RB_MOUSE
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 03-AUG-2022, entry version 222.
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";
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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-TFDP1 transcription repressor complex.
DR ComplexPortal; CPX-177; RB1-E2F2-TFDP1 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; P13405; -.
DR PeptideAtlas; P13405; -.
DR PRIDE; P13405; -.
DR ProteomicsDB; 255135; -.
DR Antibodypedia; 3758; 3530 antibodies from 52 providers.
DR DNASU; 19645; -.
DR Ensembl; ENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105.
DR GeneID; 19645; -.
DR KEGG; mmu:19645; -.
DR UCSC; uc007upp.2; mouse.
DR CTD; 5925; -.
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; IGCIFKE; -.
DR OrthoDB; 113612at2759; -.
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 78 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 267 other tissues.
DR ExpressionAtlas; P13405; baseline and differential.
DR Genevisible; P13405; MM.
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; ISO:MGI.
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: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: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 assembly; 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:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO: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:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:1902948; P:negative regulation of tau-protein kinase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO: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:0071922; P:regulation of cohesin loading; ISO:MGI.
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; 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: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
