ID RB_MOUSE Reviewed; 921 AA. AC P13405; Q4VA62; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 231. DE RecName: Full=Retinoblastoma-associated protein; DE AltName: Full=p110-RB1 {ECO:0000303|PubMed:8336704}; DE AltName: Full=pRb; DE Short=Rb; DE AltName: Full=pp105; GN Name=Rb1; Synonyms=Rb-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2671991; DOI=10.1073/pnas.86.17.6474; RA Bernards R., Schackleford G.M., Gerber M.R., Horowitz J.M., Friend S.H., RA Schartl M., Bogenmann E., Rapaport J., McGee T., Dryja T.P., Weinberg R.A.; RT "Structure and expression of the murine retinoblastoma gene and RT characterization of its encoded protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6474-6478(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wu J., Liao J.D.; RT "Sequencing of the full-length cDNA sequence of the murine retinoblastoma RT gene."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF THE NUCLEAR LOCALIZATION RP SIGNAL, MUTAGENESIS OF 733-LYS--PRO-769; 769-PRO--ILE-872; 853-LYS--ARG-869 RP AND 866-LYS--ARG-869, INTERACTION WITH ADENOVIRUS E1A PROTEIN AND SV40 RP LARGE T ANTIGEN (MICROBIAL INFECTION), INTERACTION WITH E2F1, AND RP PHOSPHORYLATION. RX PubMed=8336704; DOI=10.1128/mcb.13.8.4588-4599.1993; RA Zacksenhaus E., Bremner R., Phillips R.A., Gallie B.L.; RT "A bipartite nuclear localization signal in the retinoblastoma gene product RT and its importance for biological activity."; RL Mol. Cell. Biol. 13:4588-4599(1993). RN [5] 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 [6] RP INTERACTION WITH E4F1. RX PubMed=10869426; DOI=10.1073/pnas.130198397; RA Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E., RA Medema R., Vignais M.-L., Sardet C.; RT "pRB binds to and modulates the transrepressing activity of the E1A- RT regulated transcription factor p120E4F."; RL Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000). RN [7] RP INTERACTION WITH USP4. RX PubMed=11571651; DOI=10.1038/sj.onc.1204823; RA Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.; RT "Association of UNP, a ubiquitin-specific protease, with the pocket RT proteins pRb, p107 and p130."; RL Oncogene 20:5533-5537(2001). RN [8] RP TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle; RX PubMed=12095676; DOI=10.1016/s0378-1119(02)00585-1; RA Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A., Saeki Y., RA Okabe H.; RT "Isolation, characterization and mapping of the mouse and human RB1CC1 RT genes."; RL Gene 291:29-34(2002). RN [9] RP FUNCTION, AND INTERACTION WITH KMT5B AND KMT5C. RX PubMed=15750587; DOI=10.1038/ncb1235; RA Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., RA Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.; RT "Role of the RB1 family in stabilizing histone methylation at constitutive RT heterochromatin."; RL Nat. Cell Biol. 7:420-428(2005). RN [10] RP INTERACTION WITH ATAD5. RX PubMed=15983387; DOI=10.1073/pnas.0504222102; RA Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M., RA Croce C.M., Huebner K., Ozawa K., Furukawa Y.; RT "Frag1, a homolog of alternative replication factor C subunits, links RT replication stress surveillance with apoptosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005). RN [11] RP INTERACTION WITH PRMT2. RX PubMed=16616919; DOI=10.1016/j.yexcr.2006.03.001; RA Yoshimoto T., Boehm M., Olive M., Crook M.F., San H., Langenickel T., RA Nabel E.G.; RT "The arginine methyltransferase PRMT2 binds RB and regulates E2F RT function."; RL Exp. Cell Res. 312:2040-2053(2006). RN [12] RP FUNCTION, INTERACTION WITH KMT5B AND KMT5C, AND MUTAGENESIS OF ILE-746; RP ASN-750 AND MET-754. RX PubMed=16612004; DOI=10.1128/mcb.26.9.3659-3671.2006; RA Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A., RA Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G., RA Dyson N.J., Dick F.A.; RT "The retinoblastoma protein regulates pericentric heterochromatin."; RL Mol. Cell. Biol. 26:3659-3671(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-243; THR-246; RP THR-364; THR-367; SER-601; SER-605; SER-773; SER-800; SER-804; THR-814; RP THR-819 AND SER-848, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Kidney, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP TISSUE SPECIFICITY, ACETYLATION, AND INTERACTION WITH E2F1; EP300 AND RP KAT2B. RX PubMed=20940255; DOI=10.1242/jcs.068924; RA Pickard A., Wong P.P., McCance D.J.; RT "Acetylation of Rb by PCAF is required for nuclear localization and RT keratinocyte differentiation."; RL J. Cell Sci. 123:3718-3726(2010). RN [15] RP CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2. RX PubMed=20668449; DOI=10.1038/nature09343; RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and RT retinoblastoma protein."; RL Nature 466:1125-1128(2010). CC -!- FUNCTION: Tumor suppressor that is a key regulator of the G1/S CC transition of the cell cycle (PubMed:8336704). The hypophosphorylated CC form binds transcription regulators of the E2F family, preventing CC transcription of E2F-responsive genes. Both physically blocks E2Fs CC transactivating domain and recruits chromatin-modifying enzymes that CC actively repress transcription. Cyclin and CDK-dependent CC phosphorylation of RB1 induces its dissociation from E2Fs, thereby CC activating transcription of E2F responsive genes and triggering entry CC into S phase. RB1 also promotes the G0-G1 transition upon CC phosphorylation and activation by CDK3/cyclin-C. Directly involved in CC heterochromatin formation by maintaining overall chromatin structure CC and, in particular, that of constitutive heterochromatin by stabilizing CC histone methylation (PubMed:15750587). Recruits and targets histone CC methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic CC transcriptional repression. Controls histone H4 'Lys-20' trimethylation CC (PubMed:16612004). Inhibits the intrinsic kinase activity of TAF1. CC Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a CC histone deacetylase (HDAC) complex to the c-FOS promoter. In resting CC neurons, transcription of the c-FOS promoter is inhibited by BRG1- CC dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon CC calcium influx, RB1 is dephosphorylated by calcineurin, which leads to CC release of the repressor complex (By similarity) (PubMed:15750587, CC PubMed:16612004, PubMed:8336704). {ECO:0000250|UniProtKB:P06400, CC ECO:0000250|UniProtKB:P33568, ECO:0000269|PubMed:15750587, CC ECO:0000269|PubMed:16612004, ECO:0000269|PubMed:8336704}. 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/E2F, CC E2F3, E2F4 or E2F5, or TFDP2 and E2F4 (PubMed:8336704, CC PubMed:20940255). The unphosphorylated form interacts with EID1, CC ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N- CC terminal domain of TAF1. Interacts with SNW1, ATAD5, AATF, DNMT1, LIN9, CC LMNA, KMT5B, KMT5C, PELP1, UHRF2, TMPO-alpha and USP4. May interact CC with NDC80. Interacts with GRIP1 and UBR4. Interacts with ARID4A and CC KDM5B. Interacts with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 and CC HDAC1. Interacts with USP4. Interacts (when methylated at Lys-853) with CC L3MBTL1. Binds to CDK1 and CDK2. Interacts with CHEK2; phosphorylates CC RB1 (By similarity). Interacts with PRMT2. Interacts with CEBPA. P-TEFB CC complex interacts with RB1; promotes phosphorylation of RB1 (By CC similarity). Interacts with RBBP9; the interaction disrupts RB1 binding CC to E2F1 (By similarity). Interacts with KAT2B/PCAF and EP300/P300 CC (PubMed:20940255). Interacts with PAX5 (By similarity). CC {ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P33568, CC ECO:0000269|PubMed:10869426, ECO:0000269|PubMed:10888886, CC ECO:0000269|PubMed:11571651, ECO:0000269|PubMed:15750587, CC ECO:0000269|PubMed:15983387, ECO:0000269|PubMed:16612004, CC ECO:0000269|PubMed:16616919, ECO:0000269|PubMed:20940255, CC ECO:0000269|PubMed:8336704}. CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1a protein. CC {ECO:0000269|PubMed:8336704}. CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 large T antigen. CC {ECO:0000269|PubMed:8336704}. CC -!- INTERACTION: CC P13405; Q155P7: Cenpf; NbExp=4; IntAct=EBI-971782, EBI-2211248; CC P13405; Q80UP3: Dgkz; NbExp=2; IntAct=EBI-971782, EBI-971774; CC P13405; P17679: Gata1; NbExp=3; IntAct=EBI-971782, EBI-3903251; CC P13405; Q9R002: Ifi202; NbExp=7; IntAct=EBI-971782, EBI-3043899; CC P13405; P24610: Pax3; NbExp=3; IntAct=EBI-971782, EBI-1208116; CC P13405; P52946: Pdx1; NbExp=2; IntAct=EBI-971782, EBI-7128945; CC P13405; Q3TKT4: Smarca4; NbExp=3; IntAct=EBI-971782, EBI-1210244; CC P13405; Q61412: Vsx2; NbExp=2; IntAct=EBI-971782, EBI-1208174; CC P13405; P15976: GATA1; Xeno; NbExp=2; IntAct=EBI-971782, EBI-3909284; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8336704}. Note=During CC keratinocyte differentiation, acetylation by KAT2B/PCAF is required for CC nuclear localization. {ECO:0000250|UniProtKB:P06400}. CC -!- TISSUE SPECIFICITY: Expressed in the cell nuclei of renal tubules, CC hepatocytes and skeletal muscles. Expressed in skin (at protein level) CC (PubMed:20940255). {ECO:0000269|PubMed:12095676, CC ECO:0000269|PubMed:20940255}. CC -!- PTM: Phosphorylated (PubMed:8336704). Phosphorylated by CDK6 and CDK4, CC and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which CC is then able to activate cell growth. Dephosphorylated at the late M CC phase. Phosphorylation of threonine residues in domain C promotes CC interaction between the C-terminal domain C and the Pocket domain, and CC thereby inhibits interactions with heterodimeric E2F/DP transcription CC factor complexes. Dephosphorylated at Ser-788 by calcineruin upon CC calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-800 CC and Ser-804 is required for G0-G1 transition (By similarity). CC Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:8336704}. CC -!- PTM: Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at CC Ser-800 and Ser-804, and promotes cell cycle progression. CC Monomethylation at Lys-853 by SMYD2 promotes interaction with L3MBTL1 CC (By similarity). N-terminus is methylated by METTL11A/NTM1. CC {ECO:0000250, ECO:0000269|PubMed:20668449}. CC -!- PTM: Acetylated in the skin (PubMed:20940255). Acetylation at Lys-866 CC and Lys-867 regulates subcellular localization during keratinocytes CC differentiation (By similarity). {ECO:0000250|UniProtKB:P06400, CC ECO:0000269|PubMed:20940255}. CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Retinoblastoma protein entry; CC URL="https://en.wikipedia.org/wiki/Retinoblastoma_protein"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M26391; AAA39964.1; -; mRNA. DR EMBL; DQ400415; ABD72475.1; -; mRNA. DR EMBL; BC096525; AAH96525.1; -; mRNA. DR CCDS; CCDS27267.1; -. DR PIR; A33718; A33718. DR RefSeq; NP_033055.2; NM_009029.2. DR AlphaFoldDB; P13405; -. DR SMR; P13405; -. DR BioGRID; 202815; 61. DR ComplexPortal; CPX-160; RB1-E2F1-DP1 transcriptional repressor complex. DR ComplexPortal; CPX-177; RB1-E2F2-DP1 transcription repressor complex. DR ComplexPortal; CPX-470; L3MBTL1 complex. DR CORUM; P13405; -. DR DIP; DIP-37637N; -. DR IntAct; P13405; 26. DR MINT; P13405; -. DR STRING; 10090.ENSMUSP00000022701; -. DR iPTMnet; P13405; -. DR PhosphoSitePlus; P13405; -. DR EPD; P13405; -. DR jPOST; P13405; -. DR MaxQB; P13405; -. DR PaxDb; 10090-ENSMUSP00000022701; -. DR PeptideAtlas; P13405; -. DR ProteomicsDB; 255135; -. DR Pumba; P13405; -. DR Antibodypedia; 3758; 3917 antibodies from 52 providers. DR DNASU; 19645; -. DR Ensembl; ENSMUST00000022701.7; ENSMUSP00000022701.7; ENSMUSG00000022105.7. DR GeneID; 19645; -. DR KEGG; mmu:19645; -. DR UCSC; uc007upp.2; mouse. DR AGR; MGI:97874; -. DR MGI; MGI:97874; Rb1. DR VEuPathDB; HostDB:ENSMUSG00000022105; -. DR eggNOG; KOG1010; Eukaryota. DR GeneTree; ENSGT00950000183202; -. DR HOGENOM; CLU_015754_0_0_1; -. DR InParanoid; P13405; -. DR OMA; VKDIGCI; -. DR OrthoDB; 519973at2759; -. DR PhylomeDB; P13405; -. DR TreeFam; TF105568; -. DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1. DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF). DR Reactome; R-MMU-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes. DR Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition. DR Reactome; R-MMU-69231; Cyclin D associated events in G1. DR Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry. DR BioGRID-ORCS; 19645; 4 hits in 84 CRISPR screens. DR ChiTaRS; Rb1; mouse. DR PRO; PR:P13405; -. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; P13405; Protein. DR Bgee; ENSMUSG00000022105; Expressed in molar tooth and 270 other cell types or tissues. DR ExpressionAtlas; P13405; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0061793; C:chromatin lock complex; ISO:MGI. DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; ISS:UniProtKB. DR GO; GO:0035189; C:Rb-E2F complex; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:MGI. DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI. 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; IPI:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL. DR GO; GO:0006915; P:apoptotic process; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0051301; P:cell division; IMP:MGI. DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:MGI. DR GO; GO:0002062; P:chondrocyte differentiation; IDA:MGI. DR GO; GO:0051276; P:chromosome organization; ISO:MGI. DR GO; GO:0048565; P:digestive tract development; IMP:MGI. DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0034349; P:glial cell apoptotic process; IMP:MGI. DR GO; GO:0014009; P:glial cell proliferation; IGI:MGI. DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI. DR GO; GO:0031507; P:heterochromatin formation; ISO:MGI. DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; ISO:MGI. DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI. DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI. DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IGI:MGI. DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; ISO:MGI. DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:BHF-UCL. DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IGI:MGI. DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; IMP:BHF-UCL. DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IMP:MGI. DR GO; GO:0042551; P:neuron maturation; IMP:MGI. DR GO; GO:0031175; P:neuron projection development; IMP:MGI. DR GO; GO:1904028; P:positive regulation of collagen fibril organization; IMP:BHF-UCL. DR GO; GO:1903055; P:positive regulation of extracellular matrix organization; IMP:BHF-UCL. DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IGI:MGI. DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISO:MGI. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl. DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI. DR GO; GO:0001558; P:regulation of cell growth; IGI:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IGI:BHF-UCL. DR GO; GO:0043550; P:regulation of lipid kinase activity; ISS:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI. DR GO; GO:0031134; P:sister chromatid biorientation; ISO:MGI. DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI. DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI. DR GO; GO:0001894; P:tissue homeostasis; IGI:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI. DR CDD; cd20599; CYCLIN_RB; 1. DR Gene3D; 1.10.472.140; -; 1. DR Gene3D; 6.10.140.1380; -; 1. DR Gene3D; 6.10.250.530; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR InterPro; IPR013763; Cyclin-like_dom. 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:SF17; RETINOBLASTOMA-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 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; Cyclin-like; 2. DR Genevisible; P13405; MM. 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:0000269|PubMed:20668449" FT CHAIN 2..921 FT /note="Retinoblastoma-associated protein" FT /id="PRO_0000167837" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 341..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 367..764 FT /note="Pocket; binds T and E1A" FT /evidence="ECO:0000250" FT REGION 367..573 FT /note="Domain A" FT /evidence="ECO:0000250" FT REGION 574..632 FT /note="Spacer" FT /evidence="ECO:0000250" FT REGION 633..764 FT /note="Domain B" FT /evidence="ECO:0000250" FT REGION 756..921 FT /note="Interaction with LIMD1" FT /evidence="ECO:0000250" FT REGION 764..921 FT /note="Domain; mediates interaction with E4F1" FT /evidence="ECO:0000250" FT REGION 872..921 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 853..869 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000269|PubMed:8336704" FT COMPBIAS 1..26 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..356 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..886 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 906..921 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N,N-dimethylproline; by NTM1" FT /evidence="ECO:0000269|PubMed:20668449" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 246 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 350 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 364 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 367 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 561 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 601 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 605 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 617 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 773 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 781 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 788 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 800 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 803 FT /note="N6-methyllysine; by SMYD2" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 804 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 814 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 816 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 819 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 834 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 848 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 853 FT /note="N6-methyllysine; by SMYD2" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 866 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MOD_RES 867 FT /note="N6-acetyllysine; by PCAF" FT /evidence="ECO:0000250|UniProtKB:P06400" FT MUTAGEN 733..769 FT /note="Missing: Loss of exclusive nuclear localization. FT Complete loss of nuclear localization, loss of growth FT inhibition, when transfected in Saos-2 cells and loss of FT interaction with SV40 large T antigen, adenovirus E1a and FT E2F1; when associated with 866-N--Q-869." FT /evidence="ECO:0000269|PubMed:8336704" FT MUTAGEN 746 FT /note="I->A: Abolishes the interaction with many chromatin FT regulators but not that with KMT5B and KMT5C; when FT associated with A-750 and A-754." FT /evidence="ECO:0000269|PubMed:16612004" FT MUTAGEN 750 FT /note="N->A: Abolishes the interaction with many chromatin FT regulators but not that with KMT5B and KMT5C; when FT associated with A-746 and A-754." FT /evidence="ECO:0000269|PubMed:16612004" FT MUTAGEN 754 FT /note="M->A: Abolishes the interaction with many chromatin FT regulators but not that with KMT5B and KMT5C; when FT associated with A-746 and A-750." FT /evidence="ECO:0000269|PubMed:16612004" FT MUTAGEN 769..872 FT /note="Missing: Loss of exclusive nuclear localization and FT loss of growth inhibition, when transfected in Saos-2 FT cells. No effect on the interaction with SV40 large T FT antigen." FT /evidence="ECO:0000269|PubMed:8336704" FT MUTAGEN 853..869 FT /note="Missing: Loss of exclusive nuclear localization. FT Decreased growth inhibition activity, when transfected in FT Saos-2 cells. No effect on the interaction with SV40 large FT T antigen, adenovirus E1a, nor E2F1." FT /evidence="ECO:0000269|PubMed:8336704" FT MUTAGEN 866..869 FT /note="KKLR->NKLQ: Loss of exclusive nuclear localization, FT no effect on the interaction with SV40 large T antigen, FT adenovirus E1a, nor E2F1. Decreased growth inhibition FT activity, when transfected in Saos-2 cells. Complete loss FT of nuclear localization, loss of growth inhibition, when FT transfected in Saos-2 cells and loss of interaction with FT SV40 large T antigen, adenovirus E1a and E2F1; when FT associated with 733-K--P-769." FT /evidence="ECO:0000269|PubMed:8336704" FT CONFLICT 867..868 FT /note="KL -> NV (in Ref. 1; AAA39964)" FT /evidence="ECO:0000305" SQ SEQUENCE 921 AA; 105367 MW; AE81D35A07ADB493 CRC64; MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE FIALCQKLKV PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA AVDLDEMPFT FTELQKSIET SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN VLCALYSKLE RTCELIYLTQ PSSALSTEIN SMLVLKISWI TFLLAKGEVL QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI NGSPRTPRRG QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT PRKNNPDEEA NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN CTVNPKENIL KRVKDVGHIF KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV MESMLKSEEE RLSIQNFSKL LNDNIFHMSL LACALEVVMA TYSRSTLQHL DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM IKHLERCEHR IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL AYLRLNTLCA RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS MYGICKVKNI DLKFKIIVTA YKDLPHAAQE TFKRVLIREE EFDSIIVFYN SVFMQRLKTN ILQYASTRPP TLSPIPHIPR SPYKFSSSPL RIPGGNIYIS PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK INQMVCNSDR VLKRSAEGGN PPKPLKKLRF DIEGADEADG SKHLPAESKF QQKLAEMTST RTRMQKQRMN ESKDVSNKEE K //