Full text data of DDB1
DDB1
(XAP1)
[Confidence: high (present in two of the MS resources)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00293464
IPI00293464 DNA damage binding protein 1 Involved in the repair of UV-damaged DNA. Binds to pyrimidine dimers, peripheral blood soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band around 188 kDa
IPI00293464 DNA damage binding protein 1 Involved in the repair of UV-damaged DNA. Binds to pyrimidine dimers, peripheral blood soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band around 188 kDa
UniProt
Q16531
ID DDB1_HUMAN Reviewed; 1140 AA.
AC Q16531; A6NG77; B2R648; O15176; Q13289; Q58F96;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT DDB2) for the p127 and p48 subunits of a human damage-specific DNA
RT binding protein.";
RL Genomics 29:62-69(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=7815490;
RA Lee T.H., Elledge S.J., Butel J.S.;
RT "Hepatitis B virus X protein interacts with a probable cellular DNA
RT repair protein.";
RL J. Virol. 69:1107-1114(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT defective in xeroderma pigmentosum group E cells.";
RL Mutat. Res. 362:105-117(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT component of UV-damaged DNA recognition activity.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH DDB1, AND DNA-BINDING.
RX PubMed=9632823;
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
RT 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.
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,
RP IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB2 AND RBX1, IDENTIFICATION
RP IN THE CSA COMPLEX WITH CUL4A; ERCC8 AND RBX1, INTERACTION OF THE CSA
RP COMPLEX WITH RNA POLYMERASE II, AND INTERACTION WITH THE COP9
RP SIGNALOSOME.
RX PubMed=12732143; DOI=10.1016/S0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M.,
RA Drapkin R., 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.
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
RT similar 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
RP CDT1; 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
RT response to DNA damage.";
RL Nat. Cell Biol. 6:1003-1009(2004).
RN [17]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP CUL4A; DET1; RBX1 AND RFWD2.
RX PubMed=14739464; DOI=10.1126/science.1093549;
RA Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D.,
RA Deshaies R.J., 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.,
RA Mori T., 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
RT a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic
RT sites, and compound lesions in DNA.";
RL J. Biol. Chem. 280:39982-39989(2005).
RN [20]
RP INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V.
RX PubMed=16227264; DOI=10.1128/JVI.79.21.13434-13441.2005;
RA Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S.,
RA Randall R.E.;
RT "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2,
RT to 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,
RP AND 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
RT DNA 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.,
RA Obuse C., Tsurimoto T., Nakayama K.I., Nakayama K., Fujita M.,
RA Lygerou Z., Nishimoto T.;
RT "Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1
RT for 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; RFWD2; VPRBP; 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-
RT ROC1 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
RT antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in
RT response to DNA 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-
RT terminal 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.,
RA 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, MASS
RP 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
RT ligase 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;
RP DTL; ERCC8; DCAF6; PHIP; VPRBP; DCAF4; DCAF5; DCAF11; DCAF10; DCAF12;
RP DCAF8; DCAF7 AND WDTC1, AND MUTAGENESIS OF 316-TYR--ASN-319;
RP 840-GLU--GLU-842; 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,
RT which is required for S phase destruction of the replication factor
RT 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
RP CUL4B; DTL; NLE1; PAFAH1B1; RBBP5; RFWD2; SNRNP40; WDR5; WDR5B; WDR12;
RP WDR26; 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
RT proteins and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [31]
RP FUNCTION, INTERACTION WITH CUL4A; DDB2; HISTONE H2A AND RBX1,
RP DNA-BINDING, 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
RT pigmentosum 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-
RT protein complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [33]
RP FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB2, AND SUBCELLULAR
RP 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
RT UV-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.,
RA 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
RT essential for DNA replication and embryonic development.";
RL Mol. Cell. Biol. 28:5621-5633(2008).
RN [36]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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
RT regulates Pr-Set7/Set8-mediated cellular migration.";
RL Mol. Cell 49:1147-1158(2013).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-1140 IN COMPLEX WITH
RP SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH CUL4A AND DET1, AND
RP MUTAGENESIS OF 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
RT hijack of a propeller cluster in ubiquitin ligase.";
RL Cell 124:105-117(2006).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-1140 IN COMPLEX WITH CUL4A;
RP RBX1 AND SIMIAN VIRUS 5 PROTEIN V, AND INTERACTION WITH DDB2; DTL;
RP DCAF11; DCAF8 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
RT ligase machinery.";
RL Nature 443:590-593(2006).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA,
RP 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
RT complex.";
RL Cell 135:1213-1223(2008).
CC -!- FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-
CC damaged DNA-binding protein complex (the UV-DDB complex). The UV-
CC DDB complex may recognize UV-induced DNA damage and recruit
CC proteins of the nucleotide excision repair pathway (the NER
CC pathway) to initiate DNA repair. The UV-DDB complex preferentially
CC binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts
CC (6-4 PP), apurinic sites and short mismatches. Also appears to
CC function as a component of numerous distinct DCX (DDB1-CUL4-X-box)
CC E3 ubiquitin-protein ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. The functional specificity of the DCX E3 ubiquitin-
CC protein ligase complex is determined by the variable substrate
CC recognition component recruited by DDB1. DCX(DDB2) (also known as
CC DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate
CC histone H2A, histone H3 and histone H4 at sites of UV-induced DNA
CC damage. The ubiquitination of histones may facilitate their
CC removal from the nucleosome and promote subsequent DNA repair.
CC DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by
CC XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent
CC polyubiquitination of CDT1 and MDM2-dependent ubiquitination of
CC TP53 in response to radiation-induced DNA damage and during DNA
CC replication. DCX(ERCC8) (the CSA complex) plays a role in
CC transcription-coupled repair (TCR). May also play a role in
CC ubiquitination of CDKN1B/p27kip when associated with CUL4 and
CC SKP2.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
CC DDB2. The UV-DDB complex interacts with monoubiquitinated histone
CC H2A and binds to XPC via the DDB2 subunit. Component of numerous
CC DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which
CC consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may
CC recruit specific substrate targeting subunits to the DCX complex.
CC These substrate targeting subunits are generally known as DCAF
CC (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated
CC WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC,
CC DCAF1, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5,
CC FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1,
CC RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12,
CC DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8,
CC WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2, LRWD1 and WDTC1. DCX
CC complexes may associate with the COP9 signalosome, and this
CC inhibits the E3 ubiquitin-protein ligase activity of the complex.
CC Interacts with NF2, TSC1 and TSC2. Interacts with Simian virus 5
CC protein V and the HBV X protein. Interaction with SV5 protein V
CC may prevent the recruitment of DCAF proteins to DCX complexes.
CC Interacts with AGO1 and AGO2. Associates with the E3 ligase
CC complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP
CC complex). Interacts directly with DYRK2. DCX(DTL) complex
CC interacts with FBXO11; does not ubiquitinate and degradate FBXO11.
CC -!- INTERACTION:
CC Q9H9F9:ACTR5; NbExp=3; IntAct=EBI-350322, EBI-769418;
CC Q13619:CUL4A; NbExp=4; IntAct=EBI-350322, EBI-456106;
CC Q13620:CUL4B; NbExp=15; IntAct=EBI-350322, EBI-456067;
CC Q92466:DDB2; NbExp=3; IntAct=EBI-350322, EBI-1176171;
CC Q9NZJ0:DTL; NbExp=3; IntAct=EBI-350322, EBI-1176075;
CC O75530:EED; NbExp=4; IntAct=EBI-350322, EBI-923794;
CC Q9ULG1:INO80; NbExp=4; IntAct=EBI-350322, EBI-769345;
CC P11207:P/V (xeno); NbExp=3; IntAct=EBI-350322, EBI-6148694;
CC P42224:STAT1; NbExp=2; IntAct=EBI-350322, EBI-1057697;
CC Q04725:TLE2; NbExp=2; IntAct=EBI-350322, EBI-1176061;
CC Q9Y4B6:VPRBP; NbExp=2; IntAct=EBI-350322, EBI-1996353;
CC P18045:vpx (xeno); NbExp=2; IntAct=EBI-350322, EBI-6558105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Primarily
CC cytoplasmic. Translocates to the nucleus following UV irradiation
CC and subsequently accumulates at sites of DNA damage.
CC -!- PTM: Phosphorylated by ABL1 (By similarity).
CC -!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-
CC dependent proteolysis.
CC -!- SIMILARITY: Belongs to the DDB1 family.
CC -!- WEB RESOURCE: Name=Allelic variations of the XP genes;
CC URL="http://www.xpmutations.org/";
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; AK312436; BAG35345.1; -; mRNA.
DR EMBL; AY960579; AAX44048.1; -; 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 PIR; I38908; I38908.
DR RefSeq; NP_001914.3; NM_001923.4.
DR RefSeq; XP_005273861.1; XM_005273804.1.
DR UniGene; Hs.290758; -.
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; 4E54; X-ray; 2.85 A; A=2-1140.
DR PDB; 4E5Z; X-ray; 3.22 A; A=2-1140.
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; 4E54; -.
DR PDBsum; 4E5Z; -.
DR ProteinModelPortal; Q16531; -.
DR SMR; Q16531; 2-1140.
DR DIP; DIP-430N; -.
DR IntAct; Q16531; 67.
DR MINT; MINT-1134697; -.
DR STRING; 9606.ENSP00000301764; -.
DR PhosphoSite; Q16531; -.
DR PaxDb; Q16531; -.
DR PRIDE; Q16531; -.
DR Ensembl; ENST00000301764; ENSP00000301764; ENSG00000167986.
DR GeneID; 1642; -.
DR KEGG; hsa:1642; -.
DR UCSC; uc001nrc.5; human.
DR CTD; 1642; -.
DR GeneCards; GC11M061066; -.
DR H-InvDB; HIX0171380; -.
DR HGNC; HGNC:2717; DDB1.
DR HPA; CAB032821; -.
DR MIM; 600045; gene.
DR neXtProt; NX_Q16531; -.
DR PharmGKB; PA27187; -.
DR eggNOG; NOG247734; -.
DR HOGENOM; HOG000007241; -.
DR HOVERGEN; HBG005460; -.
DR InParanoid; Q16531; -.
DR KO; K10610; -.
DR OMA; CAVGLWT; -.
DR OrthoDB; EOG7X0VG9; -.
DR Reactome; REACT_216; DNA Repair.
DR UniPathway; UPA00143; -.
DR ChiTaRS; DDB1; human.
DR EvolutionaryTrace; Q16531; -.
DR GeneWiki; DDB1; -.
DR GenomeRNAi; 1642; -.
DR NextBio; 6750; -.
DR PRO; PR:Q16531; -.
DR ArrayExpress; Q16531; -.
DR Bgee; Q16531; -.
DR CleanEx; HS_DDB1; -.
DR Genevestigator; Q16531; -.
DR GO; GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; TAS:Reactome.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF03178; CPSF_A; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; DNA damage;
KW DNA repair; DNA-binding; Host-virus interaction; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1140 DNA damage-binding protein 1.
FT /FTId=PRO_0000079840.
FT REGION 2 768 Interaction with CDT1.
FT REGION 391 709 Interaction with CUL4A.
FT REGION 771 1140 Interaction with CDT1 and CUL4A.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 1067 1067 N6-acetyllysine.
FT VARIANT 427 427 L -> F (in dbSNP:rs28720299).
FT /FTId=VAR_023074.
FT MUTAGEN 316 319 YLDN->ALAA: Impairs interaction with
FT DDA1.
FT MUTAGEN 537 537 E->A: Slightly impairs interaction with
FT CUL4A.
FT MUTAGEN 561 561 W->A: Strongly impairs interaction with
FT CUL4A.
FT MUTAGEN 840 842 EAE->AAA: Impairs interaction with
FT AMBRA1, DTL, DET1, VPRBP, DCAF5, DCAF11
FT and DCAF8.
FT MUTAGEN 910 913 MALY->AAAA: Impairs interaction with
FT AMBRA1, DTL and DCAF5.
FT MUTAGEN 953 953 W->A: Impairs interaction with AMBRA1,
FT ERCC8, DCAF5 and DCAF11.
FT CONFLICT 422 422 D -> Y (in Ref. 3; AAA88883).
FT CONFLICT 533 533 E -> G (in Ref. 4; CAA05770).
FT CONFLICT 869 869 A -> D (in Ref. 4; CAA05770).
FT CONFLICT 898 899 EL -> DV (in Ref. 3; AAA88883 and 4;
FT CAA05770).
FT STRAND 4 10
FT STRAND 17 21
FT STRAND 26 28
FT STRAND 30 35
FT STRAND 38 45
FT STRAND 48 56
FT STRAND 61 67
FT STRAND 72 74
FT STRAND 76 81
FT TURN 82 84
FT STRAND 85 92
FT STRAND 95 97
FT STRAND 99 107
FT STRAND 121 124
FT STRAND 128 134
FT STRAND 139 144
FT STRAND 146 148
FT STRAND 155 158
FT STRAND 164 169
FT STRAND 177 184
FT STRAND 187 196
FT TURN 197 200
FT STRAND 201 204
FT STRAND 210 212
FT STRAND 218 221
FT TURN 224 226
FT STRAND 229 232
FT STRAND 237 241
FT STRAND 244 248
FT HELIX 251 255
FT STRAND 258 263
FT STRAND 268 275
FT STRAND 279 288
FT STRAND 291 293
FT STRAND 296 307
FT STRAND 312 316
FT STRAND 321 325
FT STRAND 327 329
FT STRAND 331 336
FT HELIX 342 344
FT STRAND 347 353
FT STRAND 358 365
FT STRAND 369 371
FT STRAND 374 379
FT HELIX 382 384
FT STRAND 386 394
FT STRAND 396 402
FT STRAND 409 413
FT STRAND 417 419
FT STRAND 420 422
FT STRAND 424 429
FT STRAND 432 439
FT STRAND 442 446
FT STRAND 449 451
FT STRAND 453 455
FT STRAND 457 463
FT TURN 464 466
FT STRAND 467 474
FT STRAND 476 483
FT STRAND 486 490
FT STRAND 493 495
FT STRAND 500 503
FT STRAND 505 512
FT STRAND 515 522
FT STRAND 525 533
FT STRAND 535 537
FT STRAND 538 542
FT STRAND 547 549
FT STRAND 550 552
FT STRAND 554 560
FT TURN 561 564
FT STRAND 565 570
FT TURN 571 573
FT STRAND 576 581
FT STRAND 583 585
FT STRAND 588 596
FT STRAND 599 606
FT STRAND 609 616
FT TURN 618 620
FT STRAND 623 630
FT STRAND 637 645
FT STRAND 647 655
FT STRAND 657 674
FT STRAND 678 682
FT STRAND 685 687
FT STRAND 690 694
FT STRAND 696 698
FT STRAND 699 704
FT STRAND 707 716
FT STRAND 718 727
FT HELIX 728 730
FT STRAND 732 743
FT STRAND 745 753
FT HELIX 756 759
FT STRAND 761 765
FT STRAND 781 783
FT STRAND 785 795
FT TURN 796 798
FT STRAND 801 806
FT STRAND 811 819
FT STRAND 823 826
FT STRAND 828 835
FT STRAND 840 842
FT STRAND 846 854
FT STRAND 857 868
FT STRAND 870 876
FT STRAND 879 884
FT STRAND 887 893
FT STRAND 895 897
FT STRAND 899 905
FT STRAND 911 917
FT STRAND 920 928
FT STRAND 930 936
FT TURN 937 940
FT STRAND 941 947
FT STRAND 954 961
FT STRAND 964 969
FT STRAND 972 979
FT STRAND 982 984
FT TURN 985 987
FT HELIX 988 990
FT STRAND 991 999
FT STRAND 1004 1009
FT STRAND 1017 1020
FT STRAND 1024 1032
FT STRAND 1037 1043
FT HELIX 1045 1061
FT HELIX 1065 1067
FT HELIX 1070 1074
FT STRAND 1075 1077
FT STRAND 1081 1083
FT STRAND 1086 1090
FT HELIX 1091 1095
FT HELIX 1096 1099
FT HELIX 1102 1108
FT TURN 1109 1111
FT STRAND 1117 1120
FT HELIX 1127 1136
FT HELIX 1137 1139
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
//
ID DDB1_HUMAN Reviewed; 1140 AA.
AC Q16531; A6NG77; B2R648; O15176; Q13289; Q58F96;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT DDB2) for the p127 and p48 subunits of a human damage-specific DNA
RT binding protein.";
RL Genomics 29:62-69(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=7815490;
RA Lee T.H., Elledge S.J., Butel J.S.;
RT "Hepatitis B virus X protein interacts with a probable cellular DNA
RT repair protein.";
RL J. Virol. 69:1107-1114(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT defective in xeroderma pigmentosum group E cells.";
RL Mutat. Res. 362:105-117(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT component of UV-damaged DNA recognition activity.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH DDB1, AND DNA-BINDING.
RX PubMed=9632823;
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
RT 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.
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,
RP IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB2 AND RBX1, IDENTIFICATION
RP IN THE CSA COMPLEX WITH CUL4A; ERCC8 AND RBX1, INTERACTION OF THE CSA
RP COMPLEX WITH RNA POLYMERASE II, AND INTERACTION WITH THE COP9
RP SIGNALOSOME.
RX PubMed=12732143; DOI=10.1016/S0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M.,
RA Drapkin R., 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.
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
RT similar 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
RP CDT1; 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
RT response to DNA damage.";
RL Nat. Cell Biol. 6:1003-1009(2004).
RN [17]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP CUL4A; DET1; RBX1 AND RFWD2.
RX PubMed=14739464; DOI=10.1126/science.1093549;
RA Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D.,
RA Deshaies R.J., 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.,
RA Mori T., 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
RT a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic
RT sites, and compound lesions in DNA.";
RL J. Biol. Chem. 280:39982-39989(2005).
RN [20]
RP INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V.
RX PubMed=16227264; DOI=10.1128/JVI.79.21.13434-13441.2005;
RA Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S.,
RA Randall R.E.;
RT "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2,
RT to 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,
RP AND 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
RT DNA 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.,
RA Obuse C., Tsurimoto T., Nakayama K.I., Nakayama K., Fujita M.,
RA Lygerou Z., Nishimoto T.;
RT "Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1
RT for 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; RFWD2; VPRBP; 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-
RT ROC1 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
RT antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in
RT response to DNA 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-
RT terminal 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.,
RA 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, MASS
RP 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
RT ligase 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;
RP DTL; ERCC8; DCAF6; PHIP; VPRBP; DCAF4; DCAF5; DCAF11; DCAF10; DCAF12;
RP DCAF8; DCAF7 AND WDTC1, AND MUTAGENESIS OF 316-TYR--ASN-319;
RP 840-GLU--GLU-842; 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,
RT which is required for S phase destruction of the replication factor
RT 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
RP CUL4B; DTL; NLE1; PAFAH1B1; RBBP5; RFWD2; SNRNP40; WDR5; WDR5B; WDR12;
RP WDR26; 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
RT proteins and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [31]
RP FUNCTION, INTERACTION WITH CUL4A; DDB2; HISTONE H2A AND RBX1,
RP DNA-BINDING, 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
RT pigmentosum 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-
RT protein complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [33]
RP FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB2, AND SUBCELLULAR
RP 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
RT UV-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.,
RA 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
RT essential for DNA replication and embryonic development.";
RL Mol. Cell. Biol. 28:5621-5633(2008).
RN [36]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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
RT regulates Pr-Set7/Set8-mediated cellular migration.";
RL Mol. Cell 49:1147-1158(2013).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-1140 IN COMPLEX WITH
RP SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH CUL4A AND DET1, AND
RP MUTAGENESIS OF 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
RT hijack of a propeller cluster in ubiquitin ligase.";
RL Cell 124:105-117(2006).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-1140 IN COMPLEX WITH CUL4A;
RP RBX1 AND SIMIAN VIRUS 5 PROTEIN V, AND INTERACTION WITH DDB2; DTL;
RP DCAF11; DCAF8 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
RT ligase machinery.";
RL Nature 443:590-593(2006).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA,
RP 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
RT complex.";
RL Cell 135:1213-1223(2008).
CC -!- FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-
CC damaged DNA-binding protein complex (the UV-DDB complex). The UV-
CC DDB complex may recognize UV-induced DNA damage and recruit
CC proteins of the nucleotide excision repair pathway (the NER
CC pathway) to initiate DNA repair. The UV-DDB complex preferentially
CC binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts
CC (6-4 PP), apurinic sites and short mismatches. Also appears to
CC function as a component of numerous distinct DCX (DDB1-CUL4-X-box)
CC E3 ubiquitin-protein ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. The functional specificity of the DCX E3 ubiquitin-
CC protein ligase complex is determined by the variable substrate
CC recognition component recruited by DDB1. DCX(DDB2) (also known as
CC DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate
CC histone H2A, histone H3 and histone H4 at sites of UV-induced DNA
CC damage. The ubiquitination of histones may facilitate their
CC removal from the nucleosome and promote subsequent DNA repair.
CC DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by
CC XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent
CC polyubiquitination of CDT1 and MDM2-dependent ubiquitination of
CC TP53 in response to radiation-induced DNA damage and during DNA
CC replication. DCX(ERCC8) (the CSA complex) plays a role in
CC transcription-coupled repair (TCR). May also play a role in
CC ubiquitination of CDKN1B/p27kip when associated with CUL4 and
CC SKP2.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
CC DDB2. The UV-DDB complex interacts with monoubiquitinated histone
CC H2A and binds to XPC via the DDB2 subunit. Component of numerous
CC DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which
CC consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may
CC recruit specific substrate targeting subunits to the DCX complex.
CC These substrate targeting subunits are generally known as DCAF
CC (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated
CC WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC,
CC DCAF1, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5,
CC FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1,
CC RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12,
CC DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8,
CC WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2, LRWD1 and WDTC1. DCX
CC complexes may associate with the COP9 signalosome, and this
CC inhibits the E3 ubiquitin-protein ligase activity of the complex.
CC Interacts with NF2, TSC1 and TSC2. Interacts with Simian virus 5
CC protein V and the HBV X protein. Interaction with SV5 protein V
CC may prevent the recruitment of DCAF proteins to DCX complexes.
CC Interacts with AGO1 and AGO2. Associates with the E3 ligase
CC complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP
CC complex). Interacts directly with DYRK2. DCX(DTL) complex
CC interacts with FBXO11; does not ubiquitinate and degradate FBXO11.
CC -!- INTERACTION:
CC Q9H9F9:ACTR5; NbExp=3; IntAct=EBI-350322, EBI-769418;
CC Q13619:CUL4A; NbExp=4; IntAct=EBI-350322, EBI-456106;
CC Q13620:CUL4B; NbExp=15; IntAct=EBI-350322, EBI-456067;
CC Q92466:DDB2; NbExp=3; IntAct=EBI-350322, EBI-1176171;
CC Q9NZJ0:DTL; NbExp=3; IntAct=EBI-350322, EBI-1176075;
CC O75530:EED; NbExp=4; IntAct=EBI-350322, EBI-923794;
CC Q9ULG1:INO80; NbExp=4; IntAct=EBI-350322, EBI-769345;
CC P11207:P/V (xeno); NbExp=3; IntAct=EBI-350322, EBI-6148694;
CC P42224:STAT1; NbExp=2; IntAct=EBI-350322, EBI-1057697;
CC Q04725:TLE2; NbExp=2; IntAct=EBI-350322, EBI-1176061;
CC Q9Y4B6:VPRBP; NbExp=2; IntAct=EBI-350322, EBI-1996353;
CC P18045:vpx (xeno); NbExp=2; IntAct=EBI-350322, EBI-6558105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Primarily
CC cytoplasmic. Translocates to the nucleus following UV irradiation
CC and subsequently accumulates at sites of DNA damage.
CC -!- PTM: Phosphorylated by ABL1 (By similarity).
CC -!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-
CC dependent proteolysis.
CC -!- SIMILARITY: Belongs to the DDB1 family.
CC -!- WEB RESOURCE: Name=Allelic variations of the XP genes;
CC URL="http://www.xpmutations.org/";
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; AK312436; BAG35345.1; -; mRNA.
DR EMBL; AY960579; AAX44048.1; -; 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 PIR; I38908; I38908.
DR RefSeq; NP_001914.3; NM_001923.4.
DR RefSeq; XP_005273861.1; XM_005273804.1.
DR UniGene; Hs.290758; -.
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; 4E54; X-ray; 2.85 A; A=2-1140.
DR PDB; 4E5Z; X-ray; 3.22 A; A=2-1140.
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; 4E54; -.
DR PDBsum; 4E5Z; -.
DR ProteinModelPortal; Q16531; -.
DR SMR; Q16531; 2-1140.
DR DIP; DIP-430N; -.
DR IntAct; Q16531; 67.
DR MINT; MINT-1134697; -.
DR STRING; 9606.ENSP00000301764; -.
DR PhosphoSite; Q16531; -.
DR PaxDb; Q16531; -.
DR PRIDE; Q16531; -.
DR Ensembl; ENST00000301764; ENSP00000301764; ENSG00000167986.
DR GeneID; 1642; -.
DR KEGG; hsa:1642; -.
DR UCSC; uc001nrc.5; human.
DR CTD; 1642; -.
DR GeneCards; GC11M061066; -.
DR H-InvDB; HIX0171380; -.
DR HGNC; HGNC:2717; DDB1.
DR HPA; CAB032821; -.
DR MIM; 600045; gene.
DR neXtProt; NX_Q16531; -.
DR PharmGKB; PA27187; -.
DR eggNOG; NOG247734; -.
DR HOGENOM; HOG000007241; -.
DR HOVERGEN; HBG005460; -.
DR InParanoid; Q16531; -.
DR KO; K10610; -.
DR OMA; CAVGLWT; -.
DR OrthoDB; EOG7X0VG9; -.
DR Reactome; REACT_216; DNA Repair.
DR UniPathway; UPA00143; -.
DR ChiTaRS; DDB1; human.
DR EvolutionaryTrace; Q16531; -.
DR GeneWiki; DDB1; -.
DR GenomeRNAi; 1642; -.
DR NextBio; 6750; -.
DR PRO; PR:Q16531; -.
DR ArrayExpress; Q16531; -.
DR Bgee; Q16531; -.
DR CleanEx; HS_DDB1; -.
DR Genevestigator; Q16531; -.
DR GO; GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; TAS:Reactome.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF03178; CPSF_A; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; DNA damage;
KW DNA repair; DNA-binding; Host-virus interaction; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1140 DNA damage-binding protein 1.
FT /FTId=PRO_0000079840.
FT REGION 2 768 Interaction with CDT1.
FT REGION 391 709 Interaction with CUL4A.
FT REGION 771 1140 Interaction with CDT1 and CUL4A.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 1067 1067 N6-acetyllysine.
FT VARIANT 427 427 L -> F (in dbSNP:rs28720299).
FT /FTId=VAR_023074.
FT MUTAGEN 316 319 YLDN->ALAA: Impairs interaction with
FT DDA1.
FT MUTAGEN 537 537 E->A: Slightly impairs interaction with
FT CUL4A.
FT MUTAGEN 561 561 W->A: Strongly impairs interaction with
FT CUL4A.
FT MUTAGEN 840 842 EAE->AAA: Impairs interaction with
FT AMBRA1, DTL, DET1, VPRBP, DCAF5, DCAF11
FT and DCAF8.
FT MUTAGEN 910 913 MALY->AAAA: Impairs interaction with
FT AMBRA1, DTL and DCAF5.
FT MUTAGEN 953 953 W->A: Impairs interaction with AMBRA1,
FT ERCC8, DCAF5 and DCAF11.
FT CONFLICT 422 422 D -> Y (in Ref. 3; AAA88883).
FT CONFLICT 533 533 E -> G (in Ref. 4; CAA05770).
FT CONFLICT 869 869 A -> D (in Ref. 4; CAA05770).
FT CONFLICT 898 899 EL -> DV (in Ref. 3; AAA88883 and 4;
FT CAA05770).
FT STRAND 4 10
FT STRAND 17 21
FT STRAND 26 28
FT STRAND 30 35
FT STRAND 38 45
FT STRAND 48 56
FT STRAND 61 67
FT STRAND 72 74
FT STRAND 76 81
FT TURN 82 84
FT STRAND 85 92
FT STRAND 95 97
FT STRAND 99 107
FT STRAND 121 124
FT STRAND 128 134
FT STRAND 139 144
FT STRAND 146 148
FT STRAND 155 158
FT STRAND 164 169
FT STRAND 177 184
FT STRAND 187 196
FT TURN 197 200
FT STRAND 201 204
FT STRAND 210 212
FT STRAND 218 221
FT TURN 224 226
FT STRAND 229 232
FT STRAND 237 241
FT STRAND 244 248
FT HELIX 251 255
FT STRAND 258 263
FT STRAND 268 275
FT STRAND 279 288
FT STRAND 291 293
FT STRAND 296 307
FT STRAND 312 316
FT STRAND 321 325
FT STRAND 327 329
FT STRAND 331 336
FT HELIX 342 344
FT STRAND 347 353
FT STRAND 358 365
FT STRAND 369 371
FT STRAND 374 379
FT HELIX 382 384
FT STRAND 386 394
FT STRAND 396 402
FT STRAND 409 413
FT STRAND 417 419
FT STRAND 420 422
FT STRAND 424 429
FT STRAND 432 439
FT STRAND 442 446
FT STRAND 449 451
FT STRAND 453 455
FT STRAND 457 463
FT TURN 464 466
FT STRAND 467 474
FT STRAND 476 483
FT STRAND 486 490
FT STRAND 493 495
FT STRAND 500 503
FT STRAND 505 512
FT STRAND 515 522
FT STRAND 525 533
FT STRAND 535 537
FT STRAND 538 542
FT STRAND 547 549
FT STRAND 550 552
FT STRAND 554 560
FT TURN 561 564
FT STRAND 565 570
FT TURN 571 573
FT STRAND 576 581
FT STRAND 583 585
FT STRAND 588 596
FT STRAND 599 606
FT STRAND 609 616
FT TURN 618 620
FT STRAND 623 630
FT STRAND 637 645
FT STRAND 647 655
FT STRAND 657 674
FT STRAND 678 682
FT STRAND 685 687
FT STRAND 690 694
FT STRAND 696 698
FT STRAND 699 704
FT STRAND 707 716
FT STRAND 718 727
FT HELIX 728 730
FT STRAND 732 743
FT STRAND 745 753
FT HELIX 756 759
FT STRAND 761 765
FT STRAND 781 783
FT STRAND 785 795
FT TURN 796 798
FT STRAND 801 806
FT STRAND 811 819
FT STRAND 823 826
FT STRAND 828 835
FT STRAND 840 842
FT STRAND 846 854
FT STRAND 857 868
FT STRAND 870 876
FT STRAND 879 884
FT STRAND 887 893
FT STRAND 895 897
FT STRAND 899 905
FT STRAND 911 917
FT STRAND 920 928
FT STRAND 930 936
FT TURN 937 940
FT STRAND 941 947
FT STRAND 954 961
FT STRAND 964 969
FT STRAND 972 979
FT STRAND 982 984
FT TURN 985 987
FT HELIX 988 990
FT STRAND 991 999
FT STRAND 1004 1009
FT STRAND 1017 1020
FT STRAND 1024 1032
FT STRAND 1037 1043
FT HELIX 1045 1061
FT HELIX 1065 1067
FT HELIX 1070 1074
FT STRAND 1075 1077
FT STRAND 1081 1083
FT STRAND 1086 1090
FT HELIX 1091 1095
FT HELIX 1096 1099
FT HELIX 1102 1108
FT TURN 1109 1111
FT STRAND 1117 1120
FT HELIX 1127 1136
FT HELIX 1137 1139
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
//
MIM
600045
*RECORD*
*FIELD* NO
600045
*FIELD* TI
*600045 DNA DAMAGE-BINDING PROTEIN 1; DDB1
;;DDB, p127 SUBUNIT
*FIELD* TX
CLONING
read more
Chu and Chang (1988) found that cells from 2 consanguineous patients
with xeroderma pigmentosum complementation group E (XPE; 278740) lacked
a DNA damage-binding activity that recognizes UV-irradiated DNA. Keeney
et al. (1993) purified the DDB protein to apparent homogeneity and
characterized it from human placenta and from HeLa cells. It was
apparently identical to an activity first described from human placenta.
DDB activity was associated with a polypeptide of approximately 124 kD,
which was found to be complexed with a 41-kD protein. This stable
heterodimer could, in turn, form a higher order complex. To test whether
the DNA-repair defect in the subset of XPE patients that lack DNA
damage-binding activity is caused by a defect in DDB, Keeney et al.
(1994) injected purified human DDB protein into XPE cells. The injected
DDB protein stimulated DNA repair to normal levels in those strains that
lacked the DDB activity but did not stimulate repair in cells from XPE
patients that contained the activity. These results provided direct
evidence that defective DDB activity causes the repair defect in a
subset of XPE patients and establishes a role for this activity in
nucleotide-excision repair in vivo.
The DNA damage-binding protein from HeLa cells is associated with
polypeptides of relative mass 124,000 and 41,000 (DDB2; 600811) as
determined by SDS-polyacrylamide gels. Dualan et al. (1995) isolated
full-length human cDNAs encoding each polypeptide of DDB. The predicted
peptide molecular masses based on open reading frames were 127,000 and
48,000. When expressed in an in vitro rabbit reticulocyte system, the
p48 subunit migrated with a relative mass of 41 kD on SDS-polyacrylamide
gels, similarly to the peptide purified from HeLa cells. There was no
significant homology between the derived p48 peptide sequence in any
proteins in databases, and the derived peptide sequence of p127 had
homology only with the monkey DDB p127 (98% nucleotide identity and only
1 conserved amino acid substitution).
GENE FUNCTION
Wertz et al. (2004) reported that human DET1 (608727) promotes
ubiquitination and degradation of the protooncogenic transcription
factor c-Jun (165160) by assembling a multisubunit ubiquitin ligase
containing DDB1, cullin 4A (CUL4A; 603137), regulator of cullins-1
(ROC1; 603814), and constitutively photomorphogenic-1 (COP1; 608067).
Ablation of any subunit by RNA interference stabilized c-Jun and
increased c-Jun-activated transcription. Wertz et al. (2004) concluded
that their findings characterized a c-Jun ubiquitin ligase and define a
specific function for DET1 in mammalian cells.
By analyzing proteins that immunoprecipitated with anti-CENPA (117139)
antibodies from HeLa cell nuclear lysates, Obuse et al. (2004) showed
that DDB1 associated with a centromeric complex, which also contained
the major centromeric proteins CENPB (117140), CENPC (117141), CENPH
(605607), CENPI (300065), and MIS12 (609178), and many others. DDB1
colocalized with CENPA at centromeres throughout the cell cycle in HeLa
cells; it appeared in both the cytoplasm and nucleus in interphase and
associated with chromosomes in metaphase.
By mass spectrometric analysis, Higa et al. (2006) identified over 20
WD40 repeat-containing (WDR) proteins that interacted with the
CUL4-DDB1-ROC1 complex. Sequence alignment revealed that most of the
interacting WDR proteins had a centrally positioned WDxR/K submotif.
Knockdown studies suggested that the WDR proteins functioned as
substrate-specific adaptors. For example, inactivation of L2DTL (DTL;
610617), but not other WDR proteins, prevented CUL4-DDB1-dependent
proteolysis of CDT1 (605525) following gamma irradiation. Inactivation
of WDR5 (609012) or EED (605984), but not other WDR proteins, altered
the pattern of CUL4-DDB1-dependent histone H3 (see 602810) methylation.
Ito et al. (2010) demonstrated that the thalidomide-binding protein
cereblon (CRBN; 609262) forms an E3 ubiquitin ligase complex with DDB1
and CUL4A that is important for limb outgrowth and expression of the
fibroblast growth factor FGF8 (600483) in zebrafish and chicks. The
authors found that thalidomide initiates its teratogenic effects by
binding to CRBN and inhibiting the associated ubiquitin ligase activity.
Ito et al. (2010) concluded that their study revealed a basis for
thalidomide teratogenicity and may contribute to the development of
thalidomide derivatives without teratogenic activity.
BIOCHEMICAL FEATURES
To reveal how DDB1 incorporates into the CUL4A-ROC1 complex and mediates
substrate recruitment, Angers et al. (2006) determined the 3.1-angstrom
crystal structure of a DDB1-CUL4A-ROC1 complex bound to the V protein of
simian virus 5 (SV5). DDB1 uses 1 beta-propeller domain for cullin
scaffold binding and a variably attached separate double-beta-propeller
fold for substrate presentation. Through tandem-affinity purification of
human DDB1 and CUL4A complexes followed by mass spectrometry analysis,
Angers et al. (2006) identified a novel family of WD40-repeat proteins,
which directly bind to the double-propeller fold of DDB1 and serve as
the substrate-recruiting module of the E3. Together, Angers et al.
(2006) concluded that their structural and proteomic results reveal the
structural mechanisms and molecular logic underlying the assembly and
versatility of a new family of cullin-RING E3 complexes.
MAPPING
Using fluorescence in situ hybridization (FISH), Dualan et al. (1995)
mapped the DDB p127 locus (DDB1) to 11q12-q13, and the DDB p48 locus
(DDB2) to 11p12-p11. Fernandes et al. (1998) used FISH and mouse/hamster
somatic cell hybrid analysis to map the Ddb1 gene to mouse chromosome
19.
MOLECULAR GENETICS
Nichols (1995) reported that RT-PCR mutation analysis in 5 fibroblast
XPE strains (2 without and 3 with DDB-binding activity) covering 90 to
99% of the sequence of the p127 subunit revealed no mutations.
Approximately 40% of the p48 subunit (DDB2) had been sequenced and had
revealed no mutations in 2 fibroblast XPF strains (278760). Mutations
were subsequently demonstrated in the DDB2 gene in the 3 known cases of
DDB-negative XPE (600811) (Nichols et al., 1996).
Stohr et al. (1998) investigated the possible involvement of DDB1 in the
pathogenesis of Best vitelliform macular dystrophy (VMD; 153700) because
that disorder maps to the same region on 11q and because the DDB1 gene
is abundantly expressed in retina. The mutation screening of the DDB1
gene demonstrated no sequence alterations in patients with Best disease.
ANIMAL MODEL
Cang et al. (2006) found that the deletion of the Ddb1 gene in mice
caused early embryonic lethality. Conditional inactivation of Ddb1 in
brain and lens led to neuronal and lens degeneration, brain hemorrhages,
and neonatal death. These defects stemmed from a selective elimination
of nearly all proliferating neuronal progenitor cells and lens
epithelial cells by apoptosis. Cell death was preceded by aberrant
accumulation of cell cycle regulators and increased genomic instability
and could be partially rescued by deletion of p53 (TP53; 191170).
Cang et al. (2007) found that epidermis-specific deletion of Ddb1 in
mice led to dramatic accumulation of c-Jun and p21Cip1 (CDKN1A; 116899),
arrest of cell cycle at G2/M, selective apoptosis of proliferating
cells, and as a result, nearly complete loss of the epidermis and hair
follicles. Deletion of p53 partially rescued the epithelial progenitor
cells from death and allowed for the accumulation of aneuploid cells in
the epidermis.
*FIELD* RF
1. 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.
2. Cang, Y.; Zhang, J.; Nicholas, S. A.; Bastien, J.; Li, B.; Zhou,
P.; Goff, S. P.: Deletion of DDB1 in mouse brain and lens leads to
p53-dependent elimination of proliferating cells. Cell 127: 929-940,
2006.
3. Cang, Y.; Zhang, J.; Nicholas, S. A.; Kim, A. L.; Zhou, P.; Goff,
S. P.: DDB1 is essential for genomic stability in developing epidermis. Proc.
Nat. Acad. Sci. 104: 2733-2737, 2007.
4. Chu, G.; Chang, E.: Xeroderma pigmentosum group E cells lack a
nuclear factor that binds to damaged DNA. Science 242: 564-567,
1988.
5. 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.
6. Fernandes, M.; Poirier, C.; Lespinasse, F.; Carle, G. F.: The
mouse homologs of human GIF, DDB1, and CFL1 genes are located on chromosome
19. Mammalian Genome 9: 339-342, 1998.
7. 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. Nature Cell Biol. 8: 1277-1283,
2006.
8. Ito, T.; Ando, H.; Suzuki, T.; Ogura, T.; Hotta, K.; Imamura, Y.;
Yamaguchi, Y.; Handa, H.: Identification of a primary target of thalidomide
teratogenicity. Science 327: 1345-1350, 2010.
9. Keeney, S.; Chang, G. J.; Linn, S.: Characterization of a human
DNA damage binding protein implicated in xeroderma pigmentosum E. J.
Biol. Chem. 268: 21293-21300, 1993.
10. Keeney, S.; Eker, A. P. M.; Brody, T.; Vermeulen, W.; Bootsma,
D.; Hoeijmakers, J. H. J.; Linn, S.: Correction of the DNA repair
defect in xeroderma pigmentosum group E by injection of a DNA damage-binding
protein. Proc. Nat. Acad. Sci. 91: 4053-4056, 1994.
11. Nichols, A. F.: Personal Communication. Berkeley, Calif. 10/4/1995.
12. Nichols, A. F.; Ong, P.; Linn, S.: Mutations specific to the
xeroderma pigmentosum group E Ddb- phenotype. J. Biol. Chem. 271:
24317-24320, 1996.
13. Obuse, C.; Yang, H.; Nozaki, N.; Goto, S.; Okazaki, T.; Yoda,
K.: Proteomics analysis of the centromere complex from HeLa interphase
cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
the CEN-complex, while BMI-1 is transiently co-localized with the
centromeric region in interphase. Genes Cells 9: 105-120, 2004.
14. Stohr, H.; Marquardt, A.; Rivera, A.; Kellner, U.; Weber, B. H.
F.: Refined mapping of the gene encoding the p127 kDa UV-damaged
DNA-binding protein (DDB1) within 11q12-q13.1 and its exclusion in
Best's vitelliform macular dystrophy. Europ. J. Hum. Genet. 6: 400-405,
1998.
15. 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.
*FIELD* CN
Patricia A. Hartz - updated: 03/05/2013
Ada Hamosh - updated: 4/13/2010
Patricia A. Hartz - updated: 4/30/2009
Patricia A. Hartz - updated: 8/10/2007
Patricia A. Hartz - updated: 5/8/2007
Ada Hamosh - updated: 10/24/2006
Ada Hamosh - updated: 6/10/2004
Victor A. McKusick - updated: 10/2/1998
Victor A. McKusick - updated: 9/3/1998
*FIELD* CD
Victor A. McKusick: 7/19/1994
*FIELD* ED
mgross: 03/05/2013
alopez: 2/26/2013
alopez: 4/15/2010
terry: 4/13/2010
mgross: 5/4/2009
terry: 4/30/2009
wwang: 10/4/2007
terry: 8/10/2007
wwang: 5/10/2007
terry: 5/8/2007
alopez: 11/6/2006
terry: 10/24/2006
wwang: 10/12/2006
alopez: 6/11/2004
terry: 6/10/2004
terry: 10/2/1998
alopez: 9/9/1998
carol: 9/3/1998
psherman: 5/8/1998
jamie: 1/17/1997
terry: 12/10/1996
terry: 11/13/1996
mark: 10/30/1995
mimadm: 9/23/1995
jason: 7/19/1994
*RECORD*
*FIELD* NO
600045
*FIELD* TI
*600045 DNA DAMAGE-BINDING PROTEIN 1; DDB1
;;DDB, p127 SUBUNIT
*FIELD* TX
CLONING
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Chu and Chang (1988) found that cells from 2 consanguineous patients
with xeroderma pigmentosum complementation group E (XPE; 278740) lacked
a DNA damage-binding activity that recognizes UV-irradiated DNA. Keeney
et al. (1993) purified the DDB protein to apparent homogeneity and
characterized it from human placenta and from HeLa cells. It was
apparently identical to an activity first described from human placenta.
DDB activity was associated with a polypeptide of approximately 124 kD,
which was found to be complexed with a 41-kD protein. This stable
heterodimer could, in turn, form a higher order complex. To test whether
the DNA-repair defect in the subset of XPE patients that lack DNA
damage-binding activity is caused by a defect in DDB, Keeney et al.
(1994) injected purified human DDB protein into XPE cells. The injected
DDB protein stimulated DNA repair to normal levels in those strains that
lacked the DDB activity but did not stimulate repair in cells from XPE
patients that contained the activity. These results provided direct
evidence that defective DDB activity causes the repair defect in a
subset of XPE patients and establishes a role for this activity in
nucleotide-excision repair in vivo.
The DNA damage-binding protein from HeLa cells is associated with
polypeptides of relative mass 124,000 and 41,000 (DDB2; 600811) as
determined by SDS-polyacrylamide gels. Dualan et al. (1995) isolated
full-length human cDNAs encoding each polypeptide of DDB. The predicted
peptide molecular masses based on open reading frames were 127,000 and
48,000. When expressed in an in vitro rabbit reticulocyte system, the
p48 subunit migrated with a relative mass of 41 kD on SDS-polyacrylamide
gels, similarly to the peptide purified from HeLa cells. There was no
significant homology between the derived p48 peptide sequence in any
proteins in databases, and the derived peptide sequence of p127 had
homology only with the monkey DDB p127 (98% nucleotide identity and only
1 conserved amino acid substitution).
GENE FUNCTION
Wertz et al. (2004) reported that human DET1 (608727) promotes
ubiquitination and degradation of the protooncogenic transcription
factor c-Jun (165160) by assembling a multisubunit ubiquitin ligase
containing DDB1, cullin 4A (CUL4A; 603137), regulator of cullins-1
(ROC1; 603814), and constitutively photomorphogenic-1 (COP1; 608067).
Ablation of any subunit by RNA interference stabilized c-Jun and
increased c-Jun-activated transcription. Wertz et al. (2004) concluded
that their findings characterized a c-Jun ubiquitin ligase and define a
specific function for DET1 in mammalian cells.
By analyzing proteins that immunoprecipitated with anti-CENPA (117139)
antibodies from HeLa cell nuclear lysates, Obuse et al. (2004) showed
that DDB1 associated with a centromeric complex, which also contained
the major centromeric proteins CENPB (117140), CENPC (117141), CENPH
(605607), CENPI (300065), and MIS12 (609178), and many others. DDB1
colocalized with CENPA at centromeres throughout the cell cycle in HeLa
cells; it appeared in both the cytoplasm and nucleus in interphase and
associated with chromosomes in metaphase.
By mass spectrometric analysis, Higa et al. (2006) identified over 20
WD40 repeat-containing (WDR) proteins that interacted with the
CUL4-DDB1-ROC1 complex. Sequence alignment revealed that most of the
interacting WDR proteins had a centrally positioned WDxR/K submotif.
Knockdown studies suggested that the WDR proteins functioned as
substrate-specific adaptors. For example, inactivation of L2DTL (DTL;
610617), but not other WDR proteins, prevented CUL4-DDB1-dependent
proteolysis of CDT1 (605525) following gamma irradiation. Inactivation
of WDR5 (609012) or EED (605984), but not other WDR proteins, altered
the pattern of CUL4-DDB1-dependent histone H3 (see 602810) methylation.
Ito et al. (2010) demonstrated that the thalidomide-binding protein
cereblon (CRBN; 609262) forms an E3 ubiquitin ligase complex with DDB1
and CUL4A that is important for limb outgrowth and expression of the
fibroblast growth factor FGF8 (600483) in zebrafish and chicks. The
authors found that thalidomide initiates its teratogenic effects by
binding to CRBN and inhibiting the associated ubiquitin ligase activity.
Ito et al. (2010) concluded that their study revealed a basis for
thalidomide teratogenicity and may contribute to the development of
thalidomide derivatives without teratogenic activity.
BIOCHEMICAL FEATURES
To reveal how DDB1 incorporates into the CUL4A-ROC1 complex and mediates
substrate recruitment, Angers et al. (2006) determined the 3.1-angstrom
crystal structure of a DDB1-CUL4A-ROC1 complex bound to the V protein of
simian virus 5 (SV5). DDB1 uses 1 beta-propeller domain for cullin
scaffold binding and a variably attached separate double-beta-propeller
fold for substrate presentation. Through tandem-affinity purification of
human DDB1 and CUL4A complexes followed by mass spectrometry analysis,
Angers et al. (2006) identified a novel family of WD40-repeat proteins,
which directly bind to the double-propeller fold of DDB1 and serve as
the substrate-recruiting module of the E3. Together, Angers et al.
(2006) concluded that their structural and proteomic results reveal the
structural mechanisms and molecular logic underlying the assembly and
versatility of a new family of cullin-RING E3 complexes.
MAPPING
Using fluorescence in situ hybridization (FISH), Dualan et al. (1995)
mapped the DDB p127 locus (DDB1) to 11q12-q13, and the DDB p48 locus
(DDB2) to 11p12-p11. Fernandes et al. (1998) used FISH and mouse/hamster
somatic cell hybrid analysis to map the Ddb1 gene to mouse chromosome
19.
MOLECULAR GENETICS
Nichols (1995) reported that RT-PCR mutation analysis in 5 fibroblast
XPE strains (2 without and 3 with DDB-binding activity) covering 90 to
99% of the sequence of the p127 subunit revealed no mutations.
Approximately 40% of the p48 subunit (DDB2) had been sequenced and had
revealed no mutations in 2 fibroblast XPF strains (278760). Mutations
were subsequently demonstrated in the DDB2 gene in the 3 known cases of
DDB-negative XPE (600811) (Nichols et al., 1996).
Stohr et al. (1998) investigated the possible involvement of DDB1 in the
pathogenesis of Best vitelliform macular dystrophy (VMD; 153700) because
that disorder maps to the same region on 11q and because the DDB1 gene
is abundantly expressed in retina. The mutation screening of the DDB1
gene demonstrated no sequence alterations in patients with Best disease.
ANIMAL MODEL
Cang et al. (2006) found that the deletion of the Ddb1 gene in mice
caused early embryonic lethality. Conditional inactivation of Ddb1 in
brain and lens led to neuronal and lens degeneration, brain hemorrhages,
and neonatal death. These defects stemmed from a selective elimination
of nearly all proliferating neuronal progenitor cells and lens
epithelial cells by apoptosis. Cell death was preceded by aberrant
accumulation of cell cycle regulators and increased genomic instability
and could be partially rescued by deletion of p53 (TP53; 191170).
Cang et al. (2007) found that epidermis-specific deletion of Ddb1 in
mice led to dramatic accumulation of c-Jun and p21Cip1 (CDKN1A; 116899),
arrest of cell cycle at G2/M, selective apoptosis of proliferating
cells, and as a result, nearly complete loss of the epidermis and hair
follicles. Deletion of p53 partially rescued the epithelial progenitor
cells from death and allowed for the accumulation of aneuploid cells in
the epidermis.
*FIELD* RF
1. 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.
2. Cang, Y.; Zhang, J.; Nicholas, S. A.; Bastien, J.; Li, B.; Zhou,
P.; Goff, S. P.: Deletion of DDB1 in mouse brain and lens leads to
p53-dependent elimination of proliferating cells. Cell 127: 929-940,
2006.
3. Cang, Y.; Zhang, J.; Nicholas, S. A.; Kim, A. L.; Zhou, P.; Goff,
S. P.: DDB1 is essential for genomic stability in developing epidermis. Proc.
Nat. Acad. Sci. 104: 2733-2737, 2007.
4. Chu, G.; Chang, E.: Xeroderma pigmentosum group E cells lack a
nuclear factor that binds to damaged DNA. Science 242: 564-567,
1988.
5. 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.
6. Fernandes, M.; Poirier, C.; Lespinasse, F.; Carle, G. F.: The
mouse homologs of human GIF, DDB1, and CFL1 genes are located on chromosome
19. Mammalian Genome 9: 339-342, 1998.
7. 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. Nature Cell Biol. 8: 1277-1283,
2006.
8. Ito, T.; Ando, H.; Suzuki, T.; Ogura, T.; Hotta, K.; Imamura, Y.;
Yamaguchi, Y.; Handa, H.: Identification of a primary target of thalidomide
teratogenicity. Science 327: 1345-1350, 2010.
9. Keeney, S.; Chang, G. J.; Linn, S.: Characterization of a human
DNA damage binding protein implicated in xeroderma pigmentosum E. J.
Biol. Chem. 268: 21293-21300, 1993.
10. Keeney, S.; Eker, A. P. M.; Brody, T.; Vermeulen, W.; Bootsma,
D.; Hoeijmakers, J. H. J.; Linn, S.: Correction of the DNA repair
defect in xeroderma pigmentosum group E by injection of a DNA damage-binding
protein. Proc. Nat. Acad. Sci. 91: 4053-4056, 1994.
11. Nichols, A. F.: Personal Communication. Berkeley, Calif. 10/4/1995.
12. Nichols, A. F.; Ong, P.; Linn, S.: Mutations specific to the
xeroderma pigmentosum group E Ddb- phenotype. J. Biol. Chem. 271:
24317-24320, 1996.
13. Obuse, C.; Yang, H.; Nozaki, N.; Goto, S.; Okazaki, T.; Yoda,
K.: Proteomics analysis of the centromere complex from HeLa interphase
cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
the CEN-complex, while BMI-1 is transiently co-localized with the
centromeric region in interphase. Genes Cells 9: 105-120, 2004.
14. Stohr, H.; Marquardt, A.; Rivera, A.; Kellner, U.; Weber, B. H.
F.: Refined mapping of the gene encoding the p127 kDa UV-damaged
DNA-binding protein (DDB1) within 11q12-q13.1 and its exclusion in
Best's vitelliform macular dystrophy. Europ. J. Hum. Genet. 6: 400-405,
1998.
15. 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.
*FIELD* CN
Patricia A. Hartz - updated: 03/05/2013
Ada Hamosh - updated: 4/13/2010
Patricia A. Hartz - updated: 4/30/2009
Patricia A. Hartz - updated: 8/10/2007
Patricia A. Hartz - updated: 5/8/2007
Ada Hamosh - updated: 10/24/2006
Ada Hamosh - updated: 6/10/2004
Victor A. McKusick - updated: 10/2/1998
Victor A. McKusick - updated: 9/3/1998
*FIELD* CD
Victor A. McKusick: 7/19/1994
*FIELD* ED
mgross: 03/05/2013
alopez: 2/26/2013
alopez: 4/15/2010
terry: 4/13/2010
mgross: 5/4/2009
terry: 4/30/2009
wwang: 10/4/2007
terry: 8/10/2007
wwang: 5/10/2007
terry: 5/8/2007
alopez: 11/6/2006
terry: 10/24/2006
wwang: 10/12/2006
alopez: 6/11/2004
terry: 6/10/2004
terry: 10/2/1998
alopez: 9/9/1998
carol: 9/3/1998
psherman: 5/8/1998
jamie: 1/17/1997
terry: 12/10/1996
terry: 11/13/1996
mark: 10/30/1995
mimadm: 9/23/1995
jason: 7/19/1994