Reviewed, UniProtKB/Swiss-Prot P21951 (DPOE_YEAST)

Names and origin

Protein names

Recommended name:
    DNA polymerase epsilon catalytic subunit A
      Short name=DNA polymerase II subunit A
    EC=2.7.7.7

Gene names

Name:	POL2
Synonyms:	DUN2
Ordered Locus Names:	YNL262W
ORF Names:	N0825

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.6
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4. Ref.5
Subcellular location	Nucleus.
Domain	The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C.
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 1970 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the DNA polymerase type-B family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA replication during S phase Ref.4 Inferred from expression pattern. Source: SGD DNA synthesis during DNA repair Inferred from mutant phenotype. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD double-strand break repair via nonhomologous end joining Inferred from genetic interaction. Source: SGD lagging strand elongation Traceable author statement. Source: SGD leading strand elongation Traceable author statement. Source: SGD mismatch repair Traceable author statement. Source: SGD mitotic sister chromatid cohesion Inferred from mutant phenotype. Source: SGD nucleotide-excision repair Traceable author statement. Source: SGD
Cellular component	epsilon DNA polymerase complex Inferred from direct assay. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Ref.4 Inferred from mutant phenotype. Source: SGD nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2222	2222	DNA polymerase epsilon catalytic subunit A		PRO_0000046467
Regions
	Zinc finger	2108 – 2181	74	C4-type Potential
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	644	1	M → I in POL2-9; temperature-sensitive mutant. Ref.4
	Mutagenesis	710	1	P → S in POL2-18; temperature-sensitive mutant. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P21951-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: CBCDDE2AB147D65B	FASTA	2,222	255,671
	10 20 30 40 50 60 MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM GFERYVPPQY 70 80 90 100 110 120 NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG NSNDGERVTT NQGISGVDFY 130 140 150 160 170 180 FLDEEGGSFK STVVYDPYFF IACNDESRVN DVEELVKKYL ESCLKSLQII RKEDLTMDNH 190 200 210 220 230 240 LLGLQKTLIK LSFVNSNQLF EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE 250 260 270 280 290 300 DIREYDVPYH VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF 310 320 330 340 350 360 PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF NENDEVALLQ 370 380 390 400 410 420 RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD EIGFAPDAEG EYKSSYCSHM 430 440 450 460 470 480 DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN PIELDPELMT PYAFEKPQHL SEYSVSDAVA 490 500 510 520 530 540 TYYLYMKYVH PFIFSLCTII PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE 550 560 570 580 590 600 RFYDGHLLES ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN 610 620 630 640 650 660 KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT TNRLQPDSIK 670 680 690 700 710 720 AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI KRALQNETFP NKNKFSKKKV 730 740 750 760 770 780 LTFDELSYAD QVIHIKKRLT EYSRKVYHRV KVSEIVEREA IVCQRENPFY VDTVKSFRDR 790 800 810 820 830 840 RYEFKGLAKT WKGNLSKIDP SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR 850 860 870 880 890 900 WYSMEMAGIT CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK 910 920 930 940 950 960 LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY KAMILPSSKE 970 980 990 1000 1010 1020 EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS DIFKVFLEGD TLEGCYSAVA 1030 1040 1050 1060 1070 1080 SVCNRWLDVL DSHGLMLEDE DLVSLICENR SMSKTLKEYE GQKSTSITTA RRLGDFLGED 1090 1100 1110 1120 1130 1140 MVKDKGLQCK YIISSKPFNA PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI 1150 1160 1170 1180 1190 1200 IDWGYYRERL GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF 1210 1220 1230 1240 1250 1260 SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT NEEDPLVLPS 1270 1280 1290 1300 1310 1320 EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS RERSALGSMI RKQAESYANS 1330 1340 1350 1360 1370 1380 TWEVLQYKDS GEPGVLEVFV TINGKVQNIT FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS 1390 1400 1410 1420 1430 1440 ASLPNNPKTS NPAGGQLFKI TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD 1450 1460 1470 1480 1490 1500 LGASVTFRSK AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS 1510 1520 1530 1540 1550 1560 LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV DIKEDINFEF 1570 1580 1590 1600 1610 1620 VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL LGTIRLLNQM PIVKLSLNEV 1630 1640 1650 1660 1670 1680 LLPQLNWQPT LLKKLVNHVL SSGSWISHLI KLSQYSNIPI CNLRLDSMDY IIDVLYARKL 1690 1700 1710 1720 1730 1740 KKENIVLWWN EKAPLPDHGG IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT 1750 1760 1770 1780 1790 1800 VNTILTSALI NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD 1810 1820 1830 1840 1850 1860 EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE FSALGSTIVY 1870 1880 1890 1900 1910 1920 ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL NIKRYWDLLI WMDKFNFSGL 1930 1940 1950 1960 1970 1980 ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ PEFEDWMMII LDSMLKTKQS YLKLNSGTQR 1990 2000 2010 2020 2030 2040 PTQIVNVKKQ DKEDSVENSL NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL 2050 2060 2070 2080 2090 2100 PGSHLNVKNP LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS 2110 2120 2130 2140 2150 2160 LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL RSDIESYLIQ 2170 2180 2190 2200 2210 2220 DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV FKQVAKYYGF DILLSCIADL TI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A third essential DNA polymerase in S. cerevisiae." Morrison A., Araki H., Clark A.B., Hamatake R.K., Sugino A. Cell 62:1143-1151(1990) [PubMed: 2169349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1214-1221.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The sequence of a 24,152 bp segment from the left arm of chromosome XIV from Saccharomyces cerevisiae between the BNI1 and the POL2 genes." Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H. Yeast 12:505-514(1996) [PubMed: 8740425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2221. Strain: ATCC 96604 / S288c / FY1679.
[4]	"DNA polymerase II, the probable homolog of mammalian DNA polymerase epsilon, replicates chromosomal DNA in the yeast Saccharomyces cerevisiae." Araki H., Ropp P.A., Johnson A.L., Johnston L.H., Morrison A., Sugino A. EMBO J. 11:733-740(1992) [PubMed: 1537345] [Abstract] Cited for: MUTAGENESIS OF MET-644 AND PRO-710.
[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: 11024162] [Abstract] Cited for: SUBUNIT.
[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: 12124389] [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: 12571237] [Abstract] Cited for: COMPOSITION OF THE DNA POLYMERASE EPSILON COMPLEX.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60416 Genomic DNA. Translation: AAA88711.1. X92494 Genomic DNA. Translation: CAA63235.1. Z71538 Genomic DNA. Translation: CAA96169.1.
PIR	A36028.
RefSeq	NP_014137.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2532N.
STRING	P21951.
Proteomic databases
PeptideAtlas	P21951.
PRIDE	P21951.
Genome annotation databases
Ensembl	YNL262W; YNL262W; YNL262W; Saccharomyces cerevisiae. [Genome view]
GeneID	855459.
GenomeReviews	Gene locus YNL262W in contig Y13139_GR.
KEGG	sce:YNL262W.
NMPDR	fig|4932.3.peg.5202.
Organism-specific databases
CYGD	YNL262w.
SGD	S000005206. POL2.
Phylogenomic databases
HOGENOM	P21951.
OMA	WESQEES.
Enzyme and pathway databases
BRENDA	2.7.7.7. 250.
Gene expression databases
ArrayExpress	P21951.
Genevestigator	P21951.
GermOnline	YNL262W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006172. DNA-dir_DNA_pol_B. IPR006134. DNA-dir_DNA_pol_B_cons-reg. IPR017964. DNA-dir_DNA_pol_B_CS. IPR006133. DNA-dir_DNA_pol_B_exonuc. IPR013697. DUF1744. [Graphical view]
Pfam	PF00136. DNA_pol_B. 1 hit. PF03104. DNA_pol_B_exo. 1 hit. PF08490. DUF1744. 1 hit. [Graphical view]
SMART	SM00486. POLBc. 1 hit. [Graphical view]
PROSITE	PS00116. DNA_POLYMERASE_B. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979382.

Entry information

Entry name

DPOE_YEAST

Accession

Primary (citable) accession number: P21951

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	November 3, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)