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Q92466

- DDB2_HUMAN

UniProt

Q92466 - DDB2_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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. 62 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 54-421.
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.
GeneTreeiENSGT00510000047881.
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

        10         20         30         40         50
MAPKKRPETQ KTSEIVLRPR NKRSRSPLEL EPEAKKLCAK GSGPSRRCDS
60 70 80 90 100
DCLWVGLAGP QILPPCRSIV RTLHQHKLGR ASWPSVQQGL QQSFLHTLDS
110 120 130 140 150
YRILQKAAPF DRRATSLAWH PTHPSTVAVG SKGGDIMLWN FGIKDKPTFI
160 170 180 190 200
KGIGAGGSIT GLKFNPLNTN QFYASSMEGT TRLQDFKGNI LRVFASSDTI
210 220 230 240 250
NIWFCSLDVS ASSRMVVTGD NVGNVILLNM DGKELWNLRM HKKKVTHVAL
260 270 280 290 300
NPCCDWFLAT ASVDQTVKIW DLRQVRGKAS FLYSLPHRHP VNAACFSPDG
310 320 330 340 350
ARLLTTDQKS EIRVYSASQW DCPLGLIPHP HRHFQHLTPI KAAWHPRYNL
360 370 380 390 400
IVVGRYPDPN FKSCTPYELR TIDVFDGNSG KMMCQLYDPE SSGISSLNEF
410 420
NPMGDTLASA MGYHILIWSQ EEARTRK
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.
CCDSiCCDS73284.1. [Q92466-2]
CCDS7927.1. [Q92466-1]
PIRiI38909.
RefSeqiNP_000098.1. NM_000107.2. [Q92466-1]
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]
ENST00000616278; ENSP00000478411; ENSG00000134574. [Q92466-3]
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 CCDS73284.1. [Q92466-2 ]
CCDS7927.1. [Q92466-1 ]
PIRi I38909.
RefSeqi NP_000098.1. NM_000107.2. [Q92466-1 ]
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 54-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108010. 62 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 ]
ENST00000616278 ; ENSP00000478411 ; ENSG00000134574 . [Q92466-3 ]
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.
GeneTreei ENSGT00510000047881.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 151 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

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