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UniProtKB - P28340 (DPOD1_HUMAN)

Protein

DNA polymerase delta catalytic subunit

Gene

POLD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 or abasic sites (PubMed:19074196).7 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

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

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

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
      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
      Zinc fingeri1012 – 1029CysA-typeAdd BLAST18

      GO - Molecular functioni

      • 3'-5'-exodeoxyribonuclease activity Source: GO_Central
      • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
      • chromatin binding Source: UniProtKB
      • damaged DNA binding Source: UniProtKB
      • DNA binding Source: UniProtKB
      • DNA-directed DNA polymerase activity Source: UniProtKB
      • metal ion binding Source: UniProtKB-KW
      • nucleotide binding Source: InterPro
      View the complete GO annotation on QuickGO ...

      GO - Biological processi

      View the complete GO annotation on QuickGO ...

      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

      BRENDAi2.7.7.7 2681
      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

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      DNA polymerase delta catalytic subunitCurated (EC:2.7.7.7, EC:3.1.11.-)
      Alternative name(s):
      DNA polymerase subunit delta p125
      Gene namesi
      Name:POLD1Imported
      Synonyms:POLD
      OrganismiHomo sapiens (Human)
      Taxonomic identifieri9606 [NCBI]
      Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
      Proteomesi
      • UP000005640 Componenti: Chromosome 19

      Organism-specific databases

      EuPathDBiHostDB:ENSG00000062822.12
      HGNCiHGNC:9175 POLD1
      MIMi174761 gene
      neXtProtiNX_P28340

      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; Source: COMPARTMENTS

      Keywords - Cellular componenti

      Nucleus

      Pathology & Biotechi

      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.
      See also OMIM:612591
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      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.
      See also OMIM:615381
      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
      Mutagenesisi402D → A: Loss of exonuclease activity. No effect on DNA polymerase activity. 2 Publications1

      Keywords - Diseasei

      Disease mutation

      Organism-specific databases

      DisGeNETi5424
      MalaCardsiPOLD1
      MIMi612591 phenotype
      615381 phenotype
      OpenTargetsiENSG00000062822
      Orphaneti363649 Mandibular hypoplasia-deafness-progeroid syndrome
      447877 Polymerase proofreading-related adenomatous polyposis
      PharmGKBiPA33496

      Chemistry databases

      ChEMBLiCHEMBL2735

      Polymorphism and mutation databases

      BioMutaiPOLD1
      DMDMi50403732

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      ChainiPRO_00000464421 – 1107DNA polymerase delta catalytic subunitAdd BLAST1107

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Modified residuei19Omega-N-methylarginineCombined sources1
      Cross-linki574Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

      Keywords - PTMi

      Isopeptide bond, Methylation, Ubl conjugation

      Proteomic databases

      EPDiP28340
      MaxQBiP28340
      PaxDbiP28340
      PeptideAtlasiP28340
      PRIDEiP28340
      ProteomicsDBi54478

      PTM databases

      iPTMnetiP28340
      PhosphoSitePlusiP28340

      Miscellaneous databases

      PMAP-CutDBiP28340

      Expressioni

      Tissue specificityi

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

      Developmental stagei

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

      Inductioni

      Up-regulated by serum stimulation.1 Publication

      Gene expression databases

      BgeeiENSG00000062822 Expressed in 178 organ(s), highest expression level in left lobe of thyroid gland
      CleanExiHS_POLD1
      ExpressionAtlasiP28340 baseline and differential
      GenevisibleiP28340 HS

      Organism-specific databases

      HPAiCAB004375
      HPA046524

      Interactioni

      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).13 Publications

      Binary interactionsi

      Protein-protein interaction databases

      BioGridi111420, 85 interactors
      ComplexPortaliCPX-2097 Delta DNA polymerase complex
      CORUMiP28340
      IntActiP28340, 39 interactors
      MINTiP28340
      STRINGi9606.ENSP00000406046

      Chemistry databases

      BindingDBiP28340

      Structurei

      3D structure databases

      ProteinModelPortaliP28340
      SMRiP28340
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Motifi4 – 19Nuclear localization signalSequence analysisAdd BLAST16
      Motifi1058 – 1076CysB motifAdd BLAST19

      Domaini

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

      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

      eggNOGiKOG0968 Eukaryota
      COG0417 LUCA
      GeneTreeiENSGT00560000077365
      HOGENOMiHOG000036616
      HOVERGENiHBG051395
      InParanoidiP28340
      KOiK02327
      PhylomeDBiP28340
      TreeFamiTF352785

      Family and domain databases

      Gene3Di3.30.420.10, 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
      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
      PROSITEiView protein in PROSITE
      PS00116 DNA_POLYMERASE_B, 1 hit

      Sequence (1+)i

      Sequence statusi: Complete.

      This entry has 1 described isoform and 9 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
      Checksum:i9D04D34AB4AEE810
      GO

      Computationally mapped potential isoform sequencesi

      There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      		Gene namesLengthAnnotation
      M0R2B7M0R2B7_HUMAN
      DNA polymerase
      POLD1
      		1,133Annotation score:
      M0QZR8M0QZR8_HUMAN
      DNA polymerase
      POLD1
      		1,009Annotation score:
      A0A2R8Y705A0A2R8Y705_HUMAN
      DNA polymerase
      POLD1
      		447Annotation score:
      A0A2R8Y7K6A0A2R8Y7K6_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		762Annotation score:
      M0QXE6M0QXE6_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		289Annotation score:
      M0QXQ2M0QXQ2_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		291Annotation score:
      M0QZB4M0QZB4_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		188Annotation score:
      M0R2I8M0R2I8_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		202Annotation score:
      M0R2J2M0R2J2_HUMAN
      DNA polymerase delta catalytic subu...
      POLD1
      		105Annotation score:

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      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 Publication1
      Natural variantiVAR_0193451086R → Q1 PublicationCorresponds to variant dbSNP:rs3219457EnsemblClinVar.1

      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
      UniGeneiHs.279413

      Genome annotation databases

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

      Keywords - Coding sequence diversityi

      Polymorphism

      Similar proteinsi

      Cross-referencesi

      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
      UniGeneiHs.279413

      3D structure databases

      ProteinModelPortaliP28340
      SMRiP28340
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi111420, 85 interactors
      ComplexPortaliCPX-2097 Delta DNA polymerase complex
      CORUMiP28340
      IntActiP28340, 39 interactors
      MINTiP28340
      STRINGi9606.ENSP00000406046

      Chemistry databases

      BindingDBiP28340
      ChEMBLiCHEMBL2735

      PTM databases

      iPTMnetiP28340
      PhosphoSitePlusiP28340

      Polymorphism and mutation databases

      BioMutaiPOLD1
      DMDMi50403732

      Proteomic databases

      EPDiP28340
      MaxQBiP28340
      PaxDbiP28340
      PeptideAtlasiP28340
      PRIDEiP28340
      ProteomicsDBi54478

      Protocols and materials databases

      DNASUi5424
      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

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

      Organism-specific databases

      CTDi5424
      DisGeNETi5424
      EuPathDBiHostDB:ENSG00000062822.12
      GeneCardsiPOLD1
      H-InvDBiHIX0202825
      HGNCiHGNC:9175 POLD1
      HPAiCAB004375
      HPA046524
      MalaCardsiPOLD1
      MIMi174761 gene
      612591 phenotype
      615381 phenotype
      neXtProtiNX_P28340
      OpenTargetsiENSG00000062822
      Orphaneti363649 Mandibular hypoplasia-deafness-progeroid syndrome
      447877 Polymerase proofreading-related adenomatous polyposis
      PharmGKBiPA33496
      GenAtlasiSearch...

      Phylogenomic databases

      eggNOGiKOG0968 Eukaryota
      COG0417 LUCA
      GeneTreeiENSGT00560000077365
      HOGENOMiHOG000036616
      HOVERGENiHBG051395
      InParanoidiP28340
      KOiK02327
      PhylomeDBiP28340
      TreeFamiTF352785

      Enzyme and pathway databases

      BRENDAi2.7.7.7 2681
      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

      GeneWikiiPOLD1
      GenomeRNAii5424
      PMAP-CutDBiP28340
      PROiPR:P28340
      SOURCEiSearch...

      Gene expression databases

      BgeeiENSG00000062822 Expressed in 178 organ(s), highest expression level in left lobe of thyroid gland
      CleanExiHS_POLD1
      ExpressionAtlasiP28340 baseline and differential
      GenevisibleiP28340 HS

      Family and domain databases

      Gene3Di3.30.420.10, 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
      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
      PROSITEiView protein in PROSITE
      PS00116 DNA_POLYMERASE_B, 1 hit
      ProtoNetiSearch...

      Entry informationi

      Entry nameiDPOD1_HUMAN
      AccessioniPrimary (citable) accession number: P28340
      Secondary accession number(s): Q8NER3, Q96H98
      Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
      Last sequence update: July 19, 2004
      Last modified: November 7, 2018
      This is version 192 of the entry and version 2 of the sequence. See complete history.
      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.

      Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families
      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. Human chromosome 19
        Human chromosome 19: entries, gene names and cross-references to MIM
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