ID DDB1_HUMAN Reviewed; 1140 AA. AC Q16531; A6NG77; B2R648; B4DG00; O15176; Q13289; Q58F96; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 224. DE RecName: Full=DNA damage-binding protein 1; DE AltName: Full=DDB p127 subunit; DE AltName: Full=DNA damage-binding protein a; DE Short=DDBa; DE AltName: Full=Damage-specific DNA-binding protein 1; DE AltName: Full=HBV X-associated protein 1; DE Short=XAP-1; DE AltName: Full=UV-damaged DNA-binding factor; DE AltName: Full=UV-damaged DNA-binding protein 1; DE Short=UV-DDB 1; DE AltName: Full=XPE-binding factor; DE Short=XPE-BF; DE AltName: Full=Xeroderma pigmentosum group E-complementing protein; DE Short=XPCe; GN Name=DDB1; Synonyms=XAP1; 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, and Fetal lung; 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] (ISOFORM 1). RC TISSUE=Peripheral blood; RX PubMed=7815490; DOI=10.1128/jvi.69.2.1107-1114.1995; RA Lee T.H., Elledge S.J., Butel J.S.; RT "Hepatitis B virus X protein interacts with a probable cellular DNA repair RT protein."; RL J. Virol. 69:1107-1114(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8538642; DOI=10.1016/0921-8777(95)00040-2; RA Hwang B.J., Liao J.C., Chu G.; RT "Isolation of a cDNA encoding a UV-damaged DNA binding factor defective in RT xeroderma pigmentosum group E cells."; RL Mutat. Res. 362:105-117(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Skin; RA Huang S.L., Lin-Chao S., Chao C.K.; RT "Molecular cloning and characterization of human XPE protein: a component RT of UV-damaged DNA recognition activity."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Brain; 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 [GENOMIC DNA], AND VARIANT PHE-427. RG NIEHS SNPs program; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Skin; 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 [10] RP INTERACTION WITH DDB2, AND DNA-BINDING. 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 [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 INTERACTION WITH CUL4A, SUBCELLULAR LOCATION, AND UBIQUITINATION. 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 [13] RP INTERACTION WITH HBV X PROTEIN (MICROBIAL INFECTION). RX PubMed=11531405; DOI=10.1006/viro.2001.1036; RA Lin-Marq N., Bontron S., Leupin O., Strubin M.; RT "Hepatitis B virus X protein interferes with cell viability through RT interaction with the p127-kDa UV-damaged DNA-binding protein."; RL Virology 287:266-274(2001). RN [14] RP FUNCTION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION RP IN A COMPLEX WITH CUL4A; DDB2 AND RBX1, IDENTIFICATION IN THE CSA COMPLEX RP WITH CUL4A; ERCC8 AND RBX1, INTERACTION OF THE CSA COMPLEX WITH RNA RP POLYMERASE II, AND INTERACTION WITH THE COP9 SIGNALOSOME. 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 [15] RP INTERACTION WITH HBV X PROTEIN AND SV5 PROTEIN V (MICROBIAL INFECTION). RX PubMed=12743284; DOI=10.1128/jvi.77.11.6274-6283.2003; RA Leupin O., Bontron S., Strubin M.; RT "Hepatitis B virus X protein and simian virus 5 V protein exhibit similar RT UV-DDB1 binding properties to mediate distinct activities."; RL J. Virol. 77:6274-6283(2003). RN [16] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CDT1; RP CUL4A; RBX1 AND THE COP9 SIGNALOSOME. RX PubMed=15448697; DOI=10.1038/ncb1172; RA Hu J., McCall C.M., Ohta T., Xiong Y.; RT "Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response RT to DNA damage."; RL Nat. Cell Biol. 6:1003-1009(2004). RN [17] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CUL4A; RP DET1; RBX1 AND COP1. RX PubMed=14739464; DOI=10.1126/science.1093549; RA Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., RA Dixit V.M.; RT "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin RT ligase."; RL Science 303:1371-1374(2004). RN [18] RP FUNCTION, INTERACTION WITH CUL4A; DDB2 AND RBX1, AND DNA-BINDING. 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 DDB2, AND DNA-BINDING. 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 INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V (MICROBIAL INFECTION). RX PubMed=16227264; DOI=10.1128/jvi.79.21.13434-13441.2005; RA Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.; RT "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to RT facilitate the ubiquitination of STAT1."; RL J. Virol. 79:13434-13441(2005). RN [21] RP FUNCTION, INTERACTION WITH CUL4A; DDB2; 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 [22] RP FUNCTION. RX PubMed=16482215; DOI=10.1038/sj.emboj.7601002; RA Nishitani H., Sugimoto N., Roukos V., Nakanishi Y., Saijo M., Obuse C., RA Tsurimoto T., Nakayama K.I., Nakayama K., Fujita M., Lygerou Z., RA Nishimoto T.; RT "Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for RT proteolysis."; RL EMBO J. 25:1126-1136(2006). RN [23] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RP ATG16L1; BTRC; CUL4A; DDB2; ERCC8; FBXW5; FBXW8; GRWD1; KATNB1; NUP43; RP PWP1; RBBP4; RBBP7; COP1; DCAF1; DCAF11; WSB1 AND WSB2. 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 [24] RP FUNCTION. RX PubMed=16407242; DOI=10.1074/jbc.c500464200; RA Hu J., Xiong Y.; RT "An evolutionarily conserved function of proliferating cell nuclear antigen RT for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA RT damage."; RL J. Biol. Chem. 281:3753-3756(2006). RN [25] RP FUNCTION. RX PubMed=16407252; DOI=10.1074/jbc.m512705200; RA Senga T., Sivaprasad U., Zhu W., Park J.H., Arias E.E., Walter J.C., RA Dutta A.; RT "PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal RT ubiquitination."; RL J. Biol. Chem. 281:6246-6252(2006). RN [26] RP INTERACTION WITH CUL4A AND DDB2. 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 [27] RP IDENTIFICATION IN A COMPLEX WITH DDB2; CUL4A; CUL4B AND RBX1, RP IDENTIFICATION BY MASS SPECTROMETRY, 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 [28] RP INTERACTION WITH AMBRA1; DCAF17; DCAF16; DCAF15; DDA1; DDB2; DET1; DTL; RP ERCC8; DCAF6; PHIP; DCAF1; DCAF4; DCAF5; DCAF11; DCAF10; DCAF12; DCAF8; RP DCAF7 AND WDTC1, AND MUTAGENESIS OF 316-TYR--ASN-319; 840-GLU--GLU-842; RP 910-MET--TYR-913 AND TRP-953. 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 [29] RP FUNCTION. RX PubMed=16940174; DOI=10.1128/mcb.00819-06; RA Lovejoy C.A., Lock K., Yenamandra A., Cortez D.; RT "DDB1 maintains genome integrity through regulation of Cdt1."; RL Mol. Cell. Biol. 26:7977-7990(2006). RN [30] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CUL4B; RP DTL; NLE1; PAFAH1B1; RBBP5; COP1; SNRNP40; WDR5; WDR5B; WDR12; WDR26; RP WDR39; WDR53; WDR59 AND WDR61. 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 [31] RP FUNCTION, INTERACTION WITH CUL4A; DDB2; 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 [32] RP INTERACTION WITH AGO1 AND AGO2. RX PubMed=17932509; DOI=10.1038/sj.embor.7401088; RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., RA Urlaub H., Meister G.; RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein RT complexes in human cells."; RL EMBO Rep. 8:1052-1060(2007). RN [33] RP FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB2, 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 [34] RP FUNCTION, AND INTERACTION WITH FBXW5; TSC1 AND TSC2. RX PubMed=18381890; DOI=10.1101/gad.1624008; RA Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J., Xiong Y.; RT "WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by RT DDB1-CUL4-ROC1 ligase."; RL Genes Dev. 22:866-871(2008). RN [35] RP INTERACTION WITH DCAF1/VPRBP. RX PubMed=18606781; DOI=10.1128/mcb.00232-08; RA McCall C.M., Miliani de Marval P.L., Chastain P.D. II, Jackson S.C., RA He Y.J., Kotake Y., Cook J.G., Xiong Y.; RT "Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40 RT protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is essential for RT DNA replication and embryonic development."; RL Mol. Cell. Biol. 28:5621-5633(2008). RN [36] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NF2. RX PubMed=18332868; DOI=10.1038/onc.2008.44; RA Huang J., Chen J.; RT "VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for RT degradation."; RL Oncogene 27:4056-4064(2008). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [38] RP INTERACTION WITH EDVP COMPLEX. RX PubMed=19287380; DOI=10.1038/ncb1848; RA Maddika S., Chen J.; RT "Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 RT ligase."; RL Nat. Cell Biol. 11:409-419(2009). RN [39] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1067, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [40] 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 [41] RP INTERACTION WITH LRWD1. RX PubMed=22935713; DOI=10.4161/cc.21870; RA Shen Z., Prasanth S.G.; RT "Orc2 protects ORCA from ubiquitin-mediated degradation."; RL Cell Cycle 11:3578-3589(2012). RN [42] RP INTERACTION WITH DTL. RX PubMed=23478445; DOI=10.1016/j.molcel.2013.02.003; RA Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.; RT "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr- RT Set7/Set8-mediated cellular migration."; RL Mol. Cell 49:1147-1158(2013). RN [43] 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 [44] RP FUNCTION, AND INTERACTION WITH CRY1 AND CUL4A. RX PubMed=26431207; DOI=10.1371/journal.pone.0139725; RA Tong X., Zhang D., Guha A., Arthurs B., Cazares V., Gupta N., Yin L.; RT "CUL4-DDB1-CDT2 E3 ligase regulates the molecular clock activity by RT promoting ubiquitination-dependent degradation of the mammalian CRY1."; RL PLoS ONE 10:E0139725-E0139725(2015). RN [45] RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3 AND DCUN1D5. RX PubMed=26906416; DOI=10.1242/jcs.181784; RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.; RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases."; RL J. Cell Sci. 129:1441-1454(2016). RN [46] RP FUNCTION. RX PubMed=28790135; DOI=10.2337/db16-1600; RA Tong X., Zhang D., Charney N., Jin E., VanDommelen K., Stamper K., RA Gupta N., Saldate J., Yin L.; RT "DDB1-mediated CRY1 degradation promotes FOXO1-driven gluconeogenesis in RT liver."; RL Diabetes 66:2571-2582(2017). RN [47] RP FUNCTION, ACETYLATION, AND DEACETYLATION BY SIRT7. RX PubMed=28886238; DOI=10.1111/febs.14259; RA Mo Y., Lin R., Liu P., Tan M., Xiong Y., Guan K.L., Yuan H.X.; RT "SIRT7 deacetylates DDB1 and suppresses the activity of the CRL4 E3 ligase RT complexes."; RL FEBS J. 284:3619-3636(2017). RN [48] RP IDENTIFICATION IN THE DCX(DCAF15) COMPLEX. RX PubMed=28437394; DOI=10.1038/nchembio.2363; RA Uehara T., Minoshima Y., Sagane K., Sugi N.H., Mitsuhashi K.O., RA Yamamoto N., Kamiyama H., Takahashi K., Kotake Y., Uesugi M., Yokoi A., RA Inoue A., Yoshida T., Mabuchi M., Tanaka A., Owa T.; RT "Selective degradation of splicing factor CAPERalpha by anticancer RT sulfonamides."; RL Nat. Chem. Biol. 13:675-680(2017). RN [49] RP IDENTIFICATION IN THE DCX(DCAF15) COMPLEX. RX PubMed=28302793; DOI=10.1126/science.aal3755; RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y., RA Williams N.S., Nijhawan D.; RT "Anticancer sulfonamides target splicing by inducing RBM39 degradation via RT recruitment to DCAF15."; RL Science 356:0-0(2017). RN [50] RP ERRATUM OF PUBMED:28302793. RX PubMed=28546157; DOI=10.1126/science.aan7977; RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y., RA Williams N.S., Nijhawan D.; RL Science 356:0-0(2017). RN [51] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1121, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [52] RP IDENTIFICATION IN THE DCX(DCAF13) COMPLEX. RX PubMed=30111536; DOI=10.15252/embj.201898981; RA Zhang Y.L., Zhao L.W., Zhang J., Le R., Ji S.Y., Chen C., Gao Y., Li D., RA Gao S., Fan H.Y.; RT "DCAF13 promotes pluripotency by negatively regulating SUV39H1 stability RT during early embryonic development."; RL EMBO J. 37:0-0(2018). RN [53] RP IDENTIFICATION IN THE DCX(DCAF15) COMPLEX. RX PubMed=31693891; DOI=10.1016/j.celrep.2019.09.079; RA Ting T.C., Goralski M., Klein K., Wang B., Kim J., Xie Y., Nijhawan D.; RT "Aryl sulfonamides degrade RBM39 and RBM23 by recruitment to CRL4-DCAF15."; RL Cell Rep. 29:1499-1510(2019). RN [54] RP IDENTIFICATION IN THE DCX(DCAF13) COMPLEX. RX PubMed=31492966; DOI=10.1007/s00018-019-03280-5; RA Zhang J., Zhang Y.L., Zhao L.W., Pi S.B., Zhang S.Y., Tong C., Fan H.Y.; RT "The CRL4-DCAF13 ubiquitin E3 ligase supports oocyte meiotic resumption by RT targeting PTEN degradation."; RL Cell. Mol. Life Sci. 77:2181-2197(2020). RN [55] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL145 (MICROBIAL INFECTION). RX PubMed=32075763; DOI=10.1016/j.celrep.2020.01.070; RA Le-Trilling V.T.K., Becker T., Nachshon A., Stern-Ginossar N., Schoeler L., RA Voigt S., Hengel H., Trilling M.; RT "The Human Cytomegalovirus pUL145 Isoforms Act as Viral DDB1-Cullin- RT Associated Factors to Instruct Host Protein Degradation to Impede Innate RT Immunity."; RL Cell Rep. 30:2248-2260(2020). RN [56] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL145 (MICROBIAL INFECTION). RX PubMed=35938868; DOI=10.1128/jvi.00826-22; RA Wick E.T., Treadway C.J., Li Z., Nicely N.I., Ren Z., Baldwin A.S., RA Xiong Y., Harrison J.S., Brown N.G.; RT "Insight into Viral Hijacking of CRL4 Ubiquitin Ligase through Structural RT Analysis of the pUL145-DDB1 Complex."; RL J. Virol. 0:0-0(2022). RN [57] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-1140 IN COMPLEX WITH SIMIAN RP VIRUS 5 PROTEIN V, INTERACTION WITH CUL4A AND DET1, AND MUTAGENESIS OF RP GLU-537 AND TRP-561. RX PubMed=16413485; DOI=10.1016/j.cell.2005.10.033; RA Li T., Chen X., Garbutt K.C., Zhou P., Zheng N.; RT "Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack RT of a propeller cluster in ubiquitin ligase."; RL Cell 124:105-117(2006). RN [58] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-1140 IN COMPLEX WITH CUL4A; RBX1 RP AND SIMIAN VIRUS 5 PROTEIN V, AND INTERACTION WITH DDB2; DTL; DCAF11; DCAF8 RP AND WDTC1. 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 [59] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA, WD RP BETA-PROPELLER DOMAINS, AND SUBUNIT. 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 [60] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION AS UBIQUITIN LIGASE RP COMPONENT, SUBUNIT, INTERACTION WITH TRPC4AP; DCAF4; DCAF5; DCAF6; DCAF8; RP DCAF9; DCAF12; DDB2, AND INTERACTION WITH HEPATITIS VIRUS PROTEIN HBX RP (MICROBIAL INFECTION) AND PARAMYXOVIRUS PROTEIN SV5-V (MICROBIAL RP INFECTION). 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 [61] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEXES WITH DDB2; ERCC8 AND RP CUL4B, FUNCTION, AND SUBUNIT. RX PubMed=22118460; DOI=10.1016/j.cell.2011.10.035; RA Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., RA Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., RA Sugasawa K., Thoma N.H.; RT "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, RT targeting, and activation."; RL Cell 147:1024-1039(2011). RN [62] RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS), AND DOMAIN. RX PubMed=21468892; DOI=10.1007/s13238-011-1018-1; RA Xu C., Min J.; RT "Structure and function of WD40 domain proteins."; RL Protein Cell 2:202-214(2011). RN [63] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), SUBUNIT, AND INTERACTION WITH DDB2. 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 [64] RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CRBN, INTERACTION RP WITH CRBN, AND FUNCTION IN PROTEIN UBIQUITINATION. RX PubMed=25043012; DOI=10.1038/nature13527; RA Fischer E.S., Bohm K., Lydeard J.R., Yang H., Stadler M.B., Cavadini S., RA Nagel J., Serluca F., Acker V., Lingaraju G.M., Tichkule R.B., RA Schebesta M., Forrester W.C., Schirle M., Hassiepen U., Ottl J., Hild M., RA Beckwith R.E., Harper J.W., Jenkins J.L., Thoma N.H.; RT "Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with RT thalidomide."; RL Nature 512:49-53(2014). RN [65] RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH CRBN, INTERACTION RP WITH CRBN, AND FUNCTION. RX PubMed=25108355; DOI=10.1038/nsmb.2874; RA Chamberlain P.P., Lopez-Girona A., Miller K., Carmel G., Pagarigan B., RA Chie-Leon B., Rychak E., Corral L.G., Ren Y.J., Wang M., Riley M., RA Delker S.L., Ito T., Ando H., Mori T., Hirano Y., Handa H., Hakoshima T., RA Daniel T.O., Cathers B.E.; RT "Structure of the human cereblon-DDB1-lenalidomide complex reveals basis RT for responsiveness to thalidomide analogs."; RL Nat. Struct. Mol. Biol. 21:803-809(2014). RN [66] {ECO:0007744|PDB:6DSZ} RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) IN COMPLEX WITH DDA1. RX PubMed=30564455; DOI=10.1038/s41421-018-0064-8; RA Shabek N., Ruble J., Waston C.J., Garbutt K.C., Hinds T.R., Li T., RA Zheng N.; RT "Structural insights into DDA1 function as a core component of the CRL4- RT DDB1 ubiquitin ligase."; RL Cell Discov. 4:67-67(2018). RN [67] {ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V, ECO:0007744|PDB:6Q0W} RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-395 AND 706-1140 IN COMPLEX WITH RP DDA1 AND DCAF15, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX. RX PubMed=31686031; DOI=10.1038/s41589-019-0378-3; RA Faust T.B., Yoon H., Nowak R.P., Donovan K.A., Li Z., Cai Q., RA Eleuteri N.A., Zhang T., Gray N.S., Fischer E.S.; RT "Structural complementarity facilitates E7820-mediated degradation of RBM39 RT by DCAF15."; RL Nat. Chem. Biol. 16:7-14(2020). RN [68] {ECO:0007744|PDB:6SJ7, ECO:0007744|PDB:6UD7, ECO:0007744|PDB:6UE5} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 706-1140 IN COMPLEX WITH DDA1 AND RP DCAF15, STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) IN COMPLEX WITH RP DDA1 AND DCAF15, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX. RX PubMed=31819272; DOI=10.1038/s41589-019-0411-6; RA Bussiere D.E., Xie L., Srinivas H., Shu W., Burke A., Be C., Zhao J., RA Godbole A., King D., Karki R.G., Hornak V., Xu F., Cobb J., Carte N., RA Frank A.O., Frommlet A., Graff P., Knapp M., Fazal A., Okram B., Jiang S., RA Michellys P.Y., Beckwith R., Voshol H., Wiesmann C., Solomon J.M., RA Paulk J.; RT "Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 RT ligase complex."; RL Nat. Chem. Biol. 16:15-23(2020). RN [69] {ECO:0007744|PDB:6PAI} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH DCAF15; DDA1 AND RP RBM39, AND IDENTIFICATION IN THE DCX(DCAF15) COMPLEX. RX PubMed=31693911; DOI=10.1016/j.str.2019.10.005; RA Du X., Volkov O.A., Czerwinski R.M., Tan H., Huerta C., Morton E.R., RA Rizzi J.P., Wehn P.M., Xu R., Nijhawan D., Wallace E.M.; RT "Structural basis and kinetic pathway of RBM39 recruitment to DCAF15 by a RT sulfonamide molecular glue E7820."; RL Structure 27:1625-1633(2019). RN [70] RP VARIANTS WHIKERS 184-ASP--GLN-186 DEL; GLN-188; TRP-188; LYS-213 AND RP VAL-429, AND INVOLVEMENT IN WHIKERS. RX PubMed=33743206; DOI=10.1016/j.ajhg.2021.03.007; RG Care4Rare Canada Consortium; RA White S.M., Bhoj E., Nellaaker C., Lachmeijer A.M.A., Marshall A.E., RA Boycott K.M., Li D., Smith W., Hartley T., McBride A., Ernst M.E., RA May A.S., Wieczorek D., Abou Jamra R., Koch-Hogrebe M., Ounap K., RA Pajusalu S., van Gassen K.L.I., Sadedin S., Ellingwood S., Tan T.Y., RA Christodoulou J., Barea J., Lockhart P.J., Nezarati M.M., Kernohan K.D.; RT "A DNA repair disorder caused by de novo monoallelic DDB1 variants is RT associated with a neurodevelopmental syndrome."; RL Am. J. Hum. Genet. 108:749-756(2021). 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:15448697, PubMed:14739464, CC PubMed:16260596, PubMed:16482215, PubMed:17079684, PubMed:16407242, CC PubMed:16407252, PubMed:16940174). 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:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). 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:15448697, PubMed:16260596, PubMed:16407242, CC PubMed:16940174). Also functions as a component of numerous distinct CC DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which CC mediate the ubiquitination and subsequent proteasomal degradation of CC target proteins (PubMed:14739464, PubMed:16407252, PubMed:16482215, CC PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, CC PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:28886238). CC The functional specificity of the DCX E3 ubiquitin-protein ligase CC complex is determined by the variable substrate recognition component CC recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, CC PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, CC PubMed:18381890, PubMed:19966799, PubMed:22118460). DCX(DDB2) (also CC known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may CC ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV- CC induced DNA damage (PubMed:16678110, PubMed:17041588, PubMed:16473935, CC PubMed:18593899). The ubiquitination of histones may facilitate their CC removal from the nucleosome and promote subsequent DNA repair CC (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899). CC DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC CC and promote NER (PubMed:15882621). DCX(DTL) plays a role in PCNA- CC dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination CC of TP53 in response to radiation-induced DNA damage and during DNA CC replication (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a CC role in transcription-coupled repair (TCR) (PubMed:12732143). The DDB1- CC CUL4A-DTL E3 ligase complex regulates the circadian clock function by CC mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). CC DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and CC FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting CC on TET dioxygenses, essential for oocyte maintenance at the primordial CC follicle stage, hence essential for female fertility (By similarity). CC Maternal factor required for proper zygotic genome activation and CC genome reprogramming (By similarity). {ECO:0000250|UniProtKB:Q3U1J4, CC ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, CC ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15882621, CC ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16407242, CC ECO:0000269|PubMed:16407252, ECO:0000269|PubMed:16473935, CC ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:16678110, CC ECO:0000269|PubMed:16940174, ECO:0000269|PubMed:17041588, CC ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18332868, CC ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899, CC ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460, CC ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355, CC ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:28886238}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355}. CC -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2; CC the heterodimer dimerizes to give rise to a heterotetramer when bound CC to damaged DNA (PubMed:9632823, PubMed:16223728, PubMed:16527807, CC PubMed:19109893, PubMed:22822215). The UV-DDB complex interacts with CC monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit CC (PubMed:16473935). Component of numerous DCX (DDB1-CUL4-X-box) E3 CC ubiquitin-protein ligase complexes which consist of a core of DDB1, CC CUL4A or CUL4B and RBX1 (PubMed:11673459, PubMed:12732143, CC PubMed:15882621, PubMed:16678110, PubMed:18593899, PubMed:28886238, CC PubMed:28437394, PubMed:28302793, PubMed:31693891, PubMed:31686031, CC PubMed:31819272, PubMed:31693911). DDB1 may recruit specific substrate CC targeting subunits to the DCX complex (PubMed:11673459, CC PubMed:12732143, PubMed:15882621, PubMed:18593899, PubMed:28886238). CC These substrate targeting subunits are generally known as DCAF CC (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40- CC repeat) proteins (PubMed:17079684, PubMed:16949367, PubMed:18606781, CC PubMed:19608861, PubMed:16964240, PubMed:19966799). Interacts with CC AMBRA1, ATG16L1, BTRC, CRBN, DCAF1, DCAF4, DCAF5, DCAF6, DCAF7, DCAF8, CC DCAF9, DCAF10, DCAF11, DCAF12, DCAF15, DCAF16, DCAF17, DDA1, DET1, DTL, CC ERCC8, FBXW5, FBXW8, GRWD1, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, CC RBBP4, RBBP5, RBBP7, COP1, SNRNP40, DCAF1, WDR5, WDR5B, WDR12, WDR26, CC WDR39, WDR42, WDR53, WDR59, WDR61, WSB1, WSB2, LRWD1 and WDTC1 CC (PubMed:14739464, PubMed:17079684, PubMed:16949367, PubMed:17041588, CC PubMed:18606781, PubMed:22935713, PubMed:23478445, PubMed:22118460, CC PubMed:25043012, PubMed:25108355). DCX complexes may associate with the CC COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase CC activity of the complex (PubMed:15448697, PubMed:16260596). Interacts CC with NF2, TSC1 and TSC2 (PubMed:18332868, PubMed:18381890). Interacts CC with AGO1 and AGO2 (PubMed:17932509). Associates with the E3 ligase CC complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 proteins (EDVP CC complex) (PubMed:19287380). Interacts directly with DYRK2 CC (PubMed:19287380). DCX(DTL) complex interacts with FBXO11; does not CC ubiquitinate and degradate FBXO11 (PubMed:19287380). Interacts with CC TRPC4AP (PubMed:19966799). Interacts with CRY1 and CRY2 (By CC similarity). The DDB1-CUL4A complex interacts with CRY1 CC (PubMed:26431207). May also interact with DCUN1D1, DCUN1D2, DCUN1D3 and CC DCUN1D5 (PubMed:26906416). Component of the DCX(DCAF13) E3 ubiquitin CC ligase complex, at least composed of CUL4 (CUL4A or CUL4B), DDB1, CC DCAF13 and RBX1. Interacts with DCAF13 (via WD40 domain) CC (PubMed:30111536, PubMed:31492966). {ECO:0000250|UniProtKB:Q3U1J4, CC ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:12732143, CC ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, CC ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16223728, CC ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16473935, CC ECO:0000269|PubMed:16527807, ECO:0000269|PubMed:16678110, CC ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240, CC ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17079684, CC ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18332868, CC ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899, CC ECO:0000269|PubMed:18606781, ECO:0000269|PubMed:19109893, CC ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:19608861, CC ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460, CC ECO:0000269|PubMed:22822215, ECO:0000269|PubMed:22935713, CC ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:25043012, CC ECO:0000269|PubMed:25108355, ECO:0000269|PubMed:26431207, CC ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:28302793, CC ECO:0000269|PubMed:28437394, ECO:0000269|PubMed:28886238, CC ECO:0000269|PubMed:30111536, ECO:0000269|PubMed:31492966, CC ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31693891, CC ECO:0000269|PubMed:31693911, ECO:0000269|PubMed:31819272, CC ECO:0000269|PubMed:9632823}. CC -!- SUBUNIT: (Microbial infection) Interacts with Simian virus 5 protein V. CC {ECO:0000269|PubMed:11531405, ECO:0000269|PubMed:12743284, CC ECO:0000269|PubMed:16227264, ECO:0000269|PubMed:16413485, CC ECO:0000269|PubMed:19966799}. CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus protein CC HBX; the viral protein contains a short helical motif that competes for CC the same binding site as the N-terminal helical motif found in CC endogenous DCAF proteins. {ECO:0000269|PubMed:12743284, CC ECO:0000269|PubMed:19966799}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC protein UL145; this interaction promotes STAT2 degradation. CC {ECO:0000269|PubMed:32075763, ECO:0000269|PubMed:35938868}. CC -!- INTERACTION: CC Q16531; Q9H9F9: ACTR5; NbExp=4; IntAct=EBI-350322, EBI-769418; CC Q16531; Q96SW2: CRBN; NbExp=3; IntAct=EBI-350322, EBI-2510250; CC Q16531; Q96SW2-2: CRBN; NbExp=7; IntAct=EBI-350322, EBI-10693561; CC Q16531; Q13619: CUL4A; NbExp=15; IntAct=EBI-350322, EBI-456106; CC Q16531; Q13620: CUL4B; NbExp=26; IntAct=EBI-350322, EBI-456067; CC Q16531; Q9Y4B6: DCAF1; NbExp=3; IntAct=EBI-350322, EBI-1996353; CC Q16531; Q9Y4B6-3: DCAF1; NbExp=2; IntAct=EBI-350322, EBI-9915372; CC Q16531; Q8TEB1: DCAF11; NbExp=2; IntAct=EBI-350322, EBI-2213388; CC Q16531; Q8WV16: DCAF4; NbExp=5; IntAct=EBI-350322, EBI-2559135; CC Q16531; Q5TAQ9: DCAF8; NbExp=6; IntAct=EBI-350322, EBI-740686; CC Q16531; Q9BW61: DDA1; NbExp=4; IntAct=EBI-350322, EBI-2510241; CC Q16531; Q92466: DDB2; NbExp=20; IntAct=EBI-350322, EBI-1176171; CC Q16531; Q9NZJ0: DTL; NbExp=3; IntAct=EBI-350322, EBI-1176075; CC Q16531; O75530: EED; NbExp=4; IntAct=EBI-350322, EBI-923794; CC Q16531; Q969U6-1: FBXW5; NbExp=3; IntAct=EBI-350322, EBI-16031873; CC Q16531; Q9ULG1: INO80; NbExp=5; IntAct=EBI-350322, EBI-769345; CC Q16531; Q96JM7: L3MBTL3; NbExp=2; IntAct=EBI-350322, EBI-2686809; CC Q16531; P42224: STAT1; NbExp=2; IntAct=EBI-350322, EBI-1057697; CC Q16531; Q04725: TLE2; NbExp=2; IntAct=EBI-350322, EBI-1176061; CC Q16531; Q8N5D0-4: WDTC1; NbExp=3; IntAct=EBI-350322, EBI-15821254; CC Q16531; P11207: P/V; Xeno; NbExp=4; IntAct=EBI-350322, EBI-6148694; CC Q16531; Q72500: vpr; Xeno; NbExp=4; IntAct=EBI-350322, EBI-15626381; CC Q16531; P18045: vpx; Xeno; NbExp=2; IntAct=EBI-350322, EBI-6558105; CC Q16531; Q89246: X; Xeno; NbExp=2; IntAct=EBI-350322, EBI-15821216; CC Q16531; Q9QMH9: x; Xeno; NbExp=3; IntAct=EBI-350322, EBI-15821282; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777491, CC ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:18593899}. Nucleus CC {ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11673459, CC ECO:0000269|PubMed:18593899}. Note=Primarily cytoplasmic CC (PubMed:10777491, PubMed:11673459). Translocates to the nucleus CC following UV irradiation and subsequently accumulates at sites of DNA CC damage (PubMed:10777491, PubMed:11673459). More concentrated in nuclei CC than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and CC the 2-cell stage, but distributed in the cytoplasm at the MII-stage CC oocytes (By similarity). {ECO:0000250|UniProtKB:Q3U1J4, CC ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11673459}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q16531-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16531-2; Sequence=VSP_055540; CC -!- DOMAIN: The core of the protein consists of three WD40 beta-propeller CC domains. {ECO:0000269|PubMed:21468892}. CC -!- PTM: Phosphorylated by ABL1. {ECO:0000250|UniProtKB:Q3U1J4}. CC -!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin- CC dependent proteolysis. {ECO:0000269|PubMed:11673459}. CC -!- PTM: Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and CC subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein CC ligase complexes (PubMed:28886238). Deacetylation by SIRT7 impairs the CC interaction with CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4- CC X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238). CC {ECO:0000269|PubMed:28886238}. CC -!- DISEASE: White-Kernohan syndrome (WHIKERS) [MIM:619426]: An autosomal CC dominant disorder characterized by global developmental delay, variably CC impaired intellectual development, hypotonia, and characteristic facial CC features. Some patients may have genitourinary and skeletal CC abnormalities. {ECO:0000269|PubMed:33743206}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ddb1/"; 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; U18299; AAC50349.1; -; mRNA. DR EMBL; L40326; AAA62838.1; -; mRNA. DR EMBL; U32986; AAA88883.1; -; mRNA. DR EMBL; AJ002955; CAA05770.1; -; mRNA. DR EMBL; AK294341; BAG57611.1; -; mRNA. DR EMBL; AK312436; BAG35345.1; -; mRNA. DR EMBL; AY960579; AAX44048.1; -; Genomic_DNA. DR EMBL; AP003037; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW73935.1; -; Genomic_DNA. DR EMBL; BC011686; AAH11686.1; -; mRNA. DR EMBL; BC050530; AAH50530.1; -; mRNA. DR EMBL; BC051764; AAH51764.1; -; mRNA. DR CCDS; CCDS31576.1; -. [Q16531-1] DR PIR; I38908; I38908. DR RefSeq; NP_001914.3; NM_001923.4. [Q16531-1] DR PDB; 2B5L; X-ray; 2.85 A; A/B=1-1140. DR PDB; 2B5M; X-ray; 2.92 A; A=1-1140. DR PDB; 2B5N; X-ray; 2.80 A; A/B/C/D=391-709. DR PDB; 2HYE; X-ray; 3.10 A; A=1-1140. DR PDB; 3E0C; X-ray; 2.41 A; A=1-1140. DR PDB; 3EI1; X-ray; 2.80 A; A=1-1140. DR PDB; 3EI2; X-ray; 2.60 A; A=1-1140. DR PDB; 3EI3; X-ray; 2.30 A; A=1-1140. DR PDB; 3EI4; X-ray; 3.30 A; A/C/E=1-1140. DR PDB; 3I7H; X-ray; 2.90 A; A=1-1140. DR PDB; 3I7K; X-ray; 2.80 A; A=1-1140. DR PDB; 3I7L; X-ray; 2.80 A; A=1-1140. DR PDB; 3I7N; X-ray; 2.80 A; A=1-1140. DR PDB; 3I7O; X-ray; 2.80 A; A=1-1140. DR PDB; 3I7P; X-ray; 3.00 A; A=1-1140. DR PDB; 3I89; X-ray; 3.00 A; A=1-1140. DR PDB; 3I8C; X-ray; 2.80 A; A=1-1140. DR PDB; 3I8E; X-ray; 3.40 A; A/B=1-1140. DR PDB; 4A08; X-ray; 3.00 A; A=1-1140. DR PDB; 4A09; X-ray; 3.10 A; A=1-1140. DR PDB; 4A0A; X-ray; 3.60 A; A=1-1140. DR PDB; 4A0B; X-ray; 3.80 A; A/C=1-1140. DR PDB; 4A0K; X-ray; 5.93 A; C=1-1140. DR PDB; 4A0L; X-ray; 7.40 A; A/C=1-1140. DR PDB; 4A11; X-ray; 3.31 A; A=1-1140. DR PDB; 4CI1; X-ray; 2.98 A; A=1-1140. DR PDB; 4CI2; X-ray; 2.95 A; A=1-1140. DR PDB; 4CI3; X-ray; 3.50 A; A=1-1140. DR PDB; 4E54; X-ray; 2.85 A; A=2-1140. DR PDB; 4E5Z; X-ray; 3.22 A; A=2-1140. DR PDB; 4TZ4; X-ray; 3.01 A; A=2-1140. DR PDB; 5FQD; X-ray; 2.45 A; A/D=1-395, A/D=709-1140. DR PDB; 5HXB; X-ray; 3.60 A; B/Y=1-1140. DR PDB; 5JK7; X-ray; 3.49 A; A/B=1-1140. DR PDB; 5V3O; X-ray; 3.20 A; A=1-1140. DR PDB; 6BN7; X-ray; 3.50 A; A=1-395, A=706-1140. DR PDB; 6BN8; X-ray; 3.99 A; A=1-395, A=706-1140. DR PDB; 6BN9; X-ray; 4.38 A; A=1-395, A=706-1140. DR PDB; 6BNB; X-ray; 6.34 A; A=1-395, A=706-1140. DR PDB; 6BOY; X-ray; 3.33 A; A=1-395, A=706-1140. DR PDB; 6DSZ; X-ray; 3.09 A; A/B=1-1140. DR PDB; 6FCV; X-ray; 2.92 A; A=1-1140. DR PDB; 6H0F; X-ray; 3.25 A; A/D/G/J=1-395, A/D/G/J=706-1140. DR PDB; 6H0G; X-ray; 4.25 A; A/D=1-1140. DR PDB; 6PAI; X-ray; 2.90 A; A=1-1140. DR PDB; 6Q0R; X-ray; 2.90 A; A=1-395, A=706-1140. DR PDB; 6Q0V; X-ray; 2.90 A; A=1-395, A=706-1140. DR PDB; 6Q0W; X-ray; 2.90 A; A=1-395, A=706-1140. DR PDB; 6R8Y; EM; 4.30 A; K=1-1140. DR PDB; 6R8Z; EM; 3.90 A; K=1-1140. DR PDB; 6R90; EM; 4.50 A; K=1-1140. DR PDB; 6R91; EM; 4.10 A; K=1-1140. DR PDB; 6R92; EM; 4.80 A; K=1-395, K=706-1140. DR PDB; 6SJ7; EM; 3.54 A; B=1-1140. DR PDB; 6TD3; X-ray; 3.46 A; A/D/G=1-395, A/D/G=708-1140. DR PDB; 6UD7; X-ray; 2.30 A; B=1-395, B=706-1140. DR PDB; 6UE5; X-ray; 2.61 A; B=1-395, B=706-1140. DR PDB; 6UML; X-ray; 3.58 A; A=1-1140. DR PDB; 6XK9; X-ray; 3.64 A; B/Y=1-1140. DR PDB; 6ZUE; X-ray; 3.09 A; A=1-1140. DR PDB; 6ZX9; X-ray; 2.52 A; A=1-1140. DR PDB; 7LPS; X-ray; 3.78 A; A/D/G/J=1-1140. DR PDB; 7OKQ; EM; 8.40 A; A/E/I/M=1-1140. DR PDB; 7OO3; EM; 2.80 A; d=1-1140. DR PDB; 7OOB; EM; 2.70 A; d=1-1140. DR PDB; 7OOP; EM; 2.90 A; d=1-1140. DR PDB; 7OPC; EM; 3.00 A; d=1-1140. DR PDB; 7OPD; EM; 3.00 A; d=1-1140. DR PDB; 7U8F; X-ray; 3.15 A; B/E=1-395, B/E=706-1140. DR PDB; 7UKN; X-ray; 2.90 A; A=1-1140. DR PDB; 7V7B; EM; 4.20 A; B/D=1-1140. DR PDB; 7V7C; EM; 3.70 A; B/F=1-1140. DR PDB; 7ZN7; EM; 3.78 A; A=1-396, A=706-1140. DR PDB; 7ZNN; EM; 4.80 A; A=1-396, A=706-1140. DR PDB; 8AJM; EM; 2.83 A; A=1-1140. DR PDB; 8AJN; EM; 3.00 A; A=1-1140. DR PDB; 8AJO; EM; 30.60 A; A=1-1140. DR PDB; 8B3D; EM; 2.60 A; d=1-1140. DR PDB; 8B3F; EM; 3.10 A; d=1-1140. DR PDB; 8B3I; EM; 3.50 A; d=1-1140. DR PDB; 8BU1; X-ray; 2.98 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BU2; X-ray; 3.13 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BU3; X-ray; 3.42 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BU4; X-ray; 3.09 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BU5; X-ray; 3.13 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BU6; X-ray; 3.45 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BU7; X-ray; 3.25 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BU9; X-ray; 3.51 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUA; X-ray; 3.19 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUB; X-ray; 3.42 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUC; X-ray; 3.85 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUD; X-ray; 3.20 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUE; X-ray; 3.25 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUF; X-ray; 3.30 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUG; X-ray; 3.53 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUH; X-ray; 3.79 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUI; X-ray; 3.50 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUJ; X-ray; 3.62 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUK; X-ray; 3.41 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUL; X-ray; 3.40 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUM; X-ray; 3.36 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUN; X-ray; 3.08 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUO; X-ray; 3.58 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUP; X-ray; 3.41 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUQ; X-ray; 3.20 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUR; X-ray; 3.64 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8BUS; X-ray; 3.26 A; A/D/G=1-395, A/D/G=706-1140. DR PDB; 8BUT; X-ray; 3.25 A; A/D/G=1-395, A/D/G=709-1140. DR PDB; 8CVP; EM; 3.40 A; A=1-1140. DR PDB; 8D7U; EM; 3.10 A; A=1-1140. DR PDB; 8D7V; EM; 3.20 A; A=1-1140. DR PDB; 8D7W; EM; 3.10 A; A=1-1140. DR PDB; 8D7X; EM; 3.40 A; A=1-1140. DR PDB; 8D7Y; EM; 3.40 A; A=1-1140. DR PDB; 8D7Z; EM; 3.10 A; A=1-1140. DR PDB; 8D80; EM; 3.60 A; A=1-1140. DR PDB; 8D81; EM; 3.90 A; A=1-395, A=706-1140. DR PDB; 8DEY; X-ray; 3.70 A; B/E=1-395, B/E=706-1140. DR PDB; 8G46; EM; 2.20 A; A=1-395, A=706-1140. DR PDB; 8OIZ; X-ray; 2.50 A; A=1-1140. DR PDB; 8OJH; X-ray; 2.72 A; A=1-1140. DR PDB; 8OV6; EM; 3.77 A; A=1-1140. DR PDBsum; 2B5L; -. DR PDBsum; 2B5M; -. DR PDBsum; 2B5N; -. DR PDBsum; 2HYE; -. DR PDBsum; 3E0C; -. DR PDBsum; 3EI1; -. DR PDBsum; 3EI2; -. DR PDBsum; 3EI3; -. DR PDBsum; 3EI4; -. DR PDBsum; 3I7H; -. DR PDBsum; 3I7K; -. DR PDBsum; 3I7L; -. DR PDBsum; 3I7N; -. DR PDBsum; 3I7O; -. DR PDBsum; 3I7P; -. DR PDBsum; 3I89; -. DR PDBsum; 3I8C; -. DR PDBsum; 3I8E; -. DR PDBsum; 4A08; -. DR PDBsum; 4A09; -. DR PDBsum; 4A0A; -. DR PDBsum; 4A0B; -. DR PDBsum; 4A0K; -. DR PDBsum; 4A0L; -. DR PDBsum; 4A11; -. DR PDBsum; 4CI1; -. DR PDBsum; 4CI2; -. DR PDBsum; 4CI3; -. DR PDBsum; 4E54; -. DR PDBsum; 4E5Z; -. DR PDBsum; 4TZ4; -. DR PDBsum; 5FQD; -. DR PDBsum; 5HXB; -. DR PDBsum; 5JK7; -. DR PDBsum; 5V3O; -. DR PDBsum; 6BN7; -. DR PDBsum; 6BN8; -. DR PDBsum; 6BN9; -. DR PDBsum; 6BNB; -. DR PDBsum; 6BOY; -. DR PDBsum; 6DSZ; -. DR PDBsum; 6FCV; -. DR PDBsum; 6H0F; -. DR PDBsum; 6H0G; -. DR PDBsum; 6PAI; -. DR PDBsum; 6Q0R; -. DR PDBsum; 6Q0V; -. DR PDBsum; 6Q0W; -. DR PDBsum; 6R8Y; -. DR PDBsum; 6R8Z; -. DR PDBsum; 6R90; -. DR PDBsum; 6R91; -. DR PDBsum; 6R92; -. DR PDBsum; 6SJ7; -. DR PDBsum; 6TD3; -. DR PDBsum; 6UD7; -. DR PDBsum; 6UE5; -. DR PDBsum; 6UML; -. DR PDBsum; 6XK9; -. DR PDBsum; 6ZUE; -. DR PDBsum; 6ZX9; -. DR PDBsum; 7LPS; -. DR PDBsum; 7OKQ; -. DR PDBsum; 7OO3; -. DR PDBsum; 7OOB; -. DR PDBsum; 7OOP; -. DR PDBsum; 7OPC; -. DR PDBsum; 7OPD; -. DR PDBsum; 7U8F; -. DR PDBsum; 7UKN; -. DR PDBsum; 7V7B; -. DR PDBsum; 7V7C; -. DR PDBsum; 7ZN7; -. DR PDBsum; 7ZNN; -. DR PDBsum; 8AJM; -. DR PDBsum; 8AJN; -. DR PDBsum; 8AJO; -. DR PDBsum; 8B3D; -. DR PDBsum; 8B3F; -. DR PDBsum; 8B3I; -. DR PDBsum; 8BU1; -. DR PDBsum; 8BU2; -. DR PDBsum; 8BU3; -. DR PDBsum; 8BU4; -. DR PDBsum; 8BU5; -. DR PDBsum; 8BU6; -. DR PDBsum; 8BU7; -. DR PDBsum; 8BU9; -. DR PDBsum; 8BUA; -. DR PDBsum; 8BUB; -. DR PDBsum; 8BUC; -. DR PDBsum; 8BUD; -. DR PDBsum; 8BUE; -. DR PDBsum; 8BUF; -. DR PDBsum; 8BUG; -. DR PDBsum; 8BUH; -. DR PDBsum; 8BUI; -. DR PDBsum; 8BUJ; -. DR PDBsum; 8BUK; -. DR PDBsum; 8BUL; -. DR PDBsum; 8BUM; -. DR PDBsum; 8BUN; -. DR PDBsum; 8BUO; -. DR PDBsum; 8BUP; -. DR PDBsum; 8BUQ; -. DR PDBsum; 8BUR; -. DR PDBsum; 8BUS; -. DR PDBsum; 8BUT; -. DR PDBsum; 8CVP; -. DR PDBsum; 8D7U; -. DR PDBsum; 8D7V; -. DR PDBsum; 8D7W; -. DR PDBsum; 8D7X; -. DR PDBsum; 8D7Y; -. DR PDBsum; 8D7Z; -. DR PDBsum; 8D80; -. DR PDBsum; 8D81; -. DR PDBsum; 8DEY; -. DR PDBsum; 8G46; -. DR PDBsum; 8OIZ; -. DR PDBsum; 8OJH; -. DR PDBsum; 8OV6; -. DR AlphaFoldDB; Q16531; -. DR EMDB; EMD-10213; -. DR EMDB; EMD-12964; -. DR EMDB; EMD-13004; -. DR EMDB; EMD-13009; -. DR EMDB; EMD-13010; -. DR EMDB; EMD-13015; -. DR EMDB; EMD-13016; -. DR EMDB; EMD-14802; -. DR EMDB; EMD-14812; -. DR EMDB; EMD-15484; -. DR EMDB; EMD-15485; -. DR EMDB; EMD-15486; -. DR EMDB; EMD-15825; -. DR EMDB; EMD-15826; -. DR EMDB; EMD-15829; -. DR EMDB; EMD-17172; -. DR EMDB; EMD-20553; -. DR EMDB; EMD-27012; -. DR EMDB; EMD-27234; -. DR EMDB; EMD-27235; -. DR EMDB; EMD-27236; -. DR EMDB; EMD-27237; -. DR EMDB; EMD-27238; -. DR EMDB; EMD-27240; -. DR EMDB; EMD-27241; -. DR EMDB; EMD-27242; -. DR EMDB; EMD-29714; -. DR EMDB; EMD-31765; -. DR EMDB; EMD-31766; -. DR EMDB; EMD-3313; -. DR EMDB; EMD-3314; -. DR EMDB; EMD-3315; -. DR EMDB; EMD-3316; -. DR EMDB; EMD-4762; -. DR EMDB; EMD-4763; -. DR EMDB; EMD-4764; -. DR EMDB; EMD-4765; -. DR EMDB; EMD-4766; -. DR SMR; Q16531; -. DR BioGRID; 108009; 652. DR ComplexPortal; CPX-2399; CRL4-DCAF13 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2403; CRL4-DCAF11 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2404; CRL4-DCAF11 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2405; CRL4-DCAF12 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2406; CRL4-DCAF12 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2407; CRL4-DCAF13 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2411; CRL4-DCAF14 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2412; CRL4-DCAF14 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2413; CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2414; CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2415; CRL4-DCAF17 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2416; CRL4-DCAF17 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2757; CRL4-ERCC8 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2758; CRL4-ERCC8 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2759; CRL4-CRBN E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2762; CRL4-CRBN E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2765; CRL4-DCAF15 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2766; CRL4-DCAF15 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2769; CRL4-DCAF1 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2770; CRL4-DCAF1 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2777; CRL4-CDT2 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2778; CRL4-AMBRA1 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2782; CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2783; CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2784; CRL4-DCAF6 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2785; CRL4-DCAF7 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2786; CRL4-DCAF7 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2787; CRL4-DCAF9 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2795; CRL4-CDT2 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2797; CRL4-AMBRA1 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2799; CRL4-DCAF4 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2804; CRL4-DCAF6 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2809; CRL4-DCAF9 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2816; CRL4-DCAF8 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2817; CRL4-DCAF10 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2818; CRL4-DCAF8 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2819; CRL4-DCAF10 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2859; CRL4-DCAF4 E3 ubiquitin ligase complex, CUL4B variant. 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; Q16531; -. DR DIP; DIP-430N; -. DR IntAct; Q16531; 170. DR MINT; Q16531; -. DR STRING; 9606.ENSP00000301764; -. DR BindingDB; Q16531; -. DR ChEMBL; CHEMBL3833061; -. DR ChEMBL; CHEMBL4888446; -. DR GlyCosmos; Q16531; 1 site, 1 glycan. DR GlyGen; Q16531; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q16531; -. DR MetOSite; Q16531; -. DR PhosphoSitePlus; Q16531; -. DR SwissPalm; Q16531; -. DR BioMuta; DDB1; -. DR DMDM; 12643730; -. DR EPD; Q16531; -. DR jPOST; Q16531; -. DR MassIVE; Q16531; -. DR MaxQB; Q16531; -. DR PaxDb; 9606-ENSP00000301764; -. DR PeptideAtlas; Q16531; -. DR ProteomicsDB; 4092; -. DR ProteomicsDB; 60895; -. [Q16531-1] DR Pumba; Q16531; -. DR Antibodypedia; 14613; 586 antibodies from 46 providers. DR DNASU; 1642; -. DR Ensembl; ENST00000301764.12; ENSP00000301764.7; ENSG00000167986.15. [Q16531-1] DR Ensembl; ENST00000680367.1; ENSP00000506223.1; ENSG00000167986.15. [Q16531-1] DR Ensembl; ENST00000681803.1; ENSP00000506685.1; ENSG00000167986.15. [Q16531-1] DR GeneID; 1642; -. DR KEGG; hsa:1642; -. DR MANE-Select; ENST00000301764.12; ENSP00000301764.7; NM_001923.5; NP_001914.3. DR UCSC; uc001nrc.6; human. [Q16531-1] DR AGR; HGNC:2717; -. DR CTD; 1642; -. DR DisGeNET; 1642; -. DR GeneCards; DDB1; -. DR HGNC; HGNC:2717; DDB1. DR HPA; ENSG00000167986; Low tissue specificity. DR MalaCards; DDB1; -. DR MIM; 600045; gene. DR MIM; 619426; phenotype. DR neXtProt; NX_Q16531; -. DR OpenTargets; ENSG00000167986; -. DR PharmGKB; PA27187; -. DR VEuPathDB; HostDB:ENSG00000167986; -. DR eggNOG; KOG1897; Eukaryota. DR GeneTree; ENSGT00950000183151; -. DR HOGENOM; CLU_002893_0_1_1; -. DR InParanoid; Q16531; -. DR OMA; HQDFLMR; -. DR OrthoDB; 226997at2759; -. DR PhylomeDB; Q16531; -. DR TreeFam; TF105840; -. DR PathwayCommons; Q16531; -. DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex. 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-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER). DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; Q16531; -. DR SIGNOR; Q16531; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 1642; 824 hits in 1173 CRISPR screens. DR ChiTaRS; DDB1; human. DR EvolutionaryTrace; Q16531; -. DR GeneWiki; DDB1; -. DR GenomeRNAi; 1642; -. DR Pharos; Q16531; Tbio. DR PRO; PR:Q16531; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q16531; Protein. DR Bgee; ENSG00000167986; Expressed in right adrenal gland and 206 other cell types or tissues. DR ExpressionAtlas; Q16531; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProt. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central. DR GO; GO:0097602; F:cullin family protein binding; IDA:UniProt. 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:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB. DR GO; GO:0160072; F:ubiquitin ligase complex scaffold activity; IDA:UniProt. DR GO; GO:0071987; F:WD40-repeat domain binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IDA:AgBase. DR GO; GO:0034644; P:cellular response to UV; EXP:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl. DR GO; GO:0044725; P:epigenetic programming in the zygotic pronuclei; IDA:UniProt. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl. DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl. DR GO; GO:0006289; P:nucleotide-excision repair; TAS:ProtInc. DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IMP:AgBase. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; ISS:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProt. DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase. DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:MGI. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProt. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl. DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IDA:UniProt. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0070914; P:UV-damage excision repair; IDA:UniProtKB. DR GO; GO:0019076; P:viral release from host cell; IMP:AgBase. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl. DR Gene3D; 1.10.150.910; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3. DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C. DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR10644:SF3; DNA DAMAGE-BINDING PROTEIN 1; 1. DR PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1. DR Pfam; PF03178; CPSF_A; 1. DR Pfam; PF10433; MMS1_N; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR Genevisible; Q16531; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Biological rhythms; KW Cytoplasm; Disease variant; DNA damage; DNA repair; DNA-binding; KW Host-virus interaction; Intellectual disability; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; KW Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..1140 FT /note="DNA damage-binding protein 1" FT /id="PRO_0000079840" FT REGION 2..768 FT /note="Interaction with CDT1" FT /evidence="ECO:0000269|PubMed:15448697" FT REGION 13..356 FT /note="WD repeat beta-propeller A" FT REGION 392..708 FT /note="WD repeat beta-propeller B; Interaction with CUL4A" FT REGION 709..1043 FT /note="WD repeat beta-propeller C" FT REGION 771..1140 FT /note="Interaction with CDT1 and CUL4A" FT /evidence="ECO:0000269|PubMed:15448697" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 1067 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1125 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9ESW0" FT CROSSLNK 1121 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 71..759 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055540" FT VARIANT 184..186 FT /note="Missing (in WHIKERS)" FT /evidence="ECO:0000269|PubMed:33743206" FT /id="VAR_086005" FT VARIANT 188 FT /note="R -> Q (in WHIKERS)" FT /evidence="ECO:0000269|PubMed:33743206" FT /id="VAR_086006" FT VARIANT 188 FT /note="R -> W (in WHIKERS)" FT /evidence="ECO:0000269|PubMed:33743206" FT /id="VAR_086007" FT VARIANT 213 FT /note="E -> K (in WHIKERS)" FT /evidence="ECO:0000269|PubMed:33743206" FT /id="VAR_086008" FT VARIANT 427 FT /note="L -> F (in dbSNP:rs28720299)" FT /evidence="ECO:0000269|Ref.6" FT /id="VAR_023074" FT VARIANT 429 FT /note="F -> V (in WHIKERS)" FT /evidence="ECO:0000269|PubMed:33743206" FT /id="VAR_086009" FT MUTAGEN 316..319 FT /note="YLDN->ALAA: Impairs interaction with DDA1." FT /evidence="ECO:0000269|PubMed:16949367" FT MUTAGEN 537 FT /note="E->A: Slightly impairs interaction with CUL4A." FT /evidence="ECO:0000269|PubMed:16413485" FT MUTAGEN 561 FT /note="W->A: Strongly impairs interaction with CUL4A." FT /evidence="ECO:0000269|PubMed:16413485" FT MUTAGEN 840..842 FT /note="EAE->AAA: Impairs interaction with AMBRA1, DTL, FT DET1, DCAF1, DCAF5, DCAF11 and DCAF8." FT /evidence="ECO:0000269|PubMed:16949367" FT MUTAGEN 910..913 FT /note="MALY->AAAA: Impairs interaction with AMBRA1, DTL and FT DCAF5." FT /evidence="ECO:0000269|PubMed:16949367" FT MUTAGEN 953 FT /note="W->A: Impairs interaction with AMBRA1, ERCC8, DCAF5 FT and DCAF11." FT /evidence="ECO:0000269|PubMed:16949367" FT CONFLICT 422 FT /note="D -> Y (in Ref. 3; AAA88883)" FT /evidence="ECO:0000305" FT CONFLICT 533 FT /note="E -> G (in Ref. 4; CAA05770)" FT /evidence="ECO:0000305" FT CONFLICT 869 FT /note="A -> D (in Ref. 4; CAA05770)" FT /evidence="ECO:0000305" FT CONFLICT 898..899 FT /note="EL -> DV (in Ref. 3; AAA88883 and 4; CAA05770)" FT /evidence="ECO:0000305" FT STRAND 4..10 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 17..21 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:6ZX9" FT STRAND 30..35 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 38..45 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 61..67 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:2HYE" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:3I8E" FT STRAND 85..92 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:3I7K" FT STRAND 99..107 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:6UE5" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 139..144 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:3EI4" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 177..184 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 187..196 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 197..200 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 251..255 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 258..263 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:7OO3" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 279..288 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:3I7K" FT STRAND 296..307 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:4CI2" FT STRAND 321..325 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:8CVP" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:8B3D" FT STRAND 347..353 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 358..365 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 374..379 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 386..394 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 396..402 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 409..413 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:3EI2" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:8AJM" FT STRAND 424..429 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 432..439 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 442..446 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 449..451 FT /evidence="ECO:0007829|PDB:2B5N" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 457..463 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 464..466 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 467..474 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 476..483 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 486..490 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:3I7L" FT STRAND 500..503 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 505..512 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 515..522 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 525..533 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 535..537 FT /evidence="ECO:0007829|PDB:4E5Z" FT STRAND 538..542 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 547..549 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 550..552 FT /evidence="ECO:0007829|PDB:3I7L" FT STRAND 554..560 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 561..564 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 565..570 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 571..573 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 576..581 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 583..586 FT /evidence="ECO:0007829|PDB:6ZX9" FT STRAND 588..596 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 599..606 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 609..616 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 618..620 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 623..630 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 637..645 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 647..655 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 657..674 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 678..682 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 690..694 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 696..698 FT /evidence="ECO:0007829|PDB:4E5Z" FT STRAND 699..704 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 707..716 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 718..727 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 728..730 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 732..743 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 745..753 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 756..759 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 761..765 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 772..774 FT /evidence="ECO:0007829|PDB:6ZX9" FT TURN 777..780 FT /evidence="ECO:0007829|PDB:8AJM" FT STRAND 781..783 FT /evidence="ECO:0007829|PDB:4E54" FT STRAND 785..795 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 796..798 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 801..806 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 811..819 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 823..826 FT /evidence="ECO:0007829|PDB:3EI4" FT STRAND 828..835 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 840..842 FT /evidence="ECO:0007829|PDB:6ZX9" FT STRAND 846..854 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 857..868 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 870..876 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 879..884 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 887..893 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 895..897 FT /evidence="ECO:0007829|PDB:3I7H" FT STRAND 899..905 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 911..917 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 920..928 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 930..936 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 937..940 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 941..947 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 954..961 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 964..969 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 972..979 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 982..984 FT /evidence="ECO:0007829|PDB:3I7K" FT TURN 985..987 FT /evidence="ECO:0007829|PDB:3I7K" FT HELIX 988..990 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 991..999 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 1004..1009 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 1012..1014 FT /evidence="ECO:0007829|PDB:7U8F" FT TURN 1018..1020 FT /evidence="ECO:0007829|PDB:8D7U" FT STRAND 1024..1032 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 1033..1035 FT /evidence="ECO:0007829|PDB:8B3I" FT STRAND 1037..1043 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 1045..1061 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 1065..1067 FT /evidence="ECO:0007829|PDB:3EI1" FT HELIX 1070..1074 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 1075..1077 FT /evidence="ECO:0007829|PDB:3EI3" FT STRAND 1081..1083 FT /evidence="ECO:0007829|PDB:8B3D" FT STRAND 1086..1090 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 1091..1095 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 1096..1099 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 1102..1108 FT /evidence="ECO:0007829|PDB:3EI3" FT TURN 1109..1111 FT /evidence="ECO:0007829|PDB:4A08" FT STRAND 1113..1115 FT /evidence="ECO:0007829|PDB:8AJM" FT STRAND 1117..1119 FT /evidence="ECO:0007829|PDB:8AJM" FT STRAND 1121..1123 FT /evidence="ECO:0007829|PDB:8AJM" FT HELIX 1124..1126 FT /evidence="ECO:0007829|PDB:8CVP" FT HELIX 1127..1136 FT /evidence="ECO:0007829|PDB:3EI3" FT HELIX 1137..1139 FT /evidence="ECO:0007829|PDB:3EI3" SQ SEQUENCE 1140 AA; 126968 MW; 74D082023E3D846D CRC64; MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPNRE TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS QEPKALVSEW KEPQAKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES PRKICYQEVS QCFGVLSSRI EVQDTSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH //