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UniProtKB - P28340 (DPOD1_HUMAN)

Entry version 206 (12 Aug 2020)
Sequence version 2 (19 Jul 2004)
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Protein

DNA polymerase delta catalytic subunit

Gene

POLD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities (PubMed:16510448, PubMed:19074196, PubMed:20334433, PubMed:24035200, PubMed:24022480). Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4 (PubMed:19074196, PubMed:20334433). Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated (PubMed:24035200). Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation (PubMed:20227374). Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR) (PubMed:24310611). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites (PubMed:19074196, PubMed:24191025).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by alteration of quaternary structure. Exhibits burst rates of DNA synthesis are about 5 times faster in the presence of POLD4 (Pol-delta4 complex) than in its absence (Pol-delta3 complex), while the affinity of the enzyme for its DNA and dNTP substrates appears unchanged. The Pol-delta3 complex is more likely to proofread DNA synthesis because it cleaves single-stranded DNA twice as fast and transfers mismatched DNA from the polymerase to the exonuclease sites 9 times faster compared to the Pol-delta3 complex. Pol-delta3 also extends mismatched primers 3 times more slowly in the absence of POLD4. The conversion of Pol-delta4 into Pol-delta3 is induced by genotoxic stress or by replication stress leading POLD4 degradation (PubMed:19074196, PubMed:20334433). Stimulated in the presence of PCNA (PubMed:11328591, PubMed:12403614, PubMed:12522211, PubMed:16510448, PubMed:24022480, PubMed:24939902). This stimulation is further increased in the presence of KCTD13/PDIP1, most probably via direct interaction between KCTD13 and POLD2 (By similarity).By similarity8 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 87 sec(-1) for DNA synthesis by Pol-delta4 and 19 sec(-1) for Pol-delta3. kcat for exonuclease activity determined using a 26mer/40mer duplex DNA gives a value of 0.003 sec(-1) for Pol-delta4 and 0.026 sec(-1) for Pol-delta3. When using a 26mer/40mer with a T:G mismatch at the primer terminus, the switching rates from the polymerase to the exonuclease site for Pol-delta4 and Pol-delta3 are increased 20- and 10-fold, respectively, but the rate constant for Pol-delta3 is still 5-fold faster than that for Pol-delta4.

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1012ZincBy similarity1
      Metal bindingi1015ZincBy similarity1
      Metal bindingi1026ZincBy similarity1
      Metal bindingi1029ZincBy similarity1
      Metal bindingi1058Iron-sulfur (4Fe-4S)By similarity1
      Metal bindingi1061Iron-sulfur (4Fe-4S)By similarity1
      Metal bindingi1071Iron-sulfur (4Fe-4S)By similarity1
      Metal bindingi1076Iron-sulfur (4Fe-4S)By similarity1

      Regions

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1012 – 1029CysA-typeAdd BLAST18

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      Complete GO annotation on QuickGO ...

      GO - Biological processi

      Complete GO annotation on QuickGO ...

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionDNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase
      Biological processDNA damage, DNA excision, DNA repair, DNA replication
      Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

      Enzyme and pathway databases

      BRENDA Comprehensive Enzyme Information System

      More...      BRENDAi      		2.7.7.7, 2681

      Pathway Commons web resource for biological pathway data

      More...      PathwayCommonsi      		P28340

      Reactome - a knowledgebase of biological pathways and processes

      More...      Reactomei      		R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex
      R-HSA-174411, Polymerase switching on the C-strand of the telomere
      R-HSA-174414, Processive synthesis on the C-strand of the telomere
      R-HSA-174417, Telomere C-strand (Lagging Strand) Synthesis
      R-HSA-174437, Removal of the Flap Intermediate from the C-strand
      R-HSA-2564830, Cytosolic iron-sulfur cluster assembly
      R-HSA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
      R-HSA-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
      R-HSA-5651801, PCNA-Dependent Long Patch Base Excision Repair
      R-HSA-5656169, Termination of translesion DNA synthesis
      R-HSA-5685942, HDR through Homologous Recombination (HRR)
      R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
      R-HSA-5696400, Dual Incision in GG-NER
      R-HSA-6782135, Dual incision in TC-NER
      R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
      R-HSA-69091, Polymerase switching
      R-HSA-69166, Removal of the Flap Intermediate
      R-HSA-69183, Processive synthesis on the lagging strand

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
      Recommended name:
      DNA polymerase delta catalytic subunitCurated (EC:2.7.7.72 Publications)
      Alternative name(s):
      3'-5' exodeoxyribonucleaseCurated (EC:3.1.11.-3 Publications)
      DNA polymerase subunit delta p125
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:POLD1Imported
      Synonyms:POLD
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

      Organism-specific databases

      Eukaryotic Pathogen Database Resources

      More...      EuPathDBi      		HostDB:ENSG00000062822.12

      Human Gene Nomenclature Database

      More...      HGNCi      		HGNC:9175, POLD1

      Online Mendelian Inheritance in Man (OMIM)

      More...      MIMi      		174761, gene

      neXtProt; the human protein knowledge platform

      More...      neXtProti      		NX_P28340

      <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

      Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

      Keywords - Cellular componenti

      Nucleus

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      <p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

      Colorectal cancer 10 (CRCS10)2 Publications
      Disease susceptibility is associated with variations affecting the gene represented in this entry.
      Disease descriptionA complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
      Related information in OMIM
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071966474L → P in CRCS10. 1 PublicationCorresponds to variant dbSNP:rs587777627EnsemblClinVar.1
      Natural variantiVAR_069335478S → N in CRCS10; associated with disease susceptibility. 1 PublicationCorresponds to variant dbSNP:rs397514632EnsemblClinVar.1
      Mandibular hypoplasia, deafness, progeroid features, and lipodystrophy syndrome (MDPL)1 Publication
      The disease is caused by mutations affecting the gene represented in this entry.
      Disease descriptionAn autosomal dominant systemic disorder characterized by prominent loss of subcutaneous fat, metabolic abnormalities including insulin resistance and diabetes mellitus, sclerodermatous skin, and a facial appearance characterized by mandibular hypoplasia. Sensorineural deafness occurs late in the first or second decades of life.
      Related information in OMIM
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_070231605Missing in MDPL; the mutant enzyme lacks DNA polymerase ability; has decreased exonuclease activity; can bind DNA but is unable to interact with and incorporate dNTPs. 1 Publication1

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi402D → A: Loss of exonuclease activity. No effect on DNA polymerase activity. 2 Publications1

      Keywords - Diseasei

      Disease mutation

      Organism-specific databases

      DisGeNET

      More...      DisGeNETi      		5424

      MalaCards human disease database

      More...      MalaCardsi      		POLD1
      MIMi612591, phenotype
      615381, phenotype

      Open Targets

      More...      OpenTargetsi      		ENSG00000062822

      Orphanet; a database dedicated to information on rare diseases and orphan drugs

      More...      Orphaneti      		363649, Mandibular hypoplasia-deafness-progeroid features-lipodystrophy syndrome
      447877, Polymerase proofreading-related adenomatous polyposis

      The Pharmacogenetics and Pharmacogenomics Knowledge Base

      More...      PharmGKBi      		PA33496

      Miscellaneous databases

      Pharos NIH Druggable Genome Knowledgebase

      More...      Pharosi      		P28340, Tclin

      Chemistry databases

      ChEMBL database of bioactive drug-like small molecules

      More...      ChEMBLi      		CHEMBL2735

      DrugCentral

      More...      DrugCentrali      		P28340

      Polymorphism and mutation databases

      BioMuta curated single-nucleotide variation and disease association database

      More...      BioMutai      		POLD1

      Domain mapping of disease mutations (DMDM)

      More...      DMDMi      		50403732

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000464421 – 1107DNA polymerase delta catalytic subunitAdd BLAST1107

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19Omega-N-methylarginineCombined sources1
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki574Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

      Keywords - PTMi

      Isopeptide bond, Methylation, Ubl conjugation

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...      EPDi      		P28340

      jPOST - Japan Proteome Standard Repository/Database

      More...      jPOSTi      		P28340

      MassIVE - Mass Spectrometry Interactive Virtual Environment

      More...      MassIVEi      		P28340

      MaxQB - The MaxQuant DataBase

      More...      MaxQBi      		P28340

      PaxDb, a database of protein abundance averages across all three domains of life

      More...      PaxDbi      		P28340

      PeptideAtlas

      More...      PeptideAtlasi      		P28340

      PRoteomics IDEntifications database

      More...      PRIDEi      		P28340

      ProteomicsDB: a multi-organism proteome resource

      More...      ProteomicsDBi      		54478

      PTM databases

      iPTMnet integrated resource for PTMs in systems biology context

      More...      iPTMneti      		P28340

      Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

      More...      PhosphoSitePlusi      		P28340

      <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

      <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

      Widely expressed, with high levels of expression in heart and lung.1 Publication

      <p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

      Expression is cell cycle-dependent, with highest levels in G2/M phase and lowest in G1.1 Publication

      <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

      Up-regulated by serum stimulation.1 Publication

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...      Bgeei      		ENSG00000062822, Expressed in stomach and 192 other tissues

      ExpressionAtlas, Differential and Baseline Expression

      More...      ExpressionAtlasi      		P28340, baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...      Genevisiblei      		P28340, HS

      Organism-specific databases

      Human Protein Atlas

      More...      HPAi      		ENSG00000062822, Low tissue specificity

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing both DNA polymerase and 3' to 5' proofreading exonuclease activities (PubMed:11595739, PubMed:12522211, PubMed:17317665, PubMed:22801543). Within Pol-delta4, directly interacts with POLD2 and POLD4 (PubMed:11328591, PubMed:12403614, PubMed:16510448). Following genotoxic stress by DNA-damaging agents, such as ultraviolet light and methyl methanesulfonate, or by replication stress induced by treatment with hydroxyurea or aphidicolin, Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) by POLD4 degradation. Pol-delta3 is the major form at S phase replication sites and DNA damage sites (PubMed:22801543, PubMed:17317665). POLD1 displays different catalytic properties depending upon the complex it is found in (PubMed:17317665). It exhibits higher proofreading activity and fidelity than Pol-delta4, making it particularly well suited to respond to DNA damage (PubMed:19074196, PubMed:20334433). Directly interacts with PCNA, as do POLD3 and POLD4; this interaction stimulates Pol-delta4 polymerase activity (PubMed:11328591, PubMed:12403614, PubMed:12522211, PubMed:16510448, PubMed:24022480, PubMed:24939902). As POLD2 and POLD4, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA. This stimulation may be due predominantly to an increase of initiation frequency and also to increased processivity (PubMed:15670210). Also observed as a dimeric complex with POLD2 (Pol-delta2 complex). Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold) compared to Pol-delta4 that is stimulated by over 50-fold (PubMed:12403614). The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2 (PubMed:12522211).

      Interacts with CIAO1 (PubMed:23891004).

      Interacts with POLDIP2 (PubMed:24191025).

      14 Publications

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      Hide details

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGRID)

      More...      BioGRIDi      		111420, 136 interactors

      ComplexPortal: manually curated resource of macromolecular complexes

      More...      ComplexPortali      		CPX-2097, Delta DNA polymerase complex

      CORUM comprehensive resource of mammalian protein complexes

      More...      CORUMi      		P28340

      Protein interaction database and analysis system

      More...      IntActi      		P28340, 50 interactors

      Molecular INTeraction database

      More...      MINTi      		P28340

      STRING: functional protein association networks

      More...      STRINGi      		9606.ENSP00000406046

      Chemistry databases

      BindingDB database of measured binding affinities

      More...      BindingDBi      		P28340

      Miscellaneous databases

      RNAct, Protein-RNA interaction predictions for model organisms.

      More...      RNActi      		P28340, protein

      <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

      Secondary structure

      11107
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...      SMRi      		P28340

      Database of comparative protein structure models

      More...      ModBasei      		Search...

      Protein Data Bank in Europe - Knowledge Base

      More...      PDBe-KBi      		Search...

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi4 – 19Nuclear localization signalSequence analysisAdd BLAST16
      Motifi1058 – 1076CysB motifAdd BLAST19

      <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

      The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

      <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Belongs to the DNA polymerase type-B family.Curated

      Zinc finger

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Zinc fingeri1012 – 1029CysA-typeAdd BLAST18

      Keywords - Domaini

      Zinc-finger

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...      eggNOGi      		KOG0969, Eukaryota

      Ensembl GeneTree

      More...      GeneTreei      		ENSGT00560000077365

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...      HOGENOMi      		CLU_000203_2_0_1

      InParanoid: Eukaryotic Ortholog Groups

      More...      InParanoidi      		P28340

      KEGG Orthology (KO)

      More...      KOi      		K02327

      Database for complete collections of gene phylogenies

      More...      PhylomeDBi      		P28340

      TreeFam database of animal gene trees

      More...      TreeFami      		TF352785

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...      Gene3Di      		1.10.132.60, 1 hit
      3.30.420.10, 1 hit
      3.90.1600.10, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...      InterProi      		View protein in InterPro
      IPR006172, DNA-dir_DNA_pol_B
      IPR017964, DNA-dir_DNA_pol_B_CS
      IPR006133, DNA-dir_DNA_pol_B_exonuc
      IPR006134, DNA-dir_DNA_pol_B_multi_dom
      IPR043502, DNA/RNA_pol_sf
      IPR042087, DNA_pol_B_C
      IPR023211, DNA_pol_palm_dom_sf
      IPR012337, RNaseH-like_sf
      IPR036397, RNaseH_sf
      IPR025687, Znf-C4pol

      Pfam protein domain database

      More...      Pfami      		View protein in Pfam
      PF00136, DNA_pol_B, 1 hit
      PF03104, DNA_pol_B_exo1, 1 hit
      PF14260, zf-C4pol, 1 hit

      Protein Motif fingerprint database; a protein domain database

      More...      PRINTSi      		PR00106, DNAPOLB

      Simple Modular Architecture Research Tool; a protein domain database

      More...      SMARTi      		View protein in SMART
      SM00486, POLBc, 1 hit

      Superfamily database of structural and functional annotation

      More...      SUPFAMi      		SSF53098, SSF53098, 1 hit
      SSF56672, SSF56672, 1 hit

      PROSITE; a protein domain and family database

      More...      PROSITEi      		View protein in PROSITE
      PS00116, DNA_POLYMERASE_B, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

      This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All

      P28340-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MDGKRRPGPG PGVPPKRARG GLWDDDDAPR PSQFEEDLAL MEEMEAEHRL 
              60         70         80         90        100
      QEQEEEELQS VLEGVADGQV PPSAIDPRWL RPTPPALDPQ TEPLIFQQLE 
             110        120        130        140        150
      IDHYVGPAQP VPGGPPPSRG SVPVLRAFGV TDEGFSVCCH IHGFAPYFYT 
             160        170        180        190        200
      PAPPGFGPEH MGDLQRELNL AISRDSRGGR ELTGPAVLAV ELCSRESMFG 
             210        220        230        240        250
      YHGHGPSPFL RITVALPRLV APARRLLEQG IRVAGLGTPS FAPYEANVDF 
             260        270        280        290        300
      EIRFMVDTDI VGCNWLELPA GKYALRLKEK ATQCQLEADV LWSDVVSHPP 
             310        320        330        340        350
      EGPWQRIAPL RVLSFDIECA GRKGIFPEPE RDPVIQICSL GLRWGEPEPF 
             360        370        380        390        400
      LRLALTLRPC APILGAKVQS YEKEEDLLQA WSTFIRIMDP DVITGYNIQN 
             410        420        430        440        450
      FDLPYLISRA QTLKVQTFPF LGRVAGLCSN IRDSSFQSKQ TGRRDTKVVS 
             460        470        480        490        500
      MVGRVQMDML QVLLREYKLR SYTLNAVSFH FLGEQKEDVQ HSIITDLQNG 
             510        520        530        540        550
      NDQTRRRLAV YCLKDAYLPL RLLERLMVLV NAVEMARVTG VPLSYLLSRG 
             560        570        580        590        600
      QQVKVVSQLL RQAMHEGLLM PVVKSEGGED YTGATVIEPL KGYYDVPIAT 
             610        620        630        640        650
      LDFSSLYPSI MMAHNLCYTT LLRPGTAQKL GLTEDQFIRT PTGDEFVKTS 
             660        670        680        690        700
      VRKGLLPQIL ENLLSARKRA KAELAKETDP LRRQVLDGRQ LALKVSANSV 
             710        720        730        740        750
      YGFTGAQVGK LPCLEISQSV TGFGRQMIEK TKQLVESKYT VENGYSTSAK 
             760        770        780        790        800
      VVYGDTDSVM CRFGVSSVAE AMALGREAAD WVSGHFPSPI RLEFEKVYFP 
             810        820        830        840        850
      YLLISKKRYA GLLFSSRPDA HDRMDCKGLE AVRRDNCPLV ANLVTASLRR 
             860        870        880        890        900
      LLIDRDPEGA VAHAQDVISD LLCNRIDISQ LVITKELTRA ASDYAGKQAH 
             910        920        930        940        950
      VELAERMRKR DPGSAPSLGD RVPYVIISAA KGVAAYMKSE DPLFVLEHSL 
             960        970        980        990       1000
      PIDTQYYLEQ QLAKPLLRIF EPILGEGRAE AVLLRGDHTR CKTVLTGKVG 
            1010       1020       1030       1040       1050
      GLLAFAKRRN CCIGCRTVLS HQGAVCEFCQ PRESELYQKE VSHLNALEER 
            1060       1070       1080       1090       1100
      FSRLWTQCQR CQGSLHEDVI CTSRDCPIFY MRKKVRKDLE DQEQLLRRFG 

      PPGPEAW
      Length:1,107
      Mass (Da):123,631
      Last modified:July 19, 2004 - v2
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9D04D34AB4AEE810
      GO

      <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

      There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      		Gene namesLengthAnnotation
      M0R2B7M0R2B7_HUMAN
      DNA polymerase
      POLD1
      		1,133Annotation score:

      Annotation score:3 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A087WYJ2A0A087WYJ2_HUMAN
      DNA polymerase
      POLD1
      		1,083Annotation score:

      Annotation score:3 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      M0QZR8M0QZR8_HUMAN
      DNA polymerase
      POLD1
      		1,009Annotation score:

      Annotation score:2 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A2R8Y7K6A0A2R8Y7K6_HUMAN
      DNA-directed DNA polymerase
      POLD1
      		762Annotation score:

      Annotation score:2 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      A0A2R8Y705A0A2R8Y705_HUMAN
      DNA polymerase
      POLD1
      		447Annotation score:

      Annotation score:2 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      M0QXQ2M0QXQ2_HUMAN
      DNA-directed DNA polymerase
      POLD1
      		291Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      M0QXE6M0QXE6_HUMAN
      DNA-directed DNA polymerase
      POLD1
      		289Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
      M0R2J2M0R2J2_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		105Annotation score:

      Annotation score:1 out of 5

      <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti472Y → H in AAA58439 (PubMed:1722322).Curated1
      Sequence conflicti776R → G in AAA35768 (PubMed:1542570).Curated1

      Natural variant

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_0488785R → W. Corresponds to variant dbSNP:rs9282830EnsemblClinVar.1
      Natural variantiVAR_01934019R → H1 PublicationCorresponds to variant dbSNP:rs3218773EnsemblClinVar.1
      Natural variantiVAR_04887921G → C. Corresponds to variant dbSNP:rs9282831EnsemblClinVar.1
      Natural variantiVAR_01614630R → W2 PublicationsCorresponds to variant dbSNP:rs3218772EnsemblClinVar.1
      Natural variantiVAR_019341119R → H3 PublicationsCorresponds to variant dbSNP:rs1726801EnsemblClinVar.1
      Natural variantiVAR_069333145A → D Found in a colorectal sample; somatic mutation. 1 Publication1
      Natural variantiVAR_019342173S → N2 PublicationsCorresponds to variant dbSNP:rs1726803EnsemblClinVar.1
      Natural variantiVAR_019343177R → H1 PublicationCorresponds to variant dbSNP:rs3218750EnsemblClinVar.1
      Natural variantiVAR_048880347P → L. Corresponds to variant dbSNP:rs2230243EnsemblClinVar.1
      Natural variantiVAR_069334461Q → H Found in a colorectal sample; somatic mutation. 1 Publication1
      Natural variantiVAR_071966474L → P in CRCS10. 1 PublicationCorresponds to variant dbSNP:rs587777627EnsemblClinVar.1
      Natural variantiVAR_069335478S → N in CRCS10; associated with disease susceptibility. 1 PublicationCorresponds to variant dbSNP:rs397514632EnsemblClinVar.1
      Natural variantiVAR_070231605Missing in MDPL; the mutant enzyme lacks DNA polymerase ability; has decreased exonuclease activity; can bind DNA but is unable to interact with and incorporate dNTPs. 1 Publication1
      Natural variantiVAR_069336787P → L Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs199783227EnsemblClinVar.1
      Natural variantiVAR_069337808R → H Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs771700024Ensembl.1
      Natural variantiVAR_019344849R → H1 PublicationCorresponds to variant dbSNP:rs3218775EnsemblClinVar.1
      Natural variantiVAR_069338864A → T Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs765437818EnsemblClinVar.1
      Natural variantiVAR_0193451086R → Q1 PublicationCorresponds to variant dbSNP:rs3219457EnsemblClinVar.1

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...      EMBLi

      GenBank nucleotide sequence database

      More...      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...      DDBJi
      Links Updated
      		M80397 mRNA Translation: AAA58439.1
      M81735 mRNA Translation: AAA35768.1
      AY129569 Genomic DNA Translation: AAM76971.1
      BC008800 mRNA Translation: AAH08800.1

      The Consensus CDS (CCDS) project

      More...      CCDSi      		CCDS12795.1

      Protein sequence database of the Protein Information Resource

      More...      PIRi      		A41618

      NCBI Reference Sequences

      More...      RefSeqi      		NP_001243778.1, NM_001256849.1
      NP_002682.2, NM_002691.3
      XP_011525340.1, XM_011527038.1
      XP_016882370.1, XM_017026881.1

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...      Ensembli      		ENST00000440232; ENSP00000406046; ENSG00000062822
      ENST00000599857; ENSP00000473052; ENSG00000062822
      ENST00000601098; ENSP00000472600; ENSG00000062822

      Database of genes from NCBI RefSeq genomes

      More...      GeneIDi      		5424

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...      KEGGi      		hsa:5424

      UCSC genome browser

      More...      UCSCi      		uc002psb.6, human

      Keywords - Coding sequence diversityi

      Polymorphism

      <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

      <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

      NIEHS-SNPs

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      		M80397 mRNA Translation: AAA58439.1
      M81735 mRNA Translation: AAA35768.1
      AY129569 Genomic DNA Translation: AAM76971.1
      BC008800 mRNA Translation: AAH08800.1
      CCDSiCCDS12795.1
      PIRiA41618
      RefSeqiNP_001243778.1, NM_001256849.1
      NP_002682.2, NM_002691.3
      XP_011525340.1, XM_011527038.1
      XP_016882370.1, XM_017026881.1

      3D structure databases

      Select the link destinations:

      Protein Data Bank Europe

      More...      PDBei

      Protein Data Bank RCSB

      More...      RCSB PDBi

      Protein Data Bank Japan

      More...      PDBji
      Links Updated
      		PDB entryMethodResolution (Å)ChainPositionsPDBsum
      6S1Melectron microscopy4.27A1-1107[»]
      6S1Nelectron microscopy4.86A1-1107[»]
      6S1Oelectron microscopy8.10A1-1107[»]
      6TNYelectron microscopy3.08A1-1107[»]
      6TNZelectron microscopy4.05A1-1107[»]
      SMRiP28340
      ModBaseiSearch...
      PDBe-KBiSearch...

      Protein-protein interaction databases

      BioGRIDi111420, 136 interactors
      ComplexPortaliCPX-2097, Delta DNA polymerase complex
      CORUMiP28340
      IntActiP28340, 50 interactors
      MINTiP28340
      STRINGi9606.ENSP00000406046

      Chemistry databases

      BindingDBiP28340
      ChEMBLiCHEMBL2735
      DrugCentraliP28340

      PTM databases

      iPTMnetiP28340
      PhosphoSitePlusiP28340

      Polymorphism and mutation databases

      BioMutaiPOLD1
      DMDMi50403732

      Proteomic databases

      EPDiP28340
      jPOSTiP28340
      MassIVEiP28340
      MaxQBiP28340
      PaxDbiP28340
      PeptideAtlasiP28340
      PRIDEiP28340
      ProteomicsDBi54478

      Protocols and materials databases

      Antibodypedia a portal for validated antibodies

      More...      Antibodypediai      		3821, 336 antibodies

      The DNASU plasmid repository

      More...      DNASUi      		5424

      Genome annotation databases

      EnsembliENST00000440232; ENSP00000406046; ENSG00000062822
      ENST00000599857; ENSP00000473052; ENSG00000062822
      ENST00000601098; ENSP00000472600; ENSG00000062822
      GeneIDi5424
      KEGGihsa:5424
      UCSCiuc002psb.6, human

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...      CTDi      		5424
      DisGeNETi5424
      EuPathDBiHostDB:ENSG00000062822.12

      GeneCards: human genes, protein and diseases

      More...      GeneCardsi      		POLD1
      HGNCiHGNC:9175, POLD1
      HPAiENSG00000062822, Low tissue specificity
      MalaCardsiPOLD1
      MIMi174761, gene
      612591, phenotype
      615381, phenotype
      neXtProtiNX_P28340
      OpenTargetsiENSG00000062822
      Orphaneti363649, Mandibular hypoplasia-deafness-progeroid features-lipodystrophy syndrome
      447877, Polymerase proofreading-related adenomatous polyposis
      PharmGKBiPA33496

      GenAtlas: human gene database

      More...      GenAtlasi      		Search...

      Phylogenomic databases

      eggNOGiKOG0969, Eukaryota
      GeneTreeiENSGT00560000077365
      HOGENOMiCLU_000203_2_0_1
      InParanoidiP28340
      KOiK02327
      PhylomeDBiP28340
      TreeFamiTF352785

      Enzyme and pathway databases

      BRENDAi2.7.7.7, 2681
      PathwayCommonsiP28340
      ReactomeiR-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex
      R-HSA-174411, Polymerase switching on the C-strand of the telomere
      R-HSA-174414, Processive synthesis on the C-strand of the telomere
      R-HSA-174417, Telomere C-strand (Lagging Strand) Synthesis
      R-HSA-174437, Removal of the Flap Intermediate from the C-strand
      R-HSA-2564830, Cytosolic iron-sulfur cluster assembly
      R-HSA-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
      R-HSA-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
      R-HSA-5651801, PCNA-Dependent Long Patch Base Excision Repair
      R-HSA-5656169, Termination of translesion DNA synthesis
      R-HSA-5685942, HDR through Homologous Recombination (HRR)
      R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
      R-HSA-5696400, Dual Incision in GG-NER
      R-HSA-6782135, Dual incision in TC-NER
      R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
      R-HSA-69091, Polymerase switching
      R-HSA-69166, Removal of the Flap Intermediate
      R-HSA-69183, Processive synthesis on the lagging strand

      Miscellaneous databases

      BioGRID ORCS database of CRISPR phenotype screens

      More...      BioGRID-ORCSi      		5424, 739 hits in 879 CRISPR screens

      ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

      More...      ChiTaRSi      		POLD1, human

      The Gene Wiki collection of pages on human genes and proteins

      More...      GeneWikii      		POLD1

      Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

      More...      GenomeRNAii      		5424
      PharosiP28340, Tclin

      Protein Ontology

      More...      PROi      		PR:P28340
      RNActiP28340, protein

      The Stanford Online Universal Resource for Clones and ESTs

      More...      SOURCEi      		Search...

      Gene expression databases

      BgeeiENSG00000062822, Expressed in stomach and 192 other tissues
      ExpressionAtlasiP28340, baseline and differential
      GenevisibleiP28340, HS

      Family and domain databases

      Gene3Di1.10.132.60, 1 hit
      3.30.420.10, 1 hit
      3.90.1600.10, 1 hit
      InterProiView protein in InterPro
      IPR006172, DNA-dir_DNA_pol_B
      IPR017964, DNA-dir_DNA_pol_B_CS
      IPR006133, DNA-dir_DNA_pol_B_exonuc
      IPR006134, DNA-dir_DNA_pol_B_multi_dom
      IPR043502, DNA/RNA_pol_sf
      IPR042087, DNA_pol_B_C
      IPR023211, DNA_pol_palm_dom_sf
      IPR012337, RNaseH-like_sf
      IPR036397, RNaseH_sf
      IPR025687, Znf-C4pol
      PfamiView protein in Pfam
      PF00136, DNA_pol_B, 1 hit
      PF03104, DNA_pol_B_exo1, 1 hit
      PF14260, zf-C4pol, 1 hit
      PRINTSiPR00106, DNAPOLB
      SMARTiView protein in SMART
      SM00486, POLBc, 1 hit
      SUPFAMiSSF53098, SSF53098, 1 hit
      SSF56672, SSF56672, 1 hit
      PROSITEiView protein in PROSITE
      PS00116, DNA_POLYMERASE_B, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...      ProtoNeti      		Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...      MobiDBi      		Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDPOD1_HUMAN
      <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P28340
      Secondary accession number(s): Q8NER3, Q96H98
      <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
      Last sequence update: July 19, 2004
      Last modified: August 12, 2020
      This is version 206 of the entry and version 2 of the sequence. See complete history.
      <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program
      DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

      <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      3D-structure, Reference proteome

      Documents

      1. Human chromosome 19
        Human chromosome 19: entries, gene names and cross-references to MIM
      2. Human entries with polymorphisms or disease mutations
        List of human entries with polymorphisms or disease mutations
      3. Human polymorphisms and disease mutations
        Index of human polymorphisms and disease mutations
      4. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
      5. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      6. SIMILARITY comments
        Index of protein domains and families
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