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DNA damage-binding protein 1 (DDB p127 subunit) (DNA damage-binding protein a) (DDBa) (Damage-specific DNA-binding protein 1) (HBV X-associated protein 1) (XAP-1) (UV-damaged DNA-binding factor) (UV-damaged DNA-binding protein 1) (UV-DDB 1) (XPE-binding factor) (XPE-BF) (Xeroderma pigmentosum group E-complementing protein) (XPCe)

 DDB1_HUMAN              Reviewed;        1140 AA.
Q16531; A6NG77; B2R648; B4DG00; O15176; Q13289; Q58F96;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 187.
RecName: Full=DNA damage-binding protein 1;
AltName: Full=DDB p127 subunit;
AltName: Full=DNA damage-binding protein a;
Short=DDBa;
AltName: Full=Damage-specific DNA-binding protein 1;
AltName: Full=HBV X-associated protein 1;
Short=XAP-1;
AltName: Full=UV-damaged DNA-binding factor;
AltName: Full=UV-damaged DNA-binding protein 1;
Short=UV-DDB 1;
AltName: Full=XPE-binding factor;
Short=XPE-BF;
AltName: Full=Xeroderma pigmentosum group E-complementing protein;
Short=XPCe;
Name=DDB1; Synonyms=XAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Epidermis, and Fetal lung;
PubMed=8530102; DOI=10.1006/geno.1995.1215;
Dualan R., Brody T., Keeney S., Nichols A.F., Admon A., Linn S.;
"Chromosomal localization and cDNA cloning of the genes (DDB1 and
DDB2) for the p127 and p48 subunits of a human damage-specific DNA
binding protein.";
Genomics 29:62-69(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Peripheral blood;
PubMed=7815490;
Lee T.H., Elledge S.J., Butel J.S.;
"Hepatitis B virus X protein interacts with a probable cellular DNA
repair protein.";
J. Virol. 69:1107-1114(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8538642; DOI=10.1016/0921-8777(95)00040-2;
Hwang B.J., Liao J.C., Chu G.;
"Isolation of a cDNA encoding a UV-damaged DNA binding factor
defective in xeroderma pigmentosum group E cells.";
Mutat. Res. 362:105-117(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skin;
Huang S.L., Lin-Chao S., Chao C.K.;
"Molecular cloning and characterization of human XPE protein: a
component of UV-damaged DNA recognition activity.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-427.
NIEHS SNPs program;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH DDB1, AND DNA-BINDING.
PubMed=9632823; DOI=10.1128/MCB.18.7.4391;
Hwang B.J., Toering S., Francke U., Chu G.;
"p48 Activates a UV-damaged-DNA binding factor and is defective in
xeroderma pigmentosum group E cells that lack binding activity.";
Mol. Cell. Biol. 18:4391-4399(1998).
[11]
SUBCELLULAR LOCATION.
PubMed=10777491; DOI=10.1074/jbc.M000961200;
Liu W., Nichols A.F., Graham J.A., Dualan R., Abbas A., Linn S.;
"Nuclear transport of human DDB protein induced by ultraviolet
light.";
J. Biol. Chem. 275:21429-21434(2000).
[12]
INTERACTION WITH CUL4A, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=11673459; DOI=10.1074/jbc.M106808200;
Chen X., Zhang Y., Douglas L., Zhou P.;
"UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
ubiquitination and degradation.";
J. Biol. Chem. 276:48175-48182(2001).
[13]
INTERACTION WITH HBV X PROTEIN.
PubMed=11531405; DOI=10.1006/viro.2001.1036;
Lin-Marq N., Bontron S., Leupin O., Strubin M.;
"Hepatitis B virus X protein interferes with cell viability through
interaction with the p127-kDa UV-damaged DNA-binding protein.";
Virology 287:266-274(2001).
[14]
FUNCTION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY,
IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB2 AND RBX1, IDENTIFICATION
IN THE CSA COMPLEX WITH CUL4A; ERCC8 AND RBX1, INTERACTION OF THE CSA
COMPLEX WITH RNA POLYMERASE II, AND INTERACTION WITH THE COP9
SIGNALOSOME.
PubMed=12732143; DOI=10.1016/S0092-8674(03)00316-7;
Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M.,
Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.;
"The ubiquitin ligase activity in the DDB2 and CSA complexes is
differentially regulated by the COP9 signalosome in response to DNA
damage.";
Cell 113:357-367(2003).
[15]
INTERACTION WITH HBV X PROTEIN AND SV5 PROTEIN V (MICROBIAL
INFECTION).
PubMed=12743284; DOI=10.1128/JVI.77.11.6274-6283.2003;
Leupin O., Bontron S., Strubin M.;
"Hepatitis B virus X protein and simian virus 5 V protein exhibit
similar UV-DDB1 binding properties to mediate distinct activities.";
J. Virol. 77:6274-6283(2003).
[16]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
CDT1; CUL4A; RBX1 AND THE COP9 SIGNALOSOME.
PubMed=15448697; DOI=10.1038/ncb1172;
Hu J., McCall C.M., Ohta T., Xiong Y.;
"Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in
response to DNA damage.";
Nat. Cell Biol. 6:1003-1009(2004).
[17]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
CUL4A; DET1; RBX1 AND COP1.
PubMed=14739464; DOI=10.1126/science.1093549;
Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D.,
Deshaies R.J., Dixit V.M.;
"Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin
ligase.";
Science 303:1371-1374(2004).
[18]
FUNCTION, INTERACTION WITH CUL4A; DDB2 AND RBX1, AND DNA-BINDING.
PubMed=15882621; DOI=10.1016/j.cell.2005.02.035;
Sugasawa K., Okuda Y., Saijo M., Nishi R., Matsuda N., Chu G.,
Mori T., Iwai S., Tanaka K., Tanaka K., Hanaoka F.;
"UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin
ligase complex.";
Cell 121:387-400(2005).
[19]
INTERACTION WITH DDB2, AND DNA-BINDING.
PubMed=16223728; DOI=10.1074/jbc.M507854200;
Wittschieben B.O., Iwai S., Wood R.D.;
"DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes
a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic
sites, and compound lesions in DNA.";
J. Biol. Chem. 280:39982-39989(2005).
[20]
INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V (MICROBIAL INFECTION).
PubMed=16227264; DOI=10.1128/JVI.79.21.13434-13441.2005;
Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S.,
Randall R.E.;
"Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2,
to facilitate the ubiquitination of STAT1.";
J. Virol. 79:13434-13441(2005).
[21]
FUNCTION, INTERACTION WITH CUL4A; DDB2; RBX1 AND THE COP9 SIGNALOSOME,
AND DNA-BINDING.
PubMed=16260596; DOI=10.1128/MCB.25.22.9784-9792.2005;
Kulaksiz G., Reardon J.T., Sancar A.;
"Xeroderma pigmentosum complementation group E protein (XPE/DDB2):
purification of various complexes of XPE and analyses of their damaged
DNA binding and putative DNA repair properties.";
Mol. Cell. Biol. 25:9784-9792(2005).
[22]
FUNCTION.
PubMed=16482215; DOI=10.1038/sj.emboj.7601002;
Nishitani H., Sugimoto N., Roukos V., Nakanishi Y., Saijo M.,
Obuse C., Tsurimoto T., Nakayama K.I., Nakayama K., Fujita M.,
Lygerou Z., Nishimoto T.;
"Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1
for proteolysis.";
EMBO J. 25:1126-1136(2006).
[23]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
ATG16L1; BTRC; CUL4A; DDB2; ERCC8; FBXW5; FBXW8; GRWD1; KATNB1; NUP43;
PWP1; RBBP4; RBBP7; COP1; DCAF1; DCAF11; WSB1 AND WSB2.
PubMed=17079684; DOI=10.1101/gad.1483206;
He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y.;
"DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-
ROC1 ubiquitin ligases.";
Genes Dev. 20:2949-2954(2006).
[24]
FUNCTION.
PubMed=16407242; DOI=10.1074/jbc.C500464200;
Hu J., Xiong Y.;
"An evolutionarily conserved function of proliferating cell nuclear
antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in
response to DNA damage.";
J. Biol. Chem. 281:3753-3756(2006).
[25]
FUNCTION.
PubMed=16407252; DOI=10.1074/jbc.M512705200;
Senga T., Sivaprasad U., Zhu W., Park J.H., Arias E.E., Walter J.C.,
Dutta A.;
"PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-
terminal ubiquitination.";
J. Biol. Chem. 281:6246-6252(2006).
[26]
INTERACTION WITH CUL4A AND DDB2.
PubMed=16527807; DOI=10.1074/jbc.M511834200;
El-Mahdy M.A., Zhu Q., Wang Q.-E., Wani G., Praetorius-Ibba M.,
Wani A.A.;
"Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites
regulates in vivo lesion recognition by XPC.";
J. Biol. Chem. 281:13404-13411(2006).
[27]
IDENTIFICATION IN A COMPLEX WITH DDB2; CUL4A; CUL4B AND RBX1,
IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
Tempst P., Xiong Y., Zhang Y.;
"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin
ligase facilitates cellular response to DNA damage.";
Mol. Cell 22:383-394(2006).
[28]
INTERACTION WITH AMBRA1; DCAF17; DCAF16; DCAF15; DDA1; DDB2; DET1;
DTL; ERCC8; DCAF6; PHIP; DCAF1; DCAF4; DCAF5; DCAF11; DCAF10; DCAF12;
DCAF8; DCAF7 AND WDTC1, AND MUTAGENESIS OF 316-TYR--ASN-319;
840-GLU--GLU-842; 910-MET--TYR-913 AND TRP-953.
PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
which is required for S phase destruction of the replication factor
Cdt1.";
Mol. Cell 23:709-721(2006).
[29]
FUNCTION.
PubMed=16940174; DOI=10.1128/MCB.00819-06;
Lovejoy C.A., Lock K., Yenamandra A., Cortez D.;
"DDB1 maintains genome integrity through regulation of Cdt1.";
Mol. Cell. Biol. 26:7977-7990(2006).
[30]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
CUL4B; DTL; NLE1; PAFAH1B1; RBBP5; COP1; SNRNP40; WDR5; WDR5B; WDR12;
WDR26; WDR39; WDR53; WDR59 AND WDR61.
PubMed=17041588; DOI=10.1038/ncb1490;
Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
"CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
proteins and regulates histone methylation.";
Nat. Cell Biol. 8:1277-1283(2006).
[31]
FUNCTION, INTERACTION WITH CUL4A; DDB2; HISTONE H2A AND RBX1,
DNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=16473935; DOI=10.1073/pnas.0511160103;
Kapetanaki M.G., Guerrero-Santoro J., Bisi D.C., Hsieh C.L.,
Rapic-Otrin V., Levine A.S.;
"The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma
pigmentosum group E and targets histone H2A at UV-damaged DNA sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:2588-2593(2006).
[32]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[33]
FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB2, AND SUBCELLULAR
LOCATION.
PubMed=18593899; DOI=10.1158/0008-5472.CAN-07-6162;
Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I.,
Levine A.S., Rapic-Otrin V.;
"The cullin 4B-based UV-damaged DNA-binding protein ligase binds to
UV-damaged chromatin and ubiquitinates histone H2A.";
Cancer Res. 68:5014-5022(2008).
[34]
FUNCTION, AND INTERACTION WITH FBXW5; TSC1 AND TSC2.
PubMed=18381890; DOI=10.1101/gad.1624008;
Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J.,
Xiong Y.;
"WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by
DDB1-CUL4-ROC1 ligase.";
Genes Dev. 22:866-871(2008).
[35]
INTERACTION WITH DCAF1/VPRBP.
PubMed=18606781; DOI=10.1128/MCB.00232-08;
McCall C.M., Miliani de Marval P.L., Chastain P.D. II, Jackson S.C.,
He Y.J., Kotake Y., Cook J.G., Xiong Y.;
"Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40
protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is
essential for DNA replication and embryonic development.";
Mol. Cell. Biol. 28:5621-5633(2008).
[36]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
NF2.
PubMed=18332868; DOI=10.1038/onc.2008.44;
Huang J., Chen J.;
"VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for
degradation.";
Oncogene 27:4056-4064(2008).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[38]
INTERACTION WITH EDVP COMPLEX.
PubMed=19287380; DOI=10.1038/ncb1848;
Maddika S., Chen J.;
"Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3
ligase.";
Nat. Cell Biol. 11:409-419(2009).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1067, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[41]
INTERACTION WITH LRWD1.
PubMed=22935713; DOI=10.4161/cc.21870;
Shen Z., Prasanth S.G.;
"Orc2 protects ORCA from ubiquitin-mediated degradation.";
Cell Cycle 11:3578-3589(2012).
[42]
INTERACTION WITH DTL.
PubMed=23478445; DOI=10.1016/j.molcel.2013.02.003;
Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.;
"CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and
regulates Pr-Set7/Set8-mediated cellular migration.";
Mol. Cell 49:1147-1158(2013).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1121, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-1140 IN COMPLEX WITH
SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH CUL4A AND DET1, AND
MUTAGENESIS OF GLU-537 AND TRP-561.
PubMed=16413485; DOI=10.1016/j.cell.2005.10.033;
Li T., Chen X., Garbutt K.C., Zhou P., Zheng N.;
"Structure of DDB1 in complex with a paramyxovirus V protein: viral
hijack of a propeller cluster in ubiquitin ligase.";
Cell 124:105-117(2006).
[46]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-1140 IN COMPLEX WITH CUL4A;
RBX1 AND SIMIAN VIRUS 5 PROTEIN V, AND INTERACTION WITH DDB2; DTL;
DCAF11; DCAF8 AND WDTC1.
PubMed=16964240; DOI=10.1038/nature05175;
Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
"Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
ligase machinery.";
Nature 443:590-593(2006).
[47]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA, WD
BETA-PROPELLER DOMAINS, AND SUBUNIT.
PubMed=19109893; DOI=10.1016/j.cell.2008.10.045;
Scrima A., Konickova R., Czyzewski B.K., Kawasaki Y., Jeffrey P.D.,
Groisman R., Nakatani Y., Iwai S., Pavletich N.P., Thoma N.H.;
"Structural basis of UV DNA-damage recognition by the DDB1-DDB2
complex.";
Cell 135:1213-1223(2008).
[48]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION AS UBIQUITIN LIGASE
COMPONENT, SUBUNIT, INTERACTION WITH TRPC4AP; DCAF4; DCAF5; DCAF6;
DCAF8; DCAF9; DCAF12; DDB2, AND INTERACTION WITH HEPATITIS VIRUS
PROTEIN HBX (MICROBIAL INFECTION) AND PARAMYXOVIRUS PROTEIN SV5-V
(MICROBIAL INFECTION).
PubMed=19966799; DOI=10.1038/nsmb.1719;
Li T., Robert E.I., van Breugel P.C., Strubin M., Zheng N.;
"A promiscuous alpha-helical motif anchors viral hijackers and
substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery.";
Nat. Struct. Mol. Biol. 17:105-111(2010).
[49]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEXES WITH DDB2; ERCC8
AND CUL4B, FUNCTION, AND SUBUNIT.
PubMed=22118460; DOI=10.1016/j.cell.2011.10.035;
Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M.,
Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S.,
Gut H., Sugasawa K., Thoma N.H.;
"The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture,
targeting, and activation.";
Cell 147:1024-1039(2011).
[50]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS), AND DOMAIN.
PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
Xu C., Min J.;
"Structure and function of WD40 domain proteins.";
Protein Cell 2:202-214(2011).
[51]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), SUBUNIT, AND INTERACTION WITH
DDB2.
PubMed=22822215; DOI=10.1073/pnas.1110067109;
Yeh J.I., Levine A.S., Du S., Chinte U., Ghodke H., Wang H., Shi H.,
Hsieh C.L., Conway J.F., Van Houten B., Rapic-Otrin V.;
"Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB)
dimerization and its roles in chromatinized DNA repair.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2737-E2746(2012).
[52]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CRBN,
INTERACTION WITH CRBN, AND FUNCTION IN PROTEIN UBIQUITINATION.
PubMed=25043012; DOI=10.1038/nature13527;
Fischer E.S., Bohm K., Lydeard J.R., Yang H., Stadler M.B.,
Cavadini S., Nagel J., Serluca F., Acker V., Lingaraju G.M.,
Tichkule R.B., Schebesta M., Forrester W.C., Schirle M., Hassiepen U.,
Ottl J., Hild M., Beckwith R.E., Harper J.W., Jenkins J.L.,
Thoma N.H.;
"Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with
thalidomide.";
Nature 512:49-53(2014).
[53]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH CRBN,
INTERACTION WITH CRBN, AND FUNCTION.
PubMed=25108355; DOI=10.1038/nsmb.2874;
Chamberlain P.P., Lopez-Girona A., Miller K., Carmel G., Pagarigan B.,
Chie-Leon B., Rychak E., Corral L.G., Ren Y.J., Wang M., Riley M.,
Delker S.L., Ito T., Ando H., Mori T., Hirano Y., Handa H.,
Hakoshima T., Daniel T.O., Cathers B.E.;
"Structure of the human cereblon-DDB1-lenalidomide complex reveals
basis for responsiveness to thalidomide analogs.";
Nat. Struct. Mol. Biol. 21:803-809(2014).
-!- FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-
damaged DNA-binding protein complex (the UV-DDB complex). The UV-
DDB complex may recognize UV-induced DNA damage and recruit
proteins of the nucleotide excision repair pathway (the NER
pathway) to initiate DNA repair. The UV-DDB complex preferentially
binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts
(6-4 PP), apurinic sites and short mismatches. Also appears to
function as a component of numerous distinct DCX (DDB1-CUL4-X-box)
E3 ubiquitin-protein ligase complexes which mediate the
ubiquitination and subsequent proteasomal degradation of target
proteins. The functional specificity of the DCX E3 ubiquitin-
protein ligase complex is determined by the variable substrate
recognition component recruited by DDB1. DCX(DDB2) (also known as
DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate
histone H2A, histone H3 and histone H4 at sites of UV-induced DNA
damage. The ubiquitination of histones may facilitate their
removal from the nucleosome and promote subsequent DNA repair.
DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by
XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent
polyubiquitination of CDT1 and MDM2-dependent ubiquitination of
TP53 in response to radiation-induced DNA damage and during DNA
replication. DCX(ERCC8) (the CSA complex) plays a role in
transcription-coupled repair (TCR). May also play a role in
ubiquitination of CDKN1B/p27kip when associated with CUL4 and
SKP2. {ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464,
ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15882621,
ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16407242,
ECO:0000269|PubMed:16407252, ECO:0000269|PubMed:16473935,
ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:16678110,
ECO:0000269|PubMed:16940174, ECO:0000269|PubMed:17041588,
ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:18332868,
ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:18593899,
ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:22118460,
ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355}.
-!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
DDB2; the heterodimer dimerizes to give rise to a heterotetramer
when bound to damaged DNA (PubMed:22822215). The UV-DDB complex
interacts with monoubiquitinated histone H2A and binds to XPC via
the DDB2 subunit. Component of numerous DCX (DDB1-CUL4-X-box) E3
ubiquitin-protein ligase complexes which consist of a core of
DDB1, CUL4A or CUL4B and RBX1. DDB1 may recruit specific substrate
targeting subunits to the DCX complex. These substrate targeting
subunits are generally known as DCAF (DDB1- and CUL4-associated
factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins.
Interacts with AMBRA1, ATG16L1, BTRC, CRBN, DCAF1, DCAF4, DCAF5,
DCAF6, DCAF7, DCAF8, DCAF9, DCAF10, DCAF11, DCAF12, DCAF15,
DCAF16, DCAF17, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1,
KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7,
COP1, SNRNP40, DCAF1, WDR5, WDR5B, WDR12, WDR26, WDR39, WDR42,
WDR53, WDR59, WDR61, WSB1, WSB2, LRWD1 and WDTC1. DCX complexes
may associate with the COP9 signalosome, and this inhibits the E3
ubiquitin-protein ligase activity of the complex. Interacts with
NF2, TSC1 and TSC2. Interaction with SV5 protein V may prevent the
recruitment of DCAF proteins to DCX complexes. Interacts with AGO1
and AGO2. Associates with the E3 ligase complex containing DYRK2,
EDD/UBR5, DDB1 and DCAF1 proteins (EDVP complex). Interacts
directly with DYRK2. DCX(DTL) complex interacts with FBXO11; does
not ubiquitinate and degradate FBXO11. Interacts with TRPC4AP
(PubMed:19966799). {ECO:0000269|PubMed:11531405,
ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:12732143,
ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697,
ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16223728,
ECO:0000269|PubMed:16260596, ECO:0000269|PubMed:16413485,
ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16527807,
ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16949367,
ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17041588,
ECO:0000269|PubMed:17079684, ECO:0000269|PubMed:17932509,
ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18381890,
ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:18606781,
ECO:0000269|PubMed:19109893, ECO:0000269|PubMed:19287380,
ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:22822215,
ECO:0000269|PubMed:22935713, ECO:0000269|PubMed:23478445,
ECO:0000269|PubMed:25043012, ECO:0000269|PubMed:25108355,
ECO:0000269|PubMed:9632823}.
-!- SUBUNIT: (Microbial infection) Interacts with Simian virus 5
protein V. {ECO:0000269|PubMed:12743284,
ECO:0000269|PubMed:16227264, ECO:0000269|PubMed:19966799}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus
protein HBX; the viral protein contains a short helical motif that
competes for the same binding site as the N-terminal helical motif
found in endogenous DCAF proteins. {ECO:0000269|PubMed:12743284,
ECO:0000269|PubMed:19966799}.
-!- INTERACTION:
Q9H9F9:ACTR5; NbExp=4; IntAct=EBI-350322, EBI-769418;
Q96SW2:CRBN; NbExp=3; IntAct=EBI-350322, EBI-2510250;
Q96SW2-2:CRBN; NbExp=7; IntAct=EBI-350322, EBI-10693561;
Q13619:CUL4A; NbExp=8; IntAct=EBI-350322, EBI-456106;
Q13620:CUL4B; NbExp=17; IntAct=EBI-350322, EBI-456067;
Q9Y4B6:DCAF1; NbExp=3; IntAct=EBI-350322, EBI-1996353;
Q9Y4B6-3:DCAF1; NbExp=2; IntAct=EBI-350322, EBI-9915372;
Q92466:DDB2; NbExp=19; IntAct=EBI-350322, EBI-1176171;
Q9NZJ0:DTL; NbExp=3; IntAct=EBI-350322, EBI-1176075;
O75530:EED; NbExp=4; IntAct=EBI-350322, EBI-923794;
Q969U6-1:FBXW5; NbExp=3; IntAct=EBI-350322, EBI-16031873;
Q9ULG1:INO80; NbExp=5; IntAct=EBI-350322, EBI-769345;
P11207:P/V (xeno); NbExp=4; IntAct=EBI-350322, EBI-6148694;
P42224:STAT1; NbExp=2; IntAct=EBI-350322, EBI-1057697;
Q04725:TLE2; NbExp=2; IntAct=EBI-350322, EBI-1176061;
Q72500:vpr (xeno); NbExp=4; IntAct=EBI-350322, EBI-15626381;
P18045:vpx (xeno); NbExp=2; IntAct=EBI-350322, EBI-6558105;
Q8N5D0-4:WDTC1; NbExp=2; IntAct=EBI-350322, EBI-15821254;
Q89246:X (xeno); NbExp=2; IntAct=EBI-350322, EBI-15821216;
Q9QMH9:x (xeno); NbExp=3; IntAct=EBI-350322, EBI-15821282;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Primarily
cytoplasmic. Translocates to the nucleus following UV irradiation
and subsequently accumulates at sites of DNA damage.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q16531-1; Sequence=Displayed;
Name=2;
IsoId=Q16531-2; Sequence=VSP_055540;
Note=No experimental confirmation available.;
-!- DOMAIN: The core of the protein consists of three WD40 beta-
propeller domains. {ECO:0000269|PubMed:21468892}.
-!- PTM: Phosphorylated by ABL1. {ECO:0000250}.
-!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-
dependent proteolysis. {ECO:0000269|PubMed:11673459}.
-!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ddb1/";
-----------------------------------------------------------------------
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EMBL; U18299; AAC50349.1; -; mRNA.
EMBL; L40326; AAA62838.1; -; mRNA.
EMBL; U32986; AAA88883.1; -; mRNA.
EMBL; AJ002955; CAA05770.1; -; mRNA.
EMBL; AK294341; BAG57611.1; -; mRNA.
EMBL; AK312436; BAG35345.1; -; mRNA.
EMBL; AY960579; AAX44048.1; -; Genomic_DNA.
EMBL; AP003037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW73935.1; -; Genomic_DNA.
EMBL; BC011686; AAH11686.1; -; mRNA.
EMBL; BC050530; AAH50530.1; -; mRNA.
EMBL; BC051764; AAH51764.1; -; mRNA.
CCDS; CCDS31576.1; -. [Q16531-1]
PIR; I38908; I38908.
RefSeq; NP_001914.3; NM_001923.4. [Q16531-1]
UniGene; Hs.290758; -.
PDB; 2B5L; X-ray; 2.85 A; A/B=1-1140.
PDB; 2B5M; X-ray; 2.92 A; A=1-1140.
PDB; 2B5N; X-ray; 2.80 A; A/B/C/D=391-709.
PDB; 2HYE; X-ray; 3.10 A; A=1-1140.
PDB; 3E0C; X-ray; 2.41 A; A=1-1140.
PDB; 3EI1; X-ray; 2.80 A; A=1-1140.
PDB; 3EI2; X-ray; 2.60 A; A=1-1140.
PDB; 3EI3; X-ray; 2.30 A; A=1-1140.
PDB; 3EI4; X-ray; 3.30 A; A/C/E=1-1140.
PDB; 3I7H; X-ray; 2.90 A; A=1-1140.
PDB; 3I7K; X-ray; 2.80 A; A=1-1140.
PDB; 3I7L; X-ray; 2.80 A; A=1-1140.
PDB; 3I7N; X-ray; 2.80 A; A=1-1140.
PDB; 3I7O; X-ray; 2.80 A; A=1-1140.
PDB; 3I7P; X-ray; 3.00 A; A=1-1140.
PDB; 3I89; X-ray; 3.00 A; A=1-1140.
PDB; 3I8C; X-ray; 2.80 A; A=1-1140.
PDB; 3I8E; X-ray; 3.40 A; A/B=1-1140.
PDB; 4A08; X-ray; 3.00 A; A=1-1140.
PDB; 4A09; X-ray; 3.10 A; A=1-1140.
PDB; 4A0A; X-ray; 3.60 A; A=1-1140.
PDB; 4A0B; X-ray; 3.80 A; A/C=1-1140.
PDB; 4A0K; X-ray; 5.93 A; C=1-1140.
PDB; 4A0L; X-ray; 7.40 A; A/C=1-1140.
PDB; 4A11; X-ray; 3.31 A; A=1-1140.
PDB; 4CI1; X-ray; 2.98 A; A=1-1140.
PDB; 4CI2; X-ray; 2.95 A; A=1-1140.
PDB; 4CI3; X-ray; 3.50 A; A=1-1140.
PDB; 4E54; X-ray; 2.85 A; A=2-1140.
PDB; 4E5Z; X-ray; 3.22 A; A=2-1140.
PDB; 4TZ4; X-ray; 3.01 A; A=2-1140.
PDB; 5FQD; X-ray; 2.45 A; A/D=1-395, A/D=709-1140.
PDB; 5HXB; X-ray; 3.60 A; B/Y=1-1140.
PDB; 5JK7; X-ray; 3.49 A; A/B=1-1140.
PDB; 5V3O; X-ray; 3.20 A; A=1-1140.
PDB; 6BN7; X-ray; 3.50 A; A=1-395, A=706-1140.
PDB; 6BN8; X-ray; 3.99 A; A=1-395, A=706-1140.
PDB; 6BN9; X-ray; 4.38 A; A=1-395, A=706-1140.
PDB; 6BNB; X-ray; 6.34 A; A=1-395, A=706-1140.
PDB; 6BOY; X-ray; 3.33 A; A=1-395, A=706-1140.
PDBsum; 2B5L; -.
PDBsum; 2B5M; -.
PDBsum; 2B5N; -.
PDBsum; 2HYE; -.
PDBsum; 3E0C; -.
PDBsum; 3EI1; -.
PDBsum; 3EI2; -.
PDBsum; 3EI3; -.
PDBsum; 3EI4; -.
PDBsum; 3I7H; -.
PDBsum; 3I7K; -.
PDBsum; 3I7L; -.
PDBsum; 3I7N; -.
PDBsum; 3I7O; -.
PDBsum; 3I7P; -.
PDBsum; 3I89; -.
PDBsum; 3I8C; -.
PDBsum; 3I8E; -.
PDBsum; 4A08; -.
PDBsum; 4A09; -.
PDBsum; 4A0A; -.
PDBsum; 4A0B; -.
PDBsum; 4A0K; -.
PDBsum; 4A0L; -.
PDBsum; 4A11; -.
PDBsum; 4CI1; -.
PDBsum; 4CI2; -.
PDBsum; 4CI3; -.
PDBsum; 4E54; -.
PDBsum; 4E5Z; -.
PDBsum; 4TZ4; -.
PDBsum; 5FQD; -.
PDBsum; 5HXB; -.
PDBsum; 5JK7; -.
PDBsum; 5V3O; -.
PDBsum; 6BN7; -.
PDBsum; 6BN8; -.
PDBsum; 6BN9; -.
PDBsum; 6BNB; -.
PDBsum; 6BOY; -.
ProteinModelPortal; Q16531; -.
SMR; Q16531; -.
BioGrid; 108009; 281.
ComplexPortal; CPX-308; UV DNA damage recognition complex DBB1-DBB2.
ComplexPortal; CPX-477; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant.
ComplexPortal; CPX-648; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
CORUM; Q16531; -.
DIP; DIP-430N; -.
IntAct; Q16531; 114.
MINT; Q16531; -.
STRING; 9606.ENSP00000301764; -.
ChEMBL; CHEMBL3833061; -.
iPTMnet; Q16531; -.
PhosphoSitePlus; Q16531; -.
SwissPalm; Q16531; -.
BioMuta; DDB1; -.
DMDM; 12643730; -.
EPD; Q16531; -.
MaxQB; Q16531; -.
PaxDb; Q16531; -.
PeptideAtlas; Q16531; -.
PRIDE; Q16531; -.
ProteomicsDB; 60895; -.
Ensembl; ENST00000301764; ENSP00000301764; ENSG00000167986. [Q16531-1]
GeneID; 1642; -.
KEGG; hsa:1642; -.
UCSC; uc001nrc.6; human. [Q16531-1]
CTD; 1642; -.
DisGeNET; 1642; -.
EuPathDB; HostDB:ENSG00000167986.13; -.
GeneCards; DDB1; -.
H-InvDB; HIX0171380; -.
HGNC; HGNC:2717; DDB1.
HPA; CAB032821; -.
HPA; HPA045174; -.
HPA; HPA068456; -.
MIM; 600045; gene.
neXtProt; NX_Q16531; -.
OpenTargets; ENSG00000167986; -.
PharmGKB; PA27187; -.
eggNOG; KOG1897; Eukaryota.
eggNOG; ENOG410XPF6; LUCA.
GeneTree; ENSGT00530000063396; -.
HOGENOM; HOG000007241; -.
HOVERGEN; HBG005460; -.
InParanoid; Q16531; -.
KO; K10610; -.
OMA; GIGIQEH; -.
OrthoDB; EOG091G017I; -.
PhylomeDB; Q16531; -.
TreeFam; TF105840; -.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-8951664; Neddylation.
SIGNOR; Q16531; -.
UniPathway; UPA00143; -.
ChiTaRS; DDB1; human.
EvolutionaryTrace; Q16531; -.
GeneWiki; DDB1; -.
GenomeRNAi; 1642; -.
PRO; PR:Q16531; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000167986; -.
CleanEx; HS_DDB1; -.
ExpressionAtlas; Q16531; baseline and differential.
Genevisible; Q16531; HS.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
GO; GO:0097602; F:cullin family protein binding; IPI:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0030674; F:protein binding, bridging; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
GO; GO:0071987; F:WD40-repeat domain binding; IPI:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
GO; GO:0051702; P:interaction with symbiont; IDA:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0006289; P:nucleotide-excision repair; TAS:ProtInc.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IMP:AgBase.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:AgBase.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010498; P:proteasomal protein catabolic process; IMP:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0070914; P:UV-damage excision repair; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 5.
InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
InterPro; IPR031297; DDB1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
Pfam; PF03178; CPSF_A; 1.
SUPFAM; SSF50978; SSF50978; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA damage; DNA repair; DNA-binding;
Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1140 DNA damage-binding protein 1.
/FTId=PRO_0000079840.
REGION 2 768 Interaction with CDT1.
{ECO:0000269|PubMed:15448697}.
REGION 13 356 WD repeat beta-propeller A.
REGION 392 708 WD repeat beta-propeller B; Interaction
with CUL4A.
REGION 709 1043 WD repeat beta-propeller C.
REGION 771 1140 Interaction with CDT1 and CUL4A.
{ECO:0000269|PubMed:15448697}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 1067 1067 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1125 1125 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ESW0}.
CROSSLNK 1121 1121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 71 759 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055540.
VARIANT 427 427 L -> F (in dbSNP:rs28720299).
{ECO:0000269|Ref.6}.
/FTId=VAR_023074.
MUTAGEN 316 319 YLDN->ALAA: Impairs interaction with
DDA1. {ECO:0000269|PubMed:16949367}.
MUTAGEN 537 537 E->A: Slightly impairs interaction with
CUL4A. {ECO:0000269|PubMed:16413485}.
MUTAGEN 561 561 W->A: Strongly impairs interaction with
CUL4A. {ECO:0000269|PubMed:16413485}.
MUTAGEN 840 842 EAE->AAA: Impairs interaction with
AMBRA1, DTL, DET1, DCAF1, DCAF5, DCAF11
and DCAF8. {ECO:0000269|PubMed:16949367}.
MUTAGEN 910 913 MALY->AAAA: Impairs interaction with
AMBRA1, DTL and DCAF5.
{ECO:0000269|PubMed:16949367}.
MUTAGEN 953 953 W->A: Impairs interaction with AMBRA1,
ERCC8, DCAF5 and DCAF11.
{ECO:0000269|PubMed:16949367}.
CONFLICT 422 422 D -> Y (in Ref. 3; AAA88883).
{ECO:0000305}.
CONFLICT 533 533 E -> G (in Ref. 4; CAA05770).
{ECO:0000305}.
CONFLICT 869 869 A -> D (in Ref. 4; CAA05770).
{ECO:0000305}.
CONFLICT 898 899 EL -> DV (in Ref. 3; AAA88883 and 4;
CAA05770). {ECO:0000305}.
STRAND 4 10 {ECO:0000244|PDB:3EI3}.
STRAND 17 21 {ECO:0000244|PDB:3EI3}.
STRAND 26 28 {ECO:0000244|PDB:3EI2}.
STRAND 30 35 {ECO:0000244|PDB:3EI3}.
STRAND 38 45 {ECO:0000244|PDB:3EI3}.
STRAND 48 56 {ECO:0000244|PDB:3EI3}.
STRAND 61 67 {ECO:0000244|PDB:3EI3}.
STRAND 72 74 {ECO:0000244|PDB:2HYE}.
STRAND 76 81 {ECO:0000244|PDB:3EI3}.
TURN 82 84 {ECO:0000244|PDB:3I8E}.
STRAND 85 92 {ECO:0000244|PDB:3EI3}.
STRAND 95 97 {ECO:0000244|PDB:3I7K}.
STRAND 99 107 {ECO:0000244|PDB:3EI3}.
STRAND 121 124 {ECO:0000244|PDB:3EI3}.
STRAND 128 134 {ECO:0000244|PDB:3EI3}.
STRAND 139 144 {ECO:0000244|PDB:3EI3}.
STRAND 146 148 {ECO:0000244|PDB:3EI4}.
STRAND 155 158 {ECO:0000244|PDB:3EI3}.
STRAND 164 169 {ECO:0000244|PDB:3EI3}.
STRAND 177 184 {ECO:0000244|PDB:3EI3}.
STRAND 187 196 {ECO:0000244|PDB:3EI3}.
TURN 197 200 {ECO:0000244|PDB:3EI3}.
STRAND 201 204 {ECO:0000244|PDB:3EI3}.
STRAND 210 212 {ECO:0000244|PDB:3EI3}.
STRAND 218 221 {ECO:0000244|PDB:3EI3}.
TURN 224 226 {ECO:0000244|PDB:3EI3}.
STRAND 229 232 {ECO:0000244|PDB:3EI3}.
STRAND 237 241 {ECO:0000244|PDB:3EI3}.
STRAND 244 248 {ECO:0000244|PDB:3EI3}.
HELIX 251 255 {ECO:0000244|PDB:3EI3}.
STRAND 258 263 {ECO:0000244|PDB:3EI3}.
STRAND 268 275 {ECO:0000244|PDB:3EI3}.
STRAND 279 288 {ECO:0000244|PDB:3EI3}.
STRAND 291 293 {ECO:0000244|PDB:3I7K}.
STRAND 296 307 {ECO:0000244|PDB:3EI3}.
STRAND 312 316 {ECO:0000244|PDB:3EI3}.
TURN 318 320 {ECO:0000244|PDB:4CI2}.
STRAND 321 325 {ECO:0000244|PDB:3EI3}.
STRAND 327 329 {ECO:0000244|PDB:3EI3}.
STRAND 331 336 {ECO:0000244|PDB:3EI3}.
HELIX 342 344 {ECO:0000244|PDB:3I7K}.
STRAND 347 353 {ECO:0000244|PDB:3EI3}.
STRAND 358 365 {ECO:0000244|PDB:3EI3}.
STRAND 369 371 {ECO:0000244|PDB:3EI3}.
STRAND 374 379 {ECO:0000244|PDB:3EI3}.
HELIX 382 384 {ECO:0000244|PDB:3EI3}.
STRAND 386 394 {ECO:0000244|PDB:3EI3}.
STRAND 396 402 {ECO:0000244|PDB:3EI3}.
STRAND 409 413 {ECO:0000244|PDB:3EI3}.
STRAND 417 419 {ECO:0000244|PDB:3EI2}.
STRAND 420 422 {ECO:0000244|PDB:4CI2}.
STRAND 424 429 {ECO:0000244|PDB:3EI3}.
STRAND 432 439 {ECO:0000244|PDB:3EI3}.
STRAND 442 446 {ECO:0000244|PDB:3EI3}.
STRAND 449 451 {ECO:0000244|PDB:2B5N}.
STRAND 453 455 {ECO:0000244|PDB:3EI3}.
STRAND 457 463 {ECO:0000244|PDB:3EI3}.
TURN 464 466 {ECO:0000244|PDB:3EI3}.
STRAND 467 474 {ECO:0000244|PDB:3EI3}.
STRAND 476 483 {ECO:0000244|PDB:3EI3}.
STRAND 486 490 {ECO:0000244|PDB:3EI3}.
STRAND 493 495 {ECO:0000244|PDB:3I7L}.
STRAND 500 503 {ECO:0000244|PDB:3EI3}.
STRAND 505 512 {ECO:0000244|PDB:3EI3}.
STRAND 515 522 {ECO:0000244|PDB:3EI3}.
STRAND 525 533 {ECO:0000244|PDB:3EI3}.
STRAND 535 537 {ECO:0000244|PDB:4E5Z}.
STRAND 538 542 {ECO:0000244|PDB:3EI3}.
STRAND 547 549 {ECO:0000244|PDB:3EI3}.
STRAND 550 552 {ECO:0000244|PDB:3I7L}.
STRAND 554 560 {ECO:0000244|PDB:3EI3}.
TURN 561 564 {ECO:0000244|PDB:3EI3}.
STRAND 565 570 {ECO:0000244|PDB:3EI3}.
TURN 571 573 {ECO:0000244|PDB:3EI3}.
STRAND 576 581 {ECO:0000244|PDB:3EI3}.
STRAND 583 585 {ECO:0000244|PDB:3I7K}.
STRAND 588 596 {ECO:0000244|PDB:3EI3}.
STRAND 599 606 {ECO:0000244|PDB:3EI3}.
STRAND 609 616 {ECO:0000244|PDB:3EI3}.
TURN 618 620 {ECO:0000244|PDB:3EI3}.
STRAND 623 630 {ECO:0000244|PDB:3EI3}.
STRAND 637 645 {ECO:0000244|PDB:3EI3}.
STRAND 647 655 {ECO:0000244|PDB:3EI3}.
STRAND 657 674 {ECO:0000244|PDB:3EI3}.
STRAND 678 682 {ECO:0000244|PDB:3EI3}.
STRAND 685 687 {ECO:0000244|PDB:3EI3}.
STRAND 690 694 {ECO:0000244|PDB:3EI3}.
STRAND 696 698 {ECO:0000244|PDB:4E5Z}.
STRAND 699 704 {ECO:0000244|PDB:3EI3}.
STRAND 707 716 {ECO:0000244|PDB:3EI3}.
STRAND 718 727 {ECO:0000244|PDB:3EI3}.
HELIX 728 730 {ECO:0000244|PDB:3EI3}.
STRAND 732 743 {ECO:0000244|PDB:3EI3}.
STRAND 745 753 {ECO:0000244|PDB:3EI3}.
HELIX 756 759 {ECO:0000244|PDB:3EI3}.
STRAND 761 765 {ECO:0000244|PDB:3EI3}.
STRAND 774 776 {ECO:0000244|PDB:5JK7}.
STRAND 781 783 {ECO:0000244|PDB:4E54}.
STRAND 785 795 {ECO:0000244|PDB:3EI3}.
TURN 796 798 {ECO:0000244|PDB:3EI3}.
STRAND 801 806 {ECO:0000244|PDB:3EI3}.
STRAND 811 819 {ECO:0000244|PDB:3EI3}.
STRAND 823 826 {ECO:0000244|PDB:3EI4}.
STRAND 828 835 {ECO:0000244|PDB:3EI3}.
STRAND 840 842 {ECO:0000244|PDB:3I7N}.
STRAND 846 854 {ECO:0000244|PDB:3EI3}.
STRAND 857 868 {ECO:0000244|PDB:3EI3}.
STRAND 870 876 {ECO:0000244|PDB:3EI3}.
STRAND 879 884 {ECO:0000244|PDB:3EI3}.
STRAND 887 893 {ECO:0000244|PDB:3EI3}.
STRAND 895 897 {ECO:0000244|PDB:3I7H}.
STRAND 899 905 {ECO:0000244|PDB:3EI3}.
STRAND 911 917 {ECO:0000244|PDB:3EI3}.
STRAND 920 928 {ECO:0000244|PDB:3EI3}.
STRAND 930 936 {ECO:0000244|PDB:3EI3}.
TURN 937 940 {ECO:0000244|PDB:3EI3}.
STRAND 941 947 {ECO:0000244|PDB:3EI3}.
STRAND 954 961 {ECO:0000244|PDB:3EI3}.
STRAND 964 969 {ECO:0000244|PDB:3EI3}.
STRAND 972 979 {ECO:0000244|PDB:3EI3}.
STRAND 982 984 {ECO:0000244|PDB:3I7K}.
TURN 985 987 {ECO:0000244|PDB:3I7K}.
HELIX 988 990 {ECO:0000244|PDB:3EI3}.
STRAND 991 999 {ECO:0000244|PDB:3EI3}.
STRAND 1004 1009 {ECO:0000244|PDB:3EI3}.
STRAND 1017 1020 {ECO:0000244|PDB:3EI4}.
STRAND 1024 1032 {ECO:0000244|PDB:3EI3}.
STRAND 1037 1043 {ECO:0000244|PDB:3EI3}.
HELIX 1045 1061 {ECO:0000244|PDB:3EI3}.
HELIX 1065 1067 {ECO:0000244|PDB:3EI1}.
HELIX 1070 1074 {ECO:0000244|PDB:3EI3}.
STRAND 1075 1077 {ECO:0000244|PDB:3EI3}.
STRAND 1081 1083 {ECO:0000244|PDB:3I7N}.
STRAND 1086 1090 {ECO:0000244|PDB:3EI3}.
HELIX 1091 1095 {ECO:0000244|PDB:3EI3}.
HELIX 1096 1099 {ECO:0000244|PDB:3EI3}.
HELIX 1102 1108 {ECO:0000244|PDB:3EI3}.
TURN 1109 1111 {ECO:0000244|PDB:4A08}.
STRAND 1113 1115 {ECO:0000244|PDB:5JK7}.
STRAND 1117 1120 {ECO:0000244|PDB:2B5L}.
STRAND 1121 1123 {ECO:0000244|PDB:5JK7}.
HELIX 1127 1136 {ECO:0000244|PDB:3EI3}.
HELIX 1137 1139 {ECO:0000244|PDB:3EI3}.
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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