Search Results
Overview
| Uniprot ID | P12004 |
|---|---|
| Protein Name | DNA sliding clamp PCNA |
| Gene Name | PCNA |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 13 | LVQGSILKKVLEALK |
| 138 | QEYSCVVKMPSGEFA |
| 14 | VQGSILKKVLEALKD |
| 164 | AVVISCAKDGVKFSA |
| 248 | IADMGHLKYYLAPKI |
| 80 | TSMSKILKCAGNEDI |
Function
Confers DNA tethering and processivity to DNA polymerases and other proteins (PubMed:24695737, PubMed:24939902, PubMed:35585232). Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of DNA replication by increasing the polymerases' processivity during elongation of the leading strand (PubMed:35585232). 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. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways (PubMed:24939902). Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (PubMed:24695737)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0032405 | MutLalpha complex binding |
| Molecular Function | GO:0030331 | nuclear estrogen receptor binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0000701 | purine-specific mismatch base pair DNA N-glycosylase activity |
| Molecular Function | GO:0030971 | receptor tyrosine kinase binding |
| Biological Process | GO:0070301 | cellular response to hydrogen peroxide |
| Biological Process | GO:0034644 | cellular response to UV |
| Biological Process | GO:0006325 | chromatin organization |
| Biological Process | GO:0140861 | DNA repair-dependent chromatin remodeling |
| Biological Process | GO:0030855 | epithelial cell differentiation |
| Biological Process | GO:0044849 | estrous cycle |
| Biological Process | GO:0007507 | heart development |
| Biological Process | GO:0006272 | leading strand elongation |
| Biological Process | GO:0097421 | liver regeneration |
| Biological Process | GO:0006298 | mismatch repair |
| Biological Process | GO:1902969 | mitotic DNA replication |
| Biological Process | GO:1902990 | mitotic telomere maintenance via semi-conservative replication |
| Biological Process | GO:0045739 | positive regulation of DNA repair |
| Biological Process | GO:0045740 | positive regulation of DNA replication |
| Biological Process | GO:0031297 | replication fork processing |
| Biological Process | GO:0046686 | response to cadmium ion |
| Biological Process | GO:0071548 | response to dexamethasone |
| Biological Process | GO:0032355 | response to estradiol |
| Biological Process | GO:1902065 | response to L-glutamate |
| Biological Process | GO:0019985 | translesion synthesis |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0000307 | cyclin-dependent protein kinase holoenzyme complex |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005652 | nuclear lamina |
| Cellular Component | GO:0043596 | nuclear replication fork |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0043626 | PCNA complex |
| Cellular Component | GO:0070557 | PCNA-p21 complex |
| Cellular Component | GO:0005657 | replication fork |
| Cellular Component | GO:0030894 | replisome |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003684 | damaged DNA binding |
| Molecular Function | GO:0032139 | dinucleotide insertion or deletion binding |
| Molecular Function | GO:0070182 | DNA polymerase binding |
| Molecular Function | GO:0030337 | DNA polymerase processivity factor activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0035035 | histone acetyltransferase binding |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.