DPB2_YEAST
ID DPB2_YEAST Reviewed; 689 AA.
AC P24482; D6W4H6; Q06622;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=DNA polymerase epsilon subunit B;
DE AltName: Full=DNA polymerase II subunit 2;
GN Name=DPB2; OrderedLocusNames=YPR175W; ORFNames=P9705.7;
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=YHA8;
RX PubMed=2052544; DOI=10.1073/pnas.88.11.4601;
RA Araki H., Hamatake R.K., Johnston L.H., Sugino A.;
RT "DPB2, the gene encoding DNA polymerase II subunit B, is required for
RT chromosome replication in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4601-4605(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 132-144 AND 606-622, PHOSPHORYLATION AT SER-141 AND
RP SER-613, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14747467; DOI=10.1074/jbc.m313289200;
RA Kesti T., McDonald W.H., Yates J.R. III, Wittenberg C.;
RT "Cell cycle-dependent phosphorylation of the DNA polymerase epsilon
RT subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase.";
RL J. Biol. Chem. 279:14245-14255(2004).
RN [5]
RP SUBUNIT.
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 IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP 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 complex
CC participates in chromosomal DNA replication. It is required during
CC synthesis of the leading and lagging DNA strands at the replication
CC fork and binds at/or near replication origins and moves along DNA with
CC the replication fork. It has 3'-5' proofreading exonuclease activity
CC that correct errors arising during DNA replication. It is also involved
CC in DNA synthesis during DNA repair. {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 -!- INTERACTION:
CC P24482; P21951: POL2; NbExp=7; IntAct=EBI-6071, EBI-6140;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated in a cell cycle dependent manner during late G1
CC phase. Phosphorylation may facilitate the interaction with POL2 or the
CC activity of DNA polymerase II. Phosphorylation is independent of DNA
CC replication but dependent upon CDC28 in vivo. Both Ser-141 and Ser-613
CC are phosphorylated in vivo, but in vitro only Ser-141 is phosphorylated
CC by CDC28. {ECO:0000269|PubMed:14747467}.
CC -!- MISCELLANEOUS: Present with 3110 +/- 251 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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 -!- SIMILARITY: Belongs to the DNA polymerase epsilon subunit B family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34576.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB68109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M61710; AAA34576.1; ALT_INIT; Genomic_DNA.
DR EMBL; U25842; AAB68109.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11592.1; -; Genomic_DNA.
DR PIR; S59833; S59833.
DR RefSeq; NP_015501.2; NM_001184272.1.
DR PDB; 6HV8; EM; 4.40 A; B=1-689.
DR PDB; 6HV9; EM; 4.98 A; B=1-689.
DR PDB; 6WJV; EM; 3.50 A; 2=1-689.
DR PDB; 7PMK; EM; 3.20 A; R=1-689.
DR PDB; 7PMN; EM; 3.20 A; R=1-689.
DR PDBsum; 6HV8; -.
DR PDBsum; 6HV9; -.
DR PDBsum; 6WJV; -.
DR PDBsum; 7PMK; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; P24482; -.
DR SMR; P24482; -.
DR BioGRID; 36348; 80.
DR ComplexPortal; CPX-2110; DNA polymerase epsilon complex.
DR DIP; DIP-2533N; -.
DR IntAct; P24482; 25.
DR MINT; P24482; -.
DR STRING; 4932.YPR175W; -.
DR iPTMnet; P24482; -.
DR MaxQB; P24482; -.
DR PaxDb; P24482; -.
DR PRIDE; P24482; -.
DR EnsemblFungi; YPR175W_mRNA; YPR175W; YPR175W.
DR GeneID; 856305; -.
DR KEGG; sce:YPR175W; -.
DR SGD; S000006379; DPB2.
DR VEuPathDB; FungiDB:YPR175W; -.
DR eggNOG; KOG3818; Eukaryota.
DR GeneTree; ENSGT00390000012435; -.
DR HOGENOM; CLU_010628_1_0_1; -.
DR InParanoid; P24482; -.
DR OMA; GWVDFLG; -.
DR BioCyc; YEAST:G3O-34302-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:P24482; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P24482; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:SGD.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IMP:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR016266; POLE2.
DR PANTHER; PTHR12708; PTHR12708; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cytoplasm; Direct protein sequencing;
KW DNA replication; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..689
FT /note="DNA polymerase epsilon subunit B"
FT /id="PRO_0000071573"
FT REGION 98..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 141
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:14747467"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14747467"
FT CONFLICT 458
FT /note="F -> Y (in Ref. 1; AAA34576)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="K -> R (in Ref. 1; AAA34576)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="V -> F (in Ref. 1; AAA34576)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="E -> Q (in Ref. 1; AAA34576)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="T -> I (in Ref. 1; AAA34576)"
FT /evidence="ECO:0000305"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 201..205
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 211..231
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 411..424
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 454..470
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 473..478
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 546..553
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 594..609
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:6WJV"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 624..629
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 682..688
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 689 AA; 78340 MW; 0936E3FC90552788 CRC64;
MFGSGNVLPV KIQPPLLRPL AYRVLSRKYG LSIKSDGLSA LAEFVGTNIG ANWRQGPATI
KFLEQFAAVW KQQERGLFID QSGVKEVIQE MKEREKVEWS HEHPIQHEEN ILGRTDDDEN
NSDDEMPIAA DSSLQNVSLS SPMRQPTERD EYKQPFKPES SKALDWRDYF KVINASQQQR
FSYNPHKMQF IFVPNKKQNG LGGIAGFLPD IEDKVQMFLT RYYLTNDRVM RNENFQNSDM
FNPLSSMVSL QNELSNTNRQ QQSSSMSITP IKNLLGRDAQ NFLLLGLLNK NFKGNWSLED
PSGSVEIDIS QTIPTQGHYY VPGCMVLVEG IYYSVGNKFH VTSMTLPPGE RREITLETIG
NLDLLGIHGI SNNNFIARLD KDLKIRLHLL EKELTDHKFV ILGANLFLDD LKIMTALSKI
LQKLNDDPPT LLIWQGSFTS VPVFASMSSR NISSSTQFKN NFDALATLLS RFDNLTENTT
MIFIPGPNDL WGSMVSLGAS GTLPQDPIPS AFTKKINKVC KNVVWSSNPT RIAYLSQEIV
IFRDDLSGRF KRHRLEFPFN ESEDVYTEND NMMSKDTDIV PIDELVKEPD QLPQKVQETR
KLVKTILDQG HLSPFLDSLR PISWDLDHTL TLCPIPSTMV LCDTTSAQFD LTYNGCKVIN
PGSFIHNRRA RYMEYVPSSK KTIQEEIYI
