Search Keyword:


Search option:


IID00854
 UniprotQ92466
ProteinDNA damage-binding protein 2
GeneDDB2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
427
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 2-427 Hetero dimer : IID00840Complex
 Evidence X-RAY 3ei4 B Reference
       Region 3ei4 B 10-53 disorder
       Region 3ei4 B 54-421 order
       Region 3ei4 B 422-427 disorder
 Evidence X-RAY 3ei4 D Reference
       Region 3ei4 D 10-53 disorder
       Region 3ei4 D 54-421 order
       Region 3ei4 D 422-427 disorder
 Evidence X-RAY 3ei4 F Reference
       Region 3ei4 F 10-53 disorder
       Region 3ei4 F 54-421 order
       Region 3ei4 F 422-427 disorder
 Evidence X-RAY 4e54 B Reference
       Region 4e54 B 2-19 disorder
       Region 4e54 B 20-421 order
       Region 4e54 B 422-427 disorder
 Evidence X-RAY 4e5z B Reference
       Region 4e5z B 2-19 disorder
       Region 4e5z B 20-420 order
       Region 4e5z B 421-427 disorder
Seq 68-81 Hetero dimer : IID00840Complex
 Evidence X-RAY 3i7l B Reference
       Region 3i7l B 68-81 order
SeqProS verified 20-53 Hetero dimer : IID00840Complex
       Region 4e54 B 20-421 order
       Region 4e5z B 20-420 order
       Region 3ei4 B 10-53 disorder
Seqphosphorylation
    24-24 Phosphoserine
    26-26 Phosphoserine
Seqacetylation
    35-35 N6-acetyllysine
    77-77 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-60
Order 61-427
ProS 17-60
AlphaFold
Disorder 1-67,364-364,422-427
Order 68-363,365-421
Pfam Hmmer
PF00400 232-271 5.6e-07
Function
Function in SwissProt
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, PubMed:32789493). 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, PubMed:32789493). 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).
Inhibits UV-damaged DNA repair.
Inhibits UV-damaged DNA repair.
Biological Process
See also
Diagram with PDB data
XPA/ERCC1Solution structure of a ERCC1-XPA heterodimer
XPC/CETN2Solution structure of the C-terminal domain (T94-Y172) of the human centrin 2 in complex with a 17 residues peptide (P1-XPC) from xeroderma pigmentosum group C protein