Human DDB2 protein fragment (ab91908)
- Product nameHuman DDB2 protein fragmentSee all DDB2 proteins and peptides ...
- SourceE. coli
- Amino Acid Sequence
- SequenceMAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAK GSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGR ASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWH PTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSIT GLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTI NIWFCSLDVSASSRMVVTGDNVGNVILLNMDGKELWNLRM HKKKVTHVALNPCCDWFLATA
- Amino acids1 to 261
Our Abpromise guarantee covers the use of ab91908 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
- Additional NotesProtein Identity confirmed by Mass Spectrometry (MS/MS) (acquired on initial reference batch)
- Concentration information loading...
Preparation and Storage
- Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.5% Trehalose, 6M Urea, 100mM Sodium phosphate, 10mM Sodium chloride, pH 4.5
- ReconstitutionReconstitute with 59 µl aqua dest.
- damage-specific DNA binding protein 2
- Damage-specific DNA-binding protein 2
- DDB p48 subunit
- DNA damage-binding protein 2
- UV-damaged DNA-binding protein 2
- UV-DDB 2
- Xeroderma pigmentosum group E protei
- FunctionRequired 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.
- Tissue specificityUbiquitously 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.
- PathwayProtein modification; protein ubiquitination.
- Involvement in diseaseDefects in DDB2 are a cause of xeroderma pigmentosum complementation group E (XP-E) [MIM:278740]; also known as xeroderma pigmentosum V (XP5). XP-E is a rare human autosomal recessive disease characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities.
- Sequence similaritiesBelongs to the WD repeat DDB2/WDR76 family.
Contains 5 WD repeats.
- DomainThe DWD box is required for interaction with DDB1.
modificationsPhosphorylation by ABL1 negatively regulate UV-DDB activity.
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.
- Cellular localizationNucleus. Accumulates at sites of DNA damage following UV irradiation.
Human DDB2 protein fragment images
The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.
References for Human DDB2 protein fragment (ab91908)
ab91908 has not yet been referenced specifically in any publications.