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DPOE2_DROME
ID   DPOE2_DROME             Reviewed;         525 AA.
AC   Q9VRQ7; A9UND8; D3DMG0; Q95RJ7;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=DNA polymerase epsilon subunit 2 {ECO:0000312|FlyBase:FBgn0035644};
DE   AltName: Full=DNA polymerase II subunit 2 {ECO:0000255|PIRNR:PIRNR000799};
DE   AltName: Full=DNA polymerase epsilon 58kD subunit {ECO:0000303|PubMed:24224125};
DE   AltName: Full=DNA polymerase epsilon subunit {ECO:0000255|PIRNR:PIRNR000799};
GN   Name=PolE2 {ECO:0000312|FlyBase:FBgn0035644};
GN   Synonyms=DNApol-epsilon58 {ECO:0000303|PubMed:24224125},
GN   DNApolE2 {ECO:0000305}; ORFNames=CG10489 {ECO:0000312|FlyBase:FBgn0035644};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000312|EMBL:ABY20543.1, ECO:0000312|EMBL:ADA53568.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Booth B., Carlson J., Celniker S., Frise E., Kapadia B., Park S., Wan K.,
RA   Yu C., Stapleton M.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAL28879.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-525.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAL28879.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAL28879.1};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5] {ECO:0000312|EMBL:BAD10843.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-525, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R {ECO:0000312|EMBL:BAD10843.1};
RX   PubMed=15135399; DOI=10.1016/j.pep.2004.02.001;
RA   Oshige M., Takeuchi R., Ruike T., Ruike R., Kuroda K., Sakaguchi K.;
RT   "Subunit protein-affinity isolation of Drosophila DNA polymerase catalytic
RT   subunit.";
RL   Protein Expr. Purif. 35:248-256(2004).
RN   [6] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=24224125;
RA   Sahashi R., Matsuda R., Suyari O., Kawai M., Yoshida H., Cotterill S.,
RA   Yamaguchi M.;
RT   "Functional analysis of Drosophila DNA polymerase epsilon p58 subunit.";
RL   Am. J. Cancer Res. 3:478-489(2013).
CC   -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex (By
CC       similarity). Participates in DNA repair and in chromosomal DNA
CC       replication (By similarity). Has a role in the entrance and progression
CC       through S phase (PubMed:24224125). Has a role in endoreplication
CC       (PubMed:24224125). Essential for viability and tissue development
CC       (PubMed:24224125). {ECO:0000250|UniProtKB:P24482,
CC       ECO:0000250|UniProtKB:P56282, ECO:0000269|PubMed:24224125}.
CC   -!- SUBUNIT: Component of the epsilon DNA polymerase complex consisting of
CC       four subunits: the catalytic subunit PolE1/DNApol-epsilon255 and the
CC       accessory subunits PolE2/DNApol-epsilon58, Chrac-14/DNApolE3 and PolE4.
CC       {ECO:0000250|UniProtKB:P56282}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PIRNR:PIRNR000799}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryo and larva (at protein
CC       level). {ECO:0000269|PubMed:15135399, ECO:0000269|PubMed:24224125}.
CC   -!- DISRUPTION PHENOTYPE: Pupal lethal (PubMed:24224125). Results in
CC       smaller eye, leg and wing disk, brain lobe and salivary glands
CC       (PubMed:24224125). Results in defective entry and/or progression though
CC       S phase during the cell cycle in eye imaginal disk cells
CC       (PubMed:24224125). Results in defective endoreplication in salivary
CC       glands (PubMed:24224125). {ECO:0000269|PubMed:24224125}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase epsilon subunit B family.
CC       {ECO:0000255|PIRNR:PIRNR000799}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL28879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ADA53568.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD10843.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB102715; BAD10843.1; ALT_INIT; mRNA.
DR   EMBL; AE014296; AAF50735.1; -; Genomic_DNA.
DR   EMBL; BT031302; ABY20543.1; -; mRNA.
DR   EMBL; BT120029; ADA53568.1; ALT_INIT; mRNA.
DR   EMBL; AY061331; AAL28879.1; ALT_INIT; mRNA.
DR   RefSeq; NP_647995.1; NM_139738.2.
DR   AlphaFoldDB; Q9VRQ7; -.
DR   SMR; Q9VRQ7; -.
DR   IntAct; Q9VRQ7; 6.
DR   MINT; Q9VRQ7; -.
DR   STRING; 7227.FBpp0076789; -.
DR   PaxDb; Q9VRQ7; -.
DR   EnsemblMetazoa; FBtr0077081; FBpp0076789; FBgn0035644.
DR   GeneID; 38661; -.
DR   KEGG; dme:Dmel_CG10489; -.
DR   UCSC; CG10489-RA; d. melanogaster.
DR   CTD; 38661; -.
DR   FlyBase; FBgn0035644; PolE2.
DR   VEuPathDB; VectorBase:FBgn0035644; -.
DR   eggNOG; KOG3818; Eukaryota.
DR   GeneTree; ENSGT00390000012435; -.
DR   HOGENOM; CLU_010628_2_0_1; -.
DR   InParanoid; Q9VRQ7; -.
DR   OMA; CRLQYCT; -.
DR   OrthoDB; 375960at2759; -.
DR   PhylomeDB; Q9VRQ7; -.
DR   Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR   Reactome; R-DME-6782135; Dual incision in TC-NER.
DR   Reactome; R-DME-68952; DNA replication initiation.
DR   Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR   SignaLink; Q9VRQ7; -.
DR   BioGRID-ORCS; 38661; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 38661; -.
DR   PRO; PR:Q9VRQ7; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0035644; Expressed in secondary oocyte and 14 other tissues.
DR   Genevisible; Q9VRQ7; DM.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IPI:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR   GO; GO:0045004; P:DNA replication proofreading; IDA:FlyBase.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:1902969; P:mitotic DNA replication; IMP:FlyBase.
DR   GO; GO:0090068; P:positive regulation of cell cycle process; IMP:FlyBase.
DR   GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:FlyBase.
DR   InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR   InterPro; IPR024639; DNA_pol_e_bsu_N.
DR   InterPro; IPR016266; POLE2.
DR   PANTHER; PTHR12708; PTHR12708; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
DR   Pfam; PF12213; Dpoe2NT; 1.
DR   PIRSF; PIRSF000799; DNA_pol_eps_2; 1.
PE   1: Evidence at protein level;
KW   DNA replication; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..525
FT                   /note="DNA polymerase epsilon subunit 2"
FT                   /id="PRO_0000448259"
FT   CONFLICT        301
FT                   /note="E -> D (in Ref. 3; ABY20543)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  58759 MW;  B91B497B44327373 CRC64;
     MDVDLLPLRK RITNTFKLCG FLIRSENSSY LAEQLLPFDA AERDKWLTVI TENLQSQKLL
     TPHVERAALE KAINELNRVG LDEGETVFAL IDAFTVPRFR YNQRIKKFEL DTQPRQLLTA
     PRMKSDYMQQ RYAMLLQKTL RHDLFAPAVI QDGVGAEAQA KKFKLQFAEN LLATSAMKEA
     VVLGLLTQLK EGKFYVEDPT GCVQLDLTGA RFHAGFFCEG CFVLAEGNYN NGVLKVDGLG
     FPPAEPANSS RAFFGTANTW GGESAKLLKY SAGLQELERT NTETTIVFLS DVRLDLPVVM
     EKLRQLFVGY DSCPPQAIVL MGPFTASTRN HHELRHHLDA LGGLAAGCEQ LKKQTDLILV
     PSSEDPTAPN ILPRAPIPEC LAAGLLKAWP RTQLATNPCR LQYCTQQIVV CRLDLMAKFC
     RNTLHFPEDT SQIEQHFART IVCQGHLVPI HPIAMPVHWD YDPALWLYPL PDLIVMGDSC
     QSFSSSQHGC TVLNTGSFVK SKFAFKVYIP ATRTIEDSEI PDELE
 
 
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