PaxDb; P54727; -.
DR PeptideAtlas; P54727; -.
DR PRIDE; P54727; -.
DR ProteomicsDB; 33998; -.
DR ProteomicsDB; 56701; -. [P54727-1]
DR TopDownProteomics; P54727-1; -. [P54727-1]
DR ABCD; P54727; 2 sequenced antibodies.
DR Antibodypedia; 29324; 515 antibodies from 37 providers.
DR CPTC; P54727; 2 antibodies.
DR DNASU; 5887; -.
DR Ensembl; ENST00000358015.8; ENSP00000350708.3; ENSG00000119318.13. [P54727-1]
DR Ensembl; ENST00000416373.6; ENSP00000405623.2; ENSG00000119318.13. [P54727-2]
DR GeneID; 5887; -.
DR KEGG; hsa:5887; -.
DR MANE-Select; ENST00000358015.8; ENSP00000350708.3; NM_002874.5; NP_002865.1.
DR UCSC; uc004bde.4; human. [P54727-1]
DR CTD; 5887; -.
DR DisGeNET; 5887; -.
DR GeneCards; RAD23B; -.
DR HGNC; HGNC:9813; RAD23B.
DR HPA; ENSG00000119318; Low tissue specificity.
DR MIM; 600062; gene.
DR neXtProt; NX_P54727; -.
DR OpenTargets; ENSG00000119318; -.
DR PharmGKB; PA34173; -.
DR VEuPathDB; HostDB:ENSG00000119318; -.
DR eggNOG; KOG0011; Eukaryota.
DR GeneTree; ENSGT00390000012078; -.
DR HOGENOM; CLU_040364_0_1_1; -.
DR InParanoid; P54727; -.
DR OMA; MWDEQSA; -.
DR OrthoDB; 1260050at2759; -.
DR PhylomeDB; P54727; -.
DR TreeFam; TF101216; -.
DR PathwayCommons; P54727; -.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
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; P54727; -.
DR SIGNOR; P54727; -.
DR BioGRID-ORCS; 5887; 21 hits in 1043 CRISPR screens.
DR ChiTaRS; RAD23B; human.
DR EvolutionaryTrace; P54727; -.
DR GeneWiki; RAD23B; -.
DR GenomeRNAi; 5887; -.
DR Pharos; P54727; Tbio.
DR PRO; PR:P54727; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P54727; protein.
DR Bgee; ENSG00000119318; Expressed in corpus epididymis and 216 other tissues.
DR ExpressionAtlas; P54727; baseline and differential.
DR Genevisible; P54727; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0071942; C:XPC complex; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0140612; F:DNA damage sensor activity; IDA:GO_Central.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..409
FT /note="UV excision repair protein RAD23 homolog B"
FT /id="PRO_0000114906"
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 364..404
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 236..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17323924"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
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"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15064313"
FT /id="VSP_045606"
FT VARIANT 249
FT /note="A -> V (in dbSNP:rs1805329)"
FT /evidence="ECO:0000269|PubMed:15064313,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_014350"
FT MUTAGEN 6
FT /note="K->A: Impairs interaction with EEF1A1."
FT /evidence="ECO:0000269|PubMed:16712842"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:1P1A"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1P1A"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1P1A"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1P1A"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1P1A"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1P1A"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1P1A"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1P1A"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1PVE"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:1PVE"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:1PVE"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1PVE"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:1PVE"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:1PVE"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:1PVE"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:1PVE"
SQ SEQUENCE 409 AA; 43171 MW; C026C78273BCB289 CRC64;
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILNDDTALK
EYKIDEKNFV VVMVTKPKAV STPAPATTQQ SAPASTTAVT SSTTTTVAQA PTPVPALAPT
STPASITPAS ATASSEPAPA SAAKQEKPAE KPAETPVATS PTATDSTSGD SSRSNLFEDA
TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD
PPQAASTGAP QSSAVAAAAA TTTATTTTTS SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGSGGIA EAGSGHMNYI
QVTPQEKEAI ERLKALGFPE GLVIQAYFAC EKNENLAANF LLQQNFDED
