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Entry version 174 (29 Sep 2021)
Sequence version 2 (27 Jul 2011)
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Protein

DNA polymerase delta catalytic subunit

Gene

Pold1

Organism
Mus musculus (Mouse)
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. 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. 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. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. 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). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites.

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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. Stimulated in the presence of PCNA (By similarity). This stimulation is further increased in the presence of KCTD13/PDIP1, most probably via direct interaction between KCTD13 and POLD2 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi1010ZincBy similarity1
Metal bindingi1013ZincBy similarity1
Metal bindingi1024ZincBy similarity1
Metal bindingi1027ZincBy similarity1
Metal bindingi1056Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1059Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1069Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1074Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 fingeri1010 – 1027CysA-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

GO - Biological processi

<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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-110314, Recognition of DNA damage by PCNA-containing replication complex
R-MMU-174411, Polymerase switching on the C-strand of the telomere
R-MMU-174414, Processive synthesis on the C-strand of the telomere
R-MMU-174417, Telomere C-strand (Lagging Strand) Synthesis
R-MMU-174437, Removal of the Flap Intermediate from the C-strand
R-MMU-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-MMU-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-MMU-5651801, PCNA-Dependent Long Patch Base Excision Repair
R-MMU-5656169, Termination of translesion DNA synthesis
R-MMU-5685942, HDR through Homologous Recombination (HRR)
R-MMU-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-MMU-5696400, Dual Incision in GG-NER
R-MMU-6782135, Dual incision in TC-NER
R-MMU-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-69091, Polymerase switching
R-MMU-69166, Removal of the Flap Intermediate
R-MMU-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_and_taxonomy_section">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:2.7.7.7By similarity)
Alternative name(s):
3'-5' exodeoxyribonucleaseCurated (EC:3.1.11.-By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:97741, Pold1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSMUSG00000038644

<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 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_00000464441 – 1105DNA polymerase delta catalytic subunitAdd BLAST1105

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-methylarginineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-linki572Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P52431

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P52431

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

More...
PaxDbi
P52431

PeptideAtlas

More...
PeptideAtlasi
P52431

PRoteomics IDEntifications database

More...
PRIDEi
P52431

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
277387

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P52431

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

More...
PhosphoSitePlusi
P52431

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000038644, Expressed in optic fissure and 301 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P52431, MM

<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_section">'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_section">'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. Within Pol-delta4, directly interacts with POLD2 and POLD4. 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. POLD1 displays different catalytic properties depending upon the complex it is found in. It exhibits higher proofreading activity and fidelity than Pol-delta4, making it particularly well suited to respond to DNA damage. Directly interacts with PCNA, as do POLD3 and POLD4; this interaction stimulates Pol-delta4 polymerase activity. 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. Also observed as a dimeric complex with POLD2 (Pol-delta2). Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold) compared to Pol-delta4 that is stimulated by over 50-fold. The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2.

Interacts with CIAO1.

Interacts with POLDIP2 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
202290, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2098, Delta DNA polymerase complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P52431

Database of interacting proteins

More...
DIPi
DIP-45885N

Protein interaction database and analysis system

More...
IntActi
P52431, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000039776

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P52431, 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

3D structure databases

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

More...
SMRi
P52431

Database of comparative protein structure models

More...
ModBasei
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 – 31DisorderedSequence analysisAdd BLAST31

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
Motifi1056 – 1074CysB 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 fingeri1010 – 1027CysA-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
P52431

Identification of Orthologs from Complete Genome Data

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OMAi
RVAYVMV

Database of Orthologous Groups

More...
OrthoDBi
20210at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P52431

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, 2 hits

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

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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

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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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 2 potential isoforms that are computationally mapped.Show allAlign All

P52431-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDCKRRQGPG PGVPPKRARG HLWDEDEPSP SQFEANLALL EEIEAENRLQ
60 70 80 90 100
EAEEELQLPP EGTVGGQFST ADIDPRWRRP TLRALDPSTE PLIFQQLEID
110 120 130 140 150
HYVGSAPPLP EGPLPSRNSV PILRAFGVTD EGFSVCCHIQ GFAPYFYTPA
160 170 180 190 200
PPGFGAEHLS ELQQELNAAI SRDQRGGKEL SGPAVLAIEL CSRESMFGYH
210 220 230 240 250
GHGPSPFLRI TLALPRLMAP ARRLLEQGVR VPGLGTPSFA PYEANVDFEI
260 270 280 290 300
RFMVDADIVG CNWLELPAGK YVRRAEKKAT LCQLEVDVLW SDVISHPPEG
310 320 330 340 350
QWQRIAPLRV LSFDIECAGR KGIFPEPERD PVIQICSLGL RWGEPEPFLR
360 370 380 390 400
LALTLRPCAP ILGAKVQSYE REEDLLQAWA DFILAMDPDV ITGYNIQNFD
410 420 430 440 450
LPYLISRAQA LKVDRFPFLG RVTGLRSNIR DSSFQSRQVG RRDSKVISMV
460 470 480 490 500
GRVQMDMLQV LLREHKLRSY TLNAVSFHFL GEQKEDVQHS IITDLQNGNE
510 520 530 540 550
QTRRRLAVYC LKDAFLPLRL LERLMVLVNN VEMARVTGVP LGYLLTRGQQ
560 570 580 590 600
VKVVSQLLRQ AMRQGLLMPV VKTEGSEDYT GATVIEPLKG YYDVPIATLD
610 620 630 640 650
FSSLYPSIMM AHNLCYTTLL RPGAAQKLGL KPDEFIKTPT GDEFVKSSVR
660 670 680 690 700
KGLLPQILEN LLSARKRAKA ELAQETDPLR RQVLDGRQLA LKVSANSVYG
710 720 730 740 750
FTGAQVGKLP CLEISQSVTG FGRQMIEKTK QLVESKYTVE NGYDANAKVV
760 770 780 790 800
YGDTDSVMCR FGVSSVAEAM SLGREAANWV SSHFPSPIRL EFEKVYFPYL
810 820 830 840 850
LISKKRYAGL LFSSRSDAHD KMDCKGLEAV RRDNCPLVAN LVTSSLRRIL
860 870 880 890 900
VDRDPDGAVA HAKDVISDLL CNRIDISQLV ITKELTRAAA DYAGKQAHVE
910 920 930 940 950
LAERMRKRDP GSAPSLGDRV PYVIIGAAKG VAAYMKSEDP LFVLEHSLPI
960 970 980 990 1000
DTQYYLEQQL AKPLLRIFEP ILGEGRAESV LLRGDHTRCK TVLTSKVGGL
1010 1020 1030 1040 1050
LAFTKRRNCC IGCRSVIDHQ GAVCKFCQPR ESELYQKEVS HLNALEERFS
1060 1070 1080 1090 1100
RLWTQCQRCQ GSLHEDVICT SRDCPIFYMR KKVRKDLEDQ ERLLQRFGPP

GPEAW
Length:1,105
Mass (Da):123,790
Last modified:July 27, 2011 - 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:i2AE377D42E3A6A86
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RFB8D6RFB8_MOUSE
DNA polymerase
Pold1
981Annotation 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>
D3YVY8D3YVY8_MOUSE
DNA polymerase delta catalytic subu...
Pold1
153Annotation 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 conflicti112G → R in CAA79895 (PubMed:8262377).Curated1
Sequence conflicti114L → P in AAB99910 (PubMed:9434960).Curated1
Sequence conflicti576S → G in CAA79895 (PubMed:8262377).Curated1
Sequence conflicti576S → G in AAB99910 (PubMed:9434960).Curated1
Sequence conflicti793E → K in AAB99910 (PubMed:9434960).Curated1
Sequence conflicti1000L → F in AAB99910 (PubMed:9434960).Curated1
Sequence conflicti1035Y → S in CAA79895 (PubMed:8262377).Curated1
Sequence conflicti1045 – 1052LEERFSRL → WKNGSLRF in AAB99910 (PubMed:9434960).Curated8

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z21848 mRNA Translation: CAA79895.1
AF024570 Genomic DNA Translation: AAB99910.1
AK167569 mRNA Translation: BAE39632.1
AK168967 mRNA Translation: BAE40772.1
AK169040 mRNA Translation: BAE40829.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS21210.1

Protein sequence database of the Protein Information Resource

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PIRi
S40243

NCBI Reference Sequences

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RefSeqi
NP_035261.3, NM_011131.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000049343; ENSMUSP00000039776; ENSMUSG00000038644

Database of genes from NCBI RefSeq genomes

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GeneIDi
18971

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:18971

UCSC genome browser

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UCSCi
uc009gpx.2, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21848 mRNA Translation: CAA79895.1
AF024570 Genomic DNA Translation: AAB99910.1
AK167569 mRNA Translation: BAE39632.1
AK168967 mRNA Translation: BAE40772.1
AK169040 mRNA Translation: BAE40829.1
CCDSiCCDS21210.1
PIRiS40243
RefSeqiNP_035261.3, NM_011131.3

3D structure databases

SMRiP52431
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202290, 6 interactors
ComplexPortaliCPX-2098, Delta DNA polymerase complex
CORUMiP52431
DIPiDIP-45885N
IntActiP52431, 2 interactors
STRINGi10090.ENSMUSP00000039776

PTM databases

iPTMnetiP52431
PhosphoSitePlusiP52431

Proteomic databases

EPDiP52431
MaxQBiP52431
PaxDbiP52431
PeptideAtlasiP52431
PRIDEiP52431
ProteomicsDBi277387

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
3821, 357 antibodies

The DNASU plasmid repository

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DNASUi
18971

Genome annotation databases

EnsembliENSMUST00000049343; ENSMUSP00000039776; ENSMUSG00000038644
GeneIDi18971
KEGGimmu:18971
UCSCiuc009gpx.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5424
MGIiMGI:97741, Pold1
VEuPathDBiHostDB:ENSMUSG00000038644

Phylogenomic databases

eggNOGiKOG0969, Eukaryota
GeneTreeiENSGT00560000077365
HOGENOMiCLU_000203_2_0_1
InParanoidiP52431
OMAiRVAYVMV
OrthoDBi20210at2759
PhylomeDBiP52431
TreeFamiTF352785

Enzyme and pathway databases

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
18971, 50 hits in 97 CRISPR screens

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

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ChiTaRSi
Pold1, mouse

Protein Ontology

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PROi
PR:P52431
RNActiP52431, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000038644, Expressed in optic fissure and 301 other tissues
GenevisibleiP52431, MM

Family and domain databases

Gene3Di1.10.132.60, 1 hit
3.30.420.10, 1 hit
3.90.1600.10, 2 hits
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

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MobiDBi
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<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_MOUSE
<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: P52431
Secondary accession number(s): O54883, Q3TFX6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: September 29, 2021
This is version 174 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

<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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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