lmmol · Proteins

DNA polymerase alpha catalytic subunit

UniProt P09884 Organism Homo sapiens Gene POLA, POLA1 EC 2.7.7.7

Also known as: POLA, POLA1

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.

Classification

Family (Pfam)
PF12254 DNA_pol_alpha_N, PF00136 DNA_pol_B, PF03104 DNA_pol_B_exo1, PF08996 zf-DNA_Pol
InterPro
DNA-dir_DNA_pol_B, DNA-dir_DNA_pol_B_CS, DNA-dir_DNA_pol_B_exonuc, DNA-dir_DNA_pol_B_multi_dom, DNA/RNA_pol_sf, DNA_pol_a_cat_su_N, DNA_pol_B_thumb, DNA_pol_palm_dom_sf, Pol_alpha_znc_sf, POLBc_alpha, RNaseH-like_sf, RNaseH_sf, Znf_DNA-dir_DNA_pol_B_alpha
Functional cluster
DEAD-Box RNA Helicases & Biogenesis Factors

Experimental structures · PDB · 21

A predicted model is available from AlphaFold.

Gene Ontology · 27

Disease associations

Drugs targeting this protein · 6

Related proteins · sequence + function similarity

Co-cited proteins · studied together in the literature

Literature · 20 cited papers

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