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IID00798
UniprotP35251
ProteinReplication factor C subunit 1
GeneRFC1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1148
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 375-496 Monomer :
 Evidence NMR 2k7f A Reference
       Region 2k7f A 375-480 order
       Region 2k7f A 375-381 high_rmsd
 Evidence NMR 2ebu A Reference
       Region 2ebu A 392-496 order
       Region 2ebu A 392-393 high_rmsd
       Region 2ebu A 488-496 high_rmsd
 Evidence NMR 2k6g A Reference
       Region 2k6g A 375-480 order
       Region 2k6g A 375-396 high_rmsd
Seqphosphorylation
    73-73 Phosphoserine
    69-69 Phosphoserine
    71-71 Phosphoserine
    67-67 Phosphotyrosine
    108-108 Phosphoserine
    312-312 Phosphoserine
    1106-1106 Phosphoserine
    190-190 Phosphoserine
    253-253 Phosphoserine
    281-281 Phosphoserine
    283-283 Phosphoserine
    368-368 Phosphoserine
    537-537 Phosphoserine
    1104-1104 Phosphoserine
    164-164 Phosphoserine
    173-173 Phosphoserine
    163-163 Phosphothreonine
    161-161 Phosphothreonine
    156-156 Phosphoserine
    110-110 Phosphothreonine
 
Prediction
NeProc
Disorder 1-402,438-443,486-581,628-638,707-712,950-971,1067-1148
Order 403-437,444-485,582-627,639-706,713-949,972-1066
ProS 1-9,63-69,105-109,115-118,164-169,201-211,224-227,260-265,375-385,396-402,486-498,514-523,631-638,950-971,1067-1078,1115-1120
AlphaFold
Disorder 1-200,215-228,230-376,381-381,384-384,388-388,486-493,496-580,621-640,704-712,806-806,827-830,833-833,836-847,860-861,863-863,1074-1074,1076-1148
Order 201-214,229-229,377-380,382-383,385-387,389-485,494-495,581-620,641-703,713-805,807-826,831-832,834-835,848-859,862-862,864-1073,1075-1075
Pfam Hmmer
PF00533 402-479 8.9e-22
PF00004 646-824 4.6e-11
PF08519 915-1068 2.2e-97
SEG 142-153 ,286-303 ,346-366 ,514-534 ,1101-1112 ,1121-1140
Function
Function in SwissProt
The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.
Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.
Biological Process
See also
Diagram with PDB data
XPA/ERCC1Solution structure of a ERCC1-XPA heterodimer
MSH2/MSH6/DNAhuman MutSalpha (MSH2/MSH6) bound to ADP and a G T mispair
MSH2/MSH3/DNAHuman MutSbeta complexed with an IDL of 4 bases (Loop4) and ADP