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IID00787
 UniprotP18887
ProteinDNA repair protein XRCC1
GeneXRCC1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
633
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-183 Monomer :
 Evidence X-RAY 3k77 A Reference
       Region 3k77 A 1-1 disorder
       Region 3k77 A 2-153 order
       Region 3k77 A 154-155 disorder
 Evidence X-RAY 3k77 B Reference
       Region 3k77 B 1-1 disorder
       Region 3k77 B 2-153 order
       Region 3k77 B 154-155 disorder
 Evidence X-RAY 3k77 C Reference
       Region 3k77 C 1-1 disorder
       Region 3k77 C 2-153 order
       Region 3k77 C 154-155 disorder
 Evidence X-RAY 3k77 D Reference
       Region 3k77 D 1-1 disorder
       Region 3k77 D 2-153 order
       Region 3k77 D 154-155 disorder
 Evidence X-RAY 3k77 E Reference
       Region 3k77 E 1-1 disorder
       Region 3k77 E 2-153 order
       Region 3k77 E 154-155 disorder
 Evidence X-RAY 3k77 F Reference
       Region 3k77 F 1-1 disorder
       Region 3k77 F 2-153 order
       Region 3k77 F 154-155 disorder
 Evidence X-RAY 3k77 G Reference
       Region 3k77 G 1-1 disorder
       Region 3k77 G 2-153 order
       Region 3k77 G 154-155 disorder
 Evidence X-RAY 3k77 H Reference
       Region 3k77 H 1-1 disorder
       Region 3k77 H 2-153 order
       Region 3k77 H 154-155 disorder
 Evidence NMR 1xna A Reference
       Region 1xna A 1-151 order
       Region 1xna A 152-183 disorder
 Evidence NMR 1xnt A Reference
       Region 1xnt A 1-151 order
       Region 1xnt A 152-183 disorder
Seq 1-183 Hetero dimer : P06766
 Evidence X-RAY 3k75 B Reference
       Region 3k75 B 1-1 disorder
       Region 3k75 B 2-29 order
       Region 3k75 B 30-30 disorder
       Region 3k75 B 31-153 order
       Region 3k75 B 154-183 disorder
 Evidence X-RAY 3k75 C Reference
       Region 3k75 C 1-1 disorder
       Region 3k75 C 2-28 order
       Region 3k75 C 29-30 disorder
       Region 3k75 C 31-152 order
       Region 3k75 C 153-183 disorder
 Evidence X-RAY 3lqc A Reference
       Region 3lqc A 1-1 disorder
       Region 3lqc A 2-152 order
       Region 3lqc A 153-183 disorder
Seq 241-276 Hetero dimer : IID50009Complex
 Evidence X-RAY 5e6q A Reference
       Region 5e6q A 241-243 disorder
       Region 5e6q A 244-248 order
       Region 5e6q A 249-267 disorder
       Region 5e6q A 268-276 order
Seq 305-420 Monomer :
 Evidence NMR 2d8m A Reference
       Region 2d8m A 305-420 order
       Region 2d8m A 305-310 high_rmsd
       Region 2d8m A 409-420 high_rmsd
Seq 514-522 Hetero dimer : IID00848Complex
 Evidence X-RAY 5w7x H Reference
       Region 5w7x H 514-520 order
       Region 5w7x H 521-522 disorder
 Evidence X-RAY 5w7x E Reference
       Region 5w7x E 514-521 order
       Region 5w7x E 522-522 disorder
 Evidence X-RAY 5w7x F Reference
       Region 5w7x F 514-520 order
       Region 5w7x F 521-522 disorder
 Evidence X-RAY 5w7x G Reference
       Region 5w7x G 514-521 order
       Region 5w7x G 522-522 disorder
 Evidence X-RAY 5w7y D Reference
       Region 5w7y D 514-521 order
 Evidence X-RAY 5w7y C Reference
       Region 5w7y C 514-521 order
Seq 515-522 Hetero dimer : Q96T60
 Evidence X-RAY 2w3o D Reference
       Region 2w3o D 515-522 order
 Evidence X-RAY 2w3o C Reference
       Region 2w3o C 515-522 order
Seq 538-633 Monomer :
 Evidence X-RAY 1cdz A Reference
       Region 1cdz A 538-633 order
Seq 538-633 Homo dimer :
 Evidence X-RAY 6wh2 B Reference
       Region 6wh2 B 538-633 order
 Evidence X-RAY 6wh2 A Reference
       Region 6wh2 A 538-632 order
       Region 6wh2 A 633-633 disorder
Seq 538-633 Hetero dimer : P49916
 Evidence X-RAY 6wh1 A Reference
       Region 6wh1 A 538-632 order
       Region 6wh1 A 633-633 disorder
SeqProS possible 244-248,268-276 Nuclear Localization Signal (NLS) Hetero dimer : IID50009Complex
       Region 5e6q A 244-248 order
       Region 5e6q A 268-276 order
SeqProS predicted 514-521 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00848Complex
       Region 5w7x E 514-521 order
       Region 5w7x F 514-520 order
       Region 5w7x G 514-521 order
       Region 5w7x H 514-520 order
       Region 5w7y C 514-521 order
       Region 5w7y D 514-521 order
SeqProS predicted 515-522 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : Q96T60
       Region 2w3o C 515-522 order
       Region 2w3o D 515-522 order
Seqphosphorylation
    523-523 Phosphothreonine
    518-518 Phosphoserine
    519-519 Phosphothreonine
    485-485 Phosphoserine
    488-488 Phosphothreonine
    461-461 Phosphoserine
    457-457 Phosphothreonine
    453-453 Phosphothreonine
    446-446 Phosphoserine
    447-447 Phosphoserine
    421-421 Phosphoserine
    410-410 Phosphoserine
    409-409 Phosphoserine
    371-371 Phosphoserine; by PRKDC
    408-408 Phosphoserine
    266-266 Phosphoserine
    281-281 Phosphothreonine
    259-259 Phosphoserine
    241-241 Phosphoserine
    257-257 Phosphothreonine
    204-204 Phosphoserine
    226-226 Phosphoserine
    202-202 Phosphothreonine
    199-199 Phosphoserine
    140-140 Phosphoserine
    198-198 Phosphothreonine
 
Prediction
NeProc
Disorder 154-316,410-532
Order 1-153,317-409,533-633
ProS 171-197,208-219,246-253,271-284,290-316,473-480,486-497,511-528
AlphaFold
Disorder 27-27,29-29,77-81,155-314,404-492,495-496,498-537,633-633
Order 1-26,28-28,30-76,82-154,315-403,493-494,497-497,538-632
Pfam Hmmer
PF01834 1-151 4.2e-135
PF00533 315-390 1.3e-16
PF00533 538-616 9.4e-11
SEG 210-231 ,270-291 ,297-315 ,425-443 ,530-543
Function
Function in SwissProt
Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes (PubMed:11163244, PubMed:28002403). Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity (PubMed:34102106, PubMed:34811483, PubMed:28002403). Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity (PubMed:14500814, PubMed:34102106, PubMed:34811483).