DNA damage-binding protein 2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q92466 (DDB2_HUMAN)

Last modified June 16, 2009. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    DNA damage-binding protein 2
Alternative name(s):
    Damage-specific DNA-binding protein 2
    DDB p48 subunit
      Short name=DDBb
    UV-damaged DNA-binding protein 2
      Short name=UV-DDB 2

Gene names

Name:

DDB2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. Ref.2 Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.22 Ref.27 Ref.30
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.2 Ref.16 Ref.18 Ref.27 Ref.30 Ref.6 Ref.12 Ref.17 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26
Subcellular location	Nucleus. Note: Accumulates at sites of DNA damage following UV irradiation. Ref.2 Ref.13 Ref.15 Ref.27 Ref.30 Ref.8 Ref.9 Ref.23 Ref.28
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. Ref.2
Induction	Expression is induced in response to treatment with IR or UV and this requires p53 activity. Ref.8
Domain	The DWD box is required for interaction with DDB1.
Post-translational modification	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/c-ABL. Ref.16 Ref.12 Ref.21 Ref.23
Involvement in disease	Defects in DDB2 are a cause of xeroderma pigmentosum complementation group E (XP-E) [MIM:278740]; also known as xeroderma pigmentosum V (XP5). XP-E is a rare human autosomal recessive disease characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. Ref.32
Sequence similarities	Belongs to the WD repeat DDB2/WDR76 family. Contains 5 WD repeats.

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Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Xeroderma pigmentosum
Domain	Repeat WD repeat
Ligand	DNA-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleotide-excision repair, DNA damage removal Inferred from Experiment. Source: Reactome protein autoubiquitination Ref.14 Inferred from direct assay. Source: UniProtKB protein polyubiquitination Ref.14 Inferred from direct assay. Source: UniProtKB response to UV Ref.14 Inferred from direct assay. Source: UniProtKB
Cellular component	nucleoplasm Inferred from Experiment. Source: Reactome protein complex Ref.14 Inferred from direct assay. Source: UniProtKB
Molecular function	damaged DNA binding Traceable author statement. Source: ProtInc protein binding Ref.14 Ref.26 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CUL4A	Q13619	1	EBI-1176171,EBI-456106
DDB1	Q16531	3	EBI-1176171,EBI-350322
E2F1	Q01094	2	EBI-1176171,EBI-448924

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Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92466-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform D1 (identifier: Q92466-2) The sequence of this isoform differs from the canonical sequence as follows: 153-341: Missing.

Isoform D2 (identifier: Q92466-3) The sequence of this isoform differs from the canonical sequence as follows: 153-156: IGAG → HLVL 157-427: Missing.

Isoform D3 (identifier: Q92466-4) The sequence of this isoform differs from the canonical sequence as follows: 89-152: Missing.

Isoform D4 (identifier: Q92466-5) The sequence of this isoform differs from the canonical sequence as follows: 236-244: WNLRMHKKK → VSVPMEPGS 245-427: Missing.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

DNA damage-binding protein 2

PRO_0000050953

Regions

Repeat

109 – 149

WD 1

Repeat

154 – 195

WD 2

Repeat

240 – 280

WD 3

Repeat

286 – 325

WD 4

Repeat

389 – 426

WD 5

Region

68 – 79

Required for interaction with DDB1

Region

87 – 98

Required for interaction with DDB1

Motif

256 – 274

DWD box

Amino acid modifications

Modified residue

Phosphoserine Ref.19 Ref.31

Modified residue

Phosphoserine Ref.19 Ref.31 Ref.29

Natural variations

Alternative sequence

89 – 152

Missing in isoform D3.

VSP_014674

Alternative sequence

153 – 341

189

Missing in isoform D1.

VSP_014675

Alternative sequence

153 – 156

IGAG → HLVL in isoform D2.

VSP_014676

Alternative sequence

157 – 427

271

Missing in isoform D2.

VSP_014677

Alternative sequence

236 – 244

WNLRMHKKK → VSVPMEPGS in isoform D4.

VSP_014678

Alternative sequence

245 – 427

183

Missing in isoform D4.

VSP_014679

Natural variant

215

M → T: dbSNP rs4647750. Ref.4

VAR_016337

Natural variant

244

K → E in XP-E; impairs DNA-binding of the UV-DDB complex. Ref.32

VAR_010141

Natural variant

273

R → H in XP-E; impairs interaction with DDB1 and CUL4A. Ref.32

VAR_010142

Natural variant

293

A → T: dbSNP rs4647751. Ref.4

VAR_016338

Experimental info

Mutagenesis

258

L → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

262

S → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

264

D → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

269

I → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

270

W → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

272

L → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

273

R → A: Impairs interaction with DDB1. Ref.20

Mutagenesis

350

L → P: Impairs interaction with DDB1. Ref.24

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Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: E881F21242CA44D2 Show »	FASTA	427	47,864
10 20 30 40 50 60 MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP 70 80 90 100 110 120 QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS YRILQKAAPF DRRATSLAWH 130 140 150 160 170 180 PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI KGIGAGGSIT GLKFNPLNTN QFYASSMEGT 190 200 210 220 230 240 TRLQDFKGNI LRVFASSDTI NIWFCSLDVS ASSRMVVTGD NVGNVILLNM DGKELWNLRM 250 260 270 280 290 300 HKKKVTHVAL NPCCDWFLAT ASVDQTVKIW DLRQVRGKAS FLYSLPHRHP VNAACFSPDG 310 320 330 340 350 360 ARLLTTDQKS EIRVYSASQW DCPLGLIPHP HRHFQHLTPI KAAWHPRYNL IVVGRYPDPN 370 380 390 400 410 420 FKSCTPYELR TIDVFDGNSG KMMCQLYDPE SSGISSLNEF NPMGDTLASA MGYHILIWSQ EEARTRK « Hide
Isoform D1. Checksum: F40BD646C1C26FDA Show »	FASTA	238	26,744
10 20 30 40 50 60 MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP 70 80 90 100 110 120 QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS YRILQKAAPF DRRATSLAWH 130 140 150 160 170 180 PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI KGAAWHPRYN LIVVGRYPDP NFKSCTPYEL 190 200 210 220 230 RTIDVFDGNS GKMMCQLYDP ESSGISSLNE FNPMGDTLAS AMGYHILIWS QEEARTRK « Hide
Isoform D2. Checksum: FBC8A060B4DC7A4D Show »	FASTA	156	17,434
10 20 30 40 50 60 MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP 70 80 90 100 110 120 QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS YRILQKAAPF DRRATSLAWH 130 140 150 PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI KGHLVL « Hide
Isoform D3. Checksum: 2A90D5BD9E322889 Show »	FASTA	363	40,772
10 20 30 40 50 60 MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP 70 80 90 100 110 120 QILPPCRSIV RTLHQHKLGR ASWPSVQQIG AGGSITGLKF NPLNTNQFYA SSMEGTTRLQ 130 140 150 160 170 180 DFKGNILRVF ASSDTINIWF CSLDVSASSR MVVTGDNVGN VILLNMDGKE LWNLRMHKKK 190 200 210 220 230 240 VTHVALNPCC DWFLATASVD QTVKIWDLRQ VRGKASFLYS LPHRHPVNAA CFSPDGARLL 250 260 270 280 290 300 TTDQKSEIRV YSASQWDCPL GLIPHPHRHF QHLTPIKAAW HPRYNLIVVG RYPDPNFKSC 310 320 330 340 350 360 TPYELRTIDV FDGNSGKMMC QLYDPESSGI SSLNEFNPMG DTLASAMGYH ILIWSQEEAR TRK « Hide
Isoform D4. Checksum: 367D99AA1DD984F9 Show »	FASTA	244	26,758
10 20 30 40 50 60 MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS DCLWVGLAGP 70 80 90 100 110 120 QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS YRILQKAAPF DRRATSLAWH 130 140 150 160 170 180 PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI KGIGAGGSIT GLKFNPLNTN QFYASSMEGT 190 200 210 220 230 240 TRLQDFKGNI LRVFASSDTI NIWFCSLDVS ASSRMVVTGD NVGNVILLNM DGKELVSVPM EPGS « Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Dualan R., Brody T., Keeney S., Nichols A.F., Admon A., Linn S. Genomics 29:62-69(1995) [PubMed: 8530102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Epidermis.
[2]	"Human DDB2 splicing variants are dominant negative inhibitors of UV-damaged DNA repair." Inoki T., Yamagami S., Inoki Y., Tsuru T., Hamamoto T., Kagawa Y., Mori T., Endo H. Biochem. Biophys. Res. Commun. 314:1036-1043(2004) [PubMed: 14751237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D1; D2; D3 AND D4), FUNCTION, INTERACTION WITH DDB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Epithelium.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-215 AND THR-293.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[6]	"p48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity." Hwang B.J., Toering S., Francke U., Chu G. Mol. Cell. Biol. 18:4391-4399(1998) [PubMed: 9632823] [Abstract] Cited for: INTERACTION WITH DDB1, DNA-BINDING, CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273.
[7]	"Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair." Hwang B.J., Ford J.M., Hanawalt P.C., Chu G. Proc. Natl. Acad. Sci. U.S.A. 96:424-428(1999) [PubMed: 9892649] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[8]	"Human damage-specific DNA-binding protein p48. Characterization of XPE mutations and regulation following UV irradiation." Nichols A.F., Itoh T., Graham J.A., Liu W., Yamaizumi M., Linn S. J. Biol. Chem. 275:21422-21428(2000) [PubMed: 10777490] [Abstract] Cited for: DNA-BINDING, SUBCELLULAR LOCATION, INDUCTION, CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273.
[9]	"Nuclear transport of human DDB protein induced by ultraviolet light." Liu W., Nichols A.F., Graham J.A., Dualan R., Abbas A., Linn S. J. Biol. Chem. 275:21429-21434(2000) [PubMed: 10777491] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis." Tang J.Y., Hwang B.J., Ford J.M., Hanawalt P.C., Chu G. Mol. Cell 5:737-744(2000) [PubMed: 10882109] [Abstract] Cited for: FUNCTION.
[11]	"Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A." Wakasugi M., Shimizu M., Morioka H., Linn S., Nikaido O., Matsunaga T. J. Biol. Chem. 276:15434-15440(2001) [PubMed: 11278856] [Abstract] Cited for: FUNCTION, DNA-BINDING.
[12]	"UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation." Chen X., Zhang Y., Douglas L., Zhou P. J. Biol. Chem. 276:48175-48182(2001) [PubMed: 11673459] [Abstract] Cited for: INTERACTION WITH CUL4A, UBIQUITINATION, CHARACTERIZATION OF VARIANT HIS-273.
[13]	"DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair." Wakasugi M., Kawashima A., Morioka H., Linn S., Sancar A., Mori T., Nikaido O., Matsunaga T. J. Biol. Chem. 277:1637-1640(2002) [PubMed: 11705987] [Abstract] Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION.
[14]	"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage." Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y. Cell 113:357-367(2003) [PubMed: 12732143] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB1 AND RBX1 AND THE COP9 SIGNALOSOME, DNA-BINDING.
[15]	"In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product." Fitch M.E., Nakajima S., Yasui A., Ford J.M. J. Biol. Chem. 278:46906-46910(2003) [PubMed: 12944386] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex." Sugasawa K., Okuda Y., Saijo M., Nishi R., Matsuda N., Chu G., Mori T., Iwai S., Tanaka K., Tanaka K., Hanaoka F. Cell 121:387-400(2005) [PubMed: 15882621] [Abstract] Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB1; RBX1 AND XPC, DNA-BINDING, UBIQUITINATION.
[17]	"DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA." Wittschieben B.O., Iwai S., Wood R.D. J. Biol. Chem. 280:39982-39989(2005) [PubMed: 16223728] [Abstract] Cited for: INTERACTION WITH DDB1, DNA-BINDING, CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273.
[18]	"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." Kulaksiz G., Reardon J.T., Sancar A. Mol. Cell. Biol. 25:9784-9792(2005) [PubMed: 16260596] [Abstract] Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB1; RBX1 AND THE COP9 SIGNALOSOME, DNA-BINDING.
[19]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, MASS SPECTROMETRY. Tissue: Epithelium.
[20]	"DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases." He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y. Genes Dev. 20:2949-2954(2006) [PubMed: 17079684] [Abstract] Cited for: INTERACTION WITH CUL4A AND DDB1, DWD BOX MOTIF, MUTAGENESIS OF LEU-258; SER-262; ASP-264; ILE-269; TRP-270; LEU-272 AND ARG-273.
[21]	"Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC." El-Mahdy M.A., Zhu Q., Wang Q.-E., Wani G., Praetorius-Ibba M., Wani A.A. J. Biol. Chem. 281:13404-13411(2006) [PubMed: 16527807] [Abstract] Cited for: INTERACTION WITH CUL4A AND DDB1, UBIQUITINATION.
[22]	"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage." Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y. Mol. Cell 22:383-394(2006) [PubMed: 16678110] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH DDB1; CUL4A; CUL4B AND RBX1, FUNCTION.
[23]	"A kinase-independent function of c-Abl in promoting proteolytic destruction of damaged DNA binding proteins." Chen X., Zhang J., Lee J., Lin P.S., Ford J.M., Zheng N., Zhou P. Mol. Cell 22:489-499(2006) [PubMed: 16713579] [Abstract] Cited for: SUBCELLULAR LOCATION, UBIQUITINATION.
[24]	"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1." Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C. Mol. Cell 23:709-721(2006) [PubMed: 16949367] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDB1, MUTAGENESIS OF LEU-350, CHARACTERIZATION OF VARIANT HIS-273.
[25]	"Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery." Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N. Nature 443:590-593(2006) [PubMed: 16964240] [Abstract] Cited for: INTERACTION WITH DDB1, CHARACTERIZATION OF VARIANT HIS-273.
[26]	"CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation." Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H. Nat. Cell Biol. 8:1277-1283(2006) [PubMed: 17041588] [Abstract] Cited for: INTERACTION WITH CUL4A AND CUL4B.
[27]	"The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites." Kapetanaki M.G., Guerrero-Santoro J., Bisi D.C., Hsieh C.L., Rapic-Otrin V., Levine A.S. Proc. Natl. Acad. Sci. U.S.A. 103:2588-2593(2006) [PubMed: 16473935] [Abstract] Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB1; HISTONE H2A AND RBX1, DNA-BINDING, SUBCELLULAR LOCATION.
[28]	"Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-damaged DNA is independent of damage-recognition protein XPC." Luijsterburg M.S., Goedhart J., Moser J., Kool H., Geverts B., Houtsmuller A.B., Mullenders L.H.F., Vermeulen W., van Driel R. J. Cell Sci. 120:2706-2716(2007) [PubMed: 17635991] [Abstract] Cited for: SUBCELLULAR LOCATION.
[29]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, MASS SPECTROMETRY.
[30]	"The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A." Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I., Levine A.S., Rapic-Otrin V. Cancer Res. 68:5014-5022(2008) [PubMed: 18593899] [Abstract] Cited for: FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB1, SUBCELLULAR LOCATION.
[31]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, MASS SPECTROMETRY.
[32]	"Mutations specific to the xeroderma pigmentosum group E Ddb-phenotype." Nichols A.F., Ong P., Linn S. J. Biol. Chem. 271:24317-24320(1996) [PubMed: 8798680] [Abstract] Cited for: VARIANTS XP-E GLU-244 AND HIS-273.
+	Additional computationally mapped references.

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Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

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Cross-references

Sequence databases

U18300 mRNA. Translation: AAB07897.1.
AB107037 mRNA. Translation: BAD12557.1.
AB107038 mRNA. Translation: BAD12558.1.
AB107039 mRNA. Translation: BAD12559.1.
AB107040 mRNA. Translation: BAD12560.1.
BT007139 mRNA. Translation: AAP35803.1.
AY220533 Genomic DNA. Translation: AAO25655.1.
BC000093 mRNA. Translation: AAH00093.1.

IPI

IPI00021518.
IPI00446284.
IPI00549348.
IPI00607674.
IPI00607727.

PIR

I38909.

RefSeq

NP_000098.1.

UniGene

Hs.708067

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EI4	X-ray	3.30	B/D/F	10-427	[»]

ModBase

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Protein-protein interaction databases

IntAct

Q92466. 5 interactions.

PTM databases

PhosphoSite

Q92466.

Proteomic databases

PRIDE

Q92466.

Genome annotation databases

Ensembl

ENSG00000134574. Homo sapiens. [Contig view]

GeneID

1643.

KEGG

hsa:1643.

Organism-specific databases

GeneCards

GC11P047193.

H-InvDB

HIX0009611.

HGNC

HGNC:2718. DDB2.

MIM

278740. phenotype.
600811. gene.

Orphanet

910. Xeroderma pigmentosum.

PharmGKB

PA27188.

GenAtlas

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Phylogenomic databases

HOGENOM

Q92466.

HOVERGEN

Q92466.

OMA

Q92466. VWFCSLD.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

Bgee

Q92466.

CleanEx

HS_DDB2.

GermOnline

ENSG00000134574. Homo sapiens.

Family and domain databases

InterPro

IPR015943. WD40/YVTN_repeat-like.
IPR001680. WD40_repeat.
IPR019782. WD40_repeat_2.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_region.
IPR019781. WD40_repeat_sg.
[Graphical view]

Gene3D

G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.

Pfam

PF00400. WD40. 3 hits.
[Graphical view]

SMART

SM00320. WD40. 5 hits.
[Graphical view]

PROSITE

PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

6758.

SOURCE

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Entry information

Entry name

DDB2_HUMAN

Accession

Primary (citable) accession number: Q92466
Secondary accession number(s): Q76E54

Q76E57

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents