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IID00164
 UniprotQ01831
ProteinDNA repair protein complementing XP-C cells
GeneXPC
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
940
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 109-156 Hetero dimer : IID00549Complex
 Evidence NMR 2rvb A Reference
       Region 2rvb A 109-123 disorder
       Region 2rvb A 109-125 high_rmsd
       Region 2rvb A 124-141 order
       Region 2rvb A 142-156 disorder
       Region 2rvb A 143-156 high_rmsd
Seqdisorder 109-156
 Evidence NMR Reference
       Region 109-156 disorder
Seq 847-863 Hetero dimer : IID00551Complex
 Evidence X-RAY 2ggm C Reference
       Region 2ggm C 847-863 order
 Evidence X-RAY 2ggm D Reference
       Region 2ggm D 847-863 order
Seq 847-863 Hetero tetramer : IID00551Complex
 Evidence X-RAY 2obh D Reference
       Region 2obh D 847-863 order
 Evidence X-RAY 2obh C Reference
       Region 2obh C 847-862 order
       Region 2obh C 863-863 disorder
Seqdisorder 847-863
 Evidence CD Reference
       Region 847-863 disorder
Seq 847-863 Hetero dimer : IID00551Complex
 Evidence NMR 2a4j B Reference
       Region 2a4j B 847-863 order
       Region 2a4j B 861-863 high_rmsd
SeqProS verified 124-141 Hetero dimer : IID00549Complex
       Region 2rvb A 124-141 order
       Region 109-156 disorder
SeqProS verified 847-863 Hetero tetramer : IID00551Complex
       Region 2obh C 847-862 order
       Region 2obh D 847-863 order
       Region 847-863 disorder
SeqProS verified 847-863 Hetero dimer : IID00551Complex
       Region 2a4j B 847-863 order
       Region 847-863 disorder
SeqProS verified 847-863 Hetero dimer : IID00551Complex
       Region 2ggm C 847-863 order
       Region 2ggm D 847-863 order
       Region 847-863 disorder
Seqphosphorylation
    129-129 Phosphoserine
    140-140 Phosphoserine
    169-169 Phosphothreonine
    397-397 Phosphoserine
    398-398 Phosphoserine
    399-399 Phosphoserine
    453-453 Phosphoserine
    460-460 Phosphoserine
    876-876 Phosphothreonine
    883-883 Phosphoserine
    884-884 Phosphoserine
    891-891 Phosphoserine
    903-903 Phosphoserine
    94-94 Phosphoserine
 
Prediction
NeProc
Disorder 1-12,41-186,329-521,711-726,865-940
Order 13-40,187-328,522-710,727-864
ProS 59-62,97-102,116-121,133-139,158-170,183-186,329-369,381-406,420-430,443-447,475-478,515-521,711-717,865-868,875-882,900-910,928-940
AlphaFold
Disorder 1-165,274-276,326-525,725-725,866-894,900-922,935-935,940-940
Order 166-273,277-325,526-724,726-865,895-899,923-934,936-939
Pfam Hmmer
PF03835 488-866 1.1e-268
SEG 20-50 ,71-81 ,119-141 ,303-319 ,380-399 ,432-446 ,448-465 ,501-507 ,833-843 ,911-931
Function
Function in SwissProt
In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT) (PubMed:29973595, PubMed:31527837). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes (PubMed:31527837).
Biological Process
Diagram with PDB data
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
XPC/GTF2H1Solution structure of the complex between XPC acidic domain and TFIIH p62 PH domain
See also
Diagram with PDB data
XPA/ERCC1Solution structure of a ERCC1-XPA heterodimer