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Q16531 (DDB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA damage-binding protein 1
Alternative name(s):
DDB p127 subunit
DNA damage-binding protein a
Short name=DDBa
Damage-specific DNA-binding protein 1
HBV X-associated protein 1
Short name=XAP-1
UV-damaged DNA-binding factor
UV-damaged DNA-binding protein 1
Short name=UV-DDB 1
XPE-binding factor
Short name=XPE-BF
Xeroderma pigmentosum group E-complementing protein
Short name=XPCe
Gene names
Name:DDB1
Synonyms:XAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1140 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.33 Ref.34 Ref.36

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, LRWD1 and WDTC1. DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. Interacts with NF2, TSC1 and TSC2. 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. Interacts with AGO1 and AGO2. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts directly with DYRK2. DCX(DTL) complex interacts with FBXO11; does not ubiquitinate and degradate FBXO11. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45

Subcellular location

Cytoplasm. Nucleus. Note: Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage. Ref.11 Ref.12 Ref.31 Ref.33

Post-translational modification

Phosphorylated by ABL1 By similarity.

Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis. Ref.12

Sequence similarities

Belongs to the DDB1 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Host-virus interaction
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 20223979. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of mitotic cell cycle phase transition

Inferred from mutant phenotype PubMed 17088560. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCul4-RING ubiquitin ligase complex

Inferred from direct assay Ref.34. Source: UniProtKB

Cul4A-RING ubiquitin ligase complex

Inferred from direct assay Ref.14PubMed 18794347PubMed 20129063PubMed 20223979. Source: UniProtKB

Cul4B-RING ubiquitin ligase complex

Inferred from direct assay PubMed 18794347. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.33PubMed 20223979. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.33PubMed 20223979. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 8798680. Source: ProtInc

damaged DNA binding

Traceable author statement PubMed 8407967. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.37
Chain2 – 11401139DNA damage-binding protein 1
PRO_0000079840

Regions

Region2 – 768767Interaction with CDT1
Region391 – 709319Interaction with CUL4A
Region771 – 1140370Interaction with CDT1 and CUL4A

Amino acid modifications

Modified residue21N-acetylserine Ref.37
Modified residue10671N6-acetyllysine Ref.39

Natural variations

Natural variant4271L → F. Ref.6
Corresponds to variant rs28720299 [ dbSNP | Ensembl ].
VAR_023074

Experimental info

Mutagenesis316 – 3194YLDN → ALAA: Impairs interaction with DDA1. Ref.28
Mutagenesis5371E → A: Slightly impairs interaction with CUL4A. Ref.43
Mutagenesis5611W → A: Strongly impairs interaction with CUL4A. Ref.43
Mutagenesis840 – 8423EAE → AAA: Impairs interaction with AMBRA1, DTL, DET1, VPRBP, DCAF5, DCAF11 and DCAF8. Ref.28
Mutagenesis910 – 9134MALY → AAAA: Impairs interaction with AMBRA1, DTL and DCAF5. Ref.28
Mutagenesis9531W → A: Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11. Ref.28
Sequence conflict4221D → Y in AAA88883. Ref.3
Sequence conflict5331E → G in CAA05770. Ref.4
Sequence conflict8691A → D in CAA05770. Ref.4
Sequence conflict898 – 8992EL → DV in AAA88883. Ref.3
Sequence conflict898 – 8992EL → DV in CAA05770. Ref.4

Secondary structure

.............................................................................................................................................................................................................................................................. 1140
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16531 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 74D082023E3D846D

FASTA1,140126,968
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH DDB2; CUL4A; CUL4B AND RBX1, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB2; HISTONE H2A AND RBX1, DNA-BINDING, SUBCELLULAR LOCATION.
[32]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[33]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB2, SUBCELLULAR LOCATION.
[34]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FBXW5; TSC1 AND TSC2.
[35]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCAF1/VPRBP.
[36]"VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation."
Huang J., Chen J.
Oncogene 27:4056-4064(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NF2.
[37]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[38]"Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase."
Maddika S., Chen J.
Nat. Cell Biol. 11:409-419(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EDVP COMPLEX.
[39]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"Orc2 protects ORCA from ubiquitin-mediated degradation."
Shen Z., Prasanth S.G.
Cell Cycle 11:3578-3589(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRWD1.
[42]"CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DTL.
[43]"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] [Europe PMC] [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.
[44]"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] [Europe PMC] [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.
[45]"Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex."
Scrima A., Konickova R., Czyzewski B.K., Kawasaki Y., Jeffrey P.D., Groisman R., Nakatani Y., Iwai S., Pavletich N.P., Thoma N.H.
Cell 135:1213-1223(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA, SUBUNIT.
+Additional computationally mapped references.

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.
PIRI38908.
RefSeqNP_001914.3. NM_001923.4.
UniGeneHs.290758.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B5LX-ray2.85A/B1-1140[»]
2B5MX-ray2.92A1-1140[»]
2B5NX-ray2.80A/B/C/D391-709[»]
2HYEX-ray3.10A1-1140[»]
3E0CX-ray2.41A1-1140[»]
3EI1X-ray2.80A1-1140[»]
3EI2X-ray2.60A1-1140[»]
3EI3X-ray2.30A1-1140[»]
3EI4X-ray3.30A/C/E1-1140[»]
3I7HX-ray2.90A1-1140[»]
3I7KX-ray2.80A1-1140[»]
3I7LX-ray2.80A1-1140[»]
3I7NX-ray2.80A1-1140[»]
3I7OX-ray2.80A1-1140[»]
3I7PX-ray3.00A1-1140[»]
3I89X-ray3.00A1-1140[»]
3I8CX-ray2.80A1-1140[»]
3I8EX-ray3.40A/B1-1140[»]
4A08X-ray3.00A1-1140[»]
4A09X-ray3.10A1-1140[»]
4A0AX-ray3.60A1-1140[»]
4A0BX-ray3.80A/C1-1140[»]
4A0KX-ray5.93C1-1140[»]
4A0LX-ray7.40A/C1-1140[»]
4A11X-ray3.31A1-1140[»]
4E54X-ray2.85A2-1140[»]
4E5ZX-ray3.22A2-1140[»]
ProteinModelPortalQ16531.
SMRQ16531. Positions 2-1140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108009. 188 interactions.
DIPDIP-430N.
IntActQ16531. 79 interactions.
MINTMINT-1134697.
STRING9606.ENSP00000301764.

PTM databases

PhosphoSiteQ16531.

Polymorphism databases

DMDM12643730.

Proteomic databases

PaxDbQ16531.
PRIDEQ16531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301764; ENSP00000301764; ENSG00000167986.
GeneID1642.
KEGGhsa:1642.
UCSCuc001nrc.5. human.

Organism-specific databases

CTD1642.
GeneCardsGC11M061066.
H-InvDBHIX0171380.
HGNCHGNC:2717. DDB1.
HPACAB032821.
MIM600045. gene.
neXtProtNX_Q16531.
PharmGKBPA27187.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247734.
HOGENOMHOG000007241.
HOVERGENHBG005460.
InParanoidQ16531.
KOK10610.
OMACAVGLWT.
OrthoDBEOG7X0VG9.
PhylomeDBQ16531.
TreeFamTF105840.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ16531.
BgeeQ16531.
CleanExHS_DDB1.
GenevestigatorQ16531.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR004871. Cleavage/polyA-sp_fac_asu_C.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF03178. CPSF_A. 1 hit.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDDB1. human.
EvolutionaryTraceQ16531.
GeneWikiDDB1.
GenomeRNAi1642.
NextBio6750.
PROQ16531.
SOURCESearch...

Entry information

Entry nameDDB1_HUMAN
AccessionPrimary (citable) accession number: Q16531
Secondary accession number(s): A6NG77 expand/collapse secondary AC list , B2R648, O15176, Q13289, Q58F96
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

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