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 17-JUN-2020, entry version 200. 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 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 [39] 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 [40] 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 [41] 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 [42] 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). Core component of the UV-DDB complex CC (UV-damaged DNA-binding protein complex), a complex that recognizes UV- CC induced DNA damage and recruit proteins of the nucleotide excision CC repair pathway (the NER pathway) to initiate DNA repair CC (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:16260596, CC PubMed:12944386, PubMed:14751237). The UV-DDB complex preferentially CC binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 CC PP), apurinic sites and short mismatches (PubMed:10882109, CC PubMed:11278856, PubMed:11705987, PubMed:16260596, PubMed:12944386). CC Also functions as the substrate recognition module for the DCX (DDB2- CC CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also CC known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1) (PubMed:12732143, CC PubMed:15882621, PubMed:16473935, PubMed:18593899, PubMed:26572825). CC The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and CC histone H4 at sites of UV-induced DNA damage (PubMed:16678110, CC PubMed:16473935). The ubiquitination of histones may facilitate their CC removal from the nucleosome and promote subsequent DNA repair CC (PubMed:16678110, PubMed:16473935). The DDB2-CUL4-ROC1 complex also CC ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER CC (PubMed:15882621). The DDB2-CUL4-ROC1 complex also ubiquitinates CC KAT7/HBO1 in response to DNA damage, leading to its degradation: CC recognizes KAT7/HBO1 following phosphorylation by ATR CC (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: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; 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}. CC Note=Accumulates at sites of DNA damage following UV irradiation. 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 -!- PTM: Phosphorylation by ABL1 negatively regulate UV-DDB activity. CC {ECO:0000250}. 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 -!- 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 mutations 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q92466; -. DR BioGRID; 108010; 104. 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; 49. DR STRING; 9606.ENSP00000256996; -. 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; 259 antibodies. DR DNASU; 1643; -. DR Ensembl; ENST00000256996; ENSP00000256996; ENSG00000134574. [Q92466-1] DR Ensembl; ENST00000378600; ENSP00000367863; ENSG00000134574. [Q92466-2] DR Ensembl; ENST00000378601; ENSP00000367864; ENSG00000134574. [Q92466-5] DR Ensembl; ENST00000378603; ENSP00000367866; ENSG00000134574. [Q92466-4] DR Ensembl; ENST00000616278; ENSP00000478411; ENSG00000134574. [Q92466-3] DR GeneID; 1643; -. DR KEGG; hsa:1643; -. DR UCSC; uc001neb.3; human. [Q92466-1] DR CTD; 1643; -. DR DisGeNET; 1643; -. DR EuPathDB; HostDB:ENSG00000134574.11; -. 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 eggNOG; ENOG410IMQS; Eukaryota. DR eggNOG; COG2319; LUCA. DR GeneTree; ENSGT00510000047881; -. DR HOGENOM; CLU_036401_1_0_1; -. DR InParanoid; Q92466; -. DR KO; K10140; -. DR OMA; FIKGKGP; -. DR OrthoDB; 559605at2759; -. DR PhylomeDB; Q92466; -. DR TreeFam; TF331587; -. 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; 5 hits in 792 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 183 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:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; 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:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome. DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; TAS:ProtInc. DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome. DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome. DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome. DR GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome. DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome. DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome. DR GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. DR GO; GO:0016579; P:protein deubiquitination; TAS:Reactome. 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; IPR017986; WD40_repeat_dom. 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; Alternative splicing; Disease mutation; DNA damage; KW DNA repair; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; KW 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 68..79 FT /note="Required for interaction with DDB1" FT REGION 87..98 FT /note="Required for interaction with DDB1" FT REGION 334..336 FT /note="Photolesion recognition" FT MOTIF 256..274 FT /note="DWD box" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:23186163" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163" 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 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:0000244|PDB:4E54" FT STRAND 30..32 FT /evidence="ECO:0000244|PDB:4E54" FT HELIX 39..42 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 44..47 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 49..51 FT /evidence="ECO:0000244|PDB:4E54" FT HELIX 58..62 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 63..65 FT /evidence="ECO:0000244|PDB:4E54" FT HELIX 69..77 FT /evidence="ECO:0000244|PDB:3I7L" FT HELIX 83..91 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 92..94 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 96..102 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 106..109 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 114..119 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 127..131 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 136..139 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 148..150 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 154..156 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 161..164 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 171..175 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 177..179 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 181..185 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 186..188 FT /evidence="ECO:0000244|PDB:3EI4" FT STRAND 190..195 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 198..201 FT /evidence="ECO:0000244|PDB:4E5Z" FT STRAND 207..210 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 211..214 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 215..219 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 221..232 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 241..243 FT /evidence="ECO:0000244|PDB:4E5Z" FT STRAND 245..250 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 252..254 FT /evidence="ECO:0000244|PDB:4E5Z" FT STRAND 255..262 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 263..265 FT /evidence="ECO:0000244|PDB:4E5Z" FT STRAND 269..271 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 272..274 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 277..279 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 282..286 FT /evidence="ECO:0000244|PDB:3EI4" FT STRAND 291..293 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 300..310 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 312..326 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 335..337 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 346..349 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 351..354 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 359..361 FT /evidence="ECO:0000244|PDB:4E5Z" FT STRAND 364..366 FT /evidence="ECO:0000244|PDB:3EI4" FT STRAND 372..375 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 377..379 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 382..386 FT /evidence="ECO:0000244|PDB:4E54" FT TURN 389..391 FT /evidence="ECO:0000244|PDB:3EI4" FT STRAND 397..400 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 407..410 FT /evidence="ECO:0000244|PDB:4E54" FT STRAND 412..417 FT /evidence="ECO:0000244|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 //