DDB2_HUMAN
ID DDB2_HUMAN Reviewed; 427 AA.
AC Q92466; B2R875; Q76E54; Q76E55; Q76E56; Q76E57;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=DNA damage-binding protein 2;
DE AltName: Full=DDB p48 subunit;
DE Short=DDBb;
DE AltName: Full=Damage-specific DNA-binding protein 2;
DE AltName: Full=UV-damaged DNA-binding protein 2;
DE Short=UV-DDB 2;
GN Name=DDB2;
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).
RC TISSUE=Epidermis;
RX PubMed=8530102; DOI=10.1006/geno.1995.1215;
RA Dualan R., Brody T., Keeney S., Nichols A.F., Admon A., Linn S.;
RT "Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for
RT the p127 and p48 subunits of a human damage-specific DNA binding protein.";
RL Genomics 29:62-69(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D1; D2; D3 AND D4), FUNCTION,
RP INTERACTION WITH DDB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Epithelium;
RX PubMed=14751237; DOI=10.1016/j.bbrc.2004.01.003;
RA Inoki T., Yamagami S., Inoki Y., Tsuru T., Hamamoto T., Kagawa Y., Mori T.,
RA Endo H.;
RT "Human DDB2 splicing variants are dominant negative inhibitors of UV-
RT damaged DNA repair.";
RL Biochem. Biophys. Res. Commun. 314:1036-1043(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-215 AND THR-293.
RG NIEHS SNPs program;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH DDB1, DNA-BINDING, AND CHARACTERIZATION OF VARIANTS
RP GLU-244 AND HIS-273.
RX PubMed=9632823; DOI=10.1128/mcb.18.7.4391;
RA Hwang B.J., Toering S., Francke U., Chu G.;
RT "p48 Activates a UV-damaged-DNA binding factor and is defective in
RT xeroderma pigmentosum group E cells that lack binding activity.";
RL Mol. Cell. Biol. 18:4391-4399(1998).
RN [9]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9892649; DOI=10.1073/pnas.96.2.424;
RA Hwang B.J., Ford J.M., Hanawalt P.C., Chu G.;
RT "Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is
RT involved in global genomic repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:424-428(1999).
RN [10]
RP DNA-BINDING, SUBCELLULAR LOCATION, INDUCTION, AND CHARACTERIZATION OF
RP VARIANTS GLU-244 AND HIS-273.
RX PubMed=10777490; DOI=10.1074/jbc.m000960200;
RA Nichols A.F., Itoh T., Graham J.A., Liu W., Yamaizumi M., Linn S.;
RT "Human damage-specific DNA-binding protein p48. Characterization of XPE
RT mutations and regulation following UV irradiation.";
RL J. Biol. Chem. 275:21422-21428(2000).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=10777491; DOI=10.1074/jbc.m000961200;
RA Liu W., Nichols A.F., Graham J.A., Dualan R., Abbas A., Linn S.;
RT "Nuclear transport of human DDB protein induced by ultraviolet light.";
RL J. Biol. Chem. 275:21429-21434(2000).
RN [12]
RP FUNCTION.
RX PubMed=10882109; DOI=10.1016/s1097-2765(00)80252-x;
RA Tang J.Y., Hwang B.J., Ford J.M., Hanawalt P.C., Chu G.;
RT "Xeroderma pigmentosum p48 gene enhances global genomic repair and
RT suppresses UV-induced mutagenesis.";
RL Mol. Cell 5:737-744(2000).
RN [13]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=11278856; DOI=10.1074/jbc.m011177200;
RA Wakasugi M., Shimizu M., Morioka H., Linn S., Nikaido O., Matsunaga T.;
RT "Damaged DNA-binding protein DDB stimulates the excision of cyclobutane
RT pyrimidine dimers in vitro in concert with XPA and replication protein A.";
RL J. Biol. Chem. 276:15434-15440(2001).
RN [14]
RP INTERACTION WITH CUL4A, UBIQUITINATION, AND CHARACTERIZATION OF VARIANT
RP HIS-273.
RX PubMed=11673459; DOI=10.1074/jbc.m106808200;
RA Chen X., Zhang Y., Douglas L., Zhou P.;
RT "UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
RT ubiquitination and degradation.";
RL J. Biol. Chem. 276:48175-48182(2001).
RN [15]
RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11705987; DOI=10.1074/jbc.c100610200;
RA Wakasugi M., Kawashima A., Morioka H., Linn S., Sancar A., Mori T.,
RA Nikaido O., Matsunaga T.;
RT "DDB accumulates at DNA damage sites immediately after UV irradiation and
RT directly stimulates nucleotide excision repair.";
RL J. Biol. Chem. 277:1637-1640(2002).
RN [16]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX
RP WITH CUL4A; DDB1 AND RBX1 AND THE COP9 SIGNALOSOME, AND DNA-BINDING.
RX PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12944386; DOI=10.1074/jbc.m307254200;
RA Fitch M.E., Nakajima S., Yasui A., Ford J.M.;
RT "In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by
RT the DDB2 gene product.";
RL J. Biol. Chem. 278:46906-46910(2003).
RN [18]
RP FUNCTION, INTERACTION WITH CUL4A; DDB1; RBX1 AND XPC, DNA-BINDING, AND
RP UBIQUITINATION.
RX PubMed=15882621; DOI=10.1016/j.cell.2005.02.035;
RA Sugasawa K., Okuda Y., Saijo M., Nishi R., Matsuda N., Chu G., Mori T.,
RA Iwai S., Tanaka K., Tanaka K., Hanaoka F.;
RT "UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin
RT ligase complex.";
RL Cell 121:387-400(2005).
RN [19]
RP INTERACTION WITH DDB1, DNA-BINDING, AND CHARACTERIZATION OF VARIANTS
RP GLU-244 AND HIS-273.
RX PubMed=16223728; DOI=10.1074/jbc.m507854200;
RA Wittschieben B.O., Iwai S., Wood R.D.;
RT "DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a
RT cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and
RT compound lesions in DNA.";
RL J. Biol. Chem. 280:39982-39989(2005).
RN [20]
RP FUNCTION, INTERACTION WITH CUL4A; DDB1; RBX1 AND THE COP9 SIGNALOSOME, AND
RP DNA-BINDING.
RX PubMed=16260596; DOI=10.1128/mcb.25.22.9784-9792.2005;
RA Kulaksiz G., Reardon J.T., Sancar A.;
RT "Xeroderma pigmentosum complementation group E protein (XPE/DDB2):
RT purification of various complexes of XPE and analyses of their damaged DNA
RT binding and putative DNA repair properties.";
RL Mol. Cell. Biol. 25:9784-9792(2005).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND
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 CUL4A AND DDB1, DOMAIN DWD BOX MOTIF, AND MUTAGENESIS OF
RP LEU-258; SER-262; ASP-264; ILE-269; TRP-270; LEU-272 AND ARG-273.
RX PubMed=17079684; DOI=10.1101/gad.1483206;
RA He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y.;
RT "DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1
RT ubiquitin ligases.";
RL Genes Dev. 20:2949-2954(2006).
RN [23]
RP INTERACTION WITH CUL4A AND DDB1, AND UBIQUITINATION.
RX PubMed=16527807; DOI=10.1074/jbc.m511834200;
RA El-Mahdy M.A., Zhu Q., Wang Q.-E., Wani G., Praetorius-Ibba M., Wani A.A.;
RT "Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites
RT regulates in vivo lesion recognition by XPC.";
RL J. Biol. Chem. 281:13404-13411(2006).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH DDB1;
RP CUL4A; CUL4B AND RBX1, AND FUNCTION.
RX PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
RA Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
RA Tempst P., Xiong Y., Zhang Y.;
RT "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase
RT facilitates cellular response to DNA damage.";
RL Mol. Cell 22:383-394(2006).
RN [25]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=16713579; DOI=10.1016/j.molcel.2006.04.021;
RA Chen X., Zhang J., Lee J., Lin P.S., Ford J.M., Zheng N., Zhou P.;
RT "A kinase-independent function of c-Abl in promoting proteolytic
RT destruction of damaged DNA binding proteins.";
RL Mol. Cell 22:489-499(2006).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDB1, MUTAGENESIS OF
RP LEU-350, AND CHARACTERIZATION OF VARIANT HIS-273.
RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is
RT required for S phase destruction of the replication factor Cdt1.";
RL Mol. Cell 23:709-721(2006).
RN [27]
RP INTERACTION WITH DDB1, AND CHARACTERIZATION OF VARIANT HIS-273.
RX PubMed=16964240; DOI=10.1038/nature05175;
RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase
RT machinery.";
RL Nature 443:590-593(2006).
RN [28]
RP INTERACTION WITH CUL4A AND CUL4B.
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
RT and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [29]
RP FUNCTION, INTERACTION WITH CUL4A; DDB1; HISTONE H2A AND RBX1, DNA-BINDING,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16473935; DOI=10.1073/pnas.0511160103;
RA Kapetanaki M.G., Guerrero-Santoro J., Bisi D.C., Hsieh C.L.,
RA Rapic-Otrin V., Levine A.S.;
RT "The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum
RT group E and targets histone H2A at UV-damaged DNA sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2588-2593(2006).
RN [30]
RP SUBCELLULAR LOCATION.
RX PubMed=17635991; DOI=10.1242/jcs.008367;
RA Luijsterburg M.S., Goedhart J., Moser J., Kool H., Geverts B.,
RA Houtsmuller A.B., Mullenders L.H.F., Vermeulen W., van Driel R.;
RT "Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-damaged
RT DNA is independent of damage-recognition protein XPC.";
RL J. Cell Sci. 120:2706-2716(2007).
RN [31]
RP FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB1, AND SUBCELLULAR LOCATION.
RX PubMed=18593899; DOI=10.1158/0008-5472.can-07-6162;
RA Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I.,
RA Levine A.S., Rapic-Otrin V.;
RT "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-
RT damaged chromatin and ubiquitinates histone H2A.";
RL Cancer Res. 68:5014-5022(2008).
RN [32]
RP 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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, 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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, 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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, 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 [36]
RP DEUBIQUITINATION BY USP24.
RX PubMed=23159851; DOI=10.4161/cc.22688;
RA Zhang L., Lubin A., Chen H., Sun Z., Gong F.;
RT "The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2
RT stability.";
RL Cell Cycle 11:4378-4384(2012).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND
RP 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 [38]
RP FUNCTION.
RX PubMed=26572825; DOI=10.1128/mcb.00809-15;
RA Matsunuma R., Niida H., Ohhata T., Kitagawa K., Sakai S., Uchida C.,
RA Shiotani B., Matsumoto M., Nakayama K.I., Ogura H., Shiiya N., Kitagawa M.;
RT "UV damage-induced phosphorylation of HBO1 triggers CRL4DDB2-mediated
RT degradation to regulate cell proliferation.";
RL Mol. Cell. Biol. 36:394-406(2016).
RN [39]
RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-35 AND LYS-77, AND
RP MUTAGENESIS OF LYS-35; LYS-40 AND LYS-77.
RX PubMed=32789493; DOI=10.1093/nar/gkaa661;
RA Geng A., Tang H., Huang J., Qian Z., Qin N., Yao Y., Xu Z., Chen H.,
RA Lan L., Xie H., Zhang J., Jiang Y., Mao Z.;
RT "The deacetylase SIRT6 promotes the repair of UV-induced DNA damage by
RT targeting DDB2.";
RL Nucleic Acids Res. 48:9181-9194(2020).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 10-427 IN COMPLEX WITH DDB1 AND
RP DNA, AND WD REPEATS.
RX PubMed=19109893; DOI=10.1016/j.cell.2008.10.045;
RA Scrima A., Konickova R., Czyzewski B.K., Kawasaki Y., Jeffrey P.D.,
RA Groisman R., Nakatani Y., Iwai S., Pavletich N.P., Thoma N.H.;
RT "Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex.";
RL Cell 135:1213-1223(2008).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 68-81 IN COMPLEX WITH DDB1.
RX PubMed=19966799; DOI=10.1038/nsmb.1719;
RA Li T., Robert E.I., van Breugel P.C., Strubin M., Zheng N.;
RT "A promiscuous alpha-helical motif anchors viral hijackers and substrate
RT receptors to the CUL4-DDB1 ubiquitin ligase machinery.";
RL Nat. Struct. Mol. Biol. 17:105-111(2010).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH DDB1.
RX PubMed=22822215; DOI=10.1073/pnas.1110067109;
RA Yeh J.I., Levine A.S., Du S., Chinte U., Ghodke H., Wang H., Shi H.,
RA Hsieh C.L., Conway J.F., Van Houten B., Rapic-Otrin V.;
RT "Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization
RT and its roles in chromatinized DNA repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2737-E2746(2012).
RN [43]
RP VARIANTS XP-E GLU-244 AND HIS-273.
RX PubMed=8798680; DOI=10.1074/jbc.271.40.24317;
RA Nichols A.F., Ong P., Linn S.;
RT "Mutations specific to the xeroderma pigmentosum group E Ddb-phenotype.";
RL J. Biol. Chem. 271:24317-24320(1996).
CC -!- FUNCTION: Protein, which is both involved in DNA repair and protein
CC ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box)
CC complexes, respectively (PubMed:10882109, PubMed:11278856,
CC PubMed:11705987, PubMed:9892649, PubMed:12732143, PubMed:15882621,
CC PubMed:16473935, PubMed:18593899, PubMed:32789493). Core component of
CC the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex
CC that recognizes UV-induced DNA damage and recruit proteins of the
CC nucleotide excision repair pathway (the NER pathway) to initiate DNA
CC repair (PubMed:10882109, PubMed:11278856, PubMed:11705987,
CC PubMed:16260596, PubMed:12944386, PubMed:14751237, PubMed:32789493).
CC The UV-DDB complex preferentially binds to cyclobutane pyrimidine
CC dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short
CC mismatches (PubMed:10882109, PubMed:11278856, PubMed:11705987,
CC PubMed:16260596, PubMed:12944386). Also functions as the substrate
CC recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein
CC ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-
CC DDB-RBX1) (PubMed:12732143, PubMed:15882621, PubMed:16473935,
CC PubMed:18593899, PubMed:26572825). The DDB2-CUL4-ROC1 complex may
CC ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-
CC induced DNA damage (PubMed:16678110, PubMed:16473935). The
CC ubiquitination of histones may facilitate their removal from the
CC nucleosome and promote subsequent DNA repair (PubMed:16678110,
CC PubMed:16473935). The DDB2-CUL4-ROC1 complex also ubiquitinates XPC,
CC which may enhance DNA-binding by XPC and promote NER (PubMed:15882621).
CC The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to
CC DNA damage, leading to its degradation: recognizes KAT7/HBO1 following
CC phosphorylation by ATR (PubMed:26572825). {ECO:0000269|PubMed:10882109,
CC ECO:0000269|PubMed:11278856, ECO:0000269|PubMed:11705987,
CC ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:12944386,
CC ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:15882621,
CC ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16473935,
CC ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18593899,
CC ECO:0000269|PubMed:26572825, ECO:0000269|PubMed:32789493,
CC ECO:0000269|PubMed:9892649}.
CC -!- FUNCTION: [Isoform D1]: Inhibits UV-damaged DNA repair.
CC {ECO:0000269|PubMed:14751237}.
CC -!- FUNCTION: [Isoform D2]: Inhibits UV-damaged DNA repair.
CC {ECO:0000269|PubMed:14751237}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2.
CC The UV-DDB complex interacts with monoubiquitinated histone H2A and
CC binds to XPC via the DDB2 subunit. Component of the DCX (DDB1-CUL4-X-
CC box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1 (also known as
CC CUL4-DDB-ROC1 and CUL4-DDB-RBX1), which includes CUL4A or CUL4B, DDB1,
CC DDB2 and RBX1. DDB2 may function as the substrate recognition module
CC within this complex. The DDB1-CUL4-ROC1 complex may associate with the
CC COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase
CC activity of the complex. A large number of other DCX complexes may also
CC exist in which an alternate substrate targeting subunit replaces DDB2.
CC These targeting subunits are generally known as DCAF (DDB1- and CUL4-
CC associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins.
CC Isoform D1 and isoform D2 do not interact with DDB1.
CC {ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:12732143,
CC ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:15882621,
CC ECO:0000269|PubMed:16223728, ECO:0000269|PubMed:16260596,
CC ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16527807,
CC ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17041588,
CC ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18593899,
CC ECO:0000269|PubMed:19109893, ECO:0000269|PubMed:19966799,
CC ECO:0000269|PubMed:22822215, ECO:0000269|PubMed:9632823}.
CC -!- INTERACTION:
CC Q92466; Q13619: CUL4A; NbExp=10; IntAct=EBI-1176171, EBI-456106;
CC Q92466; Q16531: DDB1; NbExp=20; IntAct=EBI-1176171, EBI-350322;
CC Q92466; Q01094: E2F1; NbExp=2; IntAct=EBI-1176171, EBI-448924;
CC Q92466; P40337-2: VHL; NbExp=3; IntAct=EBI-1176171, EBI-12157263;
CC Q92466; Q01831-1: XPC; NbExp=4; IntAct=EBI-1176171, EBI-15950383;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10777490,
CC ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11705987,
CC ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237,
CC ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16713579,
CC ECO:0000269|PubMed:17635991, ECO:0000269|PubMed:18593899}. Chromosome
CC {ECO:0000269|PubMed:32789493}. Note=Accumulates at sites of DNA damage
CC following UV irradiation. {ECO:0000269|PubMed:32789493}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q92466-1; Sequence=Displayed;
CC Name=D1;
CC IsoId=Q92466-2; Sequence=VSP_014675;
CC Name=D2;
CC IsoId=Q92466-3; Sequence=VSP_014676, VSP_014677;
CC Name=D3;
CC IsoId=Q92466-4; Sequence=VSP_014674;
CC Name=D4;
CC IsoId=Q92466-5; Sequence=VSP_014678, VSP_014679;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed; with highest levels in
CC corneal endothelium and lowest levels in brain. Isoform D1 is highly
CC expressed in brain and heart. Isoform D2, isoform D3 and isoform D4 are
CC weakly expressed. {ECO:0000269|PubMed:14751237}.
CC -!- INDUCTION: Expression is induced in response to treatment with IR or UV
CC and this requires p53/TP53 activity. {ECO:0000269|PubMed:10777490}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1.
CC {ECO:0000269|PubMed:17079684}.
CC -!- DOMAIN: Interblade loops of the WD repeat region mediate most of the
CC interaction with DNA. A hairpin between blades 5 and 6 inserts into DNA
CC minor groove and mediates recognition of lesions and separation of the
CC damaged and undamaged strands. {ECO:0000269|PubMed:17079684,
CC ECO:0000269|PubMed:19109893}.
CC -!- PTM: Phosphorylation by ABL1 negatively regulate UV-DDB activity.
CC {ECO:0000250|UniProtKB:Q99J79}.
CC -!- PTM: Ubiquitinated by CUL4A in response to UV irradiation.
CC Ubiquitination appears to both impair DNA-binding and promotes
CC ubiquitin-dependent proteolysis. Degradation of DDB2 at sites of DNA
CC damage may be a prerequisite for their recognition by XPC and
CC subsequent repair. CUL4A-mediated degradation appears to be promoted by
CC ABL1. {ECO:0000269|PubMed:23159851}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation, and
CC deubiquitinated by USP24. {ECO:0000269|PubMed:23159851}.
CC -!- PTM: Acetylated (PubMed:32789493). Deacetylation by SIRT6 in response
CC to UV stress facilitates nucleotide excision repair pathway (the NER
CC pathway) transduction (PubMed:32789493). {ECO:0000269|PubMed:32789493}.
CC -!- DISEASE: Xeroderma pigmentosum complementation group E (XP-E)
CC [MIM:278740]: An autosomal recessive pigmentary skin disorder
CC characterized by solar hypersensitivity of the skin, high
CC predisposition for developing cancers on areas exposed to sunlight and,
CC in some cases, neurological abnormalities. The skin develops marked
CC freckling and other pigmentation abnormalities. XP-E patients show a
CC mild phenotype with minimal or no neurologic features.
CC {ECO:0000269|PubMed:8798680}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/XPEID298.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ddb2/";
CC ---------------------------------------------------------------------------
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DR EMBL; U18300; AAB07897.1; -; mRNA.
DR EMBL; AB107037; BAD12557.1; -; mRNA.
DR EMBL; AB107038; BAD12558.1; -; mRNA.
DR EMBL; AB107039; BAD12559.1; -; mRNA.
DR EMBL; AB107040; BAD12560.1; -; mRNA.
DR EMBL; BT007139; AAP35803.1; -; mRNA.
DR EMBL; AY220533; AAO25655.1; -; Genomic_DNA.
DR EMBL; AK313262; BAG36072.1; -; mRNA.
DR EMBL; CH471064; EAW67952.1; -; Genomic_DNA.
DR EMBL; BC000093; AAH00093.1; -; mRNA.
DR CCDS; CCDS73284.1; -. [Q92466-2]
DR CCDS; CCDS7927.1; -. [Q92466-1]
DR PIR; I38909; I38909.
DR RefSeq; NP_000098.1; NM_000107.2. [Q92466-1]
DR RefSeq; NP_001287663.1; NM_001300734.1. [Q92466-2]
DR PDB; 3EI4; X-ray; 3.30 A; B/D/F=10-427.
DR PDB; 3I7L; X-ray; 2.80 A; B=68-81.
DR PDB; 4E54; X-ray; 2.85 A; B=2-427.
DR PDB; 4E5Z; X-ray; 3.22 A; B=2-427.
DR PDB; 6R8Y; EM; 4.30 A; L=1-427.
DR PDB; 6R8Z; EM; 3.90 A; L=1-427.
DR PDB; 6R90; EM; 4.50 A; L=1-427.
DR PDB; 6R91; EM; 4.10 A; L=1-427.
DR PDB; 6R92; EM; 4.80 A; L=1-427.
DR PDBsum; 3EI4; -.
DR PDBsum; 3I7L; -.
DR PDBsum; 4E54; -.
DR PDBsum; 4E5Z; -.
DR PDBsum; 6R8Y; -.
DR PDBsum; 6R8Z; -.
DR PDBsum; 6R90; -.
DR PDBsum; 6R91; -.
DR PDBsum; 6R92; -.
DR AlphaFoldDB; Q92466; -.
DR SMR; Q92466; -.
DR BioGRID; 108010; 139.
DR ComplexPortal; CPX-308; UV DNA damage recognition complex DBB1-DBB2.
DR ComplexPortal; CPX-477; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant.
DR ComplexPortal; CPX-648; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR CORUM; Q92466; -.
DR DIP; DIP-36670N; -.
DR IntAct; Q92466; 50.
DR STRING; 9606.ENSP00000256996; -.
DR GlyGen; Q92466; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92466; -.
DR PhosphoSitePlus; Q92466; -.
DR BioMuta; DDB2; -.
DR DMDM; 12230033; -.
DR EPD; Q92466; -.
DR jPOST; Q92466; -.
DR MassIVE; Q92466; -.
DR MaxQB; Q92466; -.
DR PaxDb; Q92466; -.
DR PeptideAtlas; Q92466; -.
DR PRIDE; Q92466; -.
DR ProteomicsDB; 75255; -. [Q92466-1]
DR ProteomicsDB; 75256; -. [Q92466-2]
DR ProteomicsDB; 75257; -. [Q92466-3]
DR ProteomicsDB; 75258; -. [Q92466-4]
DR ProteomicsDB; 75259; -. [Q92466-5]
DR Antibodypedia; 13582; 283 antibodies from 34 providers.
DR DNASU; 1643; -.
DR Ensembl; ENST00000256996.9; ENSP00000256996.4; ENSG00000134574.12. [Q92466-1]
DR Ensembl; ENST00000378600.7; ENSP00000367863.3; ENSG00000134574.12. [Q92466-2]
DR Ensembl; ENST00000378601.7; ENSP00000367864.3; ENSG00000134574.12. [Q92466-5]
DR Ensembl; ENST00000378603.7; ENSP00000367866.3; ENSG00000134574.12. [Q92466-4]
DR Ensembl; ENST00000616278.4; ENSP00000478411.1; ENSG00000134574.12. [Q92466-3]
DR GeneID; 1643; -.
DR KEGG; hsa:1643; -.
DR MANE-Select; ENST00000256996.9; ENSP00000256996.4; NM_000107.3; NP_000098.1.
DR UCSC; uc001neb.3; human. [Q92466-1]
DR CTD; 1643; -.
DR DisGeNET; 1643; -.
DR GeneCards; DDB2; -.
DR GeneReviews; DDB2; -.
DR HGNC; HGNC:2718; DDB2.
DR HPA; ENSG00000134574; Low tissue specificity.
DR MalaCards; DDB2; -.
DR MIM; 278740; phenotype.
DR MIM; 600811; gene.
DR neXtProt; NX_Q92466; -.
DR OpenTargets; ENSG00000134574; -.
DR Orphanet; 910; Xeroderma pigmentosum.
DR PharmGKB; PA27188; -.
DR VEuPathDB; HostDB:ENSG00000134574; -.
DR eggNOG; KOG4328; Eukaryota.
DR GeneTree; ENSGT00510000047881; -.
DR HOGENOM; CLU_036401_1_0_1; -.
DR InParanoid; Q92466; -.
DR OMA; FIKGKGP; -.
DR OrthoDB; 559605at2759; -.
DR PhylomeDB; Q92466; -.
DR TreeFam; TF331587; -.
DR PathwayCommons; Q92466; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q92466; -.
DR SIGNOR; Q92466; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 1643; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; DDB2; human.
DR EvolutionaryTrace; Q92466; -.
DR GeneWiki; DDB2; -.
DR GenomeRNAi; 1643; -.
DR Pharos; Q92466; Tbio.
DR PRO; PR:Q92466; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92466; protein.
DR Bgee; ENSG00000134574; Expressed in skin of abdomen and 151 other tissues.
DR ExpressionAtlas; Q92466; baseline and differential.
DR Genevisible; Q92466; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IMP:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IC:ComplexPortal.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0034644; P:cellular response to UV; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR033312; DDB2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15169; PTHR15169; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome;
KW Disease variant; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway; WD repeat; Xeroderma pigmentosum.
FT CHAIN 1..427
FT /note="DNA damage-binding protein 2"
FT /id="PRO_0000050953"
FT REPEAT 116..151
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REPEAT 159..194
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REPEAT 203..238
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REPEAT 244..287
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REPEAT 290..329
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REPEAT 343..386
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REPEAT 396..420
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:19109893"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..79
FT /note="Required for interaction with DDB1"
FT /evidence="ECO:0000269|PubMed:9632823"
FT REGION 87..98
FT /note="Required for interaction with DDB1"
FT /evidence="ECO:0000269|PubMed:9632823"
FT REGION 334..336
FT /note="Photolesion recognition"
FT MOTIF 256..274
FT /note="DWD box"
FT /evidence="ECO:0000269|PubMed:17079684"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:32789493"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:32789493"
FT VAR_SEQ 89..152
FT /note="Missing (in isoform D3)"
FT /evidence="ECO:0000303|PubMed:14751237"
FT /id="VSP_014674"
FT VAR_SEQ 153..341
FT /note="Missing (in isoform D1)"
FT /evidence="ECO:0000303|PubMed:14751237"
FT /id="VSP_014675"
FT VAR_SEQ 153..156
FT /note="IGAG -> HLVL (in isoform D2)"
FT /evidence="ECO:0000303|PubMed:14751237"
FT /id="VSP_014676"
FT VAR_SEQ 157..427
FT /note="Missing (in isoform D2)"
FT /evidence="ECO:0000303|PubMed:14751237"
FT /id="VSP_014677"
FT VAR_SEQ 236..244
FT /note="WNLRMHKKK -> VSVPMEPGS (in isoform D4)"
FT /evidence="ECO:0000303|PubMed:14751237"
FT /id="VSP_014678"
FT VAR_SEQ 245..427
FT /note="Missing (in isoform D4)"
FT /evidence="ECO:0000303|PubMed:14751237"
FT /id="VSP_014679"
FT VARIANT 215
FT /note="M -> T (in dbSNP:rs4647750)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016337"
FT VARIANT 244
FT /note="K -> E (in XP-E; impairs DNA-binding of the UV-DDB
FT complex; dbSNP:rs121434639)"
FT /evidence="ECO:0000269|PubMed:10777490,
FT ECO:0000269|PubMed:16223728, ECO:0000269|PubMed:8798680,
FT ECO:0000269|PubMed:9632823"
FT /id="VAR_010141"
FT VARIANT 273
FT /note="R -> H (in XP-E; impairs interaction with DDB1 and
FT CUL4A; dbSNP:rs121434640)"
FT /evidence="ECO:0000269|PubMed:10777490,
FT ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:16223728,
FT ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240,
FT ECO:0000269|PubMed:8798680, ECO:0000269|PubMed:9632823"
FT /id="VAR_010142"
FT VARIANT 293
FT /note="A -> T (in dbSNP:rs4647751)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016338"
FT MUTAGEN 35
FT /note="K->R: Decreased acetylation levels."
FT /evidence="ECO:0000269|PubMed:32789493"
FT MUTAGEN 40
FT /note="K->R: Does not affect acetylation levels."
FT /evidence="ECO:0000269|PubMed:32789493"
FT MUTAGEN 77
FT /note="K->R: Decreased acetylation levels."
FT /evidence="ECO:0000269|PubMed:32789493"
FT MUTAGEN 258
FT /note="L->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 262
FT /note="S->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 264
FT /note="D->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 269
FT /note="I->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 270
FT /note="W->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 272
FT /note="L->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 273
FT /note="R->A: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:17079684"
FT MUTAGEN 350
FT /note="L->P: Impairs interaction with DDB1."
FT /evidence="ECO:0000269|PubMed:16949367"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4E54"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4E54"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4E54"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3I7L"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 96..102
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3EI4"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4E5Z"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 221..232
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4E5Z"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4E5Z"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4E5Z"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3EI4"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 312..326
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4E5Z"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3EI4"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:4E54"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3EI4"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:4E54"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:4E54"
SQ SEQUENCE 427 AA; 47864 MW; E881F21242CA44D2 CRC64;
MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP
QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS YRILQKAAPF DRRATSLAWH
PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI KGIGAGGSIT GLKFNPLNTN QFYASSMEGT
TRLQDFKGNI LRVFASSDTI NIWFCSLDVS ASSRMVVTGD NVGNVILLNM DGKELWNLRM
HKKKVTHVAL NPCCDWFLAT ASVDQTVKIW DLRQVRGKAS FLYSLPHRHP VNAACFSPDG
ARLLTTDQKS EIRVYSASQW DCPLGLIPHP HRHFQHLTPI KAAWHPRYNL IVVGRYPDPN
FKSCTPYELR TIDVFDGNSG KMMCQLYDPE SSGISSLNEF NPMGDTLASA MGYHILIWSQ
EEARTRK
