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P15436

- DPOD_YEAST

UniProt

P15436 - DPOD_YEAST

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Protein

DNA polymerase delta catalytic subunit

Gene

POL3

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

Functioni

DNA polymerase delta (DNA polymerase III) 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. POL3 contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity.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 bindingi1009 – 10091Zinc
Metal bindingi1012 – 10121Zinc
Metal bindingi1024 – 10241Zinc
Metal bindingi1027 – 10271Zinc
Metal bindingi1056 – 10561Iron-sulfur (4Fe-4S)
Metal bindingi1059 – 10591Iron-sulfur (4Fe-4S)
Metal bindingi1069 – 10691Iron-sulfur (4Fe-4S)
Metal bindingi1074 – 10741Iron-sulfur (4Fe-4S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1009 – 102719CysA-typeAdd
BLAST

GO - Molecular functioni

  1. 3'-5'-exodeoxyribonuclease activity Source: SGD
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. DNA binding Source: UniProtKB-KW
  4. DNA-directed DNA polymerase activity Source: SGD
  5. metal ion binding Source: UniProtKB-KW
  6. nucleotide binding Source: InterPro

GO - Biological processi

  1. DNA catabolic process, exonucleolytic Source: GOC
  2. DNA replication Source: SGD
  3. DNA replication, removal of RNA primer Source: SGD
  4. maintenance of fidelity involved in DNA-dependent DNA replication Source: SGD
  5. RNA-dependent DNA replication Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, 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-29505-MONOMER.
ReactomeiREACT_188901. Cytosolic iron-sulfur cluster assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase delta catalytic subunit (EC:2.7.7.7)
Alternative name(s):
DNA polymerase III
Gene namesi
Name:POL3
Synonyms:CDC2, TEX1
Ordered Locus Names:YDL102W
ORF Names:D2366
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL102w.
SGDiS000002260. POL3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. delta DNA polymerase complex Source: SGD
  3. replication fork Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1009 – 10091C → A: Impairs iron-sulfur-binding. 1 Publication
Mutagenesisi1012 – 10121C → A: Impairs iron-sulfur-binding. 1 Publication
Mutagenesisi1024 – 10241C → A: Impairs iron-sulfur-binding. 1 Publication
Mutagenesisi1027 – 10271C → A: Impairs iron-sulfur-binding. 1 Publication
Mutagenesisi1056 – 10561C → A: Abolishes iron-sulfur-binding. 1 Publication
Mutagenesisi1059 – 10591C → A: Abolishes iron-sulfur-binding.
Mutagenesisi1069 – 10691C → A: Abolishes iron-sulfur-binding. 1 Publication
Mutagenesisi1074 – 10741C → A: Abolishes iron-sulfur-binding. 1 Publication
Mutagenesisi1074 – 10741C → S in pol3-13; synthetically lethal with mutations of NBP35, DRE2 and TAH18. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10971097DNA polymerase delta catalytic subunitPRO_0000046454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphoserine3 Publications
Modified residuei37 – 371Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15436.
PaxDbiP15436.
PeptideAtlasiP15436.

Expressioni

Gene expression databases

GenevestigatoriP15436.

Interactioni

Subunit structurei

DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2. Interacts with PCNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
POL31P469573EBI-6134,EBI-6080

Protein-protein interaction databases

BioGridi31960. 173 interactions.
DIPiDIP-2524N.
IntActiP15436. 4 interactions.
MINTiMINT-2781941.
STRINGi4932.YDL102W.

Structurei

Secondary structure

1
1097
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni108 – 1103Combined sources
Beta strandi113 – 12412Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi159 – 1635Combined sources
Helixi168 – 1714Combined sources
Helixi173 – 18412Combined sources
Turni185 – 1895Combined sources
Beta strandi191 – 20313Combined sources
Beta strandi211 – 22010Combined sources
Helixi223 – 23311Combined sources
Helixi238 – 2403Combined sources
Helixi254 – 2629Combined sources
Beta strandi269 – 2724Combined sources
Helixi282 – 2843Combined sources
Beta strandi290 – 2967Combined sources
Turni297 – 2993Combined sources
Beta strandi301 – 3033Combined sources
Helixi307 – 3093Combined sources
Beta strandi316 – 3249Combined sources
Turni334 – 3363Combined sources
Beta strandi339 – 34810Combined sources
Beta strandi355 – 3639Combined sources
Beta strandi371 – 3788Combined sources
Helixi379 – 39315Combined sources
Beta strandi396 – 4027Combined sources
Turni403 – 4064Combined sources
Helixi407 – 41711Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi439 – 4435Combined sources
Turni444 – 4463Combined sources
Beta strandi447 – 4515Combined sources
Beta strandi460 – 4634Combined sources
Helixi464 – 4718Combined sources
Helixi479 – 4879Combined sources
Helixi499 – 5035Combined sources
Helixi507 – 53024Combined sources
Helixi533 – 54412Combined sources
Helixi550 – 5534Combined sources
Helixi556 – 57015Combined sources
Beta strandi598 – 6003Combined sources
Beta strandi604 – 6096Combined sources
Helixi612 – 6198Combined sources
Helixi624 – 6263Combined sources
Helixi630 – 6356Combined sources
Turni641 – 6433Combined sources
Beta strandi644 – 6463Combined sources
Beta strandi652 – 6543Combined sources
Turni656 – 6583Combined sources
Helixi662 – 68221Combined sources
Helixi687 – 71125Combined sources
Beta strandi714 – 7174Combined sources
Helixi721 – 74525Combined sources
Helixi748 – 7503Combined sources
Beta strandi757 – 7604Combined sources
Beta strandi762 – 7698Combined sources
Helixi775 – 79016Combined sources
Beta strandi799 – 81214Combined sources
Beta strandi815 – 82612Combined sources
Beta strandi829 – 8357Combined sources
Helixi836 – 8383Combined sources
Helixi844 – 85815Combined sources
Helixi863 – 87816Combined sources
Helixi884 – 8874Combined sources
Beta strandi889 – 8924Combined sources
Helixi902 – 91413Combined sources
Beta strandi922 – 9298Combined sources
Beta strandi931 – 9333Combined sources
Helixi935 – 9373Combined sources
Helixi942 – 9476Combined sources
Helixi954 – 9607Combined sources
Helixi963 – 97412Combined sources
Helixi976 – 9827Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IAYX-ray2.00A67-985[»]
ProteinModelPortaliP15436.
SMRiP15436. Positions 95-985.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1056 – 107419CysB motifAdd
BLAST

Domaini

The CysA-type zinc finger is required for PCNA-binding.1 Publication
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.1 Publication

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 fingeri1009 – 102719CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0417.
GeneTreeiENSGT00560000077365.
HOGENOMiHOG000036616.
InParanoidiP15436.
KOiK02327.
OMAiQLFRKAN.
OrthoDBiEOG7KSXJ9.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15436-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEKRSLPMV DVKIDDEDTP QLEKKIKRQS IDHGVGSEPV STIEIIPSDS
60 70 80 90 100
FRKYNSQGFK AKDTDLMGTQ LESTFEQELS QMEHDMADQE EHDLSSFERK
110 120 130 140 150
KLPTDFDPSL YDISFQQIDA EQSVLNGIKD ENTSTVVRFF GVTSEGHSVL
160 170 180 190 200
CNVTGFKNYL YVPAPNSSDA NDQEQINKFV HYLNETFDHA IDSIEVVSKQ
210 220 230 240 250
SIWGYSGDTK LPFWKIYVTY PHMVNKLRTA FERGHLSFNS WFSNGTTTYD
260 270 280 290 300
NIAYTLRLMV DCGIVGMSWI TLPKGKYSMI EPNNRVSSCQ LEVSINYRNL
310 320 330 340 350
IAHPAEGDWS HTAPLRIMSF DIECAGRIGV FPEPEYDPVI QIANVVSIAG
360 370 380 390 400
AKKPFIRNVF TLNTCSPITG SMIFSHATEE EMLSNWRNFI IKVDPDVIIG
410 420 430 440 450
YNTTNFDIPY LLNRAKALKV NDFPYFGRLK TVKQEIKESV FSSKAYGTRE
460 470 480 490 500
TKNVNIDGRL QLDLLQFIQR EYKLRSYTLN AVSAHFLGEQ KEDVHYSIIS
510 520 530 540 550
DLQNGDSETR RRLAVYCLKD AYLPLRLMEK LMALVNYTEM ARVTGVPFSY
560 570 580 590 600
LLARGQQIKV VSQLFRKCLE IDTVIPNMQS QASDDQYEGA TVIEPIRGYY
610 620 630 640 650
DVPIATLDFN SLYPSIMMAH NLCYTTLCNK ATVERLNLKI DEDYVITPNG
660 670 680 690 700
DYFVTTKRRR GILPIILDEL ISARKRAKKD LRDEKDPFKR DVLNGRQLAL
710 720 730 740 750
KISANSVYGF TGATVGKLPC LAISSSVTAY GRTMILKTKT AVQEKYCIKN
760 770 780 790 800
GYKHDAVVVY GDTDSVMVKF GTTDLKEAMD LGTEAAKYVS TLFKHPINLE
810 820 830 840 850
FEKAYFPYLL INKKRYAGLF WTNPDKFDKL DQKGLASVRR DSCSLVSIVM
860 870 880 890 900
NKVLKKILIE RNVDGALAFV RETINDILHN RVDISKLIIS KTLAPNYTNP
910 920 930 940 950
QPHAVLAERM KRREGVGPNV GDRVDYVIIG GNDKLYNRAE DPLFVLENNI
960 970 980 990 1000
QVDSRYYLTN QLQNPIISIV APIIGDKQAN GMFVVKSIKI NTGSQKGGLM
1010 1020 1030 1040 1050
SFIKKVEACK SCKGPLRKGE GPLCSNCLAR SGELYIKALY DVRDLEEKYS
1060 1070 1080 1090
RLWTQCQRCA GNLHSEVLCS NKNCDIFYMR VKVKKELQEK VEQLSKW
Length:1,097
Mass (Da):124,619
Last modified:July 27, 2011 - v4
Checksum:i16E4245C5DCC66DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 792EL → DV in CAA33504. (PubMed:2670563)Curated
Sequence conflicti78 – 792EL → DV in CAA64911. (PubMed:8896274)Curated
Sequence conflicti78 – 792EL → DV in CAA98669. (PubMed:9169867)Curated
Sequence conflicti189 – 1891H → R in CAA33504. (PubMed:2670563)Curated
Sequence conflicti204 – 2041G → D in CAA33504. (PubMed:2670563)Curated
Sequence conflicti347 – 36317SIAGA…VFTLN → YLALRNHSFVMCYSD in CAA33504. (PubMed:2670563)CuratedAdd
BLAST
Sequence conflicti647 – 6493TPN → HY in CAA33504. (PubMed:2670563)Curated
Sequence conflicti870 – 8701V → D in CAA33504. (PubMed:2670563)Curated
Sequence conflicti974 – 9741Missing in CAA33504. (PubMed:2670563)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15477 Genomic DNA. Translation: CAA33504.1.
X61920 Genomic DNA. Translation: CAA43922.1.
X95644 Genomic DNA. Translation: CAA64911.1.
Z74150 Genomic DNA. Translation: CAA98669.1.
BK006938 Genomic DNA. Translation: DAA11758.2.
PIRiS67644. RNBYL3.
RefSeqiNP_010181.2. NM_001180161.2.

Genome annotation databases

EnsemblFungiiYDL102W; YDL102W; YDL102W.
GeneIDi851456.
KEGGisce:YDL102W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15477 Genomic DNA. Translation: CAA33504.1 .
X61920 Genomic DNA. Translation: CAA43922.1 .
X95644 Genomic DNA. Translation: CAA64911.1 .
Z74150 Genomic DNA. Translation: CAA98669.1 .
BK006938 Genomic DNA. Translation: DAA11758.2 .
PIRi S67644. RNBYL3.
RefSeqi NP_010181.2. NM_001180161.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IAY X-ray 2.00 A 67-985 [» ]
ProteinModelPortali P15436.
SMRi P15436. Positions 95-985.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31960. 173 interactions.
DIPi DIP-2524N.
IntActi P15436. 4 interactions.
MINTi MINT-2781941.
STRINGi 4932.YDL102W.

Proteomic databases

MaxQBi P15436.
PaxDbi P15436.
PeptideAtlasi P15436.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL102W ; YDL102W ; YDL102W .
GeneIDi 851456.
KEGGi sce:YDL102W.

Organism-specific databases

CYGDi YDL102w.
SGDi S000002260. POL3.

Phylogenomic databases

eggNOGi COG0417.
GeneTreei ENSGT00560000077365.
HOGENOMi HOG000036616.
InParanoidi P15436.
KOi K02327.
OMAi QLFRKAN.
OrthoDBi EOG7KSXJ9.

Enzyme and pathway databases

BioCyci YEAST:G3O-29505-MONOMER.
Reactomei REACT_188901. Cytosolic iron-sulfur cluster assembly.

Miscellaneous databases

NextBioi 968726.
PROi P15436.

Gene expression databases

Genevestigatori P15436.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProi IPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR025687. Znf-C4pol.
[Graphical view ]
Pfami PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF14260. zf-C4pol. 1 hit.
[Graphical view ]
PRINTSi PR00106. DNAPOLB.
SMARTi SM00486. POLBc. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 1 hit.
PROSITEi PS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and function of the Saccharomyces cerevisiae CDC2 gene encoding the large subunit of DNA polymerase III."
    Boulet A., Simon M., Faye G., Bauer G.A., Burgers M.J.
    EMBO J. 8:1849-1854(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: YAB2.
  2. "Nucleotide sequence of the POL3 gene encoding DNA polymerase III (delta) of Saccharomyces cerevisiae."
    Morrison A., Sugino A.
    Nucleic Acids Res. 20:375-375(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
  3. "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1 genes, and six new open reading frames."
    Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.
    Yeast 12:1077-1084(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 78-79.
    Strain: ATCC 204508 / S288c.
  6. "The 3' to 5' exonuclease activity located in the DNA polymerase delta subunit of Saccharomyces cerevisiae is required for accurate replication."
    Simon M., Giot L., Faye G.
    EMBO J. 10:2165-2170(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN EXONUCLEASE.
  7. "Structure of DNA polymerase delta from Saccharomyces cerevisiae."
    Johansson E., Majka J., Burgers P.M.
    J. Biol. Chem. 276:43824-43828(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE DNA POLYMERASE DELTA COMPLEX.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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, ZINC-BINDING, INTERACTION WITH PCNA, MUTAGENESIS OF CYS-1009; CYS-1012; CYS-1024; CYS-1027; CYS-1056; CYS-1069; CYS-1069 AND CYS-1074.

Entry informationi

Entry nameiDPOD_YEAST
AccessioniPrimary (citable) accession number: P15436
Secondary accession number(s): D6VRP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 152 of the entry and version 4 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.

Keywords - Technical termi

3D-structure, Complete proteome, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3