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Protein

DNA polymerase epsilon catalytic subunit A

Gene

POL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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).

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2108 – 21081ZincBy similarity
Metal bindingi2111 – 21111ZincBy similarity
Metal bindingi2130 – 21301ZincBy similarity
Metal bindingi2133 – 21331ZincBy similarity
Metal bindingi2164 – 21641Iron-sulfur (4Fe-4S)By similarity
Metal bindingi2167 – 21671Iron-sulfur (4Fe-4S)By similarity
Metal bindingi2179 – 21791Iron-sulfur (4Fe-4S)By similarity
Metal bindingi2181 – 21811Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2108 – 213326CysA-typeAdd
BLAST

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • DNA-directed DNA polymerase activity Source: SGD
  • double-stranded DNA binding Source: SGD
  • nucleotide binding Source: InterPro
  • single-stranded DNA 3'-5' exodeoxyribonuclease activity Source: SGD
  • single-stranded DNA binding Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • base-excision repair Source: SGD
  • DNA-dependent DNA replication Source: SGD
  • DNA replication proofreading Source: SGD
  • double-strand break repair Source: SGD
  • double-strand break repair via nonhomologous end joining Source: SGD
  • error-prone translesion synthesis Source: SGD
  • gene conversion Source: SGD
  • heterochromatin organization involved in chromatin silencing Source: SGD
  • intra-S DNA damage checkpoint Source: SGD
  • leading strand elongation Source: SGD
  • mitotic DNA replication checkpoint Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • nucleotide-excision repair, DNA gap filling Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33258-MONOMER.
ReactomeiR-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon catalytic subunit A (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit A
Gene namesi
Name:POL2
Synonyms:DUN2
Ordered Locus Names:YNL262W
ORF Names:N0825
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL262W.
SGDiS000005206. POL2.

Subcellular locationi

GO - Cellular componenti

  • epsilon DNA polymerase complex Source: SGD
  • replication fork Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi644 – 6441M → I in POL2-9; temperature-sensitive mutant. 1 Publication
Mutagenesisi710 – 7101P → S in POL2-18; temperature-sensitive mutant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22222222DNA polymerase epsilon catalytic subunit APRO_0000046467Add
BLAST

Proteomic databases

MaxQBiP21951.
PeptideAtlasiP21951.

PTM databases

iPTMnetiP21951.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi35577. 86 interactions.
DIPiDIP-2532N.
IntActiP21951. 18 interactions.
MINTiMINT-670401.

Structurei

Secondary structure

1
2222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4917Combined sources
Turni67 – 715Combined sources
Beta strandi72 – 8716Combined sources
Beta strandi114 – 12310Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi138 – 1447Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 15911Combined sources
Turni160 – 1634Combined sources
Beta strandi166 – 1738Combined sources
Helixi180 – 1823Combined sources
Beta strandi186 – 1927Combined sources
Helixi196 – 21520Combined sources
Turni222 – 2243Combined sources
Helixi235 – 2384Combined sources
Beta strandi239 – 2446Combined sources
Helixi249 – 2579Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi286 – 2938Combined sources
Turni303 – 3053Combined sources
Beta strandi308 – 3158Combined sources
Beta strandi318 – 3247Combined sources
Turni325 – 3273Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi346 – 3549Combined sources
Helixi355 – 36915Combined sources
Beta strandi372 – 3787Combined sources
Turni379 – 3824Combined sources
Helixi383 – 39311Combined sources
Helixi398 – 4025Combined sources
Beta strandi415 – 4217Combined sources
Helixi422 – 4298Combined sources
Helixi434 – 4363Combined sources
Helixi439 – 4479Combined sources
Helixi456 – 4583Combined sources
Helixi459 – 4657Combined sources
Helixi467 – 48721Combined sources
Helixi489 – 4979Combined sources
Beta strandi500 – 5023Combined sources
Helixi504 – 5096Combined sources
Helixi512 – 52615Combined sources
Beta strandi546 – 5538Combined sources
Beta strandi558 – 5603Combined sources
Beta strandi564 – 5674Combined sources
Beta strandi572 – 5754Combined sources
Helixi578 – 59720Combined sources
Helixi604 – 6063Combined sources
Beta strandi607 – 6093Combined sources
Helixi610 – 62617Combined sources
Beta strandi629 – 6324Combined sources
Beta strandi634 – 6418Combined sources
Helixi644 – 6529Combined sources
Helixi656 – 6583Combined sources
Beta strandi659 – 6624Combined sources
Beta strandi664 – 6663Combined sources
Beta strandi678 – 68912Combined sources
Helixi694 – 70512Combined sources
Beta strandi708 – 7103Combined sources
Beta strandi720 – 7223Combined sources
Helixi723 – 7253Combined sources
Helixi728 – 74720Combined sources
Beta strandi752 – 76615Combined sources
Helixi769 – 79729Combined sources
Turni798 – 8003Combined sources
Beta strandi801 – 8033Combined sources
Helixi808 – 83225Combined sources
Helixi833 – 8353Combined sources
Helixi844 – 86825Combined sources
Beta strandi869 – 8757Combined sources
Beta strandi878 – 8847Combined sources
Beta strandi890 – 8956Combined sources
Beta strandi900 – 9045Combined sources
Helixi905 – 91814Combined sources
Beta strandi920 – 9289Combined sources
Turni929 – 9324Combined sources
Beta strandi933 – 9397Combined sources
Beta strandi944 – 95512Combined sources
Beta strandi969 – 9724Combined sources
Beta strandi978 – 9847Combined sources
Turni985 – 9873Combined sources
Beta strandi988 – 9925Combined sources
Helixi993 – 100210Combined sources
Helixi1003 – 10075Combined sources
Beta strandi1009 – 10113Combined sources
Helixi1012 – 103120Combined sources
Turni1032 – 10365Combined sources
Helixi1039 – 10468Combined sources
Beta strandi1048 – 10514Combined sources
Helixi1056 – 10594Combined sources
Helixi1065 – 107713Combined sources
Helixi1079 – 10824Combined sources
Beta strandi1083 – 10864Combined sources
Beta strandi1088 – 10958Combined sources
Beta strandi1097 – 10993Combined sources
Helixi1102 – 11043Combined sources
Beta strandi1106 – 11083Combined sources
Helixi1109 – 11135Combined sources
Helixi1116 – 112712Combined sources
Helixi1137 – 11404Combined sources
Helixi1143 – 115715Combined sources
Helixi1159 – 11646Combined sources
Helixi1178 – 11836Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M8OX-ray2.20A1-1228[»]
4PTFX-ray2.81A1-1187[»]
ProteinModelPortaliP21951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2164 – 218118CysB motifAdd
BLAST

Domaini

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.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated
Contains 1 CysA-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2108 – 213326CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000010194.
HOGENOMiHOG000196287.
InParanoidiP21951.
KOiK02324.
OMAiIQDDGGM.
OrthoDBiEOG790G80.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR013697. DNA_pol_e_suA_C.
IPR029703. POL2.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10670. PTHR10670. 2 hits.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view]
SMARTiSM01159. DUF1744. 1 hit.
SM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.

Sequencei

Sequence statusi: Complete.

P21951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM
60 70 80 90 100
GFERYVPPQY NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG
110 120 130 140 150
NSNDGERVTT NQGISGVDFY FLDEEGGSFK STVVYDPYFF IACNDESRVN
160 170 180 190 200
DVEELVKKYL ESCLKSLQII RKEDLTMDNH LLGLQKTLIK LSFVNSNQLF
210 220 230 240 250
EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE DIREYDVPYH
260 270 280 290 300
VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF
310 320 330 340 350
PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF
360 370 380 390 400
NENDEVALLQ RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD
410 420 430 440 450
EIGFAPDAEG EYKSSYCSHM DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN
460 470 480 490 500
PIELDPELMT PYAFEKPQHL SEYSVSDAVA TYYLYMKYVH PFIFSLCTII
510 520 530 540 550
PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE RFYDGHLLES
560 570 580 590 600
ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN
610 620 630 640 650
KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT
660 670 680 690 700
TNRLQPDSIK AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI
710 720 730 740 750
KRALQNETFP NKNKFSKKKV LTFDELSYAD QVIHIKKRLT EYSRKVYHRV
760 770 780 790 800
KVSEIVEREA IVCQRENPFY VDTVKSFRDR RYEFKGLAKT WKGNLSKIDP
810 820 830 840 850
SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR WYSMEMAGIT
860 870 880 890 900
CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK
910 920 930 940 950
LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY
960 970 980 990 1000
KAMILPSSKE EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS
1010 1020 1030 1040 1050
DIFKVFLEGD TLEGCYSAVA SVCNRWLDVL DSHGLMLEDE DLVSLICENR
1060 1070 1080 1090 1100
SMSKTLKEYE GQKSTSITTA RRLGDFLGED MVKDKGLQCK YIISSKPFNA
1110 1120 1130 1140 1150
PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI IDWGYYRERL
1160 1170 1180 1190 1200
GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF
1210 1220 1230 1240 1250
SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT
1260 1270 1280 1290 1300
NEEDPLVLPS EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS
1310 1320 1330 1340 1350
RERSALGSMI RKQAESYANS TWEVLQYKDS GEPGVLEVFV TINGKVQNIT
1360 1370 1380 1390 1400
FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS ASLPNNPKTS NPAGGQLFKI
1410 1420 1430 1440 1450
TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD LGASVTFRSK
1460 1470 1480 1490 1500
AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS
1510 1520 1530 1540 1550
LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV
1560 1570 1580 1590 1600
DIKEDINFEF VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL
1610 1620 1630 1640 1650
LGTIRLLNQM PIVKLSLNEV LLPQLNWQPT LLKKLVNHVL SSGSWISHLI
1660 1670 1680 1690 1700
KLSQYSNIPI CNLRLDSMDY IIDVLYARKL KKENIVLWWN EKAPLPDHGG
1710 1720 1730 1740 1750
IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT VNTILTSALI
1760 1770 1780 1790 1800
NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD
1810 1820 1830 1840 1850
EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE
1860 1870 1880 1890 1900
FSALGSTIVY ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL
1910 1920 1930 1940 1950
NIKRYWDLLI WMDKFNFSGL ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ
1960 1970 1980 1990 2000
PEFEDWMMII LDSMLKTKQS YLKLNSGTQR PTQIVNVKKQ DKEDSVENSL
2010 2020 2030 2040 2050
NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL PGSHLNVKNP
2060 2070 2080 2090 2100
LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS
2110 2120 2130 2140 2150
LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL
2160 2170 2180 2190 2200
RSDIESYLIQ DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV
2210 2220
FKQVAKYYGF DILLSCIADL TI
Length:2,222
Mass (Da):255,671
Last modified:August 1, 1991 - v1
Checksum:iCBCDDE2AB147D65B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60416 Genomic DNA. Translation: AAA88711.1.
X92494 Genomic DNA. Translation: CAA63235.1.
Z71538 Genomic DNA. Translation: CAA96169.1.
BK006947 Genomic DNA. Translation: DAA10297.1.
PIRiA36028.
RefSeqiNP_014137.1. NM_001183100.1.

Genome annotation databases

EnsemblFungiiYNL262W; YNL262W; YNL262W.
GeneIDi855459.
KEGGisce:YNL262W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60416 Genomic DNA. Translation: AAA88711.1.
X92494 Genomic DNA. Translation: CAA63235.1.
Z71538 Genomic DNA. Translation: CAA96169.1.
BK006947 Genomic DNA. Translation: DAA10297.1.
PIRiA36028.
RefSeqiNP_014137.1. NM_001183100.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M8OX-ray2.20A1-1228[»]
4PTFX-ray2.81A1-1187[»]
ProteinModelPortaliP21951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35577. 86 interactions.
DIPiDIP-2532N.
IntActiP21951. 18 interactions.
MINTiMINT-670401.

PTM databases

iPTMnetiP21951.

Proteomic databases

MaxQBiP21951.
PeptideAtlasiP21951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL262W; YNL262W; YNL262W.
GeneIDi855459.
KEGGisce:YNL262W.

Organism-specific databases

EuPathDBiFungiDB:YNL262W.
SGDiS000005206. POL2.

Phylogenomic databases

GeneTreeiENSGT00390000010194.
HOGENOMiHOG000196287.
InParanoidiP21951.
KOiK02324.
OMAiIQDDGGM.
OrthoDBiEOG790G80.

Enzyme and pathway databases

BioCyciYEAST:G3O-33258-MONOMER.
ReactomeiR-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.

Miscellaneous databases

NextBioi979382.
PROiP21951.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR013697. DNA_pol_e_suA_C.
IPR029703. POL2.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10670. PTHR10670. 2 hits.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view]
SMARTiSM01159. DUF1744. 1 hit.
SM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2221.
    Strain: ATCC 96604 / S288c / FY1679.
  5. "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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF MET-644 AND PRO-710.
  6. "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.
  7. "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.
  8. "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.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes."
    Netz D.J., Stith C.M., Stumpfig M., Kopf G., Vogel D., Genau H.M., Stodola J.L., Lill R., Burgers P.M., Pierik A.J.
    Nat. Chem. Biol. 8:125-132(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, IRON-SULFUR-BINDING.

Entry informationi

Entry nameiDPOE_YEAST
AccessioniPrimary (citable) accession number: P21951
Secondary accession number(s): D6W0T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 11, 2016
This is version 158 of the entry and version 1 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 1970 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.