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DNA damage-binding protein 2 (DDB p48 subunit) (DDBb) (Damage-specific DNA-binding protein 2) (UV-damaged DNA-binding protein 2) (UV-DDB 2)

 DDB2_HUMAN              Reviewed;         427 AA.
Q92466; B2R875; Q76E54; Q76E55; Q76E56; Q76E57;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 180.
RecName: Full=DNA damage-binding protein 2;
AltName: Full=DDB p48 subunit;
Short=DDBb;
AltName: Full=Damage-specific DNA-binding protein 2;
AltName: Full=UV-damaged DNA-binding protein 2;
Short=UV-DDB 2;
Name=DDB2;
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;
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] (ISOFORMS D1; D2; D3 AND D4), FUNCTION,
INTERACTION WITH DDB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Epithelium;
PubMed=14751237; DOI=10.1016/j.bbrc.2004.01.003;
Inoki T., Yamagami S., Inoki Y., Tsuru T., Hamamoto T., Kagawa Y.,
Mori T., Endo H.;
"Human DDB2 splicing variants are dominant negative inhibitors of UV-
damaged DNA repair.";
Biochem. Biophys. Res. Commun. 314:1036-1043(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-215 AND THR-293.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[8]
INTERACTION WITH DDB1, DNA-BINDING, AND CHARACTERIZATION OF VARIANTS
GLU-244 AND HIS-273.
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).
[9]
FUNCTION, AND DNA-BINDING.
PubMed=9892649; DOI=10.1073/pnas.96.2.424;
Hwang B.J., Ford J.M., Hanawalt P.C., Chu G.;
"Expression of the p48 xeroderma pigmentosum gene is p53-dependent and
is involved in global genomic repair.";
Proc. Natl. Acad. Sci. U.S.A. 96:424-428(1999).
[10]
DNA-BINDING, SUBCELLULAR LOCATION, INDUCTION, AND CHARACTERIZATION OF
VARIANTS GLU-244 AND HIS-273.
PubMed=10777490; DOI=10.1074/jbc.M000960200;
Nichols A.F., Itoh T., Graham J.A., Liu W., Yamaizumi M., Linn S.;
"Human damage-specific DNA-binding protein p48. Characterization of
XPE mutations and regulation following UV irradiation.";
J. Biol. Chem. 275:21422-21428(2000).
[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]
FUNCTION.
PubMed=10882109; DOI=10.1016/S1097-2765(00)80252-X;
Tang J.Y., Hwang B.J., Ford J.M., Hanawalt P.C., Chu G.;
"Xeroderma pigmentosum p48 gene enhances global genomic repair and
suppresses UV-induced mutagenesis.";
Mol. Cell 5:737-744(2000).
[13]
FUNCTION, AND DNA-BINDING.
PubMed=11278856; DOI=10.1074/jbc.M011177200;
Wakasugi M., Shimizu M., Morioka H., Linn S., Nikaido O.,
Matsunaga T.;
"Damaged DNA-binding protein DDB stimulates the excision of
cyclobutane pyrimidine dimers in vitro in concert with XPA and
replication protein A.";
J. Biol. Chem. 276:15434-15440(2001).
[14]
INTERACTION WITH CUL4A, UBIQUITINATION, AND CHARACTERIZATION OF
VARIANT HIS-273.
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).
[15]
FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=11705987; DOI=10.1074/jbc.C100610200;
Wakasugi M., Kawashima A., Morioka H., Linn S., Sancar A., Mori T.,
Nikaido O., Matsunaga T.;
"DDB accumulates at DNA damage sites immediately after UV irradiation
and directly stimulates nucleotide excision repair.";
J. Biol. Chem. 277:1637-1640(2002).
[16]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A
COMPLEX WITH CUL4A; DDB1 AND RBX1 AND THE COP9 SIGNALOSOME, AND
DNA-BINDING.
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).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12944386; DOI=10.1074/jbc.M307254200;
Fitch M.E., Nakajima S., Yasui A., Ford J.M.;
"In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine
dimers by the DDB2 gene product.";
J. Biol. Chem. 278:46906-46910(2003).
[18]
FUNCTION, INTERACTION WITH CUL4A; DDB1; RBX1 AND XPC, DNA-BINDING, AND
UBIQUITINATION.
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 DDB1, DNA-BINDING, AND CHARACTERIZATION OF VARIANTS
GLU-244 AND HIS-273.
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]
FUNCTION, INTERACTION WITH CUL4A; DDB1; 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[22]
INTERACTION WITH CUL4A AND DDB1, DOMAIN DWD BOX MOTIF, AND MUTAGENESIS
OF LEU-258; SER-262; ASP-264; ILE-269; TRP-270; LEU-272 AND ARG-273.
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).
[23]
INTERACTION WITH CUL4A AND DDB1, AND UBIQUITINATION.
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).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
DDB1; CUL4A; CUL4B AND RBX1, 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).
[25]
SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=16713579; DOI=10.1016/j.molcel.2006.04.021;
Chen X., Zhang J., Lee J., Lin P.S., Ford J.M., Zheng N., Zhou P.;
"A kinase-independent function of c-Abl in promoting proteolytic
destruction of damaged DNA binding proteins.";
Mol. Cell 22:489-499(2006).
[26]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDB1,
MUTAGENESIS OF LEU-350, AND CHARACTERIZATION OF VARIANT HIS-273.
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).
[27]
INTERACTION WITH DDB1, AND CHARACTERIZATION OF VARIANT HIS-273.
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).
[28]
INTERACTION WITH CUL4A AND CUL4B.
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).
[29]
FUNCTION, INTERACTION WITH CUL4A; DDB1; 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).
[30]
SUBCELLULAR LOCATION.
PubMed=17635991; DOI=10.1242/jcs.008367;
Luijsterburg M.S., Goedhart J., Moser J., Kool H., Geverts B.,
Houtsmuller A.B., Mullenders L.H.F., Vermeulen W., van Driel R.;
"Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-
damaged DNA is independent of damage-recognition protein XPC.";
J. Cell Sci. 120:2706-2716(2007).
[31]
FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB1, 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).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
DEUBIQUITINATION BY USP24.
PubMed=23159851; DOI=10.4161/cc.22688;
Zhang L., Lubin A., Chen H., Sun Z., Gong F.;
"The deubiquitinating protein USP24 interacts with DDB2 and regulates
DDB2 stability.";
Cell Cycle 11:4378-4384(2012).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 10-427 IN COMPLEX WITH DDB1
AND DNA, AND WD REPEATS.
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).
[39]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 68-81 IN COMPLEX WITH DDB1.
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).
[40]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH DDB1.
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).
[41]
VARIANTS XP-E GLU-244 AND HIS-273.
PubMed=8798680; DOI=10.1074/jbc.271.40.24317;
Nichols A.F., Ong P., Linn S.;
"Mutations specific to the xeroderma pigmentosum group E Ddb-
phenotype.";
J. Biol. Chem. 271:24317-24320(1996).
-!- FUNCTION: Required for DNA repair. Binds to DDB1 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 the substrate recognition module for the DCX (DDB1-
CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-ROC1
(also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB1-CUL4-
ROC1 complex 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. The DDB1-CUL4-ROC1 complex also
ubiquitinates XPC, which may enhance DNA-binding by XPC and
promote NER. Isoform D1 and isoform D2 inhibit UV-damaged DNA
repair. {ECO:0000269|PubMed:10882109, ECO:0000269|PubMed:11278856,
ECO:0000269|PubMed:11705987, ECO:0000269|PubMed:12732143,
ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237,
ECO:0000269|PubMed:15882621, ECO:0000269|PubMed:16260596,
ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16678110,
ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:9892649}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
DDB2. The UV-DDB complex interacts with monoubiquitinated histone
H2A and binds to XPC via the DDB2 subunit. Component of the DCX
(DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB1-CUL4-
ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1), which
includes CUL4A or CUL4B, DDB1, DDB2 and RBX1. DDB2 may function as
the substrate recognition module within this complex. The DDB1-
CUL4-ROC1 complex may associate with the COP9 signalosome, and
this inhibits the E3 ubiquitin-protein ligase activity of the
complex. A large number of other DCX complexes may also exist in
which an alternate substrate targeting subunit replaces DDB2.
These targeting subunits are generally known as DCAF (DDB1- and
CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat)
proteins. Isoform D1 and isoform D2 do not interact with DDB1.
{ECO:0000269|PubMed:11673459, ECO:0000269|PubMed:12732143,
ECO:0000269|PubMed:14751237, ECO:0000269|PubMed:15882621,
ECO:0000269|PubMed:16223728, ECO:0000269|PubMed:16260596,
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:18593899,
ECO:0000269|PubMed:19109893, ECO:0000269|PubMed:19966799,
ECO:0000269|PubMed:22822215, ECO:0000269|PubMed:9632823}.
-!- INTERACTION:
Q13619:CUL4A; NbExp=5; IntAct=EBI-1176171, EBI-456106;
Q16531:DDB1; NbExp=19; IntAct=EBI-1176171, EBI-350322;
Q01094:E2F1; NbExp=2; IntAct=EBI-1176171, EBI-448924;
Q01831-1:XPC; NbExp=4; IntAct=EBI-1176171, EBI-15950383;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10777490,
ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:11705987,
ECO:0000269|PubMed:12944386, ECO:0000269|PubMed:14751237,
ECO:0000269|PubMed:16473935, ECO:0000269|PubMed:16713579,
ECO:0000269|PubMed:17635991, ECO:0000269|PubMed:18593899}.
Note=Accumulates at sites of DNA damage following UV irradiation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q92466-1; Sequence=Displayed;
Name=D1;
IsoId=Q92466-2; Sequence=VSP_014675;
Name=D2;
IsoId=Q92466-3; Sequence=VSP_014676, VSP_014677;
Name=D3;
IsoId=Q92466-4; Sequence=VSP_014674;
Name=D4;
IsoId=Q92466-5; Sequence=VSP_014678, VSP_014679;
-!- TISSUE SPECIFICITY: Ubiquitously expressed; with highest levels in
corneal endothelium and lowest levels in brain. Isoform D1 is
highly expressed in brain and heart. Isoform D2, isoform D3 and
isoform D4 are weakly expressed. {ECO:0000269|PubMed:14751237}.
-!- INDUCTION: Expression is induced in response to treatment with IR
or UV and this requires p53/TP53 activity.
{ECO:0000269|PubMed:10777490}.
-!- DOMAIN: The DWD box is required for interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
-!- DOMAIN: Interblade loops of the WD repeat region mediate most of
the interaction with DNA. A hairpin between blades 5 and 6 inserts
into DNA minor groove and mediates recognition of lesions and
separation of the damaged and undamaged strands.
{ECO:0000269|PubMed:17079684}.
-!- PTM: Phosphorylation by ABL1 negatively regulate UV-DDB activity.
{ECO:0000250}.
-!- PTM: Ubiquitinated by CUL4A in response to UV irradiation.
Ubiquitination appears to both impair DNA-binding and promotes
ubiquitin-dependent proteolysis. Degradation of DDB2 at sites of
DNA damage may be a prerequisite for their recognition by XPC and
subsequent repair. CUL4A-mediated degradation appears to be
promoted by ABL1. {ECO:0000269|PubMed:23159851}.
-!- PTM: Ubiquitinated, leading to proteasomal degradation, and
deubiquitinated by USP24. {ECO:0000269|PubMed:23159851}.
-!- DISEASE: Xeroderma pigmentosum complementation group E (XP-E)
[MIM:278740]: An autosomal recessive pigmentary skin disorder
characterized by solar hypersensitivity of the skin, high
predisposition for developing cancers on areas exposed to sunlight
and, in some cases, neurological abnormalities. The skin develops
marked freckling and other pigmentation abnormalities. XP-E
patients show a mild phenotype with minimal or no neurologic
features. {ECO:0000269|PubMed:8798680}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/XPEID298.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ddb2/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U18300; AAB07897.1; -; mRNA.
EMBL; AB107037; BAD12557.1; -; mRNA.
EMBL; AB107038; BAD12558.1; -; mRNA.
EMBL; AB107039; BAD12559.1; -; mRNA.
EMBL; AB107040; BAD12560.1; -; mRNA.
EMBL; BT007139; AAP35803.1; -; mRNA.
EMBL; AY220533; AAO25655.1; -; Genomic_DNA.
EMBL; AK313262; BAG36072.1; -; mRNA.
EMBL; CH471064; EAW67952.1; -; Genomic_DNA.
EMBL; BC000093; AAH00093.1; -; mRNA.
CCDS; CCDS73284.1; -. [Q92466-2]
CCDS; CCDS7927.1; -. [Q92466-1]
PIR; I38909; I38909.
RefSeq; NP_000098.1; NM_000107.2. [Q92466-1]
RefSeq; NP_001287663.1; NM_001300734.1. [Q92466-2]
UniGene; Hs.700338; -.
PDB; 3EI4; X-ray; 3.30 A; B/D/F=10-427.
PDB; 3I7L; X-ray; 2.80 A; B=68-81.
PDB; 4E54; X-ray; 2.85 A; B=2-427.
PDB; 4E5Z; X-ray; 3.22 A; B=2-427.
PDBsum; 3EI4; -.
PDBsum; 3I7L; -.
PDBsum; 4E54; -.
PDBsum; 4E5Z; -.
ProteinModelPortal; Q92466; -.
SMR; Q92466; -.
BioGrid; 108010; 86.
CORUM; Q92466; -.
DIP; DIP-36670N; -.
IntAct; Q92466; 27.
STRING; 9606.ENSP00000256996; -.
iPTMnet; Q92466; -.
PhosphoSitePlus; Q92466; -.
BioMuta; DDB2; -.
DMDM; 12230033; -.
EPD; Q92466; -.
MaxQB; Q92466; -.
PaxDb; Q92466; -.
PeptideAtlas; Q92466; -.
PRIDE; Q92466; -.
DNASU; 1643; -.
Ensembl; ENST00000256996; ENSP00000256996; ENSG00000134574. [Q92466-1]
Ensembl; ENST00000378600; ENSP00000367863; ENSG00000134574. [Q92466-2]
Ensembl; ENST00000378601; ENSP00000367864; ENSG00000134574. [Q92466-5]
Ensembl; ENST00000378603; ENSP00000367866; ENSG00000134574. [Q92466-4]
Ensembl; ENST00000616278; ENSP00000478411; ENSG00000134574. [Q92466-3]
GeneID; 1643; -.
KEGG; hsa:1643; -.
UCSC; uc001neb.3; human. [Q92466-1]
CTD; 1643; -.
DisGeNET; 1643; -.
EuPathDB; HostDB:ENSG00000134574.11; -.
GeneCards; DDB2; -.
GeneReviews; DDB2; -.
HGNC; HGNC:2718; DDB2.
HPA; CAB025912; -.
HPA; HPA058406; -.
MalaCards; DDB2; -.
MIM; 278740; phenotype.
MIM; 600811; gene.
neXtProt; NX_Q92466; -.
OpenTargets; ENSG00000134574; -.
Orphanet; 276261; Xeroderma pigmentosum complementation group E.
PharmGKB; PA27188; -.
eggNOG; ENOG410IMQS; Eukaryota.
eggNOG; COG2319; LUCA.
GeneTree; ENSGT00510000047881; -.
HOGENOM; HOG000231440; -.
HOVERGEN; HBG000713; -.
InParanoid; Q92466; -.
KO; K10140; -.
OMA; VTCLEWH; -.
OrthoDB; EOG091G06BL; -.
PhylomeDB; Q92466; -.
TreeFam; TF331587; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
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-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-8951664; Neddylation.
SignaLink; Q92466; -.
SIGNOR; Q92466; -.
UniPathway; UPA00143; -.
ChiTaRS; DDB2; human.
EvolutionaryTrace; Q92466; -.
GeneWiki; DDB2; -.
GenomeRNAi; 1643; -.
PRO; PR:Q92466; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134574; -.
CleanEx; HS_DDB2; -.
ExpressionAtlas; Q92466; baseline and differential.
Genevisible; Q92466; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IMP:UniProtKB.
GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0032403; F:protein complex binding; IPI:UniProtKB.
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:0006289; P:nucleotide-excision repair; TAS:ProtInc.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; 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:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0070914; P:UV-damage excision repair; IDA:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR033312; DDB2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR15169; PTHR15169; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; DNA damage; DNA repair; DNA-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation; Ubl conjugation pathway; WD repeat;
Xeroderma pigmentosum.
CHAIN 1 427 DNA damage-binding protein 2.
/FTId=PRO_0000050953.
REPEAT 116 151 WD 1. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REPEAT 159 194 WD 2. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REPEAT 203 238 WD 3. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REPEAT 244 287 WD 4. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REPEAT 290 329 WD 5. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REPEAT 343 386 WD 6. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REPEAT 396 420 WD 7. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:19109893}.
REGION 68 79 Required for interaction with DDB1.
REGION 87 98 Required for interaction with DDB1.
REGION 334 336 Photolesion recognition.
MOTIF 256 274 DWD box.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 89 152 Missing (in isoform D3).
{ECO:0000303|PubMed:14751237}.
/FTId=VSP_014674.
VAR_SEQ 153 341 Missing (in isoform D1).
{ECO:0000303|PubMed:14751237}.
/FTId=VSP_014675.
VAR_SEQ 153 156 IGAG -> HLVL (in isoform D2).
{ECO:0000303|PubMed:14751237}.
/FTId=VSP_014676.
VAR_SEQ 157 427 Missing (in isoform D2).
{ECO:0000303|PubMed:14751237}.
/FTId=VSP_014677.
VAR_SEQ 236 244 WNLRMHKKK -> VSVPMEPGS (in isoform D4).
{ECO:0000303|PubMed:14751237}.
/FTId=VSP_014678.
VAR_SEQ 245 427 Missing (in isoform D4).
{ECO:0000303|PubMed:14751237}.
/FTId=VSP_014679.
VARIANT 215 215 M -> T (in dbSNP:rs4647750).
{ECO:0000269|Ref.4}.
/FTId=VAR_016337.
VARIANT 244 244 K -> E (in XP-E; impairs DNA-binding of
the UV-DDB complex; dbSNP:rs121434639).
{ECO:0000269|PubMed:10777490,
ECO:0000269|PubMed:16223728,
ECO:0000269|PubMed:8798680,
ECO:0000269|PubMed:9632823}.
/FTId=VAR_010141.
VARIANT 273 273 R -> H (in XP-E; impairs interaction with
DDB1 and CUL4A; dbSNP:rs121434640).
{ECO:0000269|PubMed:10777490,
ECO:0000269|PubMed:11673459,
ECO:0000269|PubMed:16223728,
ECO:0000269|PubMed:16949367,
ECO:0000269|PubMed:16964240,
ECO:0000269|PubMed:8798680,
ECO:0000269|PubMed:9632823}.
/FTId=VAR_010142.
VARIANT 293 293 A -> T (in dbSNP:rs4647751).
{ECO:0000269|Ref.4}.
/FTId=VAR_016338.
MUTAGEN 258 258 L->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 262 262 S->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 264 264 D->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 269 269 I->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 270 270 W->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 272 272 L->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 273 273 R->A: Impairs interaction with DDB1.
{ECO:0000269|PubMed:17079684}.
MUTAGEN 350 350 L->P: Impairs interaction with DDB1.
{ECO:0000269|PubMed:16949367}.
HELIX 21 25 {ECO:0000244|PDB:4E54}.
STRAND 30 32 {ECO:0000244|PDB:4E54}.
HELIX 39 42 {ECO:0000244|PDB:4E54}.
TURN 44 47 {ECO:0000244|PDB:4E54}.
STRAND 49 51 {ECO:0000244|PDB:4E54}.
HELIX 58 62 {ECO:0000244|PDB:4E54}.
TURN 63 65 {ECO:0000244|PDB:4E54}.
HELIX 69 77 {ECO:0000244|PDB:3I7L}.
HELIX 83 91 {ECO:0000244|PDB:4E54}.
TURN 92 94 {ECO:0000244|PDB:4E54}.
TURN 96 102 {ECO:0000244|PDB:4E54}.
STRAND 106 109 {ECO:0000244|PDB:4E54}.
STRAND 114 119 {ECO:0000244|PDB:4E54}.
STRAND 127 131 {ECO:0000244|PDB:4E54}.
STRAND 136 139 {ECO:0000244|PDB:4E54}.
STRAND 148 150 {ECO:0000244|PDB:4E54}.
STRAND 154 156 {ECO:0000244|PDB:4E54}.
STRAND 161 164 {ECO:0000244|PDB:4E54}.
STRAND 171 175 {ECO:0000244|PDB:4E54}.
STRAND 177 179 {ECO:0000244|PDB:4E54}.
STRAND 181 185 {ECO:0000244|PDB:4E54}.
TURN 186 188 {ECO:0000244|PDB:3EI4}.
STRAND 190 195 {ECO:0000244|PDB:4E54}.
STRAND 198 201 {ECO:0000244|PDB:4E5Z}.
STRAND 207 210 {ECO:0000244|PDB:4E54}.
TURN 211 214 {ECO:0000244|PDB:4E54}.
STRAND 215 219 {ECO:0000244|PDB:4E54}.
STRAND 221 232 {ECO:0000244|PDB:4E54}.
STRAND 241 243 {ECO:0000244|PDB:4E5Z}.
STRAND 245 250 {ECO:0000244|PDB:4E54}.
TURN 252 254 {ECO:0000244|PDB:4E5Z}.
STRAND 255 262 {ECO:0000244|PDB:4E54}.
TURN 263 265 {ECO:0000244|PDB:4E5Z}.
STRAND 269 271 {ECO:0000244|PDB:4E54}.
TURN 272 274 {ECO:0000244|PDB:4E54}.
STRAND 277 279 {ECO:0000244|PDB:4E54}.
STRAND 282 286 {ECO:0000244|PDB:3EI4}.
STRAND 291 293 {ECO:0000244|PDB:4E54}.
STRAND 300 310 {ECO:0000244|PDB:4E54}.
STRAND 312 326 {ECO:0000244|PDB:4E54}.
STRAND 335 337 {ECO:0000244|PDB:4E54}.
STRAND 346 349 {ECO:0000244|PDB:4E54}.
STRAND 351 354 {ECO:0000244|PDB:4E54}.
STRAND 359 361 {ECO:0000244|PDB:4E5Z}.
STRAND 364 366 {ECO:0000244|PDB:3EI4}.
STRAND 372 375 {ECO:0000244|PDB:4E54}.
STRAND 377 379 {ECO:0000244|PDB:4E54}.
STRAND 382 386 {ECO:0000244|PDB:4E54}.
TURN 389 391 {ECO:0000244|PDB:3EI4}.
STRAND 397 400 {ECO:0000244|PDB:4E54}.
STRAND 407 410 {ECO:0000244|PDB:4E54}.
STRAND 412 417 {ECO:0000244|PDB:4E54}.
SEQUENCE 427 AA; 47864 MW; E881F21242CA44D2 CRC64;
MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP
QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS YRILQKAAPF DRRATSLAWH
PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI KGIGAGGSIT GLKFNPLNTN QFYASSMEGT
TRLQDFKGNI LRVFASSDTI NIWFCSLDVS ASSRMVVTGD NVGNVILLNM DGKELWNLRM
HKKKVTHVAL NPCCDWFLAT ASVDQTVKIW DLRQVRGKAS FLYSLPHRHP VNAACFSPDG
ARLLTTDQKS EIRVYSASQW DCPLGLIPHP HRHFQHLTPI KAAWHPRYNL IVVGRYPDPN
FKSCTPYELR TIDVFDGNSG KMMCQLYDPE SSGISSLNEF NPMGDTLASA MGYHILIWSQ
EEARTRK


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