Mouse Anti-DDB1 Recombinant Antibody (2D6-B5-E6) (CBMAB-D0454-YC)

Mouse

Human, Mouse, Rat, Monkey

2D6-B5-E6

IgG2b

WB

Human, Mouse, Rat, Monkey

IgG2b

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Damage Specific DNA Binding Protein 1

DDB1 is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex while another protein (p48) forms the small subunit. This protein complex functions in nucleotide-excision repair and binds to DNA following UV damage. Defective activity of this complex causes the repair defect in patients with xeroderma pigmentosum complementation group E (XPE)-an autosomal recessive disorder characterized by photosensitivity and early onset of carcinomas.

Damage Specific DNA Binding Protein 1; Xeroderma Pigmentosum Group E-Complementing Protein; UV-Damaged DNA-Binding Protein 1; UV-Damaged DNA-Binding Factor; DNA Damage-Binding Protein A; HBV X-Associated Protein 1; XPE-Binding Factor; DDB P127 Subunit; UV-DDB 1; XPE-BF; XAP-1;

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:15448697, PubMed:14739464, PubMed:16260596, PubMed:16482215, PubMed:17079684, PubMed:16407242, PubMed:16407252, PubMed:16940174).

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:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174).

The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174).

Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:28886238).

The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:25043012, PubMed:25108355, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460).

DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899).

The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16678110, PubMed:17041588, PubMed:16473935, PubMed:18593899).

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

DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication (PubMed:17041588).

DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143).

The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207).

DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity).

Biological process involved in interaction with symbiont Source: AgBase
Cellular response to DNA damage stimulus Source: UniProtKB
DNA damage response, detection of DNA damage Source: Reactome
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
Positive regulation by virus of viral protein levels in host cell Source: AgBase
Positive regulation of gluconeogenesis Source: UniProtKB
Positive regulation of protein catabolic process Source: UniProtKB
Positive regulation of viral genome replication Source: AgBase
Positive regulation of viral release from host cell Source: AgBase
Post-translational protein modification Source: Reactome
Proteasomal protein catabolic process Source: MGI
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Regulation of mitotic cell cycle phase transition Source: UniProtKB
Rhythmic process Source: UniProtKB-KW
Transcription-coupled nucleotide-excision repair Source: Reactome
Ubiquitin-dependent protein catabolic process Source: UniProtKB
UV-damage excision repair Source: UniProtKB
Viral process Source: UniProtKB-KW

Cytoplasm; Nucleus. Primarily cytoplasmic (PubMed:10777491, PubMed:11673459). Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage (PubMed:10777491, PubMed:11673459).

Phosphorylated by ABL1.
Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis.
Acetylated, promoting interaction with CUL4 (CUL4A or CUL4B) and subsequent formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238). Deacetylation by SIRT7 impairs the interaction with CUL4 (CUL4A or CUL4B) and formation of DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes (PubMed:28886238).