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DPB2_ARATH
ID   DPB2_ARATH              Reviewed;         526 AA.
AC   Q500V9; Q56XM7; Q9C577;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=DNA polymerase epsilon subunit B;
DE   AltName: Full=DNA polymerase II subunit 2 {ECO:0000305};
DE            Short=AtDPB2 {ECO:0000303|PubMed:16212602};
DE   AltName: Full=Protein CYCLOPS 2 {ECO:0000303|PubMed:16212602};
GN   Name=DPB2 {ECO:0000305}; Synonyms=CYL2 {ECO:0000303|PubMed:16212602};
GN   OrderedLocusNames=At5g22110 {ECO:0000312|Araport:AT5G22110};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis cDNA clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH POL2A, DEVELOPMENTAL STAGE, INDUCTION BY CELL
RP   CYCLE, AND DISRUPTION PHENOTYPE.
RX   PubMed=16212602; DOI=10.1111/j.1365-313x.2005.02521.x;
RA   Ronceret A., Guilleminot J., Lincker F., Gadea-Vacas J., Delorme V.,
RA   Bechtold N., Pelletier G., Delseny M., Chaboute M.-E., Devic M.;
RT   "Genetic analysis of two Arabidopsis DNA polymerase epsilon subunits during
RT   early embryogenesis.";
RL   Plant J. 44:223-236(2005).
CC   -!- FUNCTION: As accessory component of DNA polymerase II participates in
CC       chromosomal DNA replication. Required for the timing and determination
CC       of cell fate during plant embryogenesis and root pole development, by
CC       promoting cell cycle and cell type patterning. Necessary for proper
CC       shoot (SAM) and root apical meristem (RAM) functions (By similarity).
CC       Is essential to promote the first divisions of the zygote
CC       (PubMed:16212602). {ECO:0000250|UniProtKB:F4HW04,
CC       ECO:0000269|PubMed:16212602}.
CC   -!- SUBUNIT: Subunit of the DNA polymerase II (Probable). Interacts with
CC       POL2A (via C-terminus) (PubMed:16212602). {ECO:0000269|PubMed:16212602,
CC       ECO:0000305|PubMed:16212602}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: During plant development, expressed in the shoot
CC       and root meristematic regions, but not inthe meristems in seeds at
CC       germination nor in trichomes undergoing endoreduplication. During male
CC       gametogenesis, transiently expressed in immature pollen grains at the
CC       time of post-meiotic mitosis, but not in the female macrospores at any
CC       time of development. Expressed in the embryo sac after fertilization
CC       and the in the embryo proper and suspensor cells until the globular
CC       stage. At the triangular stage, expressed in the forming shoot apical
CC       meristem. {ECO:0000269|PubMed:16212602}.
CC   -!- INDUCTION: Cell cycle regulated. Up-regulated at the G1/S phase
CC       transition and then decreases rapidly as cells progress into S-phase.
CC       {ECO:0000269|PubMed:16212602}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous, due to
CC       embryo development arrested at one-cell stage.
CC       {ECO:0000269|PubMed:16212602}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase epsilon subunit B family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC34504.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL589883; CAC34504.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92984.1; -; Genomic_DNA.
DR   EMBL; AK221646; BAD95306.1; -; mRNA.
DR   EMBL; BT022108; AAY34169.1; -; mRNA.
DR   RefSeq; NP_680197.2; NM_147892.4.
DR   AlphaFoldDB; Q500V9; -.
DR   SMR; Q500V9; -.
DR   STRING; 3702.AT5G22110.1; -.
DR   PaxDb; Q500V9; -.
DR   PRIDE; Q500V9; -.
DR   ProteomicsDB; 220297; -.
DR   EnsemblPlants; AT5G22110.1; AT5G22110.1; AT5G22110.
DR   GeneID; 832272; -.
DR   Gramene; AT5G22110.1; AT5G22110.1; AT5G22110.
DR   KEGG; ath:AT5G22110; -.
DR   Araport; AT5G22110; -.
DR   TAIR; locus:504956460; AT5G22110.
DR   eggNOG; KOG3818; Eukaryota.
DR   HOGENOM; CLU_010628_2_1_1; -.
DR   InParanoid; Q500V9; -.
DR   OMA; CRLQYCT; -.
DR   OrthoDB; 375960at2759; -.
DR   PhylomeDB; Q500V9; -.
DR   PRO; PR:Q500V9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q500V9; baseline and differential.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IPI:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR   InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR   InterPro; IPR016266; POLE2.
DR   PANTHER; PTHR12708; PTHR12708; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
DR   PIRSF; PIRSF000799; DNA_pol_eps_2; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; DNA replication; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..526
FT                   /note="DNA polymerase epsilon subunit B"
FT                   /id="PRO_0000436752"
FT   CONFLICT        110
FT                   /note="K -> R (in Ref. 3; BAD95306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="R -> Q (in Ref. 3; BAD95306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   526 AA;  59540 MW;  00E6A60B2EE777F4 CRC64;
     MSSTSQKRKK IQKKFKNRGY NLKFDALDEI LVFADQFPDD DDGEAIDLLL DNLQETHKSS
     TVDAESVRGL INRLLGAHNA PEEPTTSASS LAIIDAFLVP KFGYDSVKKK FNEHTSSLPI
     HGEASAKTAL YRERFMLLSQ RVSRAEHFSR PAFDAEMSQF ENNEISSIQS LISQRGRKWV
     MGVISQLEDG HFYLEDLSAS VEIDLSKAKI TTGFFTENTI ILAEGEMQVN GIFQVITCGF
     PPLEDRDKTL KAHSEYDFFG GGTLTKEEMI KLADLERQAV NDTFVILSDI WLDDEEVMRK
     LETVLDGFES VETVPSLFVF MGNFCSRPCN LSFGSYSSLR EQFGKLGRMI GNHPRLKENS
     RFLFIPGPED AGPSTVLPRC ALPKYLTEEL RNIIPNAIFS SNPCRVKFYN QEIVFFRQDL
     LYRMRRSCLV TPSSEETNDP FKHLVYTITH QSHLCPLPLM VQPIIWNYDH ALRLYPTPHT
     IVLGDKSEQE VCKFGGTTCF NPGSFSTDST FVAYRPSTQE VELSAL
 
 
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