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Rabbit Anti-DDB2 Recombinant Antibody (11C1023) (CBMAB-D0467-YC)


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Summary

Host Animal
Rabbit
Specificity
Human
Clone
11C1023
Antibody Isotype
IgG
Application
WB

Basic Information

Immunogen
Synthetic peptide corresponding to AAs surrounding Ala174 of human DDB2.
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Damage Specific DNA Binding Protein 2
Introduction
DDB2 is 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. Two transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
1643
UniProt ID
Q92466
Alternative Names
Damage Specific DNA Binding Protein 2; UV-Damaged DNA-Binding Protein 2; DDB P48 Subunit; Xeroderma Pigmentosum Group E Protein; UV-DDB 2; DDBB; Damage-Specific DNA Binding Protein 2 (48kD);
Function
Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:9892649, PubMed:12732143, PubMed:15882621, PubMed:16473935, PubMed:18593899).

Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:16260596, PubMed:12944386, PubMed:14751237).

The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:10882109, PubMed:11278856, PubMed:11705987, PubMed:16260596, PubMed:12944386).

Also functions as the substrate recognition module for the DCX (DDB2-CUL4-X-box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and CUL4-DDB-RBX1) (PubMed:12732143, PubMed:15882621, PubMed:16473935, PubMed:18593899, PubMed:26572825).

The DDB2-CUL4-ROC1 complex may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16678110, PubMed:16473935).

The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16678110, PubMed:16473935).

The DDB2-CUL4-ROC1 complex also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621).

The DDB2-CUL4-ROC1 complex also ubiquitinates KAT7/HBO1 in response to DNA damage, leading to its degradation: recognizes KAT7/HBO1 following phosphorylation by ATR (PubMed:26572825).

Isoform D1:
Inhibits UV-damaged DNA repair.

Isoform D2:
Inhibits UV-damaged DNA repair.
Biological Process
DNA repair Source: GO_Central
Global genome nucleotide-excision repair Source: Reactome
Histone H2A monoubiquitination Source: UniProtKB
Nucleotide-excision repair Source: ProtInc
Nucleotide-excision repair, DNA damage recognition Source: Reactome
Nucleotide-excision repair, DNA duplex unwinding Source: Reactome
Nucleotide-excision repair, DNA incision Source: Reactome
Nucleotide-excision repair, DNA incision, 3'-to lesion Source: Reactome
Nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
Nucleotide-excision repair, preincision complex assembly Source: Reactome
Nucleotide-excision repair, preincision complex stabilization Source: Reactome
Post-translational protein modification Source: Reactome
Protein autoubiquitination Source: UniProtKB
Protein deubiquitination Source: Reactome
Protein polyubiquitination Source: UniProtKB
Pyrimidine dimer repair Source: Ensembl
Response to UV Source: UniProtKB
UV-damage excision repair Source: UniProtKB
Cellular Location
Nucleus. Accumulates at sites of DNA damage following UV irradiation.
Involvement in disease
Xeroderma pigmentosum complementation group E (XP-E):
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.
PTM
Phosphorylation 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.
Ubiquitinated, leading to proteasomal degradation, and deubiquitinated by USP24.
More Infomation

Knickelbein, K. E., Lassaline, M. E., Singer‐Berk, M., Reilly, C. M., Clode, A. B., Famula, T. R., ... & Bellone, R. R. (2020). A missense mutation in damage‐specific DNA binding protein 2 is a genetic risk factor for ocular squamous cell carcinoma in Belgian horses. Equine veterinary journal, 52(1), 34-40.

Zhou, Q., Yao, X., Wu, C., Chen, S., & Fan, D. (2020). Knockdown of ubiquitin-specific protease 53 enhances the radiosensitivity of human cervical squamous cell carcinoma by regulating DNA damage-binding protein 2. Technology in Cancer Research & Treatment, 19, 1533033820929792.

Gilson, P., Drouot, G., Witz, A., Merlin, J. L., Becuwe, P., & Harlé, A. (2019). Emerging roles of DDB2 in cancer. International Journal of Molecular Sciences, 20(20), 5168.

Singer-Berk, M. H., Knickelbein, K. E., Lounsberry, Z. T., Crausaz, M., Vig, S., Joshi, N., ... & Bellone, R. R. (2019). Additional evidence for DDB2 T338M as a genetic risk factor for ocular squamous cell carcinoma in horses. International journal of genomics, 2019.

Perucca, P., Mocchi, R., Guardamagna, I., Bassi, E., Sommatis, S., Nardo, T., ... & Cazzalini, O. (2018). A damaged DNA binding protein 2 mutation disrupting interaction with proliferating-cell nuclear antigen affects DNA repair and confers proliferation advantage. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1865(6), 898-907.

Yang, H., Liu, J., Jing, J., Wang, Z., Li, Y., Gou, K., ... & Xing, C. (2018). Expression of DDB2 Protein in the Initiation, Progression, and Prognosis of Colorectal Cancer. Digestive Diseases and Sciences, 63(11), 2959-2968.

Córdoba‐Cañero, D., Cognat, V., Ariza, R. R., Roldan Arjona, T., & Molinier, J. (2017). Dual control of ROS1‐mediated active DNA demethylation by DNA damage‐binding protein 2 (DDB2). The Plant Journal, 92(6), 1170-1181.

Bellone, R. R., Liu, J., Petersen, J. L., Mack, M., Singer‐Berk, M., Drögemüller, C., ... & Lassaline, M. (2017). A missense mutation in damage‐specific DNA binding protein 2 is a genetic risk factor for limbal squamous cell carcinoma in horses. International journal of cancer, 141(2), 342-353.

Schalk, C., Cognat, V., Graindorge, S., Vincent, T., Voinnet, O., & Molinier, J. (2017). Small RNA-mediated repair of UV-induced DNA lesions by the DNA DAMAGE-BINDING PROTEIN 2 and ARGONAUTE 1. Proceedings of the National Academy of Sciences, 114(14), E2965-E2974.

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For research use only. Not intended for any clinical use.

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