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POLA1
Anti-POLA1 Recombinant Antibody Products
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For Research Use Only. Not For Clinical Use.
Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) 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.
Protein class
Disease related genes, Enzymes, FDA approved drug targets, Human disease related genes, Metabolic proteins
Predicted location
Intracellular
Single cell type specificity
Cell type enhanced (Oligodendrocytes, Inhibitory neurons, Oligodendrocyte precursor cells, Microglial cells, Excitatory neurons, Astrocytes)
Immune cell specificity
Low immune cell specificity
Cell line specificity
Low cell line specificity
Interaction
Component of the alpha DNA polymerase complex (also known as the alpha DNA polymerase-primase complex) consisting of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the primase complex subunits PRIM1 and PRIM2 respectively (PubMed:9705292, 26975377). Interacts with PARP1; this interaction functions as part of the control of replication fork progression (PubMed:9518481). Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA (PubMed:19608746). Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp (PubMed:9214288). (Microbial infection) Interacts with SV40 Large T antigen; this interaction allows viral DNA replication. (Microbial infection) Interacts with herpes simplex virus 1/HHV-1 replication origin-binding protein UL9.
Molecular function
DNA-binding, DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase
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