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Q92466

- DDB2_HUMAN

UniProt

Q92466 - DDB2_HUMAN

Protein

DNA damage-binding protein 2

Gene

DDB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    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.12 Publications

    Pathwayi

    GO - Molecular functioni

    1. damaged DNA binding Source: ProtInc
    2. DNA binding Source: ProtInc
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. histone H2A monoubiquitination Source: UniProt
    3. nucleotide-excision repair Source: Reactome
    4. nucleotide-excision repair, DNA damage removal Source: Reactome
    5. protein autoubiquitination Source: UniProtKB
    6. protein polyubiquitination Source: UniProtKB
    7. pyrimidine dimer repair Source: Ensembl
    8. response to UV Source: UniProtKB
    9. UV-damage excision repair Source: UniProt

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    SignaLinkiQ92466.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA damage-binding protein 2
    Alternative name(s):
    DDB p48 subunit
    Short name:
    DDBb
    Damage-specific DNA-binding protein 2
    UV-damaged DNA-binding protein 2
    Short name:
    UV-DDB 2
    Gene namesi
    Name:DDB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2718. DDB2.

    Subcellular locationi

    Nucleus 9 Publications
    Note: Accumulates at sites of DNA damage following UV irradiation.

    GO - Cellular componenti

    1. Cul4B-RING E3 ubiquitin ligase complex Source: UniProt
    2. nucleoplasm Source: Reactome
    3. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti244 – 2441K → E in XP-E; impairs DNA-binding of the UV-DDB complex. 1 Publication
    VAR_010141
    Natural varianti273 – 2731R → H in XP-E; impairs interaction with DDB1 and CUL4A. 1 Publication
    VAR_010142

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581L → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi262 – 2621S → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi264 – 2641D → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi269 – 2691I → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi270 – 2701W → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi272 – 2721L → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi273 – 2731R → A: Impairs interaction with DDB1. 1 Publication
    Mutagenesisi350 – 3501L → P: Impairs interaction with DDB1. 1 Publication

    Keywords - Diseasei

    Disease mutation, Xeroderma pigmentosum

    Organism-specific databases

    MIMi278740. phenotype.
    Orphaneti276261. Xeroderma pigmentosum complementation group E.
    PharmGKBiPA27188.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427DNA damage-binding protein 2PRO_0000050953Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphoserine1 Publication
    Modified residuei26 – 261Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylation by ABL1 negatively regulate UV-DDB activity.By similarity
    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 ABL1.1 Publication
    Ubiquitinated, leading to proteasomal degradation, and deubiquitinated by USP24.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ92466.
    PaxDbiQ92466.
    PRIDEiQ92466.

    PTM databases

    PhosphoSiteiQ92466.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Inductioni

    Expression is induced in response to treatment with IR or UV and this requires p53/TP53 activity.1 Publication

    Gene expression databases

    BgeeiQ92466.
    CleanExiHS_DDB2.
    GenevestigatoriQ92466.

    Organism-specific databases

    HPAiCAB025912.

    Interactioni

    Subunit structurei

    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 DDB1.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUL4AQ136192EBI-1176171,EBI-456106
    DDB1Q165313EBI-1176171,EBI-350322
    E2F1Q010942EBI-1176171,EBI-448924

    Protein-protein interaction databases

    BioGridi108010. 51 interactions.
    DIPiDIP-36670N.
    IntActiQ92466. 9 interactions.
    STRINGi9606.ENSP00000256996.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 255
    Beta strandi30 – 323
    Helixi39 – 424
    Turni44 – 474
    Beta strandi49 – 513
    Helixi58 – 625
    Turni63 – 653
    Helixi69 – 779
    Helixi83 – 919
    Turni92 – 943
    Turni96 – 1027
    Beta strandi106 – 1094
    Beta strandi114 – 1196
    Beta strandi127 – 1315
    Beta strandi136 – 1394
    Beta strandi148 – 1503
    Beta strandi154 – 1563
    Beta strandi161 – 1644
    Beta strandi171 – 1755
    Beta strandi177 – 1793
    Beta strandi181 – 1855
    Turni186 – 1883
    Beta strandi190 – 1956
    Beta strandi198 – 2014
    Beta strandi207 – 2104
    Turni211 – 2144
    Beta strandi215 – 2195
    Beta strandi221 – 23212
    Beta strandi241 – 2433
    Beta strandi245 – 2506
    Turni252 – 2543
    Beta strandi255 – 2628
    Turni263 – 2653
    Beta strandi269 – 2713
    Turni272 – 2743
    Beta strandi277 – 2793
    Beta strandi282 – 2865
    Beta strandi291 – 2933
    Beta strandi300 – 31011
    Beta strandi312 – 32615
    Beta strandi335 – 3373
    Beta strandi346 – 3494
    Beta strandi351 – 3544
    Beta strandi359 – 3613
    Beta strandi364 – 3663
    Beta strandi372 – 3754
    Beta strandi377 – 3793
    Beta strandi382 – 3865
    Turni389 – 3913
    Beta strandi397 – 4004
    Beta strandi407 – 4104
    Beta strandi412 – 4176

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EI4X-ray3.30B/D/F10-427[»]
    3I7LX-ray2.80B68-81[»]
    4E54X-ray2.85B2-427[»]
    4E5ZX-ray3.22B2-427[»]
    ProteinModelPortaliQ92466.
    SMRiQ92466. Positions 20-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92466.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati116 – 15136WD 11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati159 – 19436WD 21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati203 – 23836WD 31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati244 – 28744WD 41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati290 – 32940WD 51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati343 – 38644WD 61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati396 – 42025WD 71 PublicationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni68 – 7912Required for interaction with DDB1Add
    BLAST
    Regioni87 – 9812Required for interaction with DDB1Add
    BLAST
    Regioni334 – 3363Photolesion recognition

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi256 – 27419DWD boxAdd
    BLAST

    Domaini

    The DWD box is required for interaction with DDB1.1 Publication
    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.1 Publication

    Sequence similaritiesi

    Belongs to the WD repeat DDB2/WDR76 family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000231440.
    HOVERGENiHBG000713.
    InParanoidiQ92466.
    KOiK10140.
    OMAiFASSMEG.
    OrthoDBiEOG72G17F.
    PhylomeDBiQ92466.
    TreeFamiTF331587.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 3 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 5 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92466-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS    50
    DCLWVGLAGP QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS 100
    YRILQKAAPF DRRATSLAWH PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI 150
    KGIGAGGSIT GLKFNPLNTN QFYASSMEGT TRLQDFKGNI LRVFASSDTI 200
    NIWFCSLDVS ASSRMVVTGD NVGNVILLNM DGKELWNLRM HKKKVTHVAL 250
    NPCCDWFLAT ASVDQTVKIW DLRQVRGKAS FLYSLPHRHP VNAACFSPDG 300
    ARLLTTDQKS EIRVYSASQW DCPLGLIPHP HRHFQHLTPI KAAWHPRYNL 350
    IVVGRYPDPN FKSCTPYELR TIDVFDGNSG KMMCQLYDPE SSGISSLNEF 400
    NPMGDTLASA MGYHILIWSQ EEARTRK 427
    Length:427
    Mass (Da):47,864
    Last modified:February 1, 1997 - v1
    Checksum:iE881F21242CA44D2
    GO
    Isoform D1 (identifier: Q92466-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-341: Missing.

    Show »
    Length:238
    Mass (Da):26,744
    Checksum:iF40BD646C1C26FDA
    GO
    Isoform D2 (identifier: Q92466-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-156: IGAG → HLVL
         157-427: Missing.

    Show »
    Length:156
    Mass (Da):17,434
    Checksum:iFBC8A060B4DC7A4D
    GO
    Isoform D3 (identifier: Q92466-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         89-152: Missing.

    Show »
    Length:363
    Mass (Da):40,772
    Checksum:i2A90D5BD9E322889
    GO
    Isoform D4 (identifier: Q92466-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         236-244: WNLRMHKKK → VSVPMEPGS
         245-427: Missing.

    Show »
    Length:244
    Mass (Da):26,758
    Checksum:i367D99AA1DD984F9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti215 – 2151M → T.1 Publication
    Corresponds to variant rs4647750 [ dbSNP | Ensembl ].
    VAR_016337
    Natural varianti244 – 2441K → E in XP-E; impairs DNA-binding of the UV-DDB complex. 1 Publication
    VAR_010141
    Natural varianti273 – 2731R → H in XP-E; impairs interaction with DDB1 and CUL4A. 1 Publication
    VAR_010142
    Natural varianti293 – 2931A → T.1 Publication
    Corresponds to variant rs4647751 [ dbSNP | Ensembl ].
    VAR_016338

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei89 – 15264Missing in isoform D3. 1 PublicationVSP_014674Add
    BLAST
    Alternative sequencei153 – 341189Missing in isoform D1. 1 PublicationVSP_014675Add
    BLAST
    Alternative sequencei153 – 1564IGAG → HLVL in isoform D2. 1 PublicationVSP_014676
    Alternative sequencei157 – 427271Missing in isoform D2. 1 PublicationVSP_014677Add
    BLAST
    Alternative sequencei236 – 2449WNLRMHKKK → VSVPMEPGS in isoform D4. 1 PublicationVSP_014678
    Alternative sequencei245 – 427183Missing in isoform D4. 1 PublicationVSP_014679Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    AK313262 mRNA. Translation: BAG36072.1.
    CH471064 Genomic DNA. Translation: EAW67952.1.
    BC000093 mRNA. Translation: AAH00093.1.
    CCDSiCCDS7927.1. [Q92466-1]
    PIRiI38909.
    RefSeqiNP_000098.1. NM_000107.2. [Q92466-1]
    XP_005252865.1. XM_005252808.2. [Q92466-2]
    XP_006718224.1. XM_006718161.1. [Q92466-1]
    UniGeneiHs.700338.

    Genome annotation databases

    EnsembliENST00000256996; ENSP00000256996; ENSG00000134574. [Q92466-1]
    ENST00000378600; ENSP00000367863; ENSG00000134574. [Q92466-2]
    ENST00000378601; ENSP00000367864; ENSG00000134574. [Q92466-5]
    ENST00000378603; ENSP00000367866; ENSG00000134574. [Q92466-4]
    GeneIDi1643.
    KEGGihsa:1643.
    UCSCiuc001neb.2. human. [Q92466-1]
    uc001nee.2. human. [Q92466-2]
    uc009yli.1. human. [Q92466-4]

    Polymorphism databases

    DMDMi12230033.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Allelic variations of the XP genes
    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    AK313262 mRNA. Translation: BAG36072.1 .
    CH471064 Genomic DNA. Translation: EAW67952.1 .
    BC000093 mRNA. Translation: AAH00093.1 .
    CCDSi CCDS7927.1. [Q92466-1 ]
    PIRi I38909.
    RefSeqi NP_000098.1. NM_000107.2. [Q92466-1 ]
    XP_005252865.1. XM_005252808.2. [Q92466-2 ]
    XP_006718224.1. XM_006718161.1. [Q92466-1 ]
    UniGenei Hs.700338.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EI4 X-ray 3.30 B/D/F 10-427 [» ]
    3I7L X-ray 2.80 B 68-81 [» ]
    4E54 X-ray 2.85 B 2-427 [» ]
    4E5Z X-ray 3.22 B 2-427 [» ]
    ProteinModelPortali Q92466.
    SMRi Q92466. Positions 20-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108010. 51 interactions.
    DIPi DIP-36670N.
    IntActi Q92466. 9 interactions.
    STRINGi 9606.ENSP00000256996.

    PTM databases

    PhosphoSitei Q92466.

    Polymorphism databases

    DMDMi 12230033.

    Proteomic databases

    MaxQBi Q92466.
    PaxDbi Q92466.
    PRIDEi Q92466.

    Protocols and materials databases

    DNASUi 1643.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256996 ; ENSP00000256996 ; ENSG00000134574 . [Q92466-1 ]
    ENST00000378600 ; ENSP00000367863 ; ENSG00000134574 . [Q92466-2 ]
    ENST00000378601 ; ENSP00000367864 ; ENSG00000134574 . [Q92466-5 ]
    ENST00000378603 ; ENSP00000367866 ; ENSG00000134574 . [Q92466-4 ]
    GeneIDi 1643.
    KEGGi hsa:1643.
    UCSCi uc001neb.2. human. [Q92466-1 ]
    uc001nee.2. human. [Q92466-2 ]
    uc009yli.1. human. [Q92466-4 ]

    Organism-specific databases

    CTDi 1643.
    GeneCardsi GC11P047237.
    GeneReviewsi DDB2.
    HGNCi HGNC:2718. DDB2.
    HPAi CAB025912.
    MIMi 278740. phenotype.
    600811. gene.
    neXtProti NX_Q92466.
    Orphaneti 276261. Xeroderma pigmentosum complementation group E.
    PharmGKBi PA27188.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000231440.
    HOVERGENi HBG000713.
    InParanoidi Q92466.
    KOi K10140.
    OMAi FASSMEG.
    OrthoDBi EOG72G17F.
    PhylomeDBi Q92466.
    TreeFami TF331587.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    SignaLinki Q92466.

    Miscellaneous databases

    ChiTaRSi DDB2. human.
    EvolutionaryTracei Q92466.
    GeneWikii DDB2.
    GenomeRNAii 1643.
    NextBioi 6758.
    PROi Q92466.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q92466.
    CleanExi HS_DDB2.
    Genevestigatori Q92466.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 3 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 5 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (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] [Europe PMC] [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. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain.
    8. "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, CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273.
    9. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    10. "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] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, SUBCELLULAR LOCATION, INDUCTION, CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273.
    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. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    14. "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, UBIQUITINATION, CHARACTERIZATION OF VARIANT HIS-273.
    15. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION.
    16. "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, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB1 AND RBX1 AND THE COP9 SIGNALOSOME, DNA-BINDING.
    17. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    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; DDB1; RBX1 AND XPC, DNA-BINDING, UBIQUITINATION.
    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 DDB1, DNA-BINDING, CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273.
    20. "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; DDB1; RBX1 AND THE COP9 SIGNALOSOME, DNA-BINDING.
    21. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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: INTERACTION WITH CUL4A AND DDB1, DOMAIN DWD BOX MOTIF, MUTAGENESIS OF LEU-258; SER-262; ASP-264; ILE-269; TRP-270; LEU-272 AND ARG-273.
    23. "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 DDB1, UBIQUITINATION.
    24. "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 BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH DDB1; CUL4A; CUL4B AND RBX1, FUNCTION.
    25. "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] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION.
    26. "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: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDB1, MUTAGENESIS OF LEU-350, CHARACTERIZATION OF VARIANT HIS-273.
    27. "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: INTERACTION WITH DDB1, CHARACTERIZATION OF VARIANT HIS-273.
    28. "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: INTERACTION WITH CUL4A AND CUL4B.
    29. "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; DDB1; HISTONE H2A AND RBX1, DNA-BINDING, SUBCELLULAR LOCATION.
    30. "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] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    31. "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 DDB1, SUBCELLULAR LOCATION.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability."
      Zhang L., Lubin A., Chen H., Sun Z., Gong F.
      Cell Cycle 11:4378-4384(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION BY USP24.
    37. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 10-427 IN COMPLEX WITH DDB1 AND DNA, WD REPEATS.
    38. "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] [Europe PMC] [Abstract]
      Cited for: VARIANTS XP-E GLU-244 AND HIS-273.

    Entry informationi

    Entry nameiDDB2_HUMAN
    AccessioniPrimary (citable) accession number: Q92466
    Secondary accession number(s): B2R875
    , Q76E54, Q76E55, Q76E56, Q76E57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3