Search Results
Overview
| Uniprot ID | P09884 |
|---|---|
| Protein Name | DNA polymerase alpha catalytic subunit |
| Gene Name | POLA1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 125 | KDKRNVKKLAVTKPN |
| 130 | VKKLAVTKPNNIKSM |
| 149 | AGKKTADKAVDLSKD |
| 206 | ATAVPSGKIASPVSR |
| 214 | IASPVSRKEPPLTPV |
| 224 | PLTPVPLKRAEFAGD |
Function
Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a regulatory subunit POLA2 and two primase subunits PRIM1 and PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses (PubMed:27019227)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005658 | alpha DNA polymerase:primase complex |
| Molecular Function | GO:0003688 | DNA replication origin binding |
| Molecular Function | GO:0003887 | DNA-directed DNA polymerase activity |
| Molecular Function | GO:0000166 | nucleotide binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0003697 | single-stranded DNA binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0006270 | DNA replication initiation |
| Biological Process | GO:0006269 | DNA replication, synthesis of primer |
| Biological Process | GO:0006271 | DNA strand elongation involved in DNA replication |
| Biological Process | GO:0000731 | DNA synthesis involved in DNA repair |
| Biological Process | GO:0006303 | double-strand break repair via nonhomologous end joining |
| Biological Process | GO:0006273 | lagging strand elongation |
| Biological Process | GO:0006272 | leading strand elongation |
| Biological Process | GO:1902975 | mitotic DNA replication initiation |
| Biological Process | GO:0032479 | regulation of type I interferon production |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003677 | DNA binding |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[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.