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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-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

Enzyme 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

      GO - Biological processi

      • base-excision repair, gap-filling Source: UniProtKB
      • cellular response to UV Source: UniProtKB
      • DNA damage response, detection of DNA damage Source: Reactome
      • DNA repair Source: ProtInc
      • DNA replication Source: UniProtKB
      • DNA replication proofreading Source: GO_Central
      • DNA strand elongation involved in DNA replication Source: Reactome
      • DNA synthesis involved in DNA repair Source: UniProtKB
      • fatty acid homeostasis Source: UniProtKB
      • mismatch repair Source: Reactome
      • nucleotide-excision repair, DNA gap filling Source: UniProtKB
      • nucleotide-excision repair, DNA incision Source: Reactome
      • nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
      • response to UV Source: ProtInc
      • telomere maintenance Source: Reactome
      • telomere maintenance via recombination Source: Reactome
      • transcription-coupled nucleotide-excision repair Source: Reactome
      • translesion synthesis Source: Reactome
      Complete GO annotation...

      Keywords - Molecular functioni

      DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

      Keywords - Biological processi

      DNA damage, DNA excision, DNA repair, DNA replication

      Keywords - Ligandi

      4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

      Enzyme and pathway databases

      BioCyciZFISH:HS00772-MONOMER.
      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 subunit (EC:2.7.7.7, EC:3.1.11.-)
      Alternative name(s):
      DNA polymerase subunit delta p125
      Gene namesi
      Name:POLD1
      Synonyms:POLD
      OrganismiHomo sapiens (Human)
      Taxonomic identifieri9606 [NCBI]
      Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
      Proteomesi
      • UP000005640 Componenti: Chromosome 19

      Organism-specific databases

      HGNCiHGNC:9175. POLD1.

      Subcellular locationi

      GO - Cellular componenti

      • aggresome Source: HPA
      • cytoplasm Source: HPA
      • delta DNA polymerase complex Source: GO_Central
      • membrane Source: UniProtKB
      • nucleoplasm Source: HPA
      • nucleotide-excision repair complex Source: UniProtKB
      • nucleus Source: UniProtKB
      Complete GO annotation...

      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 rs587777627dbSNPEnsembl.1
      Natural variantiVAR_069335478S → N in CRCS10; associated with disease susceptibility. 1 PublicationCorresponds to variant rs397514632dbSNPEnsembl.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.
      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

      Keywords - PTMi

      Methylation

      Proteomic databases

      EPDiP28340.
      MaxQBiP28340.
      PaxDbiP28340.
      PeptideAtlasiP28340.
      PRIDEiP28340.

      PTM databases

      iPTMnetiP28340.
      PhosphoSitePlusiP28340.

      Miscellaneous databases

      PMAP-CutDBP28340.

      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.
      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).12 Publications

      Binary interactionsi

      WithEntry#Exp.IntActNotes
      PCNAP120043EBI-716569,EBI-358311
      POLD2P4900510EBI-716569,EBI-372354
      POLD4Q9HCU811EBI-716569,EBI-864968
      TERF2IPQ9NYB02EBI-716569,EBI-750109
      WRNIP1Q96S552EBI-716569,EBI-2513471

      Protein-protein interaction databases

      BioGridi111420. 63 interactors.
      IntActiP28340. 31 interactors.
      MINTiMINT-1414678.
      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
      Contains 1 CysA-type zinc finger.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. 2 hits.
      InterProiIPR006172. 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.
      IPR012337. RNaseH-like_dom.
      IPR025687. Znf-C4pol.
      [Graphical view]
      PfamiPF00136. DNA_pol_B. 1 hit.
      PF03104. DNA_pol_B_exo1. 1 hit.
      PF14260. zf-C4pol. 1 hit.
      [Graphical view]
      PRINTSiPR00106. DNAPOLB.
      SMARTiSM00486. POLBc. 1 hit.
      [Graphical view]
      SUPFAMiSSF53098. SSF53098. 1 hit.
      PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

      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

      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 rs9282830dbSNPEnsembl.1
      Natural variantiVAR_01934019R → H.1 PublicationCorresponds to variant rs3218773dbSNPEnsembl.1
      Natural variantiVAR_04887921G → C.Corresponds to variant rs9282831dbSNPEnsembl.1
      Natural variantiVAR_01614630R → W.2 PublicationsCorresponds to variant rs3218772dbSNPEnsembl.1
      Natural variantiVAR_019341119R → H.3 PublicationsCorresponds to variant rs1726801dbSNPEnsembl.1
      Natural variantiVAR_069333145A → D Found in a colorectal sample; somatic mutation. 1 Publication1
      Natural variantiVAR_019342173S → N.2 PublicationsCorresponds to variant rs1726803dbSNPEnsembl.1
      Natural variantiVAR_019343177R → H.1 PublicationCorresponds to variant rs3218750dbSNPEnsembl.1
      Natural variantiVAR_048880347P → L.Corresponds to variant rs2230243dbSNPEnsembl.1
      Natural variantiVAR_069334461Q → H Found in a colorectal sample; somatic mutation. 1 Publication1
      Natural variantiVAR_071966474L → P in CRCS10. 1 PublicationCorresponds to variant rs587777627dbSNPEnsembl.1
      Natural variantiVAR_069335478S → N in CRCS10; associated with disease susceptibility. 1 PublicationCorresponds to variant rs397514632dbSNPEnsembl.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 rs199783227dbSNPEnsembl.1
      Natural variantiVAR_069337808R → H Found in a colorectal sample; somatic mutation. 1 PublicationCorresponds to variant rs771700024dbSNPEnsembl.1
      Natural variantiVAR_019344849R → H.1 PublicationCorresponds to variant rs3218775dbSNPEnsembl.1
      Natural variantiVAR_069338864A → T Found in a colorectal sample; somatic mutation. 1 Publication1
      Natural variantiVAR_0193451086R → Q.1 PublicationCorresponds to variant rs3219457dbSNPEnsembl.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

      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. 63 interactors.
      IntActiP28340. 31 interactors.
      MINTiMINT-1414678.
      STRINGi9606.ENSP00000406046.

      Chemistry databases

      BindingDBiP28340.
      ChEMBLiCHEMBL2735.

      PTM databases

      iPTMnetiP28340.
      PhosphoSitePlusiP28340.

      Polymorphism and mutation databases

      BioMutaiPOLD1.
      DMDMi50403732.

      Proteomic databases

      EPDiP28340.
      MaxQBiP28340.
      PaxDbiP28340.
      PeptideAtlasiP28340.
      PRIDEiP28340.

      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.
      GeneCardsiPOLD1.
      H-InvDBHIX0202825.
      HGNCiHGNC:9175. POLD1.
      HPAiCAB004375.
      HPA046524.
      MalaCardsiPOLD1.
      MIMi174761. gene.
      612591. phenotype.
      615381. phenotype.
      neXtProtiNX_P28340.
      OpenTargetsiENSG00000062822.
      Orphaneti363649. Mandibular hypoplasia-deafness-progeroid syndrome.
      PharmGKBiPA33496.
      GenAtlasiSearch...

      Phylogenomic databases

      eggNOGiKOG0968. Eukaryota.
      COG0417. LUCA.
      GeneTreeiENSGT00560000077365.
      HOGENOMiHOG000036616.
      HOVERGENiHBG051395.
      InParanoidiP28340.
      KOiK02327.
      PhylomeDBiP28340.
      TreeFamiTF352785.

      Enzyme and pathway databases

      BioCyciZFISH:HS00772-MONOMER.
      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-CutDBP28340.
      PROiP28340.
      SOURCEiSearch...

      Gene expression databases

      BgeeiENSG00000062822.
      CleanExiHS_POLD1.
      ExpressionAtlasiP28340. baseline and differential.
      GenevisibleiP28340. HS.

      Family and domain databases

      Gene3Di3.30.420.10. 1 hit.
      3.90.1600.10. 2 hits.
      InterProiIPR006172. 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.
      IPR012337. RNaseH-like_dom.
      IPR025687. Znf-C4pol.
      [Graphical view]
      PfamiPF00136. DNA_pol_B. 1 hit.
      PF03104. DNA_pol_B_exo1. 1 hit.
      PF14260. zf-C4pol. 1 hit.
      [Graphical view]
      PRINTSiPR00106. DNAPOLB.
      SMARTiSM00486. POLBc. 1 hit.
      [Graphical view]
      SUPFAMiSSF53098. SSF53098. 1 hit.
      PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
      [Graphical view]
      ProtoNetiSearch...

      Entry informationi

      Entry nameiDPOD1_HUMAN
      AccessioniPrimary (citable) accession number: P28340
      Secondary accession number(s): Q8NER3, Q96H98
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: December 1, 1992
      Last sequence update: July 19, 2004
      Last modified: November 30, 2016
      This is version 173 of the entry and version 2 of the sequence. [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. Human chromosome 19
        Human chromosome 19: entries, gene names and cross-references to MIM
      2. Human entries with polymorphisms or disease mutations
        List of human entries with polymorphisms or disease mutations
      3. Human polymorphisms and disease mutations
        Index of human polymorphisms and disease mutations
      4. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
      5. SIMILARITY comments
        Index of protein domains and families

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.