DPB3_YEAST
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 03-AUG-2022, entry version 170.
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 SMR; P27344; -.
DR BioGRID; 32972; 304.
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; P27344; -.
DR PRIDE; P27344; -.
DR EnsemblFungi; YBR278W_mRNA; YBR278W; YBR278W.
DR GeneID; 852580; -.
DR KEGG; sce:YBR278W; -.
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 BioCyc; YEAST:G3O-29198-MON; -.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-68952; DNA replication initiation.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
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 GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR SUPFAM; SSF47113; SSF47113; 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
