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P13382

- DPOA_YEAST

UniProt

P13382 - DPOA_YEAST

Protein

DNA polymerase alpha catalytic subunit A

Gene

POL1

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 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13.1 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 bindingi1287 – 12871ZincBy similarity
    Metal bindingi1290 – 12901ZincBy similarity
    Metal bindingi1314 – 13141ZincBy similarity
    Metal bindingi1317 – 13171ZincBy similarity
    Metal bindingi1348 – 13481Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi1353 – 13531Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi1367 – 13671Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi1372 – 13721Iron-sulfur (4Fe-4S)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1287 – 131731CysA-typeAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. DNA replication Source: SGD
    2. DNA replication initiation Source: SGD
    3. DNA synthesis involved in DNA repair Source: SGD
    4. double-strand break repair Source: SGD
    5. lagging strand elongation Source: SGD
    6. premeiotic DNA replication Source: SGD
    7. RNA-dependent DNA replication Source: SGD

    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-33130-MONOMER.
    ReactomeiREACT_189247. G1/S-Specific Transcription.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase alpha catalytic subunit A (EC:2.7.7.7)
    Alternative name(s):
    DNA polymerase I subunit A
    DNA polymerase alpha:primase complex p180 subunit
    Short name:
    DNA polymerase-primase complex p180 subunit
    Short name:
    Pol alpha-primase complex p180 subunit
    Gene namesi
    Name:POL1
    Synonyms:CDC17
    Ordered Locus Names:YNL102W
    ORF Names:N2181
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL102w.
    SGDiS000005046. POL1.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha DNA polymerase:primase complex Source: SGD
    2. replication fork Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi236 – 2361D → N: Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. 1 Publication
    Mutagenesisi238 – 2381E → K: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. 1 Publication
    Mutagenesisi241 – 2411P → T: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 14681467DNA polymerase alpha catalytic subunit APRO_0000046440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei31 – 311Phosphoserine3 Publications
    Modified residuei82 – 821Phosphoserine2 Publications
    Modified residuei83 – 831Phosphoserine2 Publications
    Modified residuei84 – 841Phosphoserine2 Publications
    Modified residuei169 – 1691Phosphoserine2 Publications
    Modified residuei170 – 1701Phosphoserine3 Publications
    Modified residuei172 – 1721Phosphothreonine2 Publications
    Modified residuei240 – 2401Phosphoserine3 Publications
    Modified residuei274 – 2741Phosphoserine3 Publications
    Modified residuei309 – 3091Phosphothreonine2 Publications
    Modified residuei313 – 3131Phosphothreonine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP13382.
    PaxDbiP13382.
    PeptideAtlasiP13382.
    PRIDEiP13382.

    Expressioni

    Gene expression databases

    GenevestigatoriP13382.

    Interactioni

    Subunit structurei

    DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits. Subunit B binds to subunit A By similarity. POL1 interacts with CDC13, POB3, SPT16 and MCM10.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC13P327974EBI-6128,EBI-4187
    CTF4Q014545EBI-6128,EBI-5209
    POL12P381215EBI-6128,EBI-6111

    Protein-protein interaction databases

    BioGridi35721. 77 interactions.
    DIPiDIP-2526N.
    IntActiP13382. 14 interactions.
    MINTiMINT-421899.
    STRINGi4932.YNL102W.

    Structurei

    Secondary structure

    1
    1468
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi141 – 1488
    Helixi217 – 23923
    Beta strandi351 – 36212
    Beta strandi365 – 3739
    Beta strandi379 – 3868
    Beta strandi390 – 3978
    Helixi403 – 41816
    Beta strandi425 – 4317
    Beta strandi441 – 45313
    Beta strandi469 – 4768
    Helixi481 – 4888
    Beta strandi496 – 4994
    Beta strandi503 – 5064
    Beta strandi511 – 52010
    Helixi522 – 5243
    Beta strandi525 – 5273
    Beta strandi536 – 54813
    Turni549 – 5524
    Beta strandi553 – 56715
    Beta strandi569 – 5713
    Beta strandi580 – 5867
    Beta strandi589 – 5935
    Helixi598 – 6058
    Beta strandi606 – 6127
    Helixi616 – 63015
    Beta strandi633 – 6397
    Turni640 – 6434
    Helixi644 – 65411
    Helixi660 – 6634
    Beta strandi664 – 6663
    Turni673 – 6764
    Helixi682 – 69110
    Beta strandi694 – 6985
    Helixi702 – 7065
    Helixi716 – 7249
    Helixi739 – 7424
    Helixi744 – 76724
    Helixi770 – 78112
    Helixi785 – 7906
    Helixi794 – 80714
    Beta strandi854 – 8563
    Beta strandi860 – 8645
    Helixi868 – 8758
    Turni880 – 8823
    Helixi905 – 92622
    Helixi930 – 94718
    Helixi948 – 9503
    Helixi951 – 9555
    Helixi964 – 98724
    Beta strandi991 – 9955
    Beta strandi997 – 10037
    Helixi1009 – 102618
    Beta strandi1033 – 104513
    Beta strandi1048 – 10547
    Beta strandi1064 – 10718
    Helixi1072 – 10743
    Helixi1080 – 109314
    Beta strandi1094 – 10974
    Helixi1101 – 111818
    Helixi1124 – 11274
    Beta strandi1129 – 11324
    Helixi1137 – 11393
    Helixi1143 – 11453
    Helixi1147 – 115812
    Beta strandi1167 – 11737
    Turni1189 – 11924
    Beta strandi1193 – 11953
    Helixi1196 – 12005
    Helixi1202 – 12043
    Helixi1210 – 12156
    Turni1216 – 12183
    Helixi1219 – 12257
    Turni1226 – 12283
    Helixi1234 – 12396
    Turni1274 – 12796
    Beta strandi1283 – 12864
    Turni1288 – 12903
    Beta strandi1293 – 12964
    Beta strandi1298 – 13003
    Beta strandi1303 – 13086
    Beta strandi1311 – 13144
    Turni1315 – 13173
    Helixi1323 – 134321
    Beta strandi1346 – 13494
    Turni1351 – 13533
    Beta strandi1356 – 13583
    Beta strandi1375 – 13806
    Helixi1382 – 139514
    Helixi1398 – 14025
    Helixi1424 – 143310
    Helixi1435 – 144915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FLOX-ray2.50B/D/F/H1263-1468[»]
    3OIQX-ray2.40B215-250[»]
    4B08X-ray2.67A349-1258[»]
    4C93X-ray2.69D/E137-149[»]
    4FVMX-ray2.30A349-1258[»]
    4FXDX-ray3.00A/B349-1258[»]
    4FYDX-ray3.10A/B349-1258[»]
    ProteinModelPortaliP13382.
    SMRiP13382. Positions 216-245, 351-1242, 1273-1452.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13382.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1246 – 1381136DNA-binding regionSequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1348 – 137225CysB motifAdd
    BLAST

    Domaini

    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 fingeri1287 – 131731CysA-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0417.
    GeneTreeiENSGT00550000074891.
    HOGENOMiHOG000163524.
    KOiK02320.
    OMAiEKYRDCE.
    OrthoDBiEOG7380D8.

    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.
    IPR024647. DNA_pol_a_cat_su_N.
    IPR023211. DNA_pol_palm_dom.
    IPR012337. RNaseH-like_dom.
    IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
    [Graphical view]
    PfamiPF12254. DNA_pol_alpha_N. 1 hit.
    PF00136. DNA_pol_B. 1 hit.
    PF03104. DNA_pol_B_exo1. 1 hit.
    PF08996. zf-DNA_Pol. 1 hit.
    [Graphical view]
    PRINTSiPR00106. DNAPOLB.
    SMARTiSM00486. POLBc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 2 hits.
    PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR     50
    QELLHDDFVV DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK 100
    NIKREKDHQI TDMLRTQHSK STLLAHAKKS QKKSIPIDNF DDILGEFESG 150
    EVEKPNILLP SKLRENLNSS PTSEFKSSIK RVNGNDESSH DAGISKKVKI 200
    DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS PVVATKRQNV 250
    LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS 300
    NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD 350
    TFQMFWLDYC EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG 400
    KTPTDIHEEI IPLLMDKYGL DNIRAKPQKM KYSFELPDIP SESDYLKVLL 450
    PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN IFESFVIQNR IMGPCWLDIK 500
    GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS LSIQTLMNPK 550
    ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA 600
    LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH 650
    RMHDLNIPTF SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA 700
    NEMGQSLTPK CQSWDLSEMY QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA 750
    LQENITNCMI SAEVSYRIQL LTLTKQLTNL AGNAWAQTLG GTRAGRNEYI 800
    LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK AKYQGGLVFE 850
    PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE 900
    VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM 950
    YGCLGYVNSR FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV 1000
    MIDTGCDNYA DAIKIGLGFK RLVNERYRLL EIDIDNVFKK LLLHAKKKYA 1050
    ALTVNLDKNG NGTTVLEVKG LDMKRREFCP LSRDVSIHVL NTILSDKDPE 1100
    EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY PGGKNMPAVQ 1150
    VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM 1200
    IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR 1250
    REGGNNNGED INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV 1300
    SSNYYRVSYN GLQCKHCEQL FTPLQLTSQI EHSIRAHISL YYAGWLQCDD 1350
    STCGIVTRQV SVFGKRCLND GCTGVMRYKY SDKQLYNQLL YFDSLFDCEK 1400
    NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET GRSVVQKYLN 1450
    DCGRRYVDMT SIFDFMLN 1468
    Length:1,468
    Mass (Da):166,809
    Last modified:October 1, 1996 - v2
    Checksum:i50C9032DBE95B5AE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti759 – 7602MI → IV in AAA34888. (PubMed:3287376)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti493 – 4931G → R in temperature sensitive mutant. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03268 Genomic DNA. Translation: AAA34888.1.
    Z50161 Genomic DNA. Translation: CAA90524.1.
    Z71378 Genomic DNA. Translation: CAA95978.1.
    Z12126 Genomic DNA. Translation: CAA78111.1.
    BK006947 Genomic DNA. Translation: DAA10443.1.
    PIRiS58250.
    RefSeqiNP_014297.3. NM_001182940.3.

    Genome annotation databases

    EnsemblFungiiYNL102W; YNL102W; YNL102W.
    GeneIDi855621.
    KEGGisce:YNL102W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03268 Genomic DNA. Translation: AAA34888.1 .
    Z50161 Genomic DNA. Translation: CAA90524.1 .
    Z71378 Genomic DNA. Translation: CAA95978.1 .
    Z12126 Genomic DNA. Translation: CAA78111.1 .
    BK006947 Genomic DNA. Translation: DAA10443.1 .
    PIRi S58250.
    RefSeqi NP_014297.3. NM_001182940.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FLO X-ray 2.50 B/D/F/H 1263-1468 [» ]
    3OIQ X-ray 2.40 B 215-250 [» ]
    4B08 X-ray 2.67 A 349-1258 [» ]
    4C93 X-ray 2.69 D/E 137-149 [» ]
    4FVM X-ray 2.30 A 349-1258 [» ]
    4FXD X-ray 3.00 A/B 349-1258 [» ]
    4FYD X-ray 3.10 A/B 349-1258 [» ]
    ProteinModelPortali P13382.
    SMRi P13382. Positions 216-245, 351-1242, 1273-1452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35721. 77 interactions.
    DIPi DIP-2526N.
    IntActi P13382. 14 interactions.
    MINTi MINT-421899.
    STRINGi 4932.YNL102W.

    Proteomic databases

    MaxQBi P13382.
    PaxDbi P13382.
    PeptideAtlasi P13382.
    PRIDEi P13382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL102W ; YNL102W ; YNL102W .
    GeneIDi 855621.
    KEGGi sce:YNL102W.

    Organism-specific databases

    CYGDi YNL102w.
    SGDi S000005046. POL1.

    Phylogenomic databases

    eggNOGi COG0417.
    GeneTreei ENSGT00550000074891.
    HOGENOMi HOG000163524.
    KOi K02320.
    OMAi EKYRDCE.
    OrthoDBi EOG7380D8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33130-MONOMER.
    Reactomei REACT_189247. G1/S-Specific Transcription.

    Miscellaneous databases

    EvolutionaryTracei P13382.
    NextBioi 979813.
    PROi P13382.

    Gene expression databases

    Genevestigatori P13382.

    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.
    IPR024647. DNA_pol_a_cat_su_N.
    IPR023211. DNA_pol_palm_dom.
    IPR012337. RNaseH-like_dom.
    IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
    [Graphical view ]
    Pfami PF12254. DNA_pol_alpha_N. 1 hit.
    PF00136. DNA_pol_B. 1 hit.
    PF03104. DNA_pol_B_exo1. 1 hit.
    PF08996. zf-DNA_Pol. 1 hit.
    [Graphical view ]
    PRINTSi PR00106. DNAPOLB.
    SMARTi SM00486. POLBc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 2 hits.
    PROSITEi PS00116. DNA_POLYMERASE_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA polymerase I gene of Saccharomyces cerevisiae: nucleotide sequence, mapping of a temperature-sensitive mutation, and protein homology with other DNA polymerases."
      Pizzagalli A., Valsasnini P., Plevani P., Lucchini G.
      Proc. Natl. Acad. Sci. U.S.A. 85:3772-3776(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-493.
    2. "The sequence of a 21.3 kb DNA fragment from the left arm of yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading frames."
      Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.
      Yeast 12:403-409(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The general amino acid control regulates MET4, which encodes a methionine-pathway-specific transcriptional activator of Saccharomyces cerevisiae."
      Mountain H.A., Bystroem A.S., Korch C.
      Mol. Microbiol. 7:215-228(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
      Strain: ATCC 204508 / S288c.
    6. Cited for: COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
    7. "Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide."
      Ferrari M., Lucchini G., Plevani P., Foiani M.
      J. Biol. Chem. 271:8661-8666(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
    8. "The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein."
      Wittmeyer J., Formosa T.
      Mol. Cell. Biol. 17:4178-4190(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POB3 AND SPT16.
    9. "The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein."
      Qi H., Zakian V.A.
      Genes Dev. 14:1777-1788(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC13, MUTAGENESIS OF ASP-236; GLU-238 AND PRO-241.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast."
      Ricke R.M., Bielinsky A.-K.
      J. Biol. Chem. 281:18414-18425(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM10.
    12. "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-170 AND THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-31; SER-240 AND SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-31; SER-82; SER-83; SER-84; SER-169; SER-170; THR-172; SER-240; SER-274; THR-309 AND THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDPOA_YEAST
    AccessioniPrimary (citable) accession number: P13382
    Secondary accession number(s): D6W177
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 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 1050 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 XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3