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P28340

- DPOD1_HUMAN

UniProt

P28340 - DPOD1_HUMAN

Protein

DNA polymerase delta catalytic subunit

Gene

POLD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.

    Catalytic activityi

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

    Cofactori

    Binds 1 4Fe-4S cluster.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1012 – 10121ZincBy similarity
    Metal bindingi1015 – 10151ZincBy similarity
    Metal bindingi1026 – 10261ZincBy similarity
    Metal bindingi1029 – 10291ZincBy similarity
    Metal bindingi1058 – 10581Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi1061 – 10611Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi1071 – 10711Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi1076 – 10761Iron-sulfur (4Fe-4S)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1012 – 102918CysA-typeAdd
    BLAST

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: RefGenome
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. chromatin binding Source: UniProtKB
    4. DNA binding Source: UniProtKB
    5. DNA-directed DNA polymerase activity Source: UniProtKB
    6. metal ion binding Source: UniProtKB-KW
    7. nucleotide binding Source: InterPro
    8. protein binding Source: UniProtKB

    GO - Biological processi

    1. base-excision repair Source: Reactome
    2. base-excision repair, gap-filling Source: UniProtKB
    3. DNA repair Source: Reactome
    4. DNA replication Source: UniProtKB
    5. DNA replication, removal of RNA primer Source: RefGenome
    6. DNA replication proofreading Source: RefGenome
    7. DNA strand elongation involved in DNA replication Source: Reactome
    8. DNA synthesis involved in DNA repair Source: UniProtKB
    9. fatty acid homeostasis Source: UniProtKB
    10. mitotic cell cycle Source: Reactome
    11. nucleic acid phosphodiester bond hydrolysis Source: GOC
    12. nucleotide-excision repair Source: Reactome
    13. nucleotide-excision repair, DNA gap filling Source: UniProtKB
    14. regulation of mitotic cell cycle Source: RefGenome
    15. response to UV Source: ProtInc
    16. small molecule metabolic process Source: Reactome
    17. telomere maintenance Source: Reactome
    18. telomere maintenance via recombination Source: Reactome
    19. telomere maintenance via semi-conservative replication Source: Reactome
    20. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
    REACT_1385. Processive synthesis on the lagging strand.
    REACT_160176. Cytosolic iron-sulfur cluster assembly.
    REACT_1792. Polymerase switching.
    REACT_1838. Leading Strand Synthesis.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2192. Removal of DNA patch containing abasic residue.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_70. Removal of the Flap Intermediate.
    REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
    REACT_7987. Polymerase switching on the C-strand of the telomere.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.
    REACT_8027. Processive synthesis on the C-strand of the telomere.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase delta catalytic subunit (EC:2.7.7.7)
    Alternative name(s):
    DNA polymerase subunit delta p125
    Gene namesi
    Name:POLD1
    Synonyms:POLD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9175. POLD1.

    Subcellular locationi

    GO - Cellular componenti

    1. aggresome Source: HPA
    2. cytoplasm Source: HPA
    3. delta DNA polymerase complex Source: RefGenome
    4. membrane Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. nucleotide-excision repair complex Source: UniProtKB
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Colorectal cancer 10 (CRCS10) [MIM:612591]: A 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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti478 – 4781S → N in CRCS10; associated with disease susceptibility. 1 Publication
    VAR_069335
    Mandibular hypoplasia, deafness, progeroid features, and lipodystrophy syndrome (MDPL) [MIM:615381]: An 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti605 – 6051Missing 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 Publication
    VAR_070231

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612591. phenotype.
    615381. phenotype.
    Orphaneti363649. Mandibular hypoplasia-deafness-progeroid syndrome.
    PharmGKBiPA33496.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11071107DNA polymerase delta catalytic subunitPRO_0000046442Add
    BLAST

    Proteomic databases

    MaxQBiP28340.
    PaxDbiP28340.
    PRIDEiP28340.

    PTM databases

    PhosphoSiteiP28340.

    Miscellaneous databases

    PMAP-CutDBP28340.

    Expressioni

    Tissue specificityi

    Expressed across a panel of tissues, with high levels of expression in heart and lung.1 Publication

    Gene expression databases

    ArrayExpressiP28340.
    BgeeiP28340.
    CleanExiHS_POLD1.
    GenevestigatoriP28340.

    Organism-specific databases

    HPAiCAB004375.
    HPA046524.

    Interactioni

    Subunit structurei

    Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. The 125 kDa subunit contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity. Interacts with WRNIP1. Interacts with POLD4 and PCNA.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PCNAP120042EBI-716569,EBI-358311
    POLD2P490059EBI-716569,EBI-372354
    POLD4Q9HCU810EBI-716569,EBI-864968
    WRNIP1Q96S552EBI-716569,EBI-2513471

    Protein-protein interaction databases

    BioGridi111420. 48 interactions.
    IntActiP28340. 18 interactions.
    MINTiMINT-1414678.
    STRINGi9606.ENSP00000262266.

    Structurei

    3D structure databases

    ProteinModelPortaliP28340.
    SMRiP28340. Positions 124-1000.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4 – 1916Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi1058 – 107619CysB motifAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1012 – 102918CysA-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0417.
    HOGENOMiHOG000036616.
    HOVERGENiHBG051395.
    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

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    MDGKRRPGPG PGVPPKRARG GLWDDDDAPR PSQFEEDLAL MEEMEAEHRL     50
    QEQEEEELQS VLEGVADGQV PPSAIDPRWL RPTPPALDPQ TEPLIFQQLE 100
    IDHYVGPAQP VPGGPPPSRG SVPVLRAFGV TDEGFSVCCH IHGFAPYFYT 150
    PAPPGFGPEH MGDLQRELNL AISRDSRGGR ELTGPAVLAV ELCSRESMFG 200
    YHGHGPSPFL RITVALPRLV APARRLLEQG IRVAGLGTPS FAPYEANVDF 250
    EIRFMVDTDI VGCNWLELPA GKYALRLKEK ATQCQLEADV LWSDVVSHPP 300
    EGPWQRIAPL RVLSFDIECA GRKGIFPEPE RDPVIQICSL GLRWGEPEPF 350
    LRLALTLRPC APILGAKVQS YEKEEDLLQA WSTFIRIMDP DVITGYNIQN 400
    FDLPYLISRA QTLKVQTFPF LGRVAGLCSN IRDSSFQSKQ TGRRDTKVVS 450
    MVGRVQMDML QVLLREYKLR SYTLNAVSFH FLGEQKEDVQ HSIITDLQNG 500
    NDQTRRRLAV YCLKDAYLPL RLLERLMVLV NAVEMARVTG VPLSYLLSRG 550
    QQVKVVSQLL RQAMHEGLLM PVVKSEGGED YTGATVIEPL KGYYDVPIAT 600
    LDFSSLYPSI MMAHNLCYTT LLRPGTAQKL GLTEDQFIRT PTGDEFVKTS 650
    VRKGLLPQIL ENLLSARKRA KAELAKETDP LRRQVLDGRQ LALKVSANSV 700
    YGFTGAQVGK LPCLEISQSV TGFGRQMIEK TKQLVESKYT VENGYSTSAK 750
    VVYGDTDSVM CRFGVSSVAE AMALGREAAD WVSGHFPSPI RLEFEKVYFP 800
    YLLISKKRYA GLLFSSRPDA HDRMDCKGLE AVRRDNCPLV ANLVTASLRR 850
    LLIDRDPEGA VAHAQDVISD LLCNRIDISQ LVITKELTRA ASDYAGKQAH 900
    VELAERMRKR DPGSAPSLGD RVPYVIISAA KGVAAYMKSE DPLFVLEHSL 950
    PIDTQYYLEQ QLAKPLLRIF EPILGEGRAE AVLLRGDHTR CKTVLTGKVG 1000
    GLLAFAKRRN CCIGCRTVLS HQGAVCEFCQ PRESELYQKE VSHLNALEER 1050
    FSRLWTQCQR CQGSLHEDVI CTSRDCPIFY MRKKVRKDLE DQEQLLRRFG 1100
    PPGPEAW 1107
    Length:1,107
    Mass (Da):123,631
    Last modified:July 19, 2004 - v2
    Checksum:i9D04D34AB4AEE810
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti472 – 4721Y → H in AAA58439. (PubMed:1722322)Curated
    Sequence conflicti776 – 7761R → G in AAA35768. (PubMed:1542570)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51R → W.
    Corresponds to variant rs9282830 [ dbSNP | Ensembl ].
    VAR_048878
    Natural varianti19 – 191R → H.1 Publication
    Corresponds to variant rs3218773 [ dbSNP | Ensembl ].
    VAR_019340
    Natural varianti21 – 211G → C.
    Corresponds to variant rs9282831 [ dbSNP | Ensembl ].
    VAR_048879
    Natural varianti30 – 301R → W.2 Publications
    Corresponds to variant rs3218772 [ dbSNP | Ensembl ].
    VAR_016146
    Natural varianti119 – 1191R → H.3 Publications
    Corresponds to variant rs1726801 [ dbSNP | Ensembl ].
    VAR_019341
    Natural varianti145 – 1451A → D Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069333
    Natural varianti173 – 1731S → N.2 Publications
    Corresponds to variant rs1726803 [ dbSNP | Ensembl ].
    VAR_019342
    Natural varianti177 – 1771R → H.1 Publication
    Corresponds to variant rs3218750 [ dbSNP | Ensembl ].
    VAR_019343
    Natural varianti347 – 3471P → L.
    Corresponds to variant rs2230243 [ dbSNP | Ensembl ].
    VAR_048880
    Natural varianti461 – 4611Q → H Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069334
    Natural varianti478 – 4781S → N in CRCS10; associated with disease susceptibility. 1 Publication
    VAR_069335
    Natural varianti605 – 6051Missing 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 Publication
    VAR_070231
    Natural varianti787 – 7871P → L Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069336
    Natural varianti808 – 8081R → H Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069337
    Natural varianti849 – 8491R → H.1 Publication
    Corresponds to variant rs3218775 [ dbSNP | Ensembl ].
    VAR_019344
    Natural varianti864 – 8641A → T Found in a colorectal sample; somatic mutation. 1 Publication
    VAR_069338
    Natural varianti1086 – 10861R → Q.1 Publication
    Corresponds to variant rs3219457 [ dbSNP | Ensembl ].
    VAR_019345

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiHs.279413.

    Genome annotation databases

    EnsembliENST00000440232; ENSP00000406046; ENSG00000062822.
    ENST00000599857; ENSP00000473052; ENSG00000062822.
    GeneIDi5424.
    KEGGihsa:5424.
    UCSCiuc002psb.5. human.

    Polymorphism databases

    DMDMi50403732.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80397 mRNA. Translation: AAA58439.1 .
    M81735 mRNA. Translation: AAA35768.1 .
    AY129569 Genomic DNA. Translation: AAM76971.1 .
    BC008800 mRNA. Translation: AAH08800.1 .
    CCDSi CCDS12795.1.
    PIRi A41618.
    RefSeqi NP_001243778.1. NM_001256849.1.
    NP_002682.2. NM_002691.3.
    UniGenei Hs.279413.

    3D structure databases

    ProteinModelPortali P28340.
    SMRi P28340. Positions 124-1000.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111420. 48 interactions.
    IntActi P28340. 18 interactions.
    MINTi MINT-1414678.
    STRINGi 9606.ENSP00000262266.

    Chemistry

    BindingDBi P28340.
    ChEMBLi CHEMBL2735.

    PTM databases

    PhosphoSitei P28340.

    Polymorphism databases

    DMDMi 50403732.

    Proteomic databases

    MaxQBi P28340.
    PaxDbi P28340.
    PRIDEi P28340.

    Protocols and materials databases

    DNASUi 5424.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000440232 ; ENSP00000406046 ; ENSG00000062822 .
    ENST00000599857 ; ENSP00000473052 ; ENSG00000062822 .
    GeneIDi 5424.
    KEGGi hsa:5424.
    UCSCi uc002psb.5. human.

    Organism-specific databases

    CTDi 5424.
    GeneCardsi GC19P050889.
    H-InvDB HIX0202825.
    HGNCi HGNC:9175. POLD1.
    HPAi CAB004375.
    HPA046524.
    MIMi 174761. gene.
    612591. phenotype.
    615381. phenotype.
    neXtProti NX_P28340.
    Orphaneti 363649. Mandibular hypoplasia-deafness-progeroid syndrome.
    PharmGKBi PA33496.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0417.
    HOGENOMi HOG000036616.
    HOVERGENi HBG051395.
    KOi K02327.
    PhylomeDBi P28340.
    TreeFami TF352785.

    Enzyme and pathway databases

    Reactomei REACT_1128. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
    REACT_1385. Processive synthesis on the lagging strand.
    REACT_160176. Cytosolic iron-sulfur cluster assembly.
    REACT_1792. Polymerase switching.
    REACT_1838. Leading Strand Synthesis.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2192. Removal of DNA patch containing abasic residue.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_70. Removal of the Flap Intermediate.
    REACT_7961. Telomere C-strand (Lagging Strand) Synthesis.
    REACT_7987. Polymerase switching on the C-strand of the telomere.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.
    REACT_8027. Processive synthesis on the C-strand of the telomere.

    Miscellaneous databases

    GeneWikii POLD1.
    GenomeRNAii 5424.
    NextBioi 20985.
    PMAP-CutDB P28340.
    PROi P28340.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28340.
    Bgeei P28340.
    CleanExi HS_POLD1.
    Genevestigatori P28340.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    3.90.1600.10. 2 hits.
    InterProi 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.
    IPR012337. RNaseH-like_dom.
    IPR025687. Znf-C4pol.
    [Graphical view ]
    Pfami PF00136. DNA_pol_B. 1 hit.
    PF03104. DNA_pol_B_exo1. 1 hit.
    PF14260. zf-C4pol. 1 hit.
    [Graphical view ]
    PRINTSi PR00106. DNAPOLB.
    SMARTi SM00486. POLBc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    PROSITEi PS00116. DNA_POLYMERASE_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the catalytic subunit of human DNA polymerase delta and chromosomal location of the gene."
      Chung D.W., Zhang J., Tan C.-K., Davie E.W., So A.G., Downey K.M.
      Proc. Natl. Acad. Sci. U.S.A. 88:11197-11201(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TRP-30.
    2. "Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase delta."
      Yang C.-L., Chang L.-S., Zhang P., Hao H., Zhu L., Toomey N.L., Lee M.Y.W.T.
      Nucleic Acids Res. 20:735-745(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-119 AND ASN-173.
    3. NIEHS SNPs program
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-19; TRP-30; HIS-119; ASN-173; HIS-177; HIS-849 AND GLN-1086.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-119.
      Tissue: Lymph.
    5. "Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta."
      Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.
      Genes Cells 10:13-22(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WRNIP1.
    6. "Functional roles of p12, the fourth subunit of human DNA polymerase delta."
      Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., Lee M.Y.
      J. Biol. Chem. 281:14748-14755(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLD4 AND PCNA.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: TISSUE SPECIFICITY, VARIANT MDPL SER-605 DEL.
    10. Cited for: VARIANT CRCS10 ASN-478, VARIANTS ASP-145; HIS-461; LEU-787; HIS-808 AND THR-864.

    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: October 1, 2014
    This is version 149 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

    Miscellaneous

    In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

    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

    External Data

    Dasty 3