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P13382

- DPOA_YEAST

UniProt

P13382 - DPOA_YEAST

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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

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

[4Fe-4S] cluster1 PublicationNote: 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

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
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-33130-MONOMER.
ReactomeiREACT_189247. G1/S-Specific Transcription.
REACT_233106. Polymerase switching on the C-strand of the telomere.
REACT_234989. DNA replication initiation.
REACT_235491. Telomere C-strand synthesis initiation.
REACT_243575. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_246435. Polymerase switching.
REACT_252076. Activation of the pre-replicative complex.
REACT_252897. E2F mediated regulation of DNA replication.

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
Complete GO annotation...

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 – 311Phosphoserine2 Publications
Modified residuei82 – 821Phosphoserine1 Publication
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei169 – 1691Phosphoserine1 Publication
Modified residuei170 – 1701Phosphoserine2 Publications
Modified residuei172 – 1721Phosphothreonine1 Publication
Modified residuei240 – 2401Phosphoserine2 Publications
Modified residuei274 – 2741Phosphoserine2 Publications
Modified residuei309 – 3091Phosphothreonine1 Publication
Modified residuei313 – 3131Phosphothreonine2 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. 78 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 – 1488Combined sources
Helixi217 – 23923Combined sources
Beta strandi351 – 36212Combined sources
Beta strandi365 – 3739Combined sources
Beta strandi379 – 3868Combined sources
Beta strandi390 – 3978Combined sources
Helixi403 – 41816Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi441 – 45313Combined sources
Beta strandi469 – 4768Combined sources
Helixi481 – 4888Combined sources
Beta strandi496 – 4994Combined sources
Beta strandi503 – 5064Combined sources
Beta strandi511 – 52010Combined sources
Helixi522 – 5243Combined sources
Beta strandi525 – 5273Combined sources
Beta strandi536 – 54813Combined sources
Turni549 – 5524Combined sources
Beta strandi553 – 56715Combined sources
Beta strandi569 – 5713Combined sources
Beta strandi580 – 5867Combined sources
Beta strandi589 – 5935Combined sources
Helixi598 – 6058Combined sources
Beta strandi606 – 6127Combined sources
Helixi616 – 63015Combined sources
Beta strandi633 – 6397Combined sources
Turni640 – 6434Combined sources
Helixi644 – 65411Combined sources
Helixi660 – 6634Combined sources
Beta strandi664 – 6663Combined sources
Turni673 – 6764Combined sources
Helixi682 – 69110Combined sources
Beta strandi694 – 6985Combined sources
Helixi702 – 7065Combined sources
Helixi716 – 7249Combined sources
Helixi739 – 7424Combined sources
Helixi744 – 76724Combined sources
Helixi770 – 78112Combined sources
Helixi785 – 7906Combined sources
Helixi794 – 80714Combined sources
Beta strandi854 – 8563Combined sources
Beta strandi860 – 8645Combined sources
Helixi868 – 8758Combined sources
Turni880 – 8823Combined sources
Helixi905 – 92622Combined sources
Helixi930 – 94718Combined sources
Helixi948 – 9503Combined sources
Helixi951 – 9555Combined sources
Helixi964 – 98724Combined sources
Beta strandi991 – 9955Combined sources
Beta strandi997 – 10037Combined sources
Helixi1009 – 102618Combined sources
Beta strandi1033 – 104513Combined sources
Beta strandi1048 – 10547Combined sources
Beta strandi1064 – 10718Combined sources
Helixi1072 – 10743Combined sources
Helixi1080 – 109314Combined sources
Beta strandi1094 – 10974Combined sources
Helixi1101 – 111818Combined sources
Helixi1124 – 11274Combined sources
Beta strandi1129 – 11324Combined sources
Helixi1137 – 11393Combined sources
Helixi1143 – 11453Combined sources
Helixi1147 – 115812Combined sources
Beta strandi1167 – 11737Combined sources
Turni1189 – 11924Combined sources
Beta strandi1193 – 11953Combined sources
Helixi1196 – 12005Combined sources
Helixi1202 – 12043Combined sources
Helixi1210 – 12156Combined sources
Turni1216 – 12183Combined sources
Helixi1219 – 12257Combined sources
Turni1226 – 12283Combined sources
Helixi1234 – 12396Combined sources
Turni1274 – 12796Combined sources
Beta strandi1283 – 12864Combined sources
Turni1288 – 12903Combined sources
Beta strandi1293 – 12964Combined sources
Beta strandi1298 – 13003Combined sources
Beta strandi1303 – 13086Combined sources
Beta strandi1311 – 13144Combined sources
Turni1315 – 13173Combined sources
Helixi1323 – 134321Combined sources
Beta strandi1346 – 13494Combined sources
Turni1351 – 13533Combined sources
Beta strandi1356 – 13583Combined sources
Beta strandi1375 – 13806Combined sources
Helixi1382 – 139514Combined sources
Helixi1398 – 14025Combined sources
Helixi1424 – 143310Combined sources
Helixi1435 – 144915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP13382.
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.
IPR029702. POLA/Pol1.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PANTHERiPTHR10322:SF18. PTHR10322:SF18. 1 hit.
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

        10         20         30         40         50
MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR
60 70 80 90 100
QELLHDDFVV DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK
110 120 130 140 150
NIKREKDHQI TDMLRTQHSK STLLAHAKKS QKKSIPIDNF DDILGEFESG
160 170 180 190 200
EVEKPNILLP SKLRENLNSS PTSEFKSSIK RVNGNDESSH DAGISKKVKI
210 220 230 240 250
DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS PVVATKRQNV
260 270 280 290 300
LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS
310 320 330 340 350
NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD
360 370 380 390 400
TFQMFWLDYC EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG
410 420 430 440 450
KTPTDIHEEI IPLLMDKYGL DNIRAKPQKM KYSFELPDIP SESDYLKVLL
460 470 480 490 500
PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN IFESFVIQNR IMGPCWLDIK
510 520 530 540 550
GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS LSIQTLMNPK
560 570 580 590 600
ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA
610 620 630 640 650
LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH
660 670 680 690 700
RMHDLNIPTF SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA
710 720 730 740 750
NEMGQSLTPK CQSWDLSEMY QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA
760 770 780 790 800
LQENITNCMI SAEVSYRIQL LTLTKQLTNL AGNAWAQTLG GTRAGRNEYI
810 820 830 840 850
LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK AKYQGGLVFE
860 870 880 890 900
PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE
910 920 930 940 950
VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM
960 970 980 990 1000
YGCLGYVNSR FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV
1010 1020 1030 1040 1050
MIDTGCDNYA DAIKIGLGFK RLVNERYRLL EIDIDNVFKK LLLHAKKKYA
1060 1070 1080 1090 1100
ALTVNLDKNG NGTTVLEVKG LDMKRREFCP LSRDVSIHVL NTILSDKDPE
1110 1120 1130 1140 1150
EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY PGGKNMPAVQ
1160 1170 1180 1190 1200
VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM
1210 1220 1230 1240 1250
IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR
1260 1270 1280 1290 1300
REGGNNNGED INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV
1310 1320 1330 1340 1350
SSNYYRVSYN GLQCKHCEQL FTPLQLTSQI EHSIRAHISL YYAGWLQCDD
1360 1370 1380 1390 1400
STCGIVTRQV SVFGKRCLND GCTGVMRYKY SDKQLYNQLL YFDSLFDCEK
1410 1420 1430 1440 1450
NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET GRSVVQKYLN
1460
DCGRRYVDMT SIFDFMLN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 78 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.
InParanoidi P13382.
KOi K02320.
OMAi EKYRDCE.
OrthoDBi EOG7380D8.

Enzyme and pathway databases

BioCyci YEAST:G3O-33130-MONOMER.
Reactomei REACT_189247. G1/S-Specific Transcription.
REACT_233106. Polymerase switching on the C-strand of the telomere.
REACT_234989. DNA replication initiation.
REACT_235491. Telomere C-strand synthesis initiation.
REACT_243575. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_246435. Polymerase switching.
REACT_252076. Activation of the pre-replicative complex.
REACT_252897. E2F mediated regulation of DNA replication.

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.
IPR029702. POLA/Pol1.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view ]
PANTHERi PTHR10322:SF18. PTHR10322:SF18. 1 hit.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 152 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