NP_035261.3
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
123,790 Da
NCBI Official Full Name
DNA polymerase delta catalytic subunit
NCBI Official Synonym Full Names
polymerase (DNA directed), delta 1, catalytic subunit
NCBI Official Synonym Symbols
NCBI Protein Information
DNA polymerase delta catalytic subunit
UniProt Protein Name
DNA polymerase delta catalytic subunit
UniProt Entry Name
DPOD1_MOUSE
UniProt Comments for POLD1
POLD1: Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex. Belongs to the DNA polymerase type-B family.
Protein type: EC 2.7.7.7; Nucleotide Metabolism - purine; DNA repair, damage; Nucleotide Metabolism - pyrimidine; Transferase; DNA replication; Hydrolase
Cellular Component: delta DNA polymerase complex; nucleoplasm; nucleotide-excision repair complex; membrane; cytoplasm; nucleus
Molecular Function: nuclease activity; hydrolase activity; metal ion binding; iron-sulfur cluster binding; 3'-5'-exodeoxyribonuclease activity; DNA-directed DNA polymerase activity; nucleotide binding; nucleotidyltransferase activity; transferase activity; nucleic acid binding; DNA binding; 4 iron, 4 sulfur cluster binding; exonuclease activity; chromatin binding; 3'-5' exonuclease activity
Biological Process: base-excision repair, gap-filling; DNA synthesis during DNA repair; DNA replication proofreading; fatty acid homeostasis; nucleotide-excision repair, DNA gap filling; DNA replication; DNA-dependent DNA replication
Research Articles on POLD1
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Products associated with POLD1 sirna
Pathways associated with POLD1 sirna
Diseases associated with POLD1 sirna
Organs/Tissues associated with POLD1 sirna
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