DDB1_HUMAN
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 03-AUG-2022, entry version 215.
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. 16:7-14(2020).
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. 16:15-23(2020).
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).
RN [66]
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).
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=6; 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 -!- 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/";
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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 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 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 AlphaFoldDB; Q16531; -.
DR SMR; Q16531; -.
DR BioGRID; 108009; 479.
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; 167.
DR MINT; Q16531; -.
DR STRING; 9606.ENSP00000301764; -.
DR BindingDB; Q16531; -.
DR ChEMBL; CHEMBL3833061; -.
DR GlyGen; Q16531; 1 site, 1 O-linked glycan (1 site).
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; 535 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 CTD; 1642; -.
DR DisGeNET; 1642; -.
DR GeneCards; DDB1; -.
DR HGNC; HGNC:2717; DDB1.
DR HPA; ENSG00000167986; Low tissue specificity.
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; CTEMEHE; -.
DR OrthoDB; 146622at2759; -.
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; 796 hits in 1098 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 204 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: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:0035861; C:site of double-strand break; IBA:GO_Central.
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:0006915; P:apoptotic process; IEA:Ensembl.
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:0034644; P:cellular response to UV; IC:ComplexPortal.
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:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
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; IMP:UniProtKB.
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; IMP:UniProtKB.
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: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; 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; 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 STRAND 342..344
FT /evidence="ECO:0007829|PDB:7OOB"
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:4CI2"
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 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:6H0F"
FT STRAND 1017..1020
FT /evidence="ECO:0007829|PDB:3EI4"
FT STRAND 1024..1032
FT /evidence="ECO:0007829|PDB:3EI3"
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:7OOB"
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:6H0F"
FT STRAND 1117..1120
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 1121..1123
FT /evidence="ECO:0007829|PDB:6H0F"
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
