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Protein

DNA polymerase alpha catalytic subunit

Gene

DNApol-alpha180

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polymerase alpha in a complex with DNA primase is a replicative polymerase. In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.1 Publication

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Degradation of single-stranded DNA. It acts progressively in a 3'- to 5'-direction, releasing nucleoside 5'-phosphates.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1296 – 12961ZincBy similarity
Metal bindingi1299 – 12991ZincBy similarity
Metal bindingi1324 – 13241ZincBy similarity
Metal bindingi1329 – 13291ZincBy similarity
Metal bindingi1362 – 13621Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1367 – 13671Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1385 – 13851Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1388 – 13881Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1296 – 132732CysA-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-DME-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-DME-113510. E2F mediated regulation of DNA replication.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-174430. Telomere C-strand synthesis initiation.
R-DME-68952. DNA replication initiation.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69091. Polymerase switching.
R-DME-69166. Removal of the Flap Intermediate.
R-DME-69183. Processive synthesis on the lagging strand.
R-DME-69205. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha catalytic subunit (EC:2.7.7.7)
Gene namesi
Name:DNApol-alpha180
Synonyms:DNApol-alpha, POLA
ORF Names:CG6349
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0259113. DNApol-alpha180.

Subcellular locationi

  • Nucleus 2 Publications

GO - Cellular componenti

  • alpha DNA polymerase:primase complex Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6039.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14881488DNA polymerase alpha catalytic subunitPRO_0000046432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei262 – 2621Phosphoserine1 Publication
Modified residuei269 – 2691Phosphoserine1 Publication
Modified residuei314 – 3141Phosphothreonine1 Publication
Modified residuei317 – 3171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP26019.

PTM databases

iPTMnetiP26019.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Highest level of zygotic expression seen in second-instar larva, level is reduced at other stages of development.1 Publication

Gene expression databases

BgeeiP26019.
GenevisibleiP26019. DM.

Interactioni

Protein-protein interaction databases

BioGridi67519. 3 interactions.
DIPiDIP-23937N.
IntActiP26019. 6 interactions.
MINTiMINT-206832.
STRINGi7227.FBpp0083514.

Chemistry

BindingDBiP26019.

Structurei

3D structure databases

ProteinModelPortaliP26019.
SMRiP26019. Positions 364-1237, 1323-1429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni638 – 758121Contains conserved residues essential for 3' -> 5' exonuclease activitiesAdd
BLAST
Regioni675 – 73460DNA-binding regionSequence analysisAdd
BLAST
Regioni1255 – 1380126DNA-binding regionSequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1038Nuclear localization signalSequence analysis
Motifi1362 – 138827CysB 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 fingeri1296 – 132732CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
GeneTreeiENSGT00550000074891.
InParanoidiP26019.
KOiK02320.
OMAiRLMCELN.
OrthoDBiEOG7CNZDZ.
PhylomeDBiP26019.

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:SF21. PTHR10322:SF21. 5 hits.
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.

P26019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESPSEPRA KRQRVDKNGR FAAMERLRQL KGTKNKCKVE DQVDDVYDVV
60 70 80 90 100
DEREYAKRAQ EKYGDDWIEE DGTGYAEDLR DFFEDEDEYS DGEEDRKDSK
110 120 130 140 150
KKKGVAPNSK KRPRENEKPV TGKASIKNLF SNAVPKKMDV KTSVKDDDIL
160 170 180 190 200
ADILGEIKEE PAATSEKAEK VIAPAKISVT SRKFDAAAAK EYMNSFLNNI
210 220 230 240 250
KVQEQERKKA EASSDNEMLE RILKPKAAVP NTKVAFFSSP TIKKEPMPEK
260 270 280 290 300
TPAKKATEDP FSDNEMDFSC LDDDENQFDV EKTQQTEKVS QTKTAAEKTS
310 320 330 340 350
QSKVAEKSAP KKETTGSPKE SESEDISRLL NNWESICQMD DDFEKSVLTT
360 370 380 390 400
EQDSTISSDQ QLRFWYWEAY EDPVKMPGEV FLFGRTADGK SVCLRVQNIN
410 420 430 440 450
RVLYLLPRQF LLDPISKEPT KQKVTVADIY KEFDSEVANQ LKLEFFRSRK
460 470 480 490 500
VTKSFAHHAI GIEVPQSCDY LEVHYDGKKP LPNLSADKKY NSIAHIFGAT
510 520 530 540 550
TNALERFLLD RKIKGPCWLQ VTGFKVSPTP MSWCNTEVTL TEPKNVELVQ
560 570 580 590 600
DKGKPAPPPP LTLLSLNVRT SMNPKTSRNE ICMISMLTHN RFHIDRPAPQ
610 620 630 640 650
PAFNRHMCAL TRPAVVSWPL DLNFEMAKYK STTVHKHDSE RALLSWFLAQ
660 670 680 690 700
YQKIDADLIV TFDSMDCQLN VITDQIVALK IPQWSRMGRL RLSQSFGKRL
710 720 730 740 750
LEHFVGRMVC DVKRSAEECI RARSYDLQTL CKQVLKLKES ERMEVNADDL
760 770 780 790 800
LEMYEKGESI TKLISLTMQD NSYLLRLMCE LNIMPLALQI TNICGNTMTR
810 820 830 840 850
TLQGGRSERN EFLLLHAFHE KNYIVPDKKP VSKRSGAGDT DATLSGADAT
860 870 880 890 900
MQTKKKAAYA GGLVLEPMRG LYEKYVLLMD FNSLYPSIIQ EYNICFTTVQ
910 920 930 940 950
QPVDADELPT LPDSKTEPGI LPLQLKRLVE SRKEVKKLMA APDLSPELQM
960 970 980 990 1000
QYHIRQMALK LTANSMYGCL GFAHSRFFAQ HLAALVTHKG REILTNTQQL
1010 1020 1030 1040 1050
VQKMNYDVVY GDTDSLMINT NITDYDQVYK IGHNIKQSVN KLYKQLELDI
1060 1070 1080 1090 1100
DGVFGCLLLL KKKKYAAIKL SKDSKGNLRR EQEHKGLDIV RRDWSQLAVM
1110 1120 1130 1140 1150
VGKAVLDEVL SEKPLEEKLD AVHAQLEKIK TQIAEGVVPL PLFVITKQLT
1160 1170 1180 1190 1200
RTPQEYANSA SLPHVQVALR MNRERNRRYK KGDMVDYVIC LDGTTNAAMQ
1210 1220 1230 1240 1250
RAYHLDELKT SEDKKLQLDT NYYLGHQIHP VVTRMVEVLE GTDASRIAEC
1260 1270 1280 1290 1300
LGMDPTKFRQ NAQRTQRENT EQSEGESLLK TTLQLYRLCE PFRFQCVTCK
1310 1320 1330 1340 1350
TEQLMASAYR PGPSNSHIAV LQQCAKSECQ TAPIQYLASV RNQLQLSMRQ
1360 1370 1380 1390 1400
YVQRFYKNWL VCDHPDCNFN TRTHSLRKKS HRPLCQKCRS GSLLRQYTER
1410 1420 1430 1440 1450
DLYNQLCYLR FMFDLGKQTL QQKPTLTPEL EQAYQLLYET VDQQLQSSSY
1460 1470 1480
VIISLSKLFA RSLAQMSLQP SVAQPQIEAI PSALADVV
Length:1,488
Mass (Da):169,903
Last modified:March 15, 2004 - v2
Checksum:i76C65EE2E2D5B065
GO

Sequence cautioni

The sequence AAL48000.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA14340.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA32745.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991S → L in S48157 (PubMed:1429896).Curated
Sequence conflicti117 – 1171E → A in BAA14340 (PubMed:1923767).Curated
Sequence conflicti117 – 1171E → A in BAA32745 (PubMed:9858578).Curated
Sequence conflicti137 – 1371K → KK in S48157 (PubMed:1429896).Curated
Sequence conflicti148 – 1481D → DD in S48157 (PubMed:1429896).Curated
Sequence conflicti200 – 2001I → M in BAA14340 (PubMed:1923767).Curated
Sequence conflicti200 – 2001I → M in BAA32745 (PubMed:9858578).Curated
Sequence conflicti210 – 22718AEASS…LKPKA → RRPVAITRCWSAFSPRQ in S48157 (PubMed:1429896).CuratedAdd
BLAST
Sequence conflicti364 – 3641F → L in BAA14340 (PubMed:1923767).Curated
Sequence conflicti364 – 3641F → L in BAA32745 (PubMed:9858578).Curated
Sequence conflicti376 – 3761M → I in BAA14340 (PubMed:1923767).Curated
Sequence conflicti376 – 3761M → I in BAA32745 (PubMed:9858578).Curated
Sequence conflicti379 – 3791E → Q in BAA14340 (PubMed:1923767).Curated
Sequence conflicti379 – 3791E → Q in BAA32745 (PubMed:9858578).Curated
Sequence conflicti478 – 4781K → N in BAA14340 (PubMed:1923767).Curated
Sequence conflicti478 – 4781K → N in BAA32745 (PubMed:9858578).Curated
Sequence conflicti739 – 7391E → G in S48157 (PubMed:1429896).Curated
Sequence conflicti818 – 8192FH → ST in BAA14340 (PubMed:1923767).Curated
Sequence conflicti818 – 8192FH → ST in BAA32745 (PubMed:9858578).Curated
Sequence conflicti819 – 8191H → Y in AAL48000 (PubMed:12537569).Curated
Sequence conflicti842 – 8421A → R in BAA14340 (PubMed:1923767).Curated
Sequence conflicti842 – 8421A → R in BAA32745 (PubMed:9858578).Curated
Sequence conflicti881 – 8811F → L in BAA14340 (PubMed:1923767).Curated
Sequence conflicti881 – 8811F → L in BAA32745 (PubMed:9858578).Curated
Sequence conflicti897 – 8982TT → NP in BAA14340 (PubMed:1923767).Curated
Sequence conflicti897 – 8982TT → NP in BAA32745 (PubMed:9858578).Curated
Sequence conflicti992 – 9932EI → D in BAA14340 (PubMed:1923767).Curated
Sequence conflicti992 – 9932EI → D in BAA32745 (PubMed:9858578).Curated
Sequence conflicti1155 – 11573EYA → DYR in BAA14340 (PubMed:1923767).Curated
Sequence conflicti1155 – 11573EYA → DYR in BAA32745 (PubMed:9858578).Curated
Sequence conflicti1178 – 11781R → L in S48157 (PubMed:1429896).Curated
Sequence conflicti1187 – 11893YVI → LCD in BAA14340 (PubMed:1923767).Curated
Sequence conflicti1187 – 11893YVI → LCD in BAA32745 (PubMed:9858578).Curated
Sequence conflicti1197 – 12059AAMQRAYHL → WPCSEHTIS in S48157 (PubMed:1429896).Curated
Sequence conflicti1222 – 12232YY → LL in S48157 (PubMed:1429896).Curated
Sequence conflicti1292 – 131019FRFQC…ASAYR → SASSALPVRRSSWRLRTD in S48157 (PubMed:1429896).CuratedAdd
BLAST
Sequence conflicti1325 – 135127AKSEC…SMRQY → VSPSAKRHRFSTWQACAILQ LSM in BAA14340 (PubMed:1923767).CuratedAdd
BLAST
Sequence conflicti1392 – 13921S → T in S48157 (PubMed:1429896).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90310 Genomic DNA. Translation: BAA14340.1. Sequence problems.
S48157 mRNA. No translation available.
AB011813 Genomic DNA. Translation: BAA32745.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55908.2.
AY070529 mRNA. Translation: AAL48000.1. Different initiation.
PIRiS28079.
RefSeqiNP_536736.2. NM_080488.3.
UniGeneiDm.1592.

Genome annotation databases

EnsemblMetazoaiFBtr0084115; FBpp0083514; FBgn0259113.
GeneIDi42553.
KEGGidme:Dmel_CG6349.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90310 Genomic DNA. Translation: BAA14340.1. Sequence problems.
S48157 mRNA. No translation available.
AB011813 Genomic DNA. Translation: BAA32745.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAF55908.2.
AY070529 mRNA. Translation: AAL48000.1. Different initiation.
PIRiS28079.
RefSeqiNP_536736.2. NM_080488.3.
UniGeneiDm.1592.

3D structure databases

ProteinModelPortaliP26019.
SMRiP26019. Positions 364-1237, 1323-1429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67519. 3 interactions.
DIPiDIP-23937N.
IntActiP26019. 6 interactions.
MINTiMINT-206832.
STRINGi7227.FBpp0083514.

Chemistry

BindingDBiP26019.
ChEMBLiCHEMBL6039.

PTM databases

iPTMnetiP26019.

Proteomic databases

PaxDbiP26019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084115; FBpp0083514; FBgn0259113.
GeneIDi42553.
KEGGidme:Dmel_CG6349.

Organism-specific databases

CTDi42553.
FlyBaseiFBgn0259113. DNApol-alpha180.

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
GeneTreeiENSGT00550000074891.
InParanoidiP26019.
KOiK02320.
OMAiRLMCELN.
OrthoDBiEOG7CNZDZ.
PhylomeDBiP26019.

Enzyme and pathway databases

ReactomeiR-DME-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-DME-113510. E2F mediated regulation of DNA replication.
R-DME-174411. Polymerase switching on the C-strand of the telomere.
R-DME-174430. Telomere C-strand synthesis initiation.
R-DME-68952. DNA replication initiation.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69091. Polymerase switching.
R-DME-69166. Removal of the Flap Intermediate.
R-DME-69183. Processive synthesis on the lagging strand.
R-DME-69205. G1/S-Specific Transcription.

Miscellaneous databases

ChiTaRSiDNApol-alpha50. fly.
GenomeRNAii42553.
PROiP26019.

Gene expression databases

BgeeiP26019.
GenevisibleiP26019. DM.

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:SF21. PTHR10322:SF21. 5 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression during development of Drosophila melanogaster gene for DNA polymerase alpha."
    Hirose F., Yamaguchi M., Nishida Y., Masutani M., Miyazawa H., Hanaoka F., Matsukage A.
    Nucleic Acids Res. 19:4991-4998(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 131-136; 181-188 AND 238-251.
    Strain: Oregon-R.
  2. "Molecular characterisation of the gene for the 180 kDa subunit of the DNA polymerase-primase of Drosophila melanogaster."
    Melov S., Vaughan H., Cotterill S.
    J. Cell Sci. 102:847-856(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  3. "Specification of regions of DNA replication initiation during embryogenesis in the 65-kilobase DNApolalpha-dE2F locus of Drosophila melanogaster."
    Sasaki T., Sawado T., Yamaguchi M., Shinomiya T.
    Mol. Cell. Biol. 19:547-555(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: Oregon-R.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1488.
    Strain: Berkeley.
    Tissue: Ovary.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-262; SER-269; THR-314 AND SER-317, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDPOLA_DROME
AccessioniPrimary (citable) accession number: P26019
Secondary accession number(s): O77034, Q8T992, Q9VD90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: July 6, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

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

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.