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Q04049

- POLH_YEAST

UniProt

Q04049 - POLH_YEAST

Protein

DNA polymerase eta

Gene

RAD30

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 107 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.34 Publications

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi30 – 301MagnesiumPROSITE-ProRule annotation
    Metal bindingi155 – 1551MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. chromosome segregation Source: SGD
    2. DNA-dependent DNA replication Source: GOC
    3. error-free translesion synthesis Source: SGD
    4. error-prone translesion synthesis Source: SGD
    5. mitotic sister chromatid cohesion Source: SGD

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication, DNA synthesis

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29960-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase eta (EC:2.7.7.7)
    Alternative name(s):
    Radiation-sensitive protein 30
    Gene namesi
    Name:RAD30
    Synonyms:DBH1
    Ordered Locus Names:YDR419W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR419w.
    SGDiS000002827. RAD30.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: SGD
    2. nucleus Source: SGD
    3. replication fork Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301D → A: Abolishes DNA polymerase activity. 1 Publication
    Mutagenesisi34 – 341F → L: Alters translesion activity. 1 Publication
    Mutagenesisi39 – 391E → A: Abolishes DNA polymerase activity. 1 Publication
    Mutagenesisi64 – 641Y → F or A: Decreases efficiency of nucleotide incorporation. 1 Publication
    Mutagenesisi67 – 671R → A: Decreases efficiency of nucleotide incorporation. 1 Publication
    Mutagenesisi155 – 1551D → A: Abolishes DNA polymerase activity and increases UV-induced mutations. 1 Publication
    Mutagenesisi156 – 1561E → A: Decreases efficiency of nucleotide incorporation. 1 Publication
    Mutagenesisi279 – 2791K → A: Decreases efficiency of nucleotide incorporation. 1 Publication
    Mutagenesisi627 – 6271F → A: Abolishes POL30-binding; when associated with A-628.
    Mutagenesisi628 – 6281F → A: Abolishes POL30-binding; when associated with A-627.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632DNA polymerase etaPRO_0000268698Add
    BLAST

    Proteomic databases

    MaxQBiQ04049.
    PaxDbiQ04049.
    PRIDEiQ04049.

    Expressioni

    Inductioni

    By UV radiation and heat shock. The mRNA is stabilized during stationary phase.2 Publications

    Gene expression databases

    GenevestigatoriQ04049.

    Interactioni

    Subunit structurei

    Interacts with POL30. This interaction is essential for the polymerase eta function.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    POL30P158733EBI-36214,EBI-12993

    Protein-protein interaction databases

    BioGridi32477. 84 interactions.
    DIPiDIP-6500N.
    IntActiQ04049. 8 interactions.
    MINTiMINT-708283.
    STRINGi4932.YDR419W.

    Structurei

    Secondary structure

    632
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 55
    Helixi6 – 105
    Helixi11 – 133
    Turni15 – 173
    Helixi18 – 203
    Beta strandi21 – 233
    Beta strandi26 – 316
    Helixi34 – 429
    Beta strandi51 – 555
    Beta strandi58 – 625
    Helixi64 – 674
    Turni68 – 703
    Helixi77 – 815
    Beta strandi88 – 914
    Beta strandi93 – 964
    Beta strandi100 – 1034
    Helixi115 – 1173
    Beta strandi123 – 1275
    Helixi129 – 14517
    Beta strandi149 – 1535
    Beta strandi156 – 1605
    Helixi162 – 17110
    Beta strandi176 – 1783
    Helixi183 – 1864
    Helixi188 – 1969
    Beta strandi203 – 2064
    Helixi210 – 2145
    Beta strandi219 – 2213
    Helixi233 – 25624
    Beta strandi260 – 2678
    Helixi268 – 2758
    Turni276 – 2783
    Beta strandi280 – 2856
    Helixi288 – 2903
    Helixi291 – 2955
    Beta strandi297 – 2993
    Helixi302 – 3043
    Helixi306 – 3083
    Helixi311 – 3199
    Beta strandi324 – 3263
    Helixi327 – 3348
    Helixi339 – 35113
    Beta strandi352 – 3554
    Turni357 – 3593
    Helixi364 – 3663
    Helixi367 – 37711
    Turni378 – 3803
    Beta strandi395 – 4006
    Turni403 – 4064
    Helixi409 – 43426
    Beta strandi436 – 44813
    Beta strandi454 – 4607
    Helixi466 – 4683
    Helixi469 – 48719
    Turni488 – 4903
    Beta strandi497 – 51014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JIHX-ray2.25A/B1-513[»]
    2R8JX-ray3.10A/B1-531[»]
    2R8KX-ray3.30A/B1-531[»]
    2WTFX-ray2.50A/B1-513[»]
    2XGPX-ray2.70A/B1-513[»]
    2XGQX-ray2.70A/B1-513[»]
    3MFHX-ray2.00A1-513[»]
    3MFIX-ray1.76A1-513[»]
    3OHAX-ray2.00A1-513[»]
    3OHBX-ray2.00A1-513[»]
    ProteinModelPortaliQ04049.
    SMRiQ04049. Positions 1-512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04049.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 309284UmuCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni625 – 6328POL30-binding

    Sequence similaritiesi

    Belongs to the DNA polymerase type-Y family.Curated
    Contains 1 umuC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0389.
    HOGENOMiHOG000065930.
    KOiK03509.
    OMAiGYTTSCG.
    OrthoDBiEOG7RFTT2.

    Family and domain databases

    Gene3Di3.30.1490.100. 1 hit.
    InterProiIPR017961. DNA_pol_Y-fam_little_finger.
    IPR001126. DNA_repair_prot_UmuC-like.
    IPR017963. DNA_repair_prot_UmuC-like_N.
    [Graphical view]
    PfamiPF00817. IMS. 1 hit.
    PF11799. IMS_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF100879. SSF100879. 1 hit.
    PROSITEiPS50173. UMUC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04049-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKFTWKELI QLGSPSKAYE SSLACIAHID MNAFFAQVEQ MRCGLSKEDP    50
    VVCVQWNSII AVSYAARKYG ISRMDTIQEA LKKCSNLIPI HTAVFKKGED 100
    FWQYHDGCGS WVQDPAKQIS VEDHKVSLEP YRRESRKALK IFKSACDLVE 150
    RASIDEVFLD LGRICFNMLM FDNEYELTGD LKLKDALSNI REAFIGGNYD 200
    INSHLPLIPE KIKSLKFEGD VFNPEGRDLI TDWDDVILAL GSQVCKGIRD 250
    SIKDILGYTT SCGLSSTKNV CKLASNYKKP DAQTIVKNDC LLDFLDCGKF 300
    EITSFWTLGG VLGKELIDVL DLPHENSIKH IRETWPDNAG QLKEFLDAKV 350
    KQSDYDRSTS NIDPLKTADL AEKLFKLSRG RYGLPLSSRP VVKSMMSNKN 400
    LRGKSCNSIV DCISWLEVFC AELTSRIQDL EQEYNKIVIP RTVSISLKTK 450
    SYEVYRKSGP VAYKGINFQS HELLKVGIKF VTDLDIKGKN KSYYPLTKLS 500
    MTITNFDIID LQKTVVDMFG NQVHTFKSSA GKEDEEKTTS SKADEKTPKL 550
    ECCKYQVTFT DQKALQEHAD YHLALKLSEG LNGAEESSKN LSFGEKRLLF 600
    SRKRPNSQHT ATPQKKQVTS SKNILSFFTR KK 632
    Length:632
    Mass (Da):71,515
    Last modified:November 1, 1996 - v1
    Checksum:iCFB1A9FBC8AFE39B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33007 Genomic DNA. Translation: AAB64856.1.
    BK006938 Genomic DNA. Translation: DAA12259.1.
    PIRiS69702.
    RefSeqiNP_010707.3. NM_001180727.3.

    Genome annotation databases

    EnsemblFungiiYDR419W; YDR419W; YDR419W.
    GeneIDi852028.
    KEGGisce:YDR419W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33007 Genomic DNA. Translation: AAB64856.1 .
    BK006938 Genomic DNA. Translation: DAA12259.1 .
    PIRi S69702.
    RefSeqi NP_010707.3. NM_001180727.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JIH X-ray 2.25 A/B 1-513 [» ]
    2R8J X-ray 3.10 A/B 1-531 [» ]
    2R8K X-ray 3.30 A/B 1-531 [» ]
    2WTF X-ray 2.50 A/B 1-513 [» ]
    2XGP X-ray 2.70 A/B 1-513 [» ]
    2XGQ X-ray 2.70 A/B 1-513 [» ]
    3MFH X-ray 2.00 A 1-513 [» ]
    3MFI X-ray 1.76 A 1-513 [» ]
    3OHA X-ray 2.00 A 1-513 [» ]
    3OHB X-ray 2.00 A 1-513 [» ]
    ProteinModelPortali Q04049.
    SMRi Q04049. Positions 1-512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32477. 84 interactions.
    DIPi DIP-6500N.
    IntActi Q04049. 8 interactions.
    MINTi MINT-708283.
    STRINGi 4932.YDR419W.

    Proteomic databases

    MaxQBi Q04049.
    PaxDbi Q04049.
    PRIDEi Q04049.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR419W ; YDR419W ; YDR419W .
    GeneIDi 852028.
    KEGGi sce:YDR419W.

    Organism-specific databases

    CYGDi YDR419w.
    SGDi S000002827. RAD30.

    Phylogenomic databases

    eggNOGi COG0389.
    HOGENOMi HOG000065930.
    KOi K03509.
    OMAi GYTTSCG.
    OrthoDBi EOG7RFTT2.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29960-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q04049.
    NextBioi 970255.
    PROi Q04049.

    Gene expression databases

    Genevestigatori Q04049.

    Family and domain databases

    Gene3Di 3.30.1490.100. 1 hit.
    InterProi IPR017961. DNA_pol_Y-fam_little_finger.
    IPR001126. DNA_repair_prot_UmuC-like.
    IPR017963. DNA_repair_prot_UmuC-like_N.
    [Graphical view ]
    Pfami PF00817. IMS. 1 hit.
    PF11799. IMS_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100879. SSF100879. 1 hit.
    PROSITEi PS50173. UMUC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia coli dinB and umuC, is DNA damage inducible and functions in a novel error-free postreplication repair mechanism."
      McDonald J.P., Levine A.S., Woodgate R.
      Genetics 147:1557-1568(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    4. "Requirement of DNA polymerase activity of yeast Rad30 protein for its biological function."
      Johnson R.E., Prakash S., Prakash L.
      J. Biol. Chem. 274:15975-15977(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 155-ASP-GLU-156.
    5. "Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase eta."
      Washington M.T., Johnson R.E., Prakash S., Prakash L.
      J. Biol. Chem. 274:36835-36838(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Poleta."
      Johnson R.E., Prakash S., Prakash L.
      Science 283:1001-1004(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways."
      Xiao W., Chow B.L., Broomfield S., Hanna M.
      Genetics 155:1633-1641(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Specificity of DNA lesion bypass by the yeast DNA polymerase eta."
      Yuan F., Zhang Y., Rajpal D.K., Wu X., Guo D., Wang M., Taylor J.-S., Wang Z.
      J. Biol. Chem. 275:8233-8239(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Replication past O(6)-methylguanine by yeast and human DNA polymerase eta."
      Haracska L., Prakash S., Prakash L.
      Mol. Cell. Biol. 20:8001-8007(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta."
      Haracska L., Yu S.-L., Johnson R.E., Prakash L., Prakash S.
      Nat. Genet. 25:458-461(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase eta."
      Washington M.T., Johnson R.E., Prakash S., Prakash L.
      Proc. Natl. Acad. Sci. U.S.A. 97:3094-3099(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Translesion DNA synthesis by yeast DNA polymerase eta on templates containing N2-guanine adducts of 1,3-butadiene metabolites."
      Minko I.G., Washington M.T., Prakash L., Prakash S., Lloyd R.S.
      J. Biol. Chem. 276:2517-2522(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Interaction with PCNA is essential for yeast DNA polymerase eta function."
      Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.
      Mol. Cell 8:407-415(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH POL30, MUTAGENESIS OF 627-PHE-PHE-628.
    14. "Requirement of DNA polymerase eta for error-free bypass of UV-induced CC and TC photoproducts."
      Yu S.-L., Johnson R.E., Prakash S., Prakash L.
      Mol. Cell. Biol. 21:185-188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Acidic residues critical for the activity and biological function of yeast DNA polymerase eta."
      Kondratick C.M., Washington M.T., Prakash S., Prakash L.
      Mol. Cell. Biol. 21:2018-2025(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF ASP-30; GLU-39; ASP-155 AND GLU-156.
    16. "Mismatch extension ability of yeast and human DNA polymerase eta."
      Washington M.T., Johnson R.E., Prakash S., Prakash L.
      J. Biol. Chem. 276:2263-2266(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Lesion bypass in yeast cells: Pol eta participates in a multi-DNA polymerase process."
      Bresson A., Fuchs R.P.
      EMBO J. 21:3881-3887(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "UV-induced T-->C transition at a TT photoproduct site is dependent on Saccharomyces cerevisiae polymerase eta in vivo."
      Zhang H., Siede W.
      Nucleic Acids Res. 30:1262-1267(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Yeast pol eta holds a cis-syn thymine dimer loosely in the active site during elongation opposite the 3'-T of the dimer, but tightly opposite the 5'-T."
      Sun L., Zhang K., Zhou L., Hohler P., Kool E.T., Yuan F., Wang Z., Taylor J.-S.
      Biochemistry 42:9431-9437(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Deoxynucleotide triphosphate binding mode conserved in Y family DNA polymerases."
      Johnson R.E., Trincao J., Aggarwal A.K., Prakash S., Prakash L.
      Mol. Cell. Biol. 23:3008-3012(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-64; ARG-67 AND LYS-279.
    21. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    22. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    23. "Roles of Saccharomyces cerevisiae DNA polymerases Poleta and Polzeta in response to irradiation by simulated sunlight."
      Kozmin S.G., Pavlov Y.I., Kunkel T.A., Sage E.
      Nucleic Acids Res. 31:4541-4552(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "Yeast DNA polymerase eta makes functional contacts with the DNA minor groove only at the incoming nucleoside triphosphate."
      Washington M.T., Wolfle W.T., Spratt T.E., Prakash L., Prakash S.
      Proc. Natl. Acad. Sci. U.S.A. 100:5113-5118(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Mechanism of nucleotide incorporation opposite a thymine-thymine dimer by yeast DNA polymerase eta."
      Washington M.T., Prakash L., Prakash S.
      Proc. Natl. Acad. Sci. U.S.A. 100:12093-12098(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "LC-MS/MS identification and yeast polymerase eta bypass of a novel gamma-irradiation-induced intrastrand cross-link lesion G[8-5]C."
      Gu C., Wang Y.
      Biochemistry 43:6745-6750(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "Role of base stacking and sequence context in the inhibition of yeast DNA polymerase eta by pyrene nucleotide."
      Hwang H., Taylor J.-S.
      Biochemistry 43:14612-14623(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "Role of DNA polymerase eta in the bypass of abasic sites in yeast cells."
      Zhao B., Xie Z., Shen H., Wang Z.
      Nucleic Acids Res. 32:3984-3994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Enzymatic switching for efficient and accurate translesion DNA replication."
      McCulloch S.D., Kokoska R.J., Chilkova O., Welch C.M., Johansson E., Burgers P.M.J., Kunkel T.A.
      Nucleic Acids Res. 32:4665-4675(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "Palm mutants in DNA polymerases alpha and eta alter DNA replication fidelity and translesion activity."
      Niimi A., Limsirichaikul S., Yoshida S., Iwai S., Masutani C., Hanaoka F., Kool E.T., Nishiyama Y., Suzuki M.
      Mol. Cell. Biol. 24:2734-2746(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PHE-34.
    31. "Evidence for Watson-Crick and not Hoogsteen or wobble base pairing in the selection of nucleotides for insertion opposite pyrimidines and a thymine dimer by yeast DNA pol eta."
      Hwang H., Taylor J.-S.
      Biochemistry 44:4850-4860(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "Transcript copy number of genes for DNA repair and translesion synthesis in yeast: contribution of transcription rate and mRNA stability to the steady-state level of each mRNA along with growth in glucose-fermentative medium."
      Michan C., Monje-Casas F., Pueyo C.
      DNA Repair 4:469-478(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    33. "The p-benzoquinone DNA adducts derived from benzene are highly mutagenic."
      Xie Z., Zhang Y., Guliaev A.B., Shen H., Hang B., Singer B., Wang Z.
      DNA Repair 4:1399-1409(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    34. "The relative roles in vivo of Saccharomyces cerevisiae Pol eta, Pol zeta, Rev1 protein and Pol32 in the bypass and mutation induction of an abasic site, T-T (6-4) photoadduct and T-T cis-syn cyclobutane dimer."
      Gibbs P.E.M., McDonald J.P., Woodgate R., Lawrence C.W.
      Genetics 169:575-582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    35. "Base pairing and replicative processing of the formamidopyrimidine-dG DNA lesion."
      Ober M., Mueller H., Pieck C., Gierlich J., Carell T.
      J. Am. Chem. Soc. 127:18143-18149(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    36. "Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase eta."
      Carlson K.D., Washington M.T.
      Mol. Cell. Biol. 25:2169-2176(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    37. "DNA synthesis past a 5-methylC-containing cis-syn-cyclobutane pyrimidine dimer by yeast pol eta is highly nonmutagenic."
      Vu B., Cannistraro V.J., Sun L., Taylor J.-S.
      Biochemistry 45:9327-9335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    38. "The in vivo characterization of translesion synthesis across UV-induced lesions in Saccharomyces cerevisiae: insights into Pol zeta- and Pol eta-dependent frameshift mutagenesis."
      Abdulovic A.L., Jinks-Robertson S.
      Genetics 172:1487-1498(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    39. "Poleta, Polzeta and Rev1 together are required for G to T transversion mutations induced by the (+)- and (-)-trans-anti-BPDE-N2-dG DNA adducts in yeast cells."
      Zhao B., Wang J., Geacintov N.E., Wang Z.
      Nucleic Acids Res. 34:417-425(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    40. "Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis."
      Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L., Aggarwal A.K.
      Mol. Cell 8:417-426(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-531.

    Entry informationi

    Entry nameiPOLH_YEAST
    AccessioniPrimary (citable) accession number: Q04049
    Secondary accession number(s): D6VT49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1860 molecules/cell in log phase SD medium.1 Publication

    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