RBR1_ARATH
ID RBR1_ARATH Reviewed; 1013 AA.
AC Q9LKZ3; Q93ZS5; Q9C7C9; Q9LHH8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Retinoblastoma-related protein 1;
DE Short=AtRBR;
DE Short=AtRBR1;
GN Name=RBR1; Synonyms=RBR; OrderedLocusNames=At3g12280; ORFNames=F28J15.11;
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], AND INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS
RP REP.
RX PubMed=10880461; DOI=10.1093/emboj/19.13.3485;
RA Kong L.-J., Orozco B.M., Roe J.L., Nagar S., Ou S., Feiler H.S., Durfee T.,
RA Miller A.B., Gruissem W., Robertson D., Hanley-Bowdoin L.;
RT "A geminivirus replication protein interacts with the retinoblastoma
RT protein through a novel domain to determine symptoms and tissue specificity
RT of infection in plants.";
RL EMBO J. 19:3485-3495(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PHOSPHORYLATION BY A CDKA/CYCLIN D KINASE COMPLEX.
RX PubMed=11722776; DOI=10.1046/j.1365-313x.2001.01160.x;
RA Boniotti M.B., Gutierrez C.;
RT "A cell-cycle-regulated kinase activity phosphorylates plant retinoblastoma
RT protein and contains, in Arabidopsis, a CDKA/cyclin D complex.";
RL Plant J. 28:341-350(2001).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15201912; DOI=10.1038/nature02637;
RA Ebel C., Mariconti L., Gruissem W.;
RT "Plant retinoblastoma homologues control nuclear proliferation in the
RT female gametophyte.";
RL Nature 429:776-780(2004).
RN [8]
RP FUNCTION.
RX PubMed=16377572; DOI=10.1016/j.cell.2005.09.042;
RA Wildwater M., Campilho A., Perez-Perez J.M., Heidstra R., Blilou I.,
RA Korthout H., Chatterjee J., Mariconti L., Gruissem W., Scheres B.;
RT "The RETINOBLASTOMA-RELATED gene regulates stem cell maintenance in
RT Arabidopsis roots.";
RL Cell 123:1337-1349(2005).
RN [9]
RP INTERACTION WITH E2FB.
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 [10]
RP FUNCTION, AND INTERACTION WITH WHEAT DWARF VIRUS REPA; E2FA; E2FB AND E2FC.
RX PubMed=16361519; DOI=10.1104/pp.105.071027;
RA Desvoyes B., Ramirez-Parra E., Xie Q., Chua N.-H., Gutierrez C.;
RT "Cell type-specific role of the retinoblastoma/E2F pathway during
RT Arabidopsis leaf development.";
RL Plant Physiol. 140:67-80(2006).
RN [11]
RP FUNCTION.
RX PubMed=16815954; DOI=10.1104/pp.106.083022;
RA Wyrzykowska J., Schorderet M., Pien S., Gruissem W., Fleming A.J.;
RT "Induction of differentiation in the shoot apical meristem by transient
RT overexpression of a retinoblastoma-related protein.";
RL Plant Physiol. 141:1338-1348(2006).
RN [12]
RP INTERACTION WITH NANOVIRUS CLINK PROTEIN.
RX PubMed=17267511; DOI=10.1128/jvi.02103-06;
RA Lageix S., Catrice O., Deragon J.-M., Gronenborn B., Pelissier T.,
RA Ramirez B.C.;
RT "The nanovirus-encoded Clink protein affects plant cell cycle regulation
RT through interaction with the retinoblastoma-related protein.";
RL J. Virol. 81:4177-4185(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [14]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH E2FA.
RX PubMed=18064404; DOI=10.1007/s11103-007-9268-2;
RA Hirano H., Harashima H., Shinmyo A., Sekine M.;
RT "Arabidopsis RETINOBLASTOMA-RELATED PROTEIN 1 is involved in G1 phase cell
RT cycle arrest caused by sucrose starvation.";
RL Plant Mol. Biol. 66:259-275(2008).
RN [15]
RP FUNCTION, AND INTERACTION WITH MSI1.
RX PubMed=18700816; DOI=10.1371/journal.pbio.0060194;
RA Jullien P.E., Mosquna A., Ingouff M., Sakata T., Ohad N., Berger F.;
RT "Retinoblastoma and its binding partner MSI1 control imprinting in
RT Arabidopsis.";
RL PLoS Biol. 6:E194-E194(2008).
RN [16]
RP FUNCTION, AND INDUCTION.
RX PubMed=18976913; DOI=10.1016/j.cub.2008.09.026;
RA Johnston A.J., Matveeva E., Kirioukhova O., Grossniklaus U., Gruissem W.;
RT "A dynamic reciprocal RBR-PRC2 regulatory circuit controls Arabidopsis
RT gametophyte development.";
RL Curr. Biol. 18:1680-1686(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-885 AND SER-898, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [19]
RP FUNCTION.
RX PubMed=19359496; DOI=10.1073/pnas.0810992106;
RA Chen Z., Hafidh S., Poh S.H., Twell D., Berger F.;
RT "Proliferation and cell fate establishment during Arabidopsis male
RT gametogenesis depends on the Retinoblastoma protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7257-7262(2009).
RN [20]
RP FUNCTION, AND REVIEW.
RX PubMed=19704913; DOI=10.4161/cib.8319;
RA Johnston A.J., Gruissem W.;
RT "Gametophyte differentiation and imprinting control in plants: Crosstalk
RT between RBR and chromatin.";
RL Commun. Integr. Biol. 2:144-146(2009).
RN [21]
RP FUNCTION.
RX PubMed=20525851; DOI=10.1105/tpc.110.074591;
RA Borghi L., Gutzat R., Futterer J., Laizet Y., Hennig L., Gruissem W.;
RT "Arabidopsis RETINOBLASTOMA-RELATED is required for stem cell maintenance,
RT cell differentiation, and lateral organ production.";
RL Plant Cell 22:1792-1811(2010).
RN [22]
RP FUNCTION.
RX PubMed=20585548; DOI=10.1371/journal.pgen.1000988;
RA Johnston A.J., Kirioukhova O., Barrell P.J., Rutten T., Moore J.M.,
RA Baskar R., Grossniklaus U., Gruissem W.;
RT "Dosage-sensitive function of retinoblastoma related and convergent
RT epigenetic control are required during the Arabidopsis life cycle.";
RL PLoS Genet. 6:E1000988-E1000988(2010).
RN [23]
RP FUNCTION, INTERACTION WITH ATPK1/S6K1 AND E2FB, AND SUBCELLULAR LOCATION.
RX PubMed=20683442; DOI=10.1038/emboj.2010.164;
RA Henriques R., Magyar Z., Monardes A., Khan S., Zalejski C., Orellana J.,
RA Szabados L., de la Torre C., Koncz C., Bogre L.;
RT "Arabidopsis S6 kinase mutants display chromosome instability and altered
RT RBR1-E2F pathway activity.";
RL EMBO J. 29:2979-2993(2010).
RN [24]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=21217641; DOI=10.1038/emboj.2010.344;
RA Chen Z., Higgins J.D., Hui J.T., Li J., Franklin F.C., Berger F.;
RT "Retinoblastoma protein is essential for early meiotic events in
RT Arabidopsis.";
RL EMBO J. 30:744-755(2011).
RN [25]
RP FUNCTION, AND DEGRADATION BY THE PROTEASOME PATHWAY.
RX PubMed=21444209; DOI=10.1016/j.plaphy.2011.03.001;
RA Hirano H., Shinmyo A., Sekine M.;
RT "Arabidopsis G1 cell cycle proteins undergo proteasome-dependent
RT degradation during sucrose starvation.";
RL Plant Physiol. Biochem. 49:687-691(2011).
RN [26]
RP FUNCTION.
RX PubMed=21693514; DOI=10.1242/dev.060830;
RA Gutzat R., Borghi L., Futterer J., Bischof S., Laizet Y., Hennig L.,
RA Feil R., Lunn J., Gruissem W.;
RT "RETINOBLASTOMA-RELATED PROTEIN controls the transition to autotrophic
RT plant development.";
RL Development 138:2977-2986(2011).
RN [27]
RP INDUCTION BY TCP15.
RX PubMed=21992944; DOI=10.1093/mp/ssr086;
RA Li Z.Y., Li B., Dong A.W.;
RT "The Arabidopsis transcription factor AtTCP15 regulates endoreduplication
RT by modulating expression of key cell-cycle genes.";
RL Mol. Plant 5:270-280(2012).
RN [28]
RP REVIEW.
RX PubMed=22240181; DOI=10.1016/j.tplants.2011.12.001;
RA Gutzat R., Borghi L., Gruissem W.;
RT "Emerging roles of RETINOBLASTOMA-RELATED proteins in evolution and plant
RT development.";
RL Trends Plant Sci. 17:139-148(2012).
RN [29]
RP FUNCTION, AND PHOSPHORYLATION BY CDKA-1.
RX PubMed=22595674; DOI=10.1016/j.devcel.2012.02.015;
RA Nowack M.K., Harashima H., Dissmeyer N., Zhao X., Bouyer D., Weimer A.K.,
RA De Winter F., Yang F., Schnittger A.;
RT "Genetic framework of cyclin-dependent kinase function in Arabidopsis.";
RL Dev. Cell 22:1030-1040(2012).
RN [30]
RP FUNCTION, AND INTERACTION WITH E2FA AND E2FB.
RX PubMed=22307083; DOI=10.1038/emboj.2012.13;
RA Magyar Z., Horvath B., Khan S., Mohammed B., Henriques R., De Veylder L.,
RA Bako L., Scheres B., Bogre L.;
RT "Arabidopsis E2FA stimulates proliferation and endocycle separately through
RT RBR-bound and RBR-free complexes.";
RL EMBO J. 31:1480-1493(2012).
RN [31]
RP FUNCTION, AND INTERACTION WITH SCR.
RX PubMed=22921914; DOI=10.1016/j.cell.2012.07.017;
RA Cruz-Ramirez A., Diaz-Trivino S., Blilou I., Grieneisen V.A., Sozzani R.,
RA Zamioudis C., Miskolczi P., Nieuwland J., Benjamins R., Dhonukshe P.,
RA Caballero-Perez J., Horvath B., Long Y., Mahonen A.P., Zhang H., Xu J.,
RA Murray J.A., Benfey P.N., Bako L., Maree A.F., Scheres B.;
RT "A bistable circuit involving SCARECROW-RETINOBLASTOMA integrates cues to
RT inform asymmetric stem cell division.";
RL Cell 150:1002-1015(2012).
RN [32]
RP FUNCTION.
RX PubMed=23104828; DOI=10.1105/tpc.112.104620;
RA Weimer A.K., Nowack M.K., Bouyer D., Zhao X., Harashima H., Naseer S.,
RA De Winter F., Dissmeyer N., Geldner N., Schnittger A.;
RT "Retinoblastoma related1 regulates asymmetric cell divisions in
RT Arabidopsis.";
RL Plant Cell 24:4083-4095(2012).
RN [33]
RP FUNCTION.
RX PubMed=24118480; DOI=10.1111/tpj.12342;
RA Dorca-Fornell C., Pajor R., Lehmeier C., Perez-Bueno M., Bauch M.,
RA Sloan J., Osborne C., Rolfe S., Sturrock C., Mooney S., Fleming A.;
RT "Increased leaf mesophyll porosity following transient retinoblastoma-
RT related protein silencing is revealed by microcomputed tomography imaging
RT and leads to a system-level physiological response to the altered cell
RT division pattern.";
RL Plant J. 76:914-929(2013).
RN [34]
RP FUNCTION.
RX PubMed=24285791; DOI=10.1105/tpc.113.116632;
RA Perilli S., Perez-Perez J.M., Di Mambro R., Peris C.L., Diaz-Trivino S.,
RA Del Bianco M., Pierdonati E., Moubayidin L., Cruz-Ramirez A.,
RA Costantino P., Scheres B., Sabatini S.;
RT "RETINOBLASTOMA-RELATED protein stimulates cell differentiation in the
RT Arabidopsis root meristem by interacting with cytokinin signaling.";
RL Plant Cell 25:4469-4478(2013).
RN [35]
RP FUNCTION, INTERACTION WITH HAT2, AND MUTAGENESIS OF ASN-849.
RX PubMed=24302889; DOI=10.1371/journal.pbio.1001724;
RA Cruz-Ramirez A., Diaz-Trivino S., Wachsman G., Du Y., Arteaga-Vazquez M.,
RA Zhang H., Benjamins R., Blilou I., Neef A.B., Chandler V., Scheres B.;
RT "A SCARECROW-RETINOBLASTOMA protein network controls protective quiescence
RT in the Arabidopsis root stem cell organizer.";
RL PLoS Biol. 11:E1001724-E1001724(2013).
RN [36]
RP ERRATUM OF PUBMED:24302889.
RX DOI=10.1371/journal.pbio.1001997;
RA Cruz-Ramirez A., Diaz-Trivino S., Wachsman G., Du Y., Arteaga-Vazquez M.,
RA Zhang H., Benjamins R., Blilou I., Neef A.B., Chandler V., Scheres B.;
RL PLoS Biol. 12:E1001997-E1001997(2014).
RN [37]
RP REVIEW.
RX PubMed=24638900; DOI=10.1093/jxb/eru069;
RA Kuwabara A., Gruissem W.;
RT "Arabidopsis RETINOBLASTOMA-RELATED and Polycomb group proteins:
RT cooperation during plant cell differentiation and development.";
RL J. Exp. Bot. 65:2667-2676(2014).
RN [38]
RP FUNCTION, AND INTERACTION WITH FAMA.
RX PubMed=25303364; DOI=10.7554/elife.03271;
RA Matos J.L., Lau O.S., Hachez C., Cruz-Ramirez A., Scheres B.,
RA Bergmann D.C.;
RT "Irreversible fate commitment in the Arabidopsis stomatal lineage requires
RT a FAMA and RETINOBLASTOMA-RELATED module.";
RL Elife 3:0-0(2014).
RN [39]
RP INTERACTION WITH FAMA; MYB124 AND MYB88.
RC STRAIN=cv. Columbia;
RX PubMed=24571519; DOI=10.1111/tpj.12489;
RA Lee E., Lucas J.R., Sack F.D.;
RT "Deep functional redundancy between FAMA and FOUR LIPS in stomatal
RT development.";
RL Plant J. 78:555-565(2014).
RN [40]
RP INTERACTION WITH MYB3R3 AND 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: Key regulator of entry into cell division. Acts as a
CC transcription repressor of E2F target genes, whose activity is required
CC for progress from the G1 to the S phase of the cell cycle.
CC Hyperphosphorylation by CDKA-1 prevents the binding to E2F
CC transcription factors, allowing G1 to S phase transition to operate
CC (PubMed:18064404, PubMed:21444209). Forms a stable complex with E2FA
CC that functions in maintaining cell proliferation through repression of
CC cell differentiation (PubMed:22307083). Plays a central role in the
CC mechanism controlling meristem cell differentiation, cell fate
CC establishment and cell fate maintenance during organogenesis and
CC gametogenesis (PubMed:16377572, PubMed:16815954, PubMed:19359496,
CC PubMed:20525851, PubMed:20585548, PubMed:20683442, PubMed:22595674,
CC PubMed:24285791, PubMed:25303364). Required during lateral organ
CC production (PubMed:20525851). Also involved in controlling asymmetric
CC divisions of stem cells in different stem cell niches (PubMed:22921914,
CC PubMed:23104828, PubMed:24302889). Acts as negative regulator of cell
CC proliferation during leaf and gametophytes development
CC (PubMed:15201912, PubMed:16361519, PubMed:18976913). At later stages of
CC development, restricts the progression through additional endocycles
CC (PubMed:16361519). In the leaf, plays a role in the control of the
CC mesophyll differentiation (PubMed:24118480). Another role is its
CC implication in the regulation of imprinted genes. Acts together with
CC MSI1 to repress the expression of MET1 during gametogenesis. This in
CC turn activates expression of the imprinted genes FIS2 and FWA
CC (PubMed:18700816). Regulates many genes of the polycomb repressive
CC complex 2 (PRC2) (PubMed:18976913, PubMed:19704913, PubMed:20585548).
CC Plays an important role in meiosis affecting different aspects of this
CC complex process (PubMed:21217641). Functions as a positive regulator of
CC the developmental switch from embryonic heterotrophic growth to
CC autotrophic growth (PubMed:21693514). Interaction with mastrevirus RepA
CC or nanovirus Clink protein disrupts the RBR/E2F interaction and
CC releases the transcription of replicative enzymes needed by the virus
CC by increasing the E2F DNA-binding activity (PubMed:16361519).
CC {ECO:0000269|PubMed:15201912, ECO:0000269|PubMed:16361519,
CC ECO:0000269|PubMed:16377572, ECO:0000269|PubMed:16815954,
CC ECO:0000269|PubMed:18064404, ECO:0000269|PubMed:18700816,
CC ECO:0000269|PubMed:18976913, ECO:0000269|PubMed:19359496,
CC ECO:0000269|PubMed:19704913, ECO:0000269|PubMed:20525851,
CC ECO:0000269|PubMed:20585548, ECO:0000269|PubMed:20683442,
CC ECO:0000269|PubMed:21217641, ECO:0000269|PubMed:21444209,
CC ECO:0000269|PubMed:21693514, ECO:0000269|PubMed:22307083,
CC ECO:0000269|PubMed:22921914, ECO:0000269|PubMed:23104828,
CC ECO:0000269|PubMed:24118480, ECO:0000269|PubMed:24285791,
CC ECO:0000269|PubMed:24302889, ECO:0000269|PubMed:24571519,
CC ECO:0000269|PubMed:25303364}.
CC -!- SUBUNIT: Interacts with the begomovirus replication-associated protein
CC (Rep) (PubMed:10880461), the nanovirus Clink protein (PubMed:17267511),
CC the mastrevirus RepA protein, E2FA, E2FB and E2FC (PubMed:16361519,
CC PubMed:18064404, PubMed:16055635, PubMed:20683442, PubMed:22307083).
CC Interacts with MSI1 through its Domain A (PubMed:18700816). Interacts
CC with ATPK1/S6K1 (PubMed:20683442). Interacts with SCR (PubMed:22921914,
CC PubMed:24302889). Interacts with HAT2 (PubMed:24302889). Interacts with
CC FAMA (PubMed:25303364, PubMed:24571519). Interacts with MYB124 and
CC MYB88 (PubMed:24571519). Component of a DREAM-like complex which
CC modulates a variety of developmentally regulated genes and of the
CC mitotic genes in proliferating and differentiated cells. Associates
CC with MYB3R3 in both earlier and later stages of leaves development.
CC Interacts with MYB3R4 only at early stages of leaves development
CC (PubMed:26069325). {ECO:0000269|PubMed:10880461,
CC ECO:0000269|PubMed:16055635, ECO:0000269|PubMed:16361519,
CC ECO:0000269|PubMed:17267511, ECO:0000269|PubMed:18064404,
CC ECO:0000269|PubMed:18700816, ECO:0000269|PubMed:20683442,
CC ECO:0000269|PubMed:22307083, ECO:0000269|PubMed:22921914,
CC ECO:0000269|PubMed:24302889, ECO:0000269|PubMed:25303364,
CC ECO:0000269|PubMed:26069325}.
CC -!- INTERACTION:
CC Q9LKZ3; P42818: ATPK1; NbExp=2; IntAct=EBI-398590, EBI-8107038;
CC Q9LKZ3; Q9FNY0: E2FA; NbExp=4; IntAct=EBI-398590, EBI-1774747;
CC Q9LKZ3; Q9FV71: E2FB; NbExp=4; IntAct=EBI-398590, EBI-1774719;
CC Q9LKZ3; Q9FV70: E2FC; NbExp=2; IntAct=EBI-398590, EBI-2131346;
CC Q9LKZ3; Q9LT47: FIE; NbExp=2; IntAct=EBI-398590, EBI-307146;
CC Q9LKZ3; O22467: MSI1; NbExp=2; IntAct=EBI-398590, EBI-632891;
CC Q9LKZ3; Q9M384: SCR; NbExp=4; IntAct=EBI-398590, EBI-1250484;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20683442}. Note=RBR1
CC nuclear localization is mediated by the RBR1-ATPK1 interaction.
CC {ECO:0000269|PubMed:20683442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LKZ3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in actively dividing cells. Detected in
CC the shoot apical meristem, in young leaf primordia and in both
CC sporophytic tissue and the megagametophyte.
CC {ECO:0000269|PubMed:15201912}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed before and after fertilization
CC (PubMed:15201912). During meiosis, found to localize along the
CC chromosome axes during late G2/early leptotene. As prophase I
CC progressed, a lower expression is detectable at zygotene then more
CC reduced at pachytene. Not detected at later stages (PubMed:21217641).
CC {ECO:0000269|PubMed:15201912, ECO:0000269|PubMed:21217641}.
CC -!- INDUCTION: The polycomb repressive complex 2 (PRC2) containing MSI1,
CC MEA, FIS2 and FIE repress the paternal RBR allele during pollen and
CC seed development (PubMed:18976913). Down-regulated by TCP15
CC (PubMed:21992944). {ECO:0000269|PubMed:18976913,
CC ECO:0000269|PubMed:21992944}.
CC -!- PTM: Highly phosphorylated by CDKA-1 during G1 to S phase transition.
CC Once hyper-phosphorylated, becomes inactive and unable to interact with
CC E2F. {ECO:0000269|PubMed:11722776, ECO:0000269|PubMed:18064404,
CC ECO:0000269|PubMed:22595674}.
CC -!- PTM: Ubiquitinated (Probable). Subject to proteasome-dependent
CC degradation during sucrose starvation (PubMed:21444209).
CC {ECO:0000269|PubMed:21444209, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Plants are gametophytic lethals
CC (PubMed:15201912). During meiosis, reduction in the formation of
CC meiotic crossing-overs and a failure of chromosome synapsis, leading to
CC a dramatic reduction in fertility (PubMed:21217641).
CC {ECO:0000269|PubMed:15201912, ECO:0000269|PubMed:21217641}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51072.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB03137.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF245395; AAF79146.1; -; mRNA.
DR EMBL; AP002047; BAB03137.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069472; AAG51072.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75179.1; -; Genomic_DNA.
DR EMBL; AY056293; AAL07142.1; -; mRNA.
DR EMBL; AY150438; AAN12980.1; -; mRNA.
DR RefSeq; NP_566417.3; NM_112064.5. [Q9LKZ3-1]
DR AlphaFoldDB; Q9LKZ3; -.
DR SMR; Q9LKZ3; -.
DR BioGRID; 5742; 29.
DR DIP; DIP-33046N; -.
DR IntAct; Q9LKZ3; 17.
DR MINT; Q9LKZ3; -.
DR STRING; 3702.AT3G12280.1; -.
DR iPTMnet; Q9LKZ3; -.
DR PaxDb; Q9LKZ3; -.
DR PRIDE; Q9LKZ3; -.
DR ProteomicsDB; 225977; -. [Q9LKZ3-1]
DR EnsemblPlants; AT3G12280.1; AT3G12280.1; AT3G12280. [Q9LKZ3-1]
DR GeneID; 820408; -.
DR Gramene; AT3G12280.1; AT3G12280.1; AT3G12280. [Q9LKZ3-1]
DR KEGG; ath:AT3G12280; -.
DR Araport; AT3G12280; -.
DR TAIR; locus:2082194; AT3G12280.
DR eggNOG; KOG1010; Eukaryota.
DR InParanoid; Q9LKZ3; -.
DR OMA; CAIHLHV; -.
DR PhylomeDB; Q9LKZ3; -.
DR PRO; PR:Q9LKZ3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LKZ3; baseline and differential.
DR Genevisible; Q9LKZ3; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0070176; C:DRM complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IEP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0048229; P:gametophyte development; IMP:UniProtKB.
DR GO; GO:0022619; P:generative cell differentiation; IMP:TAIR.
DR GO; GO:0010377; P:guard cell fate commitment; IGI:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1903866; P:palisade mesophyll development; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:TAIR.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; IMP:TAIR.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IPI:TAIR.
DR GO; GO:2000653; P:regulation of genetic imprinting; IDA:UniProtKB.
DR GO; GO:0051783; P:regulation of nuclear division; IMP:TAIR.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742; PTHR13742; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; DNA-binding; Host-virus interaction;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1013
FT /note="Retinoblastoma-related protein 1"
FT /id="PRO_0000335252"
FT REGION 406..858
FT /note="Pocket"
FT REGION 406..607
FT /note="Domain A"
FT REGION 608..727
FT /note="Spacer"
FT REGION 728..858
FT /note="Domain B"
FT REGION 979..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MUTAGEN 849
FT /note="N->F: Abolishes interaction with HAT2."
FT /evidence="ECO:0000269|PubMed:24302889"
FT CONFLICT 628
FT /note="M -> I (in Ref. 5; AAL07142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 112175 MW; F3CD279ED508C263 CRC64;
MEEVQPPVTP PIEPNGKRSE ASLLDICEKV LSLDGSTCDE ALKLFTETKR ILSASMSNIG
SGTREEVERF WFAFILYSVK RLSVRKEADG LSVSGDNEFN LCQILRALKL NIVDFFKELP
QFVVKAGSVL GELYGADWEN RLQAKEVQAN FVHLSLLSKY YKRGFREFFL TYDANAEKNS
ANSSTYLLDS YRFGWLLFLA LRNHAFSRFK DLVTCSNGVV SILAILIIHV PCRFRNFSIQ
DSSRFVKKGD KGVDLVASLC KIYDASEDEL RIVIDKANNL VETILKKKPS PASECQTDKL
DNIDPDGLTY FEDLLEETSI STSLITLEKD YYDGKGELDE RVFINEEDSL LGSGSLSAGA
VNITGVKRKI DALSSPARTF ISPLSPHKSP AAKTNGISGA TKLAATPVST AMTTAKWLRT
VISPLLPKPS PGLEHFLKSC DRDITNDVTR RAHIILEAIF PNSSLGAQCG GGSLQAVDLM
DDIWAEQRRL EACKLYYRVL EAMCKAEAQI LHANNLNSLL TNERFHRCML ACSAELVLAT
HKTITMLFPA VLERTGITAF DLSKVIESFI RHEDSLPREL RRHLNSLEER LLESMVWEKG
SSMYNSLIVA RPSLALEINQ LGLLAEPMPS LDAIAALINF SDGANHASSV QKHETCPGQN
GGIRSPKRLC TDYRSILVER NSFTSPVKDR LLALGNVKSK MLPPPLQSAF ASPTRPNPGG
GGETCAETGI NIFFTKINKL AAVRINGMVE RLQLSQQIRE SVYCFFQHVL AQRTSLLFSR
HIDQIILCCF YGVAKISQMS LTFREIIYNY RKQPQCKPLV FRSVYVDALQ CRRQGRIGPD
HVDIITFYNE IFIPAVKPLL VELGPVRNDR AVEANNKPEG QCPGSPKVSV FPSVPDMSPK
KVSAVHNVYV SPLRGSKMDA LISHSTKSYY ACVGESTHAY QSPSKDLSAI NNRLNNSSSN
RKRTLNFDAE AGMVSDSMVA NSLNLQNQNQ NQNGSDASSS GGAAPLKTEP TDS
