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P27344

- DPB3_YEAST

UniProt

P27344 - DPB3_YEAST

Protein

DNA polymerase epsilon subunit C

Gene

DPB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. DNA-dependent DNA replication Source: SGD
    2. error-prone translesion synthesis Source: SGD
    3. heterochromatin organization involved in chromatin silencing Source: SGD
    4. leading strand elongation Source: SGD
    5. replicative senescence Source: SGD

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29198-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase epsilon subunit C (EC:2.7.7.7)
    Alternative name(s):
    DNA polymerase II subunit C
    Gene namesi
    Name:DPB3
    Ordered Locus Names:YBR278W
    ORF Names:YBR2015
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR278w.
    SGDiS000000482. DPB3.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. epsilon DNA polymerase complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201DNA polymerase epsilon subunit CPRO_0000208350Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei186 – 1861Phosphoserine3 Publications
    Modified residuei188 – 1881Phosphoserine1 Publication
    Modified residuei189 – 1891Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP27344.
    PaxDbiP27344.
    PeptideAtlasiP27344.

    Expressioni

    Gene expression databases

    GenevestigatoriP27344.

    Interactioni

    Subunit structurei

    DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DPB4Q046033EBI-6076,EBI-29938

    Protein-protein interaction databases

    BioGridi32972. 178 interactions.
    DIPiDIP-4803N.
    IntActiP27344. 13 interactions.
    MINTiMINT-482796.
    STRINGi4932.YBR278W.

    Structurei

    3D structure databases

    ProteinModelPortaliP27344.
    SMRiP27344. Positions 12-93.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi120 – 15435Asp/Glu-rich (acidic)Add
    BLAST

    Phylogenomic databases

    eggNOGiNOG309481.
    KOiK03506.
    OMAiSMEEDIP.
    OrthoDBiEOG7T1RQJ.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27344-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNLVKEKAP VFPISKVKKI AKCDPEYVIT SNVAISATAF AAELFVQNLV    50
    EESLVLAQLN SKGKTSLRLS LNSIEECVEK RDNFRFLEDA IKQLKKNSAL 100
    DKKRELNMQP GRSDQEVVIE EPELHEDDGV EEEEEEDEVS EEEEPVHNEE 150
    LLDDSKDQQN DKSTRSVASL LSRFQYKSAL DVGEHSDSSD IEVDHTKSTD 200
    P 201
    Length:201
    Mass (Da):22,665
    Last modified:October 1, 1994 - v2
    Checksum:i288913917D49C7F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1961T → M in CAA41403. (PubMed:1923754)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58500 Genomic DNA. Translation: CAA41403.1.
    X76053 Genomic DNA. Translation: CAA53641.1.
    Z36146 Genomic DNA. Translation: CAA85242.1.
    BK006936 Genomic DNA. Translation: DAA07393.1.
    PIRiS44540.
    RefSeqiNP_009837.1. NM_001178626.1.

    Genome annotation databases

    EnsemblFungiiYBR278W; YBR278W; YBR278W.
    GeneIDi852580.
    KEGGisce:YBR278W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58500 Genomic DNA. Translation: CAA41403.1 .
    X76053 Genomic DNA. Translation: CAA53641.1 .
    Z36146 Genomic DNA. Translation: CAA85242.1 .
    BK006936 Genomic DNA. Translation: DAA07393.1 .
    PIRi S44540.
    RefSeqi NP_009837.1. NM_001178626.1.

    3D structure databases

    ProteinModelPortali P27344.
    SMRi P27344. Positions 12-93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32972. 178 interactions.
    DIPi DIP-4803N.
    IntActi P27344. 13 interactions.
    MINTi MINT-482796.
    STRINGi 4932.YBR278W.

    Proteomic databases

    MaxQBi P27344.
    PaxDbi P27344.
    PeptideAtlasi P27344.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR278W ; YBR278W ; YBR278W .
    GeneIDi 852580.
    KEGGi sce:YBR278W.

    Organism-specific databases

    CYGDi YBR278w.
    SGDi S000000482. DPB3.

    Phylogenomic databases

    eggNOGi NOG309481.
    KOi K03506.
    OMAi SMEEDIP.
    OrthoDBi EOG7T1RQJ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29198-MONOMER.

    Miscellaneous databases

    NextBioi 971724.

    Gene expression databases

    Genevestigatori P27344.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning DPB3, the gene encoding the third subunit of DNA polymerase II of Saccharomyces cerevisiae."
      Araki H., Hamatake R.K., Morrison A., Johnson A.L., Johnston L.H., Sugino A.
      Nucleic Acids Res. 19:4867-4872(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204626 / S288c / A364A.
    2. "The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae."
      Holmstroem K., Brandt T., Kallesoe T.
      Yeast 10:S47-S62(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Structure and function of the fourth subunit (Dpb4p) of DNA polymerase epsilon in Saccharomyces cerevisiae."
      Ohya T., Maki S., Kawasaki Y., Sugino A.
      Nucleic Acids Res. 28:3846-3852(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    6. "Fidelity of DNA polymerase epsilon holoenzyme from budding yeast Saccharomyces cerevisiae."
      Shimizu K., Hashimoto K., Kirchner J.M., Nakai W., Nishikawa H., Resnick M.A., Sugino A.
      J. Biol. Chem. 277:37422-37429(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The quaternary structure of DNA polymerase epsilon from Saccharomyces cerevisiae."
      Chilkova O., Jonsson B.-H., Johansson E.
      J. Biol. Chem. 278:14082-14086(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPOSITION OF THE DNA POLYMERASE EPSILON COMPLEX.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-188 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDPB3_YEAST
    AccessioniPrimary (citable) accession number: P27344
    Secondary accession number(s): D6VQS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
    Present with 784 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3