This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'- 5' exonuclease and 3'-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Homotrimer. Forms a complex with activator 1 heteropentamer in the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, FEN1, CDC6 and POLDIP2. Interacts with APEX2; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA. Forms a ternary complex with DNTTIP2 and core histone. Interacts with KCTD10 and PPP1R15A. Interacts with POLD1, POLD3 and POLD4. Interacts with BAZ1B; the interaction is direct. Interacts with HLTF and SHPRH. Interacts with NUDT15. Interaction is disrupted in response to UV irradiation and acetylation. Interacts with p21Cip1/p21(CIP1) and CDT1; interacts via their PIP-box which also recruits the DCX(DTL) complex. Interacts with DDX11. Interacts with EGFR; positively regulates PCNA. Interacts with C12orf48/PARI. Interacts with SMARCAD1. Belongs to the PCNA family. Note: This description may include information from UniProtKB.
Protein type: DNA replication; Cell cycle regulation
Chromosomal Location of Human Ortholog: 20pter-p12
Cellular Component: nucleoplasm; centrosome; nuclear chromosome, telomeric region; PCNA complex; nuclear replication fork; DNA replication factor C complex; cytoplasm; nucleus
Molecular Function: identical protein binding; histone acetyltransferase binding; protein binding; DNA polymerase processivity factor activity; damaged DNA binding; estrogen receptor binding; MutLalpha complex binding; purine-specific mismatch base pair DNA N-glycosylase activity; chromatin binding; receptor tyrosine kinase binding; dinucleotide insertion or deletion binding
Biological Process: heart development; error-prone postreplication DNA repair; DNA strand elongation during DNA replication; response to lipid; epithelial cell differentiation; base-excision repair; transcription-coupled nucleotide-excision repair; telomere maintenance via recombination; telomere maintenance; positive regulation of DNA repair; mismatch repair; positive regulation of deoxyribonuclease activity; DNA damage response, detection of DNA damage; leading strand elongation; DNA repair; G1/S-specific transcription in mitotic cell cycle; telomere maintenance via semi-conservative replication; cell proliferation; bypass DNA synthesis; response to cadmium ion; nucleotide-excision repair; nucleotide-excision repair, DNA gap filling; mitotic cell cycle; positive regulation of DNA replication; G1/S transition of mitotic cell cycle
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.