Reviewed, UniProtKB/Swiss-Prot Q16531 (DDB1_HUMAN)

Names and origin

Protein names

Recommended name:
DNA damage-binding protein 1

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

Gene names

Name:	DDB1
Synonyms:	XAP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1140 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2. Ref.14 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35
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 numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may recruit specific substrate targeting subunits to the DCX complex. These substrate targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC, DCAF1, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12, DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8, WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2 and WDTC1. DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. Interacts with NF2, TSC1 and TSC2. Interacts with Simian virus 5 protein V and the HBV X protein. Interaction with SV5 protein V may prevent the recruitment of DCAF proteins to DCX complexes. Ref.14 Ref.16 Ref.17 Ref.18 Ref.21 Ref.23 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.10 Ref.12 Ref.13 Ref.15 Ref.19 Ref.20 Ref.26 Ref.28 Ref.38 Ref.39
Subcellular location	Cytoplasm. Nucleus. Note: Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage. Ref.31 Ref.32 Ref.12 Ref.11
Post-translational modification	Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis. Ref.12
Sequence similarities	Belongs to the DDB1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Host-virus interaction Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle checkpoint Inferred from mutant phenotype. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nucleotide-excision repair, DNA damage removal Inferred from Experiment. Source: Reactome protein ubiquitination during ubiquitin-dependent protein catabolic process Ref.12 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Ref.32 Inferred from direct assay. Source: UniProtKB nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	damaged DNA binding Traceable author statement. Source: ProtInc protein binding Ref.14 Ref.30 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDB2	Q92466	3	EBI-350322,EBI-1176171
ddb2	Q2YDS1	1	EBI-350322,EBI-2213320	From a different organism.
DTL	Q9NZJ0	1	EBI-350322,EBI-1176075
EED	O75530	1	EBI-350322,EBI-923794
TLE2	Q04725	1	EBI-350322,EBI-1176061
WDR23	Q8TEB1	1	EBI-350322,EBI-2213388

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1140

1140

DNA damage-binding protein 1

PRO_0000079840

Regions

Region

1 – 768

768

Interaction with CDT1

Region

391 – 709

319

Interaction with CUL4A

Region

771 – 1140

370

Interaction with CDT1 and CUL4A

Amino acid modifications

Modified residue

8

1

Phosphothreonine By similarity

Modified residue

153

1

N6-acetyllysine Ref.37

Modified residue

757

1

Phosphoserine By similarity

Modified residue

766

1

Phosphoserine By similarity

Modified residue

1067

1

N6-acetyllysine Ref.37

Natural variations

Natural variant

427

1

L → F: dbSNP rs28720299. Ref.6

VAR_023074

Experimental info

Mutagenesis

316 – 319

4

YLDN → ALAA: Impairs interaction with DDA1.

Mutagenesis

537

1

E → A: Slightly impairs interaction with CUL4A. Ref.38

Mutagenesis

561

1

W → A: Strongly impairs interaction with CUL4A. Ref.38

Mutagenesis

840 – 842

3

EAE → AAA: Impairs interaction with AMBRA1, DTL, DET1, VPRBP, DCAF5, DCAF11 and DCAF8.

Mutagenesis

910 – 913

4

MALY → AAAA: Impairs interaction with AMBRA1, DTL and DCAF5.

Mutagenesis

953

1

W → A: Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11. Ref.28

Sequence conflict

422

1

D → Y in AAA88883. Ref.3

Sequence conflict

533

1

E → G in CAA05770. Ref.4

Sequence conflict

869

1

A → D in CAA05770. Ref.4

Sequence conflict

898 – 899

2

EL → DV in AAA88883. Ref.3

Sequence conflict

898 – 899

2

EL → DV in CAA05770. Ref.4

Secondary structure

1

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1140

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

17 – 21

5

Beta strand

30 – 34

5

Beta strand

36 – 44

9

Beta strand

46 – 56

11

Beta strand

61 – 67

7

Beta strand

76 – 81

6

Beta strand

85 – 96

12

Beta strand

98 – 107

10

Beta strand

121 – 124

4

Beta strand

128 – 134

7

Beta strand

139 – 144

6

Beta strand

155 – 158

4

Beta strand

164 – 169

6

Beta strand

177 – 184

8

Beta strand

187 – 196

10

Turn

197 – 200

4

Beta strand

218 – 221

4

Turn

224 – 226

3

Beta strand

228 – 232

5

Beta strand

237 – 241

5

Beta strand

244 – 248

5

Helix

251 – 254

4

Beta strand

260 – 265

6

Beta strand

268 – 274

7

Beta strand

276 – 289

14

Beta strand

291 – 293

3

Beta strand

295 – 307

13

Beta strand

311 – 316

6

Beta strand

321 – 329

9

Beta strand

331 – 336

6

Beta strand

346 – 353

8

Beta strand

358 – 364

7

Beta strand

369 – 371

3

Beta strand

375 – 379

5

Helix

382 – 384

3

Beta strand

386 – 391

6

Beta strand

396 – 402

7

Beta strand

409 – 413

5

Beta strand

416 – 418

3

Beta strand

424 – 428

5

Beta strand

433 – 439

7

Beta strand

442 – 446

5

Beta strand

453 – 455

3

Beta strand

457 – 463

7

Turn

464 – 466

3

Beta strand

467 – 474

8

Beta strand

476 – 479

4

Beta strand

481 – 483

3

Beta strand

485 – 490

6

Beta strand

500 – 503

4

Beta strand

505 – 512

8

Beta strand

515 – 522

8

Beta strand

525 – 533

9

Beta strand

538 – 542

5

Beta strand

554 – 563

10

Beta strand

565 – 570

6

Turn

571 – 574

4

Beta strand

575 – 581

7

Beta strand

584 – 586

3

Beta strand

588 – 598

11

Beta strand

600 – 606

7

Beta strand

609 – 616

8

Turn

618 – 620

3

Beta strand

623 – 630

8

Beta strand

637 – 641

5

Beta strand

643 – 646

4

Beta strand

648 – 655

8

Beta strand

657 – 674

18

Beta strand

677 – 682

6

Beta strand

685 – 687

3

Beta strand

690 – 694

5

Beta strand

699 – 704

6

Beta strand

711 – 716

6

Beta strand

718 – 724

7

Turn

728 – 731

4

Beta strand

732 – 743

12

Beta strand

747 – 749

3

Turn

756 – 758

3

Beta strand

785 – 795

11

Turn

796 – 798

3

Beta strand

801 – 806

6

Beta strand

811 – 815

5

Beta strand

818 – 821

4

Beta strand

824 – 835

12

Beta strand

840 – 842

3

Beta strand

846 – 852

7

Beta strand

854 – 857

4

Beta strand

859 – 862

4

Beta strand

865 – 868

4

Beta strand

872 – 876

5

Beta strand

879 – 883

5

Beta strand

888 – 893

6

Beta strand

899 – 905

7

Beta strand

911 – 917

7

Beta strand

920 – 928

9

Beta strand

930 – 936

7

Turn

937 – 940

4

Beta strand

941 – 947

7

Beta strand

954 – 961

8

Beta strand

964 – 969

6

Turn

970 – 972

3

Beta strand

973 – 979

7

Turn

986 – 990

5

Beta strand

991 – 999

9

Beta strand

1004 – 1009

6

Beta strand

1023 – 1032

10

Beta strand

1037 – 1042

6

Helix

1045 – 1061

17

Helix

1070 – 1073

4

Beta strand

1075 – 1077

3

Beta strand

1086 – 1090

5

Helix

1091 – 1096

6

Helix

1097 – 1099

3

Helix

1102 – 1109

8

Beta strand

1117 – 1120

4

Helix

1126 – 1137

12

Sequences

	Sequence		Length	Mass (Da)
	Q16531-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 74D082023E3D846D	FASTA	1,140	126,968
	10 20 30 40 50 60 MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK 70 80 90 100 110 120 IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI 130 140 150 160 170 180 IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF 190 200 210 220 230 240 VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH 250 260 270 280 290 300 NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL 310 320 330 340 350 360 RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV 370 380 390 400 410 420 DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPNRE 430 440 450 460 470 480 TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS 490 500 510 520 530 540 QEPKALVSEW KEPQAKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC 550 560 570 580 590 600 LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH 610 620 630 640 650 660 YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY 670 680 690 700 710 720 SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES 730 740 750 760 770 780 PRKICYQEVS QCFGVLSSRI EVQDTSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET 790 800 810 820 830 840 SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE 850 860 870 880 890 900 AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR 910 920 930 940 950 960 TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL 970 980 990 1000 1010 1020 DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET 1030 1040 1050 1060 1070 1080 STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER 1090 1100 1110 1120 1130 1140 KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH

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]. Tissue: Epidermis and Fetal lung.
[2]	"Hepatitis B virus X protein interacts with a probable cellular DNA repair protein." Lee T.H., Elledge S.J., Butel J.S. J. Virol. 69:1107-1114(1995) [PubMed: 7815490] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Peripheral blood.
[3]	"Isolation of a cDNA encoding a UV-damaged DNA binding factor defective in xeroderma pigmentosum group E cells." Hwang B.J., Liao J.C., Chu G. Mutat. Res. 362:105-117(1996) [PubMed: 8538642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Molecular cloning and characterization of human XPE protein: a component of UV-damaged DNA recognition activity." Huang S.L., Lin-Chao S., Chao C.K. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta and Skin.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	NIEHS SNPs program Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-427.
[7]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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]. Tissue: Placenta and Skin.
[10]	"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.
[11]	"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.
[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, SUBCELLULAR LOCATION, UBIQUITINATION.
[13]	"Hepatitis B virus X protein interferes with cell viability through interaction with the p127-kDa UV-damaged DNA-binding protein." Lin-Marq N., Bontron S., Leupin O., Strubin M. Virology 287:266-274(2001) [PubMed: 11531405] [Abstract] Cited for: INTERACTION WITH HBV X PROTEIN.
[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, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB2 AND RBX1, IDENTIFICATION IN THE CSA COMPLEX WITH CUL4A; ERCC8 AND RBX1, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II, INTERACTION WITH THE COP9 SIGNALOSOME.
[15]	"Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities." Leupin O., Bontron S., Strubin M. J. Virol. 77:6274-6283(2003) [PubMed: 12743284] [Abstract] Cited for: INTERACTION WITH HBV X PROTEIN AND SV5 PROTEIN V.
[16]	"Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage." Hu J., McCall C.M., Ohta T., Xiong Y. Nat. Cell Biol. 6:1003-1009(2004) [PubMed: 15448697] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDT1; CUL4A; RBX1 AND THE COP9 SIGNALOSOME.
[17]	"Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase." Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M. Science 303:1371-1374(2004) [PubMed: 14739464] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL4A; DET1; RBX1 AND RFWD2.
[18]	"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; DDB2 AND RBX1, DNA-BINDING.
[19]	"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 DDB2, DNA-BINDING.
[20]	"Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1." Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E. J. Virol. 79:13434-13441(2005) [PubMed: 16227264] [Abstract] Cited for: INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V.
[21]	"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; DDB2; RBX1 AND THE COP9 SIGNALOSOME, DNA-BINDING.
[22]	"Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for proteolysis." Nishitani H., Sugimoto N., Roukos V., Nakanishi Y., Saijo M., Obuse C., Tsurimoto T., Nakayama K.I., Nakayama K., Fujita M., Lygerou Z., Nishimoto T. EMBO J. 25:1126-1136(2006) [PubMed: 16482215] [Abstract] Cited for: FUNCTION.
[23]	"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: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ATG16L1; BTRC; CUL4A; DDB2; ERCC8; FBXW5; FBXW8; GRWD1; KATNB1; NUP43; PWP1; RBBP4; RBBP7; RFWD2; VPRBP; DCAF11; WSB1 AND WSB2.
[24]	"An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage." Hu J., Xiong Y. J. Biol. Chem. 281:3753-3756(2006) [PubMed: 16407242] [Abstract] Cited for: FUNCTION.
[25]	"PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination." Senga T., Sivaprasad U., Zhu W., Park J.H., Arias E.E., Walter J.C., Dutta A. J. Biol. Chem. 281:6246-6252(2006) [PubMed: 16407252] [Abstract] Cited for: FUNCTION.
[26]	"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 DDB2.
[27]	"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 IN A COMPLEX WITH DDB2; CUL4A; CUL4B AND RBX1, MASS SPECTROMETRY, FUNCTION.
[28]	"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: INTERACTION WITH AMBRA1; DCAF17; DCAF16; DCAF15; DDA1; DDB2; DET1; DTL; ERCC8; DCAF6; PHIP; VPRBP; DCAF4; DCAF5; DCAF11; DCAF10; DCAF12; DCAF8; DCAF7 AND WDTC1, MUTAGENESIS OF 316-TYR--ASN-319; 840-GLU--GLU-842; 910-MET--TYR-913 AND TRP-953.
[29]	"DDB1 maintains genome integrity through regulation of Cdt1." Lovejoy C.A., Lock K., Yenamandra A., Cortez D. Mol. Cell. Biol. 26:7977-7990(2006) [PubMed: 16940174] [Abstract] Cited for: FUNCTION.
[30]	"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: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL4B; DTL; NLE1; PAFAH1B1; RBBP5; RFWD2; SNRNP40; WDR5; WDR5B; WDR12; WDR26; WDR39; WDR53; WDR59 AND WDR61.
[31]	"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; DDB2; HISTONE H2A AND RBX1, DNA-BINDING, SUBCELLULAR LOCATION.
[32]	"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 DDB2, SUBCELLULAR LOCATION.
[33]	"WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase." Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J., Xiong Y. Genes Dev. 22:866-871(2008) [PubMed: 18381890] [Abstract] Cited for: FUNCTION, INTERACTION WITH FBXW5; TSC1 AND TSC2.
[34]	"Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40 protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is essential for DNA replication and embryonic development." McCall C.M., Miliani de Marval P.L., Chastain P.D. II, Jackson S.C., He Y.J., Kotake Y., Cook J.G., Xiong Y. Mol. Cell. Biol. 28:5621-5633(2008) [PubMed: 18606781] [Abstract] Cited for: INTERACTION WITH DCAF1/VPRBP.
[35]	"VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation." Huang J., Chen J. Oncogene 27:4056-4064(2008) [PubMed: 18332868] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NF2.
[36]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[37]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-153 AND LYS-1067, MASS SPECTROMETRY.
[38]	"Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase." Li T., Chen X., Garbutt K.C., Zhou P., Zheng N. Cell 124:105-117(2006) [PubMed: 16413485] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-1140 IN COMPLEX WITH SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH CUL4A AND DET1, MUTAGENESIS OF GLU-537 AND TRP-561.
[39]	"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: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-1140 IN COMPLEX WITH CUL4A; RBX1 AND SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH DDB2; DTL; DCAF11; DCAF8 AND WDTC1.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18299 mRNA. Translation: AAC50349.1.
L40326 mRNA. Translation: AAA62838.1.
U32986 mRNA. Translation: AAA88883.1.
AJ002955 mRNA. Translation: CAA05770.1.
AK312436 mRNA. Translation: BAG35345.1.
AY960579 Genomic DNA. Translation: AAX44048.1.
AP003108 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73935.1.
BC011686 mRNA. Translation: AAH11686.1.
BC050530 mRNA. Translation: AAH50530.1.
BC051764 mRNA. Translation: AAH51764.1.

IPI

IPI00293464.

PIR

I38908.

RefSeq

NP_001914.3.
XP_002347285.1.

UniGene

Hs.290758
Hs.705536

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B5L	X-ray	2.85	A/B	1-1140	[»]
2B5M	X-ray	2.92	A	1-1140	[»]
2B5N	X-ray	2.80	A/B/C/D	391-709	[»]
2HYE	X-ray	3.10	A	1-1140	[»]
3E0C	X-ray	2.41	A	1-1140	[»]
3EI1	X-ray	2.80	A	1-1140	[»]
3EI2	X-ray	2.60	A	1-1140	[»]
3EI3	X-ray	2.30	A	1-1140	[»]
3EI4	X-ray	3.30	A/C/E	1-1140	[»]
3I7H	X-ray	2.90	A	1-1140	[»]
3I7K	X-ray	2.80	A	1-1140	[»]
3I7L	X-ray	2.80	A	1-1140	[»]
3I7N	X-ray	2.80	A	1-1140	[»]
3I7O	X-ray	2.80	A	1-1140	[»]
3I7P	X-ray	3.00	A	1-1140	[»]
3I89	X-ray	3.00	A	1-1140	[»]
3I8C	X-ray	2.80	A	1-1140	[»]
3I8E	X-ray	3.40	A/B	1-1140	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-430N.

IntAct

Q16531. 37 interactions.

STRING

Q16531.

PTM databases

PhosphoSite

Q16531.

Proteomic databases

PRIDE

Q16531.

Genome annotation databases

Ensembl

ENST00000301764; ENSP00000301764; ENSG00000167986; Homo sapiens. [Genome view]

GeneID

100290337.
1642.

KEGG

hsa:100290337.
hsa:1642.

UCSC

uc001nrc.2. human.

Organism-specific databases

CTD

1642.

GeneCards

GC11M060823.

H-InvDB

HIX0009685.

HGNC

HGNC:2717. DDB1.

MIM

600045. gene.

PharmGKB

PA27187.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12562.

HOGENOM

HBG318519.

HOVERGEN

HBG005460.

InParanoid

Q16531.

OMA

EHSFWRS.

OrthoDB

EOG91G5PF.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q16531.

Bgee

Q16531.

CleanEx

HS_DDB1.

Genevestigator

Q16531.

GermOnline

ENSG00000167986. Homo sapiens.

Family and domain databases

InterPro

IPR004871. Cleavage/polyA-sp_fac_asu_C.
[Graphical view]

Pfam

PF03178. CPSF_A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

6750.

SOURCE

Search...

Entry information

Entry name

DDB1_HUMAN

Accession

Primary (citable) accession number: Q16531
Secondary accession number(s): A6NG77 , B2R648, O15176, Q13289, Q58F96

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1996
Last modified:	March 2, 2010
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.