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P15436

- DPOD_YEAST

UniProt

P15436 - DPOD_YEAST

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
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    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

    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
    7. protein binding Source: IntAct

    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

    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

    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. 172 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 – 1103
    Beta strandi113 – 12412
    Beta strandi126 – 1283
    Beta strandi135 – 1439
    Beta strandi148 – 1558
    Beta strandi159 – 1635
    Helixi168 – 1714
    Helixi173 – 18412
    Turni185 – 1895
    Beta strandi191 – 20313
    Beta strandi211 – 22010
    Helixi223 – 23311
    Helixi238 – 2403
    Helixi254 – 2629
    Beta strandi269 – 2724
    Helixi282 – 2843
    Beta strandi290 – 2967
    Turni297 – 2993
    Beta strandi301 – 3033
    Helixi307 – 3093
    Beta strandi316 – 3249
    Turni334 – 3363
    Beta strandi339 – 34810
    Beta strandi355 – 3639
    Beta strandi371 – 3788
    Helixi379 – 39315
    Beta strandi396 – 4027
    Turni403 – 4064
    Helixi407 – 41711
    Beta strandi427 – 4293
    Beta strandi439 – 4435
    Turni444 – 4463
    Beta strandi447 – 4515
    Beta strandi460 – 4634
    Helixi464 – 4718
    Helixi479 – 4879
    Helixi499 – 5035
    Helixi507 – 53024
    Helixi533 – 54412
    Helixi550 – 5534
    Helixi556 – 57015
    Beta strandi598 – 6003
    Beta strandi604 – 6096
    Helixi612 – 6198
    Helixi624 – 6263
    Helixi630 – 6356
    Turni641 – 6433
    Beta strandi644 – 6463
    Beta strandi652 – 6543
    Turni656 – 6583
    Helixi662 – 68221
    Helixi687 – 71125
    Beta strandi714 – 7174
    Helixi721 – 74525
    Helixi748 – 7503
    Beta strandi757 – 7604
    Beta strandi762 – 7698
    Helixi775 – 79016
    Beta strandi799 – 81214
    Beta strandi815 – 82612
    Beta strandi829 – 8357
    Helixi836 – 8383
    Helixi844 – 85815
    Helixi863 – 87816
    Helixi884 – 8874
    Beta strandi889 – 8924
    Helixi902 – 91413
    Beta strandi922 – 9298
    Beta strandi931 – 9333
    Helixi935 – 9373
    Helixi942 – 9476
    Helixi954 – 9607
    Helixi963 – 97412
    Helixi976 – 9827

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSEKRSLPMV DVKIDDEDTP QLEKKIKRQS IDHGVGSEPV STIEIIPSDS     50
    FRKYNSQGFK AKDTDLMGTQ LESTFEQELS QMEHDMADQE EHDLSSFERK 100
    KLPTDFDPSL YDISFQQIDA EQSVLNGIKD ENTSTVVRFF GVTSEGHSVL 150
    CNVTGFKNYL YVPAPNSSDA NDQEQINKFV HYLNETFDHA IDSIEVVSKQ 200
    SIWGYSGDTK LPFWKIYVTY PHMVNKLRTA FERGHLSFNS WFSNGTTTYD 250
    NIAYTLRLMV DCGIVGMSWI TLPKGKYSMI EPNNRVSSCQ LEVSINYRNL 300
    IAHPAEGDWS HTAPLRIMSF DIECAGRIGV FPEPEYDPVI QIANVVSIAG 350
    AKKPFIRNVF TLNTCSPITG SMIFSHATEE EMLSNWRNFI IKVDPDVIIG 400
    YNTTNFDIPY LLNRAKALKV NDFPYFGRLK TVKQEIKESV FSSKAYGTRE 450
    TKNVNIDGRL QLDLLQFIQR EYKLRSYTLN AVSAHFLGEQ KEDVHYSIIS 500
    DLQNGDSETR RRLAVYCLKD AYLPLRLMEK LMALVNYTEM ARVTGVPFSY 550
    LLARGQQIKV VSQLFRKCLE IDTVIPNMQS QASDDQYEGA TVIEPIRGYY 600
    DVPIATLDFN SLYPSIMMAH NLCYTTLCNK ATVERLNLKI DEDYVITPNG 650
    DYFVTTKRRR GILPIILDEL ISARKRAKKD LRDEKDPFKR DVLNGRQLAL 700
    KISANSVYGF TGATVGKLPC LAISSSVTAY GRTMILKTKT AVQEKYCIKN 750
    GYKHDAVVVY GDTDSVMVKF GTTDLKEAMD LGTEAAKYVS TLFKHPINLE 800
    FEKAYFPYLL INKKRYAGLF WTNPDKFDKL DQKGLASVRR DSCSLVSIVM 850
    NKVLKKILIE RNVDGALAFV RETINDILHN RVDISKLIIS KTLAPNYTNP 900
    QPHAVLAERM KRREGVGPNV GDRVDYVIIG GNDKLYNRAE DPLFVLENNI 950
    QVDSRYYLTN QLQNPIISIV APIIGDKQAN GMFVVKSIKI NTGSQKGGLM 1000
    SFIKKVEACK SCKGPLRKGE GPLCSNCLAR SGELYIKALY DVRDLEEKYS 1050
    RLWTQCQRCA GNLHSEVLCS NKNCDIFYMR VKVKKELQEK VEQLSKW 1097
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 172 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.
    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

    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: October 1, 2014
    This is version 150 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