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UniProtKB - P28340 (DPOD1_HUMAN)

Entry version 213 (23 Feb 2022)
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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P28340

SIGNOR Signaling Network Open Resource

More...SIGNORi		P28340

<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

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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000062822

<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

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 variants 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 variants 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 variant

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

Genetic variation 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 193 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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111420, 185 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P28340

Protein interaction database and analysis system

More...IntActi		P28340, 53 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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 34DisorderedSequence analysisAdd BLAST34

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi19 – 34Basic and acidic residuesSequence analysisAdd BLAST16

<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

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_thumb
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: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>
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>
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>
M0QXQ2M0QXQ2_HUMAN
DNA-directed DNA polymerase
POLD1
291Annotation 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>
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:rs771700024EnsemblClinVar.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

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000440232.7; ENSP00000406046.1; NM_002691.4; NP_002682.2

UCSC genome browser

More...UCSCi		uc002psb.6, human

<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, 185 interactors
ComplexPortaliCPX-2097, DNA polymerase delta complex
CORUMiP28340
IntActiP28340, 53 interactors
MINTiP28340
STRINGi9606.ENSP00000406046

Chemistry databases

BindingDBiP28340
ChEMBLiCHEMBL2735
DrugCentraliP28340

PTM databases

iPTMnetiP28340
PhosphoSitePlusiP28340

Genetic variation 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, 358 antibodies from 36 providers

The CPTC Antibody Portal

More...CPTCi		P28340, 1 antibody

The DNASU plasmid repository

More...DNASUi		5424

Genome annotation databases

EnsembliENST00000440232; ENSP00000406046; ENSG00000062822
ENST00000599857; ENSP00000473052; ENSG00000062822
ENST00000601098; ENSP00000472600; ENSG00000062822
GeneIDi5424
KEGGihsa:5424
MANE-SelectiENST00000440232.7; ENSP00000406046.1; NM_002691.4; NP_002682.2
UCSCiuc002psb.6, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5424
DisGeNETi5424

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
VEuPathDBiHostDB:ENSG00000062822

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0969, Eukaryota
GeneTreeiENSGT00560000077365
HOGENOMiCLU_000203_2_0_1
InParanoidiP28340
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
SignaLinkiP28340
SIGNORiP28340

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5424, 772 hits in 1051 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 193 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_thumb
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

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: February 23, 2022
This is version 213 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 genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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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