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Protein

DNA damage-binding protein 2

Gene

DDB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • damaged DNA binding Source: ProtInc
  • DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134574-MONOMER.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
SignaLinkiQ92466.
SIGNORiQ92466.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2718. DDB2.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum complementation group E (XP-E)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:278740
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010141244K → E in XP-E; impairs DNA-binding of the UV-DDB complex. 4 PublicationsCorresponds to variant rs121434639dbSNPEnsembl.1
Natural variantiVAR_010142273R → H in XP-E; impairs interaction with DDB1 and CUL4A. 7 PublicationsCorresponds to variant rs121434640dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi258L → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi262S → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi264D → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi269I → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi270W → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi272L → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi273R → A: Impairs interaction with DDB1. 1 Publication1
Mutagenesisi350L → P: Impairs interaction with DDB1. 1 Publication1

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

DisGeNETi1643.
MalaCardsiDDB2.
MIMi278740. phenotype.
OpenTargetsiENSG00000134574.
Orphaneti276261. Xeroderma pigmentosum complementation group E.
PharmGKBiPA27188.

Polymorphism and mutation databases

BioMutaiDDB2.
DMDMi12230033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000509531 – 427DNA damage-binding protein 2Add BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1

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

EPDiQ92466.
MaxQBiQ92466.
PaxDbiQ92466.
PeptideAtlasiQ92466.
PRIDEiQ92466.

PTM databases

iPTMnetiQ92466.
PhosphoSitePlusiQ92466.

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

BgeeiENSG00000134574.
CleanExiHS_DDB2.
ExpressionAtlasiQ92466. baseline and differential.
GenevisibleiQ92466. HS.

Organism-specific databases

HPAiCAB025912.
HPA058406.

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 DDB1.18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL4AQ136193EBI-1176171,EBI-456106
DDB1Q165313EBI-1176171,EBI-350322
E2F1Q010942EBI-1176171,EBI-448924

Protein-protein interaction databases

BioGridi108010. 81 interactors.
DIPiDIP-36670N.
IntActiQ92466. 25 interactors.
STRINGi9606.ENSP00000256996.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 25Combined sources5
Beta strandi30 – 32Combined sources3
Helixi39 – 42Combined sources4
Turni44 – 47Combined sources4
Beta strandi49 – 51Combined sources3
Helixi58 – 62Combined sources5
Turni63 – 65Combined sources3
Helixi69 – 77Combined sources9
Helixi83 – 91Combined sources9
Turni92 – 94Combined sources3
Turni96 – 102Combined sources7
Beta strandi106 – 109Combined sources4
Beta strandi114 – 119Combined sources6
Beta strandi127 – 131Combined sources5
Beta strandi136 – 139Combined sources4
Beta strandi148 – 150Combined sources3
Beta strandi154 – 156Combined sources3
Beta strandi161 – 164Combined sources4
Beta strandi171 – 175Combined sources5
Beta strandi177 – 179Combined sources3
Beta strandi181 – 185Combined sources5
Turni186 – 188Combined sources3
Beta strandi190 – 195Combined sources6
Beta strandi198 – 201Combined sources4
Beta strandi207 – 210Combined sources4
Turni211 – 214Combined sources4
Beta strandi215 – 219Combined sources5
Beta strandi221 – 232Combined sources12
Beta strandi241 – 243Combined sources3
Beta strandi245 – 250Combined sources6
Turni252 – 254Combined sources3
Beta strandi255 – 262Combined sources8
Turni263 – 265Combined sources3
Beta strandi269 – 271Combined sources3
Turni272 – 274Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi282 – 286Combined sources5
Beta strandi291 – 293Combined sources3
Beta strandi300 – 310Combined sources11
Beta strandi312 – 326Combined sources15
Beta strandi335 – 337Combined sources3
Beta strandi346 – 349Combined sources4
Beta strandi351 – 354Combined sources4
Beta strandi359 – 361Combined sources3
Beta strandi364 – 366Combined sources3
Beta strandi372 – 375Combined sources4
Beta strandi377 – 379Combined sources3
Beta strandi382 – 386Combined sources5
Turni389 – 391Combined sources3
Beta strandi397 – 400Combined sources4
Beta strandi407 – 410Combined sources4
Beta strandi412 – 417Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ92466.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati116 – 151WD 1PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati159 – 194WD 2PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati203 – 238WD 3PROSITE-ProRule annotation1 PublicationAdd BLAST36
Repeati244 – 287WD 4PROSITE-ProRule annotation1 PublicationAdd BLAST44
Repeati290 – 329WD 5PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati343 – 386WD 6PROSITE-ProRule annotation1 PublicationAdd BLAST44
Repeati396 – 420WD 7PROSITE-ProRule annotation1 PublicationAdd BLAST25

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 79Required for interaction with DDB1Add BLAST12
Regioni87 – 98Required for interaction with DDB1Add BLAST12
Regioni334 – 336Photolesion recognition3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi256 – 274DWD boxAdd BLAST19

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

eggNOGiENOG410IMQS. Eukaryota.
COG2319. LUCA.
GeneTreeiENSGT00510000047881.
HOGENOMiHOG000231440.
HOVERGENiHBG000713.
InParanoidiQ92466.
KOiK10140.
OMAiVTCLEWH.
OrthoDBiEOG091G06BL.
PhylomeDBiQ92466.
TreeFamiTF331587.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR033312. DDB2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR15169:SF0. PTHR15169:SF0. 1 hit.
PfamiPF00400. WD40. 1 hit.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_016337215M → T.1 PublicationCorresponds to variant rs4647750dbSNPEnsembl.1
Natural variantiVAR_010141244K → E in XP-E; impairs DNA-binding of the UV-DDB complex. 4 PublicationsCorresponds to variant rs121434639dbSNPEnsembl.1
Natural variantiVAR_010142273R → H in XP-E; impairs interaction with DDB1 and CUL4A. 7 PublicationsCorresponds to variant rs121434640dbSNPEnsembl.1
Natural variantiVAR_016338293A → T.1 PublicationCorresponds to variant rs4647751dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01467489 – 152Missing in isoform D3. 1 PublicationAdd BLAST64
Alternative sequenceiVSP_014675153 – 341Missing in isoform D1. 1 PublicationAdd BLAST189
Alternative sequenceiVSP_014676153 – 156IGAG → HLVL in isoform D2. 1 Publication4
Alternative sequenceiVSP_014677157 – 427Missing in isoform D2. 1 PublicationAdd BLAST271
Alternative sequenceiVSP_014678236 – 244WNLRMHKKK → VSVPMEPGS in isoform D4. 1 Publication9
Alternative sequenceiVSP_014679245 – 427Missing in isoform D4. 1 PublicationAdd BLAST183

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
NP_001287663.1. NM_001300734.1. [Q92466-2]
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.3. human. [Q92466-1]

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:
EMBLi
GenBanki
DDBJi
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]
NP_001287663.1. NM_001300734.1. [Q92466-2]
UniGeneiHs.700338.

3D structure databases

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

Protein-protein interaction databases

BioGridi108010. 81 interactors.
DIPiDIP-36670N.
IntActiQ92466. 25 interactors.
STRINGi9606.ENSP00000256996.

PTM databases

iPTMnetiQ92466.
PhosphoSitePlusiQ92466.

Polymorphism and mutation databases

BioMutaiDDB2.
DMDMi12230033.

Proteomic databases

EPDiQ92466.
MaxQBiQ92466.
PaxDbiQ92466.
PeptideAtlasiQ92466.
PRIDEiQ92466.

Protocols and materials databases

DNASUi1643.
Structural Biology KnowledgebaseSearch...

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.3. human. [Q92466-1]

Organism-specific databases

CTDi1643.
DisGeNETi1643.
GeneCardsiDDB2.
GeneReviewsiDDB2.
HGNCiHGNC:2718. DDB2.
HPAiCAB025912.
HPA058406.
MalaCardsiDDB2.
MIMi278740. phenotype.
600811. gene.
neXtProtiNX_Q92466.
OpenTargetsiENSG00000134574.
Orphaneti276261. Xeroderma pigmentosum complementation group E.
PharmGKBiPA27188.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IMQS. Eukaryota.
COG2319. LUCA.
GeneTreeiENSGT00510000047881.
HOGENOMiHOG000231440.
HOVERGENiHBG000713.
InParanoidiQ92466.
KOiK10140.
OMAiVTCLEWH.
OrthoDBiEOG091G06BL.
PhylomeDBiQ92466.
TreeFamiTF331587.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000134574-MONOMER.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
SignaLinkiQ92466.
SIGNORiQ92466.

Miscellaneous databases

ChiTaRSiDDB2. human.
EvolutionaryTraceiQ92466.
GeneWikiiDDB2.
GenomeRNAii1643.
PROiQ92466.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134574.
CleanExiHS_DDB2.
ExpressionAtlasiQ92466. baseline and differential.
GenevisibleiQ92466. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR033312. DDB2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR15169:SF0. PTHR15169:SF0. 1 hit.
PfamiPF00400. WD40. 1 hit.
[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]
ProtoNetiSearch...

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: November 2, 2016
This is version 172 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.