ID   DPB3_YEAST              Reviewed;         201 AA.
AC   P27344; D6VQS3;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=DNA polymerase epsilon subunit C;
DE   AltName: Full=DNA polymerase II subunit C;
GN   Name=DPB3; OrderedLocusNames=YBR278W; ORFNames=YBR2015;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204626 / S288c / A364A;
RX   PubMed=1923754; DOI=10.1093/nar/19.18.4867;
RA   Araki H., Hamatake R.K., Morrison A., Johnson A.L., Johnston L.H.,
RA   Sugino A.;
RT   "Cloning DPB3, the gene encoding the third subunit of DNA polymerase II of
RT   Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 19:4867-4872(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091861; DOI=10.1002/yea.320100007;
RA   Holmstroem K., Brandt T., Kallesoe T.;
RT   "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT   II from Saccharomyces cerevisiae.";
RL   Yeast 10:S47-S62(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11024162; DOI=10.1093/nar/28.20.3846;
RA   Ohya T., Maki S., Kawasaki Y., Sugino A.;
RT   "Structure and function of the fourth subunit (Dpb4p) of DNA polymerase
RT   epsilon in Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 28:3846-3852(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=12124389; DOI=10.1074/jbc.m204476200;
RA   Shimizu K., Hashimoto K., Kirchner J.M., Nakai W., Nishikawa H.,
RA   Resnick M.A., Sugino A.;
RT   "Fidelity of DNA polymerase epsilon holoenzyme from budding yeast
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 277:37422-37429(2002).
RN   [7]
RP   COMPOSITION OF THE DNA POLYMERASE EPSILON COMPLEX.
RX   PubMed=12571237; DOI=10.1074/jbc.m211818200;
RA   Chilkova O., Jonsson B.-H., Johansson E.;
RT   "The quaternary structure of DNA polymerase epsilon from Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 278:14082-14086(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-188 AND SER-189, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: As accessory component of the DNA polymerase epsilon (DNA
CC       polymerase II) participates in chromosomal DNA replication. It is
CC       required during synthesis of the leading and lagging DNA strands at the
CC       replication fork and binds at/or near replication origins and moves
CC       along DNA with the replication fork. It has 3'-5' proofreading
CC       exonuclease activity that correct errors arising during DNA
CC       replication. It is also involved in DNA synthesis during DNA repair.
CC       {ECO:0000269|PubMed:12124389}.
CC   -!- SUBUNIT: DNA polymerase epsilon is a heterotetramer consisting of POL2,
CC       DPB2, DPB3 and DPB4. {ECO:0000269|PubMed:11024162}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11024162}.
CC   -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC       beta, gamma, delta, and epsilon which are responsible for different
CC       reactions of DNA synthesis.
CC   -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X58500; CAA41403.1; -; Genomic_DNA.
DR   EMBL; X76053; CAA53641.1; -; Genomic_DNA.
DR   EMBL; Z36146; CAA85242.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07393.1; -; Genomic_DNA.
DR   PIR; S44540; S44540.
DR   RefSeq; NP_009837.1; NM_001178626.1.
DR   PDB; 6WJV; EM; 3.50 A; 3=1-201.
DR   PDBsum; 6WJV; -.
DR   AlphaFoldDB; P27344; -.
DR   EMDB; EMD-21701; -.
DR   SMR; P27344; -.
DR   BioGRID; 32972; 308.
DR   ComplexPortal; CPX-2110; DNA polymerase epsilon complex.
DR   DIP; DIP-4803N; -.
DR   IntAct; P27344; 17.
DR   MINT; P27344; -.
DR   STRING; 4932.YBR278W; -.
DR   iPTMnet; P27344; -.
DR   MaxQB; P27344; -.
DR   PaxDb; 4932-YBR278W; -.
DR   PeptideAtlas; P27344; -.
DR   EnsemblFungi; YBR278W_mRNA; YBR278W; YBR278W.
DR   GeneID; 852580; -.
DR   KEGG; sce:YBR278W; -.
DR   AGR; SGD:S000000482; -.
DR   SGD; S000000482; DPB3.
DR   VEuPathDB; FungiDB:YBR278W; -.
DR   eggNOG; KOG1658; Eukaryota.
DR   GeneTree; ENSGT00940000166127; -.
DR   HOGENOM; CLU_1332610_0_0_1; -.
DR   InParanoid; P27344; -.
DR   OMA; ALDGWPK; -.
DR   OrthoDB; 2031893at2759; -.
DR   BioCyc; YEAST:G3O-29198-MONOMER; -.
DR   Reactome; R-SCE-68952; DNA replication initiation.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   BioGRID-ORCS; 852580; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P27344; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P27344; Protein.
DR   GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IDA:SGD.
DR   GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IDA:SGD.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR   GO; GO:0006272; P:leading strand elongation; IMP:SGD.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   PANTHER; PTHR10252:SF54; CHROMATIN ACCESSIBILITY COMPLEX PROTEIN 1; 1.
DR   PANTHER; PTHR10252; HISTONE-LIKE TRANSCRIPTION FACTOR CCAAT-RELATED; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..201
FT                   /note="DNA polymerase epsilon subunit C"
FT                   /id="PRO_0000208350"
FT   REGION          102..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..148
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        196
FT                   /note="T -> M (in Ref. 1; CAA41403)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..19
FT                   /evidence="ECO:0007829|PDB:6WJV"
FT   HELIX           34..52
FT                   /evidence="ECO:0007829|PDB:6WJV"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:6WJV"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:6WJV"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:6WJV"
FT   HELIX           71..80
FT                   /evidence="ECO:0007829|PDB:6WJV"
FT   TURN            83..86
FT                   /evidence="ECO:0007829|PDB:6WJV"
SQ   SEQUENCE   201 AA;  22665 MW;  288913917D49C7F9 CRC64;
     MSNLVKEKAP VFPISKVKKI AKCDPEYVIT SNVAISATAF AAELFVQNLV EESLVLAQLN
     SKGKTSLRLS LNSIEECVEK RDNFRFLEDA IKQLKKNSAL DKKRELNMQP GRSDQEVVIE
     EPELHEDDGV EEEEEEDEVS EEEEPVHNEE LLDDSKDQQN DKSTRSVASL LSRFQYKSAL
     DVGEHSDSSD IEVDHTKSTD P
//