E2FB_ARATH
ID E2FB_ARATH Reviewed; 469 AA.
AC Q9FV71; Q9FMS8; Q9FNY1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transcription factor E2FB;
DE AltName: Full=E2F transcription factor-1;
DE Short=AtE2F1;
GN Name=E2FB; Synonyms=E2F1; OrderedLocusNames=At5g22220; ORFNames=T6G21;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH DPA AND DPB.
RX PubMed=11108847; DOI=10.1016/s0014-5793(00)02238-9;
RA Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.;
RT "Characterization of two distinct DP-related genes from Arabidopsis
RT thaliana.";
RL FEBS Lett. 486:79-87(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MAIZE
RP RBR1, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11669580; DOI=10.1023/a:1011848528377;
RA de Jager S.M., Menges M., Bauer U.M., Murra J.A.;
RT "Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-
RT regulated gene AtCDC6 and is a member of a multigene family with
RT differential activities.";
RL Plant Mol. Biol. 47:555-568(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 62-469.
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP FUNCTION, INTERACTION WITH DPA AND DPB, DEVELOPMENTAL STAGE, GENE FAMILY,
RP AND NOMENCLATURE.
RX PubMed=11786543; DOI=10.1074/jbc.m110616200;
RA Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C.,
RA Cella R., Albani D.;
RT "The E2F family of transcription factors from Arabidopsis thaliana. Novel
RT and conserved components of the retinoblastoma/E2F pathway in plants.";
RL J. Biol. Chem. 277:9911-9919(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH PURA1.
RX PubMed=11862494; DOI=10.1007/s00438-001-0624-7;
RA Rossignol P., Stevens R., Perennes C., Jasinski S., Cella R.,
RA Tremousaygue D., Bergounioux C.;
RT "AtE2F-a and AtDP-a, members of the E2F family of transcription factors,
RT induce Arabidopsis leaf cells to re-enter S phase.";
RL Mol. Genet. Genomics 266:995-1003(2002).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DPA AND DPB.
RC STRAIN=cv. Columbia;
RX PubMed=11891240; DOI=10.1104/pp.010642;
RA Kosugi S., Ohashi Y.;
RT "Interaction of the Arabidopsis E2F and DP proteins confers their
RT concomitant nuclear translocation and transactivation.";
RL Plant Physiol. 128:833-843(2002).
RN [11]
RP FUNCTION.
RX PubMed=12913157; DOI=10.1104/pp.103.025080;
RA Kosugi S., Ohashi Y.;
RT "Constitutive E2F expression in tobacco plants exhibits altered cell cycle
RT control and morphological change in a cell type-specific manner.";
RL Plant Physiol. 132:2012-2022(2003).
RN [12]
RP FUNCTION, INDUCTION BY AUXIN, PHOSPHORYLATION, AND INTERACTION WITH DPA AND
RP RBR1.
RX PubMed=16055635; DOI=10.1105/tpc.105.033761;
RA Magyar Z., De Veylder L., Atanassova A., Bako L., Inze D., Boegre L.;
RT "The role of the Arabidopsis E2FB transcription factor in regulating auxin-
RT dependent cell division.";
RL Plant Cell 17:2527-2541(2005).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16514015; DOI=10.1104/pp.106.077990;
RA Sozzani R., Maggio C., Varotto S., Canova S., Bergounioux C., Albani D.,
RA Cella R.;
RT "Interplay between Arabidopsis activating factors E2Fb and E2Fa in cell
RT cycle progression and development.";
RL Plant Physiol. 140:1355-1366(2006).
RN [14]
RP INDUCTION BY LIGHT.
RX PubMed=18424613; DOI=10.1105/tpc.107.057075;
RA Lopez-Juez E., Dillon E., Magyar Z., Khan S., Hazeldine S., de Jager S.M.,
RA Murray J.A., Beemster G.T., Boegre L., Shanahan H.;
RT "Distinct light-initiated gene expression and cell cycle programs in the
RT shoot apex and cotyledons of Arabidopsis.";
RL Plant Cell 20:947-968(2008).
RN [15]
RP INTERACTION WITH MYB3R4.
RC STRAIN=cv. Columbia;
RX PubMed=26069325; DOI=10.15252/embj.201490899;
RA Kobayashi K., Suzuki T., Iwata E., Nakamichi N., Suzuki T., Chen P.,
RA Ohtani M., Ishida T., Hosoya H., Mueller S., Leviczky T.,
RA Pettko-Szandtner A., Darula Z., Iwamoto A., Nomoto M., Tada Y.,
RA Higashiyama T., Demura T., Doonan J.H., Hauser M.T., Sugimoto K., Umeda M.,
RA Magyar Z., Boegre L., Ito M.;
RT "Transcriptional repression by MYB3R proteins regulates plant organ
RT growth.";
RL EMBO J. 34:1992-2007(2015).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes whose products are involved in
CC cell cycle regulation or in DNA replication. The binding of
CC retinoblastoma-related proteins represses transactivation. Involved in
CC the control of cell-cycle progression from G1 to S phase and from G2 to
CC M phase. Stimulates cell proliferation and delays differentiation.
CC Represses cell enlargement and endoreduplication in auxin-free
CC conditions. {ECO:0000269|PubMed:11669580, ECO:0000269|PubMed:11786543,
CC ECO:0000269|PubMed:11862494, ECO:0000269|PubMed:11891240,
CC ECO:0000269|PubMed:12913157, ECO:0000269|PubMed:16055635,
CC ECO:0000269|PubMed:16514015}.
CC -!- SUBUNIT: Heterodimer with DP proteins. Interacts (via dimerization
CC domain) preferentially with DPA, but also with DPB. Interacts with
CC PURA1 and retinoblastoma-related protein RBR1. Component of a DREAM-
CC like complex which modulates a variety of developmentally regulated
CC genes and of the mitotic genes in proliferating and differentiated
CC cells. Interacts with MYB3R4 only at early stages of leaves development
CC (PubMed:26069325). {ECO:0000269|PubMed:11108847,
CC ECO:0000269|PubMed:11669580, ECO:0000269|PubMed:11786543,
CC ECO:0000269|PubMed:11862494, ECO:0000269|PubMed:11891240,
CC ECO:0000269|PubMed:16055635, ECO:0000269|PubMed:26069325}.
CC -!- INTERACTION:
CC Q9FV71; P42818: ATPK1; NbExp=3; IntAct=EBI-1774719, EBI-8107038;
CC Q9FV71; Q9FNY3: DPA; NbExp=10; IntAct=EBI-1774719, EBI-1774763;
CC Q9FV71; Q9FNY2: DPB; NbExp=6; IntAct=EBI-1774719, EBI-1774876;
CC Q9FV71; Q9LKZ3: RBR1; NbExp=4; IntAct=EBI-1774719, EBI-398590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Interaction with DPA
CC induces an exclusive nuclear localization, but an interaction with DPB
CC has no effect.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FV71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FV71-2; Sequence=VSP_040804;
CC -!- TISSUE SPECIFICITY: Expressed in proliferating cells and several
CC differentiated tissues. Detected in inflorescence and shoot apical
CC meristems, cotyledonary vascular tissues, leaf primordia, young leaves,
CC base of trichomes, central cylinder and elongation zone of roots,
CC lateral root primordia, flowers, pistils of immature flowers and pollen
CC grains. {ECO:0000269|PubMed:16514015}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a cell cycle-dependent manner. Most
CC abundant at the G1/S transition. Lower but constant level in the
CC following phases. {ECO:0000269|PubMed:11669580,
CC ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:16514015}.
CC -!- INDUCTION: Up-regulated by light and by auxin. May be up-regulated by
CC E2FA. {ECO:0000269|PubMed:16055635, ECO:0000269|PubMed:16514015,
CC ECO:0000269|PubMed:18424613}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16055635}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB17029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ294533; CAC15485.1; -; mRNA.
DR EMBL; AF242580; AAG17608.1; -; mRNA.
DR EMBL; AL589883; CAC34515.1; -; Genomic_DNA.
DR EMBL; AB007651; BAB17029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92998.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92999.1; -; Genomic_DNA.
DR EMBL; AY136479; AAM97144.1; -; mRNA.
DR EMBL; BT006610; AAP31954.1; -; mRNA.
DR RefSeq; NP_001031921.3; NM_001036844.3. [Q9FV71-2]
DR RefSeq; NP_568413.1; NM_122128.3. [Q9FV71-1]
DR AlphaFoldDB; Q9FV71; -.
DR SMR; Q9FV71; -.
DR BioGRID; 17558; 9.
DR IntAct; Q9FV71; 11.
DR MINT; Q9FV71; -.
DR STRING; 3702.AT5G22220.2; -.
DR iPTMnet; Q9FV71; -.
DR PaxDb; Q9FV71; -.
DR PRIDE; Q9FV71; -.
DR ProteomicsDB; 222033; -. [Q9FV71-1]
DR EnsemblPlants; AT5G22220.2; AT5G22220.2; AT5G22220. [Q9FV71-1]
DR EnsemblPlants; AT5G22220.3; AT5G22220.3; AT5G22220. [Q9FV71-2]
DR GeneID; 832283; -.
DR Gramene; AT5G22220.2; AT5G22220.2; AT5G22220. [Q9FV71-1]
DR Gramene; AT5G22220.3; AT5G22220.3; AT5G22220. [Q9FV71-2]
DR KEGG; ath:AT5G22220; -.
DR Araport; AT5G22220; -.
DR TAIR; locus:3685148; AT5G22220.
DR eggNOG; KOG2577; Eukaryota.
DR OMA; DYHRFPS; -.
DR PhylomeDB; Q9FV71; -.
DR PRO; PR:Q9FV71; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FV71; baseline and differential.
DR Genevisible; Q9FV71; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0070176; C:DRM complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:TAIR.
DR GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..469
FT /note="Transcription factor E2FB"
FT /id="PRO_0000406290"
FT DNA_BIND 129..194
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..238
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT REGION 319..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..419
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT REGION 426..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 202..246
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 423..426
FT /note="SGPD -> Y (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040804"
FT CONFLICT 337
FT /note="V -> E (in Ref. 1; CAC15485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51653 MW; ADE1104B34651B7C CRC64;
MSEEVPQQFP SSKRQLHPSL SSMKPPLVAP GEYHRFDAAE TRGGGAVADQ VVSDAIVIKS
TLKRKTDLVN QIVEVNELNT GVLQTPVSGK GGKAKKTSRS AKSNKSGTLA SGSNAGSPGN
NFAQAGTCRY DSSLGLLTKK FINLIKQAED GILDLNKAAD TLEVQKRRIY DITNVLEGIG
LIEKTLKNRI QWKGLDVSKP GETIESIANL QDEVQNLAAE EARLDDQIRE SQERLTSLSE
DENNKRLLFV TENDIKNLPC FQNKTLIAVK APHGTTLEVP DPDEAGGYQR RYRIILRSTM
GPIDVYLVSQ FEESFEDIPQ ADEPSNVPDE PSNVPDVPSN LPSTSGLPEN HDVSMPMKEE
STERNMETQE VDDTQRVYSD IESHDFVDGI MKIVPPDLDM GVDYWFRSEV GEVSITDMWP
DESGPDWNQM ITFDQDHAGP SDNKILEQPQ TPSSPTPEES TATRSPTGS
