RB_RAT
ID RB_RAT Reviewed; 920 AA.
AC P33568; Q63527;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Retinoblastoma-associated protein;
DE AltName: Full=pRb;
DE Short=Rb;
DE AltName: Full=pp105;
GN Name=Rb1; Synonyms=Rb-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-920.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7665085; DOI=10.1016/0378-1119(95)00154-x;
RA Esumi M., Idutsu T., Kinugasa S., Ohno M., Nakabayashi H., Ikeda T.,
RA Shikata T.;
RT "Isolation and sequence polymorphism of a rat retinoblastoma (RB) cDNA.";
RL Gene 161:231-235(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 806-920.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8441612; DOI=10.1093/nar/21.1.170;
RA Roy N.K., Ballesteros A., Garte S.J.;
RT "Cloning and sequence of the rat retinoblastoma (Rb) gene cDNA.";
RL Nucleic Acids Res. 21:170-170(1993).
RN [4]
RP INTERACTION WITH RBBP9.
RX PubMed=9697699; DOI=10.1038/1258;
RA Woitach J.T., Zhang M., Niu C.-H., Thorgeirsson S.S.;
RT "A retinoblastoma-binding protein that affects cell-cycle control and
RT confers transforming ability.";
RL Nat. Genet. 19:371-374(1998).
RN [5]
RP PHOSPHORYLATION BY CDK1 AND CDK2, AND INTERACTION WITH CDK1 AND CDK2.
RX PubMed=10542199; DOI=10.1074/jbc.274.45.31775;
RA Choi K.S., Eom Y.W., Kang Y., Ha M.J., Rhee H., Yoon J.-W., Kim S.-J.;
RT "Cdc2 and Cdk2 kinase activated by transforming growth factor-beta1 trigger
RT apoptosis through the phosphorylation of retinoblastoma protein in FaO
RT hepatoma cells.";
RL J. Biol. Chem. 274:31775-31783(1999).
RN [6]
RP INTERACTION WITH DNMT1.
RX PubMed=10888886; DOI=10.1038/77124;
RA Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
RA Wolffe A.P.;
RT "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription
RT from E2F-responsive promoters.";
RL Nat. Genet. 25:338-342(2000).
RN [7]
RP FUNCTION, INTERACTION WITH SMARCA4 AND HDAC1, PHOSPHORYLATION AT SER-787,
RP DEPHOSPHORYLATION, AND MUTAGENESIS OF SER-772; SER-780 AND SER-787.
RX PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA Qiu Z., Ghosh A.;
RT "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-
RT dependent gene expression.";
RL Neuron 60:775-787(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-363; THR-366 AND
RP SER-799, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Tumor suppressor that is a key regulator of the G1/S
CC transition of the cell cycle. The hypophosphorylated form binds
CC transcription regulators of the E2F family, preventing transcription of
CC E2F-responsive genes. Both physically blocks E2Fs transactivating
CC domain and recruits chromatin-modifying enzymes that actively repress
CC transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces
CC its dissociation from E2Fs, thereby activating transcription of E2F
CC responsive genes and triggering entry into S phase. RB1 also promotes
CC the G0-G1 transition upon phosphorylation and activation by
CC CDK3/cyclin-C. Directly involved in heterochromatin formation by
CC maintaining overall chromatin structure and, in particular, that of
CC constitutive heterochromatin by stabilizing histone methylation.
CC Recruits and targets histone methyltransferases SUV39H1, KMT5B and
CC KMT5C, leading to epigenetic transcriptional repression. Controls
CC histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase
CC activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1
CC by recruiting a histone deacetylase (HDAC) complex to the c-FOS
CC promoter (PubMed:19081374). In resting neurons, transcription of the c-
CC FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-
CC RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is
CC dephosphorylated by calcineurin, which leads to release of the
CC repressor complex (By similarity). {ECO:0000250|UniProtKB:P06400,
CC ECO:0000250|UniProtKB:P13405, ECO:0000269|PubMed:19081374}.
CC -!- SUBUNIT: The hypophosphorylated form interacts with and sequesters the
CC E2F1 transcription factor. Interacts with heterodimeric E2F/DP
CC transcription factor complexes containing TFDP1 and either E2F1, E2F3,
CC E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form interacts
CC with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts
CC with the N-terminal domain of TAF1. Interacts with SNW1, ATAD5, AATF,
CC DNMT1, LIN9, LMNA, KMT5B, KMT5C, PELP1, UHRF2 and TMPO-alpha. May
CC interact with NDC80. Interacts with GRIP1 and UBR4. Interacts with
CC ARID4A and KDM5B. Interacts with E4F1, LIMD1 and USP4. Interacts with
CC PRMT2. Interacts (when methylated at Lys-852) with L3MBTL. Interacts
CC with CHEK2; phosphorylates RB1 (By similarity). Interacts with
CC SMARCA4/BRG1 and HDAC1. Binds to CDK1 and CDK2. P-TEFB complex
CC interacts with RB1; promotes phosphorylation of RB1 (By similarity).
CC Interacts with RBBP9; the interaction disrupts RB1 binding to E2F1
CC (PubMed:9697699). Interacts with KAT2B/PCAF and EP300/P300 (By
CC similarity). Interacts with PAX5 (By similarity).
CC {ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P13405,
CC ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:10888886,
CC ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:9697699}.
CC -!- INTERACTION:
CC P33568; O09139: E2f1; NbExp=2; IntAct=EBI-1162932, EBI-1211101;
CC P33568; O88350: Rbbp9; NbExp=4; IntAct=EBI-1162932, EBI-1211014;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13405}.
CC -!- PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-
CC 560 in G1, thereby releasing E2F1 which is then able to activate cell
CC growth. Dephosphorylated at the late M phase. Phosphorylation of
CC threonine residues in domain C promotes interaction between the C-
CC terminal domain C and the Pocket domain, and thereby inhibits
CC interactions with heterodimeric E2F/DP transcription factor complexes.
CC CDK3/cyclin-C-mediated phosphorylation at Ser-799 and Ser-803 is
CC required for G0-G1 transition (By similarity). Dephosphorylated at Ser-
CC 787 by calcineruin upon calcium stimulation. {ECO:0000250,
CC ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:19081374}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1. Monomethylation at Lys-
CC 802 by SMYD2 enhances phosphorylation at Ser-799 and Ser-803, and
CC promotes cell cycle progression. Monomethylation at Lys-852 by SMYD2
CC promotes interaction with L3MBTL1 (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated during keratinocyte differentiation. Acetylation at
CC Ser-799 and Ser-803 regulates subcellular localization. Can be
CC deacetylated by SIRT1. {ECO:0000250|UniProtKB:P06400}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
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DR EMBL; D25233; BAA04958.1; -; mRNA.
DR EMBL; L07126; AAA42090.1; -; mRNA.
DR PIR; S35544; S35544.
DR RefSeq; NP_058741.1; NM_017045.1.
DR AlphaFoldDB; P33568; -.
DR SMR; P33568; -.
DR BioGRID; 246837; 5.
DR IntAct; P33568; 3.
DR STRING; 10116.ENSRNOP00000021752; -.
DR iPTMnet; P33568; -.
DR PhosphoSitePlus; P33568; -.
DR PaxDb; P33568; -.
DR PRIDE; P33568; -.
DR DNASU; 24708; -.
DR Ensembl; ENSRNOT00000021752; ENSRNOP00000021752; ENSRNOG00000016029.
DR GeneID; 24708; -.
DR KEGG; rno:24708; -.
DR UCSC; RGD:3540; rat.
DR CTD; 5925; -.
DR RGD; 3540; Rb1.
DR eggNOG; KOG1010; Eukaryota.
DR InParanoid; P33568; -.
DR OrthoDB; 113612at2759; -.
DR PhylomeDB; P33568; -.
DR TreeFam; TF105568; -.
DR Reactome; R-RNO-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-RNO-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-RNO-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-RNO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR Reactome; R-RNO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR PRO; PR:P33568; -.
DR Proteomes; UP000002494; Chromosome 15.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0061793; C:chromatin lock complex; ISO:RGD.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0035189; C:Rb-E2F complex; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; ISO:RGD.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; ISO:RGD.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0034349; P:glial cell apoptotic process; ISO:RGD.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISO:RGD.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:RGD.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:ARUK-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IMP:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:ARUK-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:RGD.
DR GO; GO:1902948; P:negative regulation of tau-protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0042551; P:neuron maturation; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:1904028; P:positive regulation of collagen fibril organization; ISO:RGD.
DR GO; GO:1903055; P:positive regulation of extracellular matrix organization; ISO:RGD.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:RGD.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:RGD.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:0071922; P:regulation of cohesin loading; ISO:RGD.
DR GO; GO:0043550; P:regulation of lipid kinase activity; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0031134; P:sister chromatid biorientation; ISO:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR015030; RB_C.
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 Pfam; PF08934; Rb_C; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Chromatin regulator; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT CHAIN 2..920
FT /note="Retinoblastoma-associated protein"
FT /id="PRO_0000167838"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..763
FT /note="Pocket; binds T and E1A"
FT /evidence="ECO:0000250"
FT REGION 366..572
FT /note="Domain A"
FT /evidence="ECO:0000250"
FT REGION 573..631
FT /note="Spacer"
FT /evidence="ECO:0000250"
FT REGION 632..763
FT /note="Domain B"
FT /evidence="ECO:0000250"
FT REGION 755..920
FT /note="Interaction with LIMD1"
FT /evidence="ECO:0000250"
FT REGION 763..920
FT /note="Domain C; mediates interaction with E4F1"
FT /evidence="ECO:0000250"
FT REGION 895..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 852..868
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N-dimethylproline"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 242
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 245
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 560
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT MOD_RES 604
FT /note="Phosphoserine; by CHEK2 and CHEK1"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06400, ECO:0000255"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06400, ECO:0000255"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19081374"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 802
FT /note="N6-methyllysine; by SMYD2"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 803
FT /note="Phosphoserine; by CDK1 and CDK3"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 813
FT /note="Phosphothreonine; by CDK6"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 815
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 818
FT /note="Phosphothreonine; by CDK4"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 833
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 852
FT /note="N6-methyllysine; by SMYD2"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 865
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MOD_RES 866
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000250|UniProtKB:P06400"
FT MUTAGEN 772
FT /note="S->A: Decreased association with HDAC1; when
FT associated with A-780 and A-787."
FT /evidence="ECO:0000269|PubMed:19081374"
FT MUTAGEN 780
FT /note="S->A: Decreased association with HDAC1; when
FT associated with A-772 and A-787."
FT /evidence="ECO:0000269|PubMed:19081374"
FT MUTAGEN 787
FT /note="S->A: Decreased association with HDAC1; when
FT associated with A-772 and A-780."
FT /evidence="ECO:0000269|PubMed:19081374"
FT CONFLICT 668
FT /note="L -> P (in Ref. 2; BAA04958)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="I -> M (in Ref. 2; BAA04958)"
FT /evidence="ECO:0000305"
FT CONFLICT 866..867
FT /note="KL -> TW (in Ref. 3; AAA42090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 920 AA; 105025 MW; 3BA735EA59927301 CRC64;
MPPKAPRRTA AAEPPPPPPP PPEDDPAQDS DPEELPLIRL EFEKIEEPEF IALCQKLKVP
DHVRERAWLT WEKVSSVDGI LEGYIQKKKE LWGICIFIAA VDLDEMPFTF TELQKSIETS
VYKFFDLLKE IDTSTKVDNA VSRLLKKYNV LCALYSKLER TCGLIYLTQP SSGLSTEINS
MLVLKVSWIT FLLAKGEVVQ MEDDLVISFQ LMLCVLDYFI KLSPPALLRE PYKTAATPIN
GSPRTPRRGQ NRSARIAKQL ESDTRTIEVL CKEHECNVDE VKNVYFKNFI PFISSLGIVS
SNGLPELESL SKRYEEVYLK SKDLDARLFL DHDKTLQTDT IDSFETERTP RKSNPDEEAN
MVTPHTPVRT VMNTIQQLMV ILNSASDQPS ENLISYFSNC TVNPKENILK RVKDVGHIFK
EKFASAVGQG CIDIGAQRYK LGVRLYYRVM ESMLKSEEER LSIQNFSKLL NDNIFHMSLL
ACALEVVMAT YSRSMLQNLD SGTDLSFPWI LNVLNLKAFD FYKVIESFIK VEANLTREMI
KHLERCEHRI MESLAWLSDS PLFDLIKQSK DGEGPDHLES ACSLSLPLQS NHTAADMYLS
PIRSPKKRTS TTRVNSAANT ETQAASAFHT QKPLKSTSLS LFYKKVYRLA YLRLNTLCAR
LLSDHPELEH IIWTLFQHTL ENEYELMKDR HLDQIMMCSM YGICKVKNID LKFKIIVTAY
KDLPHAAQET FKRVLIREEE FDSIIVFYNS VFMQRLKTNI LQYASTRPPT LSPIPHIPRS
PYKFSSSPLR IPGGNIYISP LKSPYKISEG LPTPTKMTPR SRILVSIGES FGTSEKFQKI
NQMVCNSDRV LKRSAEGGNP PKPLKKLRFD IEGSDEADGS KHLPAESKFQ QKLAEMTSTR
TRMQKQKLND SMEISNKEEK
