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Human DDB2 Protein expressed in Wheat germ - ABIN1351259
Robu, Shah, Petitclerc, BrindAmour, Kandan-Kulangara, Shah: Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair. in Proceedings of the National Academy of Sciences of the United States of America 2013
Results identified a missense mutation in damage-specific DNA binding protein 2 as a genetic risk factor for limbal squamous cell carcinoma in horses.
UVRAG (show UVRAG Proteins) is a regulator of CRL4(DDB2)-mediated nucleotide excision repair and its expression levels may influence melanoma predisposition.
Results indicate a transcriptional regulatory pathway of DDB2 that is directly linked to the mechanisms that suppress metastasis of colon cancer.
Data indicate that poly(ADP-ribose) polymerase-1 (PARP-1 (show PARP1 Proteins))collaborates with DNA-binding protein (show HSF4 Proteins) 2 (DDB2) to increase the efficiency of the lesion recognition step of global genomic subpathway of NER (show NR1H2 Proteins) (GG-NER (show NR1H2 Proteins)).
the anti-proliferative and the pro-senescence pathways of DDB2 and p21 are critical protection mechanisms against skin malignancies.
These results demonstrate direct activation of the human DDB2 gene by p53 (show TP53 Proteins). The corresponding region in the mouse DDB2 gene shared significant sequence identity with the human gene but was deficient for p53 (show TP53 Proteins) binding and transcriptional activation.
results demonstrate that DDB2 is well conserved between humans and mice and functions as a tumor suppressor, at least in part, by controlling p53 (show TP53 Proteins)-mediated apoptosis after UV-irradiation
DDB2-deficient mice developed spontaneous malignant tumors at a high rate between the ages of 20 and 25 months.
DDB2 is involved in global repair in mouse epithelial cells.
Ddb2 heterozygosity can facilitate tumor development as a haploinsufficient tumor suppressor
results indicate the bulk of DDB2 interacts with lesions independent of XPC (show XPC Proteins) & there is little interaction between the two recognition proteins on damaged DNA; propose a scenario in which DDB2 prepares UV-damaged chromatin for assembly of the NER (show NR1H2 Proteins) complex
DDB2 is modified by SUMOylation upon ultraviolet irradiation, and this post-translational modification plays an important role in the initial recognition and processing of ultraviolet irradiation-induced DNA damage occurring within the context of chromatin.
Results show that DDB2 is critical for chromatin association of XRCC5 (show XRCC5 Proteins)/6 in the absence of DNA damage and provide evidence that XRCC5 (show XRCC5 Proteins)/6 are functional partners of DDB2 in its transcriptional stimulatory activity.
High DDB2 expression is associated with increased radioresistance of non-small cell lung cancer.
data revealed that DDB2 is involved in early events occurring during metastatic progression of breast cancer cells and will contribute to define this protein as a new marker of metastatic progression in this type of cancer.
DDB2 polymorphisms are associated with gastric cancer and atrophic gastritis risks.
the release of NER (show NR1H2 Proteins) components such as DNA damage binding protein 2 (DDB2) and Xeroderma Pigmentosum complementation group C (show XPC Proteins) protein (XPC (show XPC Proteins)) following oxidative stress might putatively involve their apoptotic role rather than DNA repair function.
PKM2 interacts with DDB2 and reduces cell survival upon UV irradiation.
DDB2 can bind to the promoter region of NEDD4L (show NEDD4L Proteins) and recruit enhancer of zeste homolog 2 (show EZH2 Proteins) histone methyltransferase to repress NEDD4L (show NEDD4L Proteins) transcription by enhancing histone H3 (show HIST3H3 Proteins) lysine 27 trimethylation at the NEDD4L (show NEDD4L Proteins) promoter.
data demonstrated that the DDB2 IRES activity was promoted during stress conditions. These results reveal a novel mechanism contributing to DDB2 expression
This gene encodes a protein that is necessary for the repair of ultraviolet light-damaged DNA. This protein is the smaller subunit of a heterodimeric protein complex that participates in nucleotide excision repair, and this complex mediates the ubiquitylation of histones H3 and H4, which facilitates the cellular response to DNA damage. This subunit appears to be required for DNA binding. Mutations in this gene cause xeroderma pigmentosum complementation group E, a recessive disease that is characterized by an increased sensitivity to UV light and a high predisposition for skin cancer development, in some cases accompanied by neurological abnormalities.
damage-specific DNA binding protein 2 (48kD)
, damage-specific DNA binding protein 2, 48kDa
, DNA damage-binding protein 2
, Damage-specific DNA-binding protein 2
, DNA damage-binding protein 2-like
, damage-specific DNA-binding protein 2
, DDB p48 subunit
, UV-DDB 2
, UV-damaged DNA-binding protein 2
, xeroderma pigmentosum group E protein