Names & Taxonomy

Uniprot ID:
P09884
Entry Name:
DPOLA_HUMAN
Status:
reviewed
Protein Names:
DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (DNA polymerase alpha catalytic subunit p180)
Gene Names:
POLA1 POLA
Gene Names Primary:
POLA1
Organism:
Homo sapiens (Human)

Structure

Length:
1462
Sequence:
MAPVHGDDSLSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDKRNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMILKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEEEQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSFLPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVFLFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEKIATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVMAFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKEVIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWSKIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTERVVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPELPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQKQDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDALLGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPLTFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQPEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQFLSRSGYSEVNLSKLFAGCAVKS
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Nucleus.

Function

Function:
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.
Catalytic Activity:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor:
COFACTOR: Name= cluster; Xref=ChEBI:CHEBI:49883;
Cross Reference Drug Bank:
DB00242 DB00631 DB01073 DB01280
Gene Ontology Go:
alpha DNA polymerase:primase complex
cytoplasm
nuclear envelope
nuclear matrix
nucleolus
nucleoplasm
nucleus
3'-5' exonuclease activity
4 iron, 4 sulfur cluster binding
chromatin binding
DNA binding
DNA-directed DNA polymerase activity
metal ion binding
nucleoside binding
nucleotide binding
protein kinase binding
cell proliferation
DNA biosynthetic process
DNA replication
DNA replication initiation
DNA replication, synthesis of RNA primer
DNA strand elongation involved in DNA replication
double-strand break repair via nonhomologous end joining
G1/S transition of mitotic cell cycle
lagging strand elongation
leading strand elongation
mitotic cell cycle
regulation of transcription involved in G1/S transition of mitotic cell cycle
telomere maintenance
telomere maintenance via recombination
telomere maintenance via semi-conservative replication
viral process
Gene Ontology Biological Process:
cell proliferation
DNA biosynthetic process
DNA replication
DNA replication, synthesis of RNA primer
DNA replication initiation
DNA strand elongation involved in DNA replication
double-strand break repair via nonhomologous end joining
G1/S transition of mitotic cell cycle
lagging strand elongation
leading strand elongation
mitotic cell cycle
regulation of transcription involved in G1/S transition of mitotic cell cycle
telomere maintenance
telomere maintenance via recombination
telomere maintenance via semi-conservative replication
viral process
Gene Ontology Molecular Function:
3'-5' exonuclease activity
4 iron, 4 sulfur cluster binding
chromatin binding
DNA binding
DNA-directed DNA polymerase activity
metal ion binding
nucleoside binding
nucleotide binding
protein kinase binding
Gene Ontology Cellular Component:
alpha DNA polymerase:primase complex
cytoplasm
nuclear envelope
nuclear matrix
nucleolus
nucleoplasm
nucleus
Keywords:
3D-structure
4Fe-4S
Acetylation
Complete proteome
DNA replication
DNA-binding
DNA-directed DNA polymerase
Direct protein sequencing
Host-virus interaction
Iron
Iron-sulfur
Metal-binding
Nucleotidyltransferase
Nucleus
Phosphoprotein
Polymorphism
Reference proteome
Transferase
Zinc
Zinc-finger
Interacts With:
P03070; P04014; P27694; P10193

Publication

PubMed ID:
3359994 2005899 2243771 3025630 7644508 9214288 9518481 18669648 19608746 19690332 20068231 21269460 21406692 14499601