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Database: UniProt
Entry: Q16531
LinkDB: Q16531
Original site: Q16531 
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   07-APR-2021, entry version 210.
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(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   [53]
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   [54]
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   [55]
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   [56]
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   [57]
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   [58]
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   [59]
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   [60]
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   [61]
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   [62] {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   [63] {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. 0:0-0(2019).
RN   [64] {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. 0:0-0(2019).
RN   [65] {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).
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).
CC       {ECO:0000250|UniProtKB:Q3U1J4, ECO:0000269|PubMed:12732143,
CC       ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697,
CC       ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596,
CC       ECO:0000269|PubMed:16407242, ECO:0000269|PubMed:16407252,
CC       ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16482215,
CC       ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16940174,
CC       ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17079684,
CC       ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18381890,
CC       ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19966799,
CC       ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:25043012,
CC       ECO:0000269|PubMed:25108355, ECO:0000269|PubMed:26431207,
CC       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). {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: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   -!- 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=12; IntAct=EBI-350322, EBI-456106;
CC       Q16531; Q13620: CUL4B; NbExp=21; 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=2; IntAct=EBI-350322, EBI-2559135;
CC       Q16531; Q5TAQ9: DCAF8; NbExp=5; IntAct=EBI-350322, EBI-740686;
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; 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).
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   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ddb1/";
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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   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   SMR; Q16531; -.
DR   BioGRID; 108009; 422.
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; 142.
DR   MINT; Q16531; -.
DR   STRING; 9606.ENSP00000301764; -.
DR   BindingDB; Q16531; -.
DR   ChEMBL; CHEMBL3833061; -.
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; Q16531; -.
DR   PeptideAtlas; Q16531; -.
DR   PRIDE; Q16531; -.
DR   ProteomicsDB; 4092; -.
DR   ProteomicsDB; 60895; -. [Q16531-1]
DR   Antibodypedia; 14613; 505 antibodies.
DR   Ensembl; ENST00000301764; ENSP00000301764; ENSG00000167986. [Q16531-1]
DR   GeneID; 1642; -.
DR   KEGG; hsa:1642; -.
DR   UCSC; uc001nrc.6; human. [Q16531-1]
DR   CTD; 1642; -.
DR   DisGeNET; 1642; -.
DR   GeneCards; DDB1; -.
DR   HGNC; HGNC:2717; DDB1.
DR   HPA; ENSG00000167986; Low tissue specificity.
DR   MIM; 600045; gene.
DR   neXtProt; NX_Q16531; -.
DR   OpenTargets; ENSG00000167986; -.
DR   PharmGKB; PA27187; -.
DR   VEuPathDB; HostDB:ENSG00000167986.13; -.
DR   eggNOG; KOG1897; Eukaryota.
DR   GeneTree; ENSGT00950000183151; -.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; Q16531; -.
DR   OMA; GDGSMYY; -.
DR   OrthoDB; 146622at2759; -.
DR   PhylomeDB; Q16531; -.
DR   TreeFam; TF105840; -.
DR   BRENDA; 6.3.2.19; 2681.
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   SIGNOR; Q16531; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 1642; 779 hits in 1004 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 left adrenal gland and 242 other tissues.
DR   ExpressionAtlas; Q16531; baseline and differential.
DR   Genevisible; Q16531; HS.
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:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
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: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:0097602; F:cullin family protein binding; IPI: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:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR   GO; GO:0071987; F:WD40-repeat domain binding; IPI:UniProtKB.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; IDA:AgBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR   GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
DR   GO; GO:0006281; P:DNA repair; TAS:ProtInc.
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; IBA:GO_Central.
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: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; IMP:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
DR   GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:AgBase.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IMP:MGI.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
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:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR031297; DDB1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW   Cytoplasm; DNA damage; DNA repair; DNA-binding; Host-virus interaction;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation; 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         427
FT                   /note="L -> F (in dbSNP:rs28720299)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_023074"
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:0007744|PDB:3EI3"
FT   STRAND          17..21
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          26..28
FT                   /evidence="ECO:0007744|PDB:3EI2"
FT   STRAND          30..35
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          38..45
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          48..56
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          61..67
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          72..74
FT                   /evidence="ECO:0007744|PDB:2HYE"
FT   STRAND          76..81
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            82..84
FT                   /evidence="ECO:0007744|PDB:3I8E"
FT   STRAND          85..92
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          95..97
FT                   /evidence="ECO:0007744|PDB:3I7K"
FT   STRAND          99..107
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          111..113
FT                   /evidence="ECO:0007744|PDB:6UE5"
FT   STRAND          121..124
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          128..134
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          139..144
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          146..148
FT                   /evidence="ECO:0007744|PDB:3EI4"
FT   STRAND          155..158
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          164..169
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          177..184
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          187..196
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            197..200
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          201..204
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          210..212
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          218..221
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            224..226
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          229..232
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          237..241
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          244..248
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           251..255
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          258..263
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          268..275
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          279..288
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          291..293
FT                   /evidence="ECO:0007744|PDB:3I7K"
FT   STRAND          296..307
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          312..316
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            318..320
FT                   /evidence="ECO:0007744|PDB:4CI2"
FT   STRAND          321..325
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          327..329
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          331..336
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           342..344
FT                   /evidence="ECO:0007744|PDB:3I7K"
FT   STRAND          347..353
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          358..365
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          369..371
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          374..379
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           382..384
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          386..394
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          396..402
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          409..413
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          417..419
FT                   /evidence="ECO:0007744|PDB:3EI2"
FT   STRAND          420..422
FT                   /evidence="ECO:0007744|PDB:4CI2"
FT   STRAND          424..429
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          432..439
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          442..446
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          449..451
FT                   /evidence="ECO:0007744|PDB:2B5N"
FT   STRAND          453..455
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          457..463
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            464..466
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          467..474
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          476..483
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          486..490
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          493..495
FT                   /evidence="ECO:0007744|PDB:3I7L"
FT   STRAND          500..503
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          505..512
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          515..522
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          525..533
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          535..537
FT                   /evidence="ECO:0007744|PDB:4E5Z"
FT   STRAND          538..542
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          547..549
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          550..552
FT                   /evidence="ECO:0007744|PDB:3I7L"
FT   STRAND          554..560
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            561..564
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          565..570
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            571..573
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          576..581
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          583..585
FT                   /evidence="ECO:0007744|PDB:3I7K"
FT   STRAND          588..596
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          599..606
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          609..616
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            618..620
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          623..630
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          637..645
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          647..655
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          657..674
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          678..682
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          685..687
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          690..694
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          696..698
FT                   /evidence="ECO:0007744|PDB:4E5Z"
FT   STRAND          699..704
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          707..716
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          718..727
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           728..730
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          732..743
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          745..753
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           756..759
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          761..765
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           770..773
FT                   /evidence="ECO:0007744|PDB:6H0F"
FT   STRAND          774..776
FT                   /evidence="ECO:0007744|PDB:5JK7"
FT   STRAND          781..783
FT                   /evidence="ECO:0007744|PDB:4E54"
FT   STRAND          785..795
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            796..798
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          801..806
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          811..819
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          823..826
FT                   /evidence="ECO:0007744|PDB:3EI4"
FT   STRAND          828..835
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          840..842
FT                   /evidence="ECO:0007744|PDB:3I7N"
FT   STRAND          846..854
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          857..868
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          870..876
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          879..884
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          887..893
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          895..897
FT                   /evidence="ECO:0007744|PDB:3I7H"
FT   STRAND          899..905
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          911..917
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          920..928
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          930..936
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            937..940
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          941..947
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          954..961
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          964..969
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          972..979
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          982..984
FT                   /evidence="ECO:0007744|PDB:3I7K"
FT   TURN            985..987
FT                   /evidence="ECO:0007744|PDB:3I7K"
FT   HELIX           988..990
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          991..999
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          1004..1009
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          1012..1014
FT                   /evidence="ECO:0007744|PDB:6H0F"
FT   STRAND          1017..1020
FT                   /evidence="ECO:0007744|PDB:3EI4"
FT   STRAND          1024..1032
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          1037..1043
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           1045..1061
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           1065..1067
FT                   /evidence="ECO:0007744|PDB:3EI1"
FT   HELIX           1070..1074
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          1075..1077
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   STRAND          1081..1083
FT                   /evidence="ECO:0007744|PDB:3I7N"
FT   STRAND          1086..1090
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           1091..1095
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           1096..1099
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           1102..1108
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   TURN            1109..1111
FT                   /evidence="ECO:0007744|PDB:4A08"
FT   STRAND          1113..1115
FT                   /evidence="ECO:0007744|PDB:6H0F"
FT   STRAND          1117..1120
FT                   /evidence="ECO:0007744|PDB:2B5L"
FT   STRAND          1121..1123
FT                   /evidence="ECO:0007744|PDB:6H0F"
FT   HELIX           1127..1136
FT                   /evidence="ECO:0007744|PDB:3EI3"
FT   HELIX           1137..1139
FT                   /evidence="ECO:0007744|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
//
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