ID RB_HUMAN Reviewed; 928 AA.
AC P06400; A8K5E3; P78499; Q5VW46; Q8IZL4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 27-MAR-2024, entry version 278.
DE RecName: Full=Retinoblastoma-associated protein;
DE AltName: Full=p105-Rb;
DE AltName: Full=p110-RB1 {ECO:0000303|PubMed:8336704};
DE AltName: Full=pRb;
DE Short=Rb;
DE AltName: Full=pp110;
GN Name=RB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3657987; DOI=10.1038/329642a0;
RA Lee W.-H., Shew J.-Y., Hong F.D., Sery T.W., Donoso L.A., Young L.-J.S.,
RA Bookstein R., Lee E.Y.-H.P.;
RT "The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein
RT associated with DNA binding activity.";
RL Nature 329:642-645(1987).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=3823889; DOI=10.1126/science.3823889;
RA Lee W.-H., Bookstein R., Hong F.D., Young L.-J., Shew J.-Y., Lee E.Y.-H.P.;
RT "Human retinoblastoma susceptibility gene: cloning, identification, and
RT sequence.";
RL Science 235:1394-1399(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3480530; DOI=10.1073/pnas.84.24.9059;
RA Friend S.H., Horowitz J.M., Gerber M.R., Wang X.-F., Bogenmann E., Li F.P.,
RA Weinberg R.A.;
RT "Deletions of a DNA sequence in retinoblastomas and mesenchymal tumors:
RT organization of the sequence and its encoded protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:9059-9063(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2701949; DOI=10.1016/0378-1119(89)90256-4;
RA McGee T.L., Yandell D.W., Dryja T.P.;
RT "Structure and partial genomic sequence of the human retinoblastoma
RT susceptibility gene.";
RL Gene 80:119-128(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Carcinoma;
RX PubMed=1352398;
RA Hogg A., Onadim Z., Baird P.N., Cowell J.K.;
RT "Detection of heterozygous mutations in the RB1 gene in retinoblastoma
RT patients using single-strand conformation polymorphism analysis and
RT polymerase chain reaction sequencing.";
RL Oncogene 7:1445-1451(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7902321; DOI=10.1006/geno.1993.1368;
RA Toguchida J., McGee T.L., Paterson J.C., Eagle J.R., Tucker S.,
RA Yandell D.W., Dryja T.P.;
RT "Complete genomic sequence of the human retinoblastoma susceptibility
RT gene.";
RL Genomics 17:535-543(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-436 AND GLY-525.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Testis;
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 [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=2717184;
RA T'Ang A., Wu K.J., Hashimoto T., Liu W.Y., Takahashi R., Shi X.H.,
RA Mihara K., Zhang F.H., Chen Y.Y., Du C., Qian J., Lin Y.G., Murphree A.L.,
RA Qiu W.R., Thompson T., Benedict W.F., Fung Y.K.T.;
RT "Genomic organization of the human retinoblastoma gene.";
RL Oncogene 4:401-407(1989).
RN [13]
RP PROTEIN SEQUENCE OF 47-65, AND INVOLVEMENT IN RETINOBLASTOMA.
RX PubMed=7881418; DOI=10.1093/hmg/3.12.2187;
RA Lohmann D.R., Brandt B., Hopping W., Passarge E., Horsthemke B.;
RT "Spectrum of small length germline mutations in the RB1 gene.";
RL Hum. Mol. Genet. 3:2187-2193(1994).
RN [14]
RP INTERACTION WITH SV40 LARGE T ANTIGEN AND HPV E7 PROTEIN (MICROBIAL
RP INFECTION).
RX PubMed=1316611; DOI=10.1073/pnas.89.10.4549;
RA Chellappan S., Kraus V.B., Kroger B., Munger K., Howley P.M., Phelps W.C.,
RA Nevins J.R.;
RT "Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7
RT protein share the capacity to disrupt the interaction between transcription
RT factor E2F and the retinoblastoma gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4549-4553(1992).
RN [15]
RP INTERACTION WITH E2F1.
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 [16]
RP PHOSPHORYLATION BY CDK6.
RX PubMed=8114739; DOI=10.1128/mcb.14.3.2077-2086.1994;
RA Meyerson M., Harlow E.;
RT "Identification of G1 kinase activity for cdk6, a novel cyclin D partner.";
RL Mol. Cell. Biol. 14:2077-2086(1994).
RN [17]
RP INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION).
RX PubMed=2839300; DOI=10.1016/0092-8674(88)90559-4;
RA Decaprio J.A., Ludlow J.W., Figge J., Shew J.-Y., Huang C.-M., Lee W.-H.,
RA Marsilio E., Paucha E., Livingston D.M.;
RT "SV40 large tumor antigen forms a specific complex with the product of the
RT retinoblastoma susceptibility gene.";
RL Cell 54:275-283(1988).
RN [18]
RP INVOLVEMENT IN RETINOBLASTOMA.
RX PubMed=3413073; DOI=10.1073/pnas.85.16.6017;
RA Lee E.Y.-H.P., Bookstein R., Young L.-J., Lin C.-J., Rosenfeld M.G.,
RA Lee W.-H.;
RT "Molecular mechanism of retinoblastoma gene inactivation in retinoblastoma
RT cell line Y79.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6017-6021(1988).
RN [19]
RP PHOSPHORYLATION AT SER-249; THR-252; THR-373; SER-807 AND SER-811.
RX PubMed=1756735; DOI=10.1002/j.1460-2075.1991.tb05006.x;
RA Lees J.A., Buchkovich K.J., Marshak D.R., Anderson C.W., Harlow E.;
RT "The retinoblastoma protein is phosphorylated on multiple sites by human
RT cdc2.";
RL EMBO J. 10:4279-4290(1991).
RN [20]
RP INTERACTION WITH KDM5A AND ARID4A.
RX PubMed=8414517;
RA Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A.,
RA Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.;
RT "Characterization of the retinoblastoma binding proteins RBP1 and RBP2.";
RL Oncogene 8:3149-3156(1993).
RN [21]
RP INTERACTION WITH THOC1.
RX PubMed=7525595; DOI=10.1083/jcb.127.3.609;
RA Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.;
RT "The amino-terminal region of the retinoblastoma gene product binds a novel
RT nuclear matrix protein that co-localizes to centers for RNA processing.";
RL J. Cell Biol. 127:609-622(1994).
RN [22]
RP INTERACTION WITH KDM5A.
RX PubMed=7935440; DOI=10.1128/mcb.14.11.7256-7264.1994;
RA Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J.;
RT "Differential specificity for binding of retinoblastoma binding protein 2
RT to RB, p107, and TATA-binding protein.";
RL Mol. Cell. Biol. 14:7256-7264(1994).
RN [23]
RP INTERACTION WITH HHV-5 PROTEIN UL123 (MICROBIAL INFECTION).
RX PubMed=8892909; DOI=10.1128/jvi.70.11.7867-7877.1996;
RA Poma E.E., Kowalik T.F., Zhu L., Sinclair J.H., Huang E.S.;
RT "The human cytomegalovirus IE1-72 protein interacts with the cellular p107
RT protein and relieves p107-mediated transcriptional repression of an E2F-
RT responsive promoter.";
RL J. Virol. 70:7867-7877(1996).
RN [24]
RP INTERACTION WITH ARID3B.
RX PubMed=10446990;
RA Numata S., Claudio P.P., Dean C., Giordano A., Croce C.M.;
RT "Bdp, a new member of a family of DNA-binding proteins, associates with the
RT retinoblastoma gene product.";
RL Cancer Res. 59:3741-3747(1999).
RN [25]
RP FUNCTION, PHOSPHORYLATION AT SER-567 BY CDK2, AND PHOSPHORYLATION BY CDK4
RP AND CDK6.
RX PubMed=10499802; DOI=10.1016/s0092-8674(00)81519-6;
RA Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.;
RT "Cdk phosphorylation triggers sequential intramolecular interactions that
RT progressively block Rb functions as cells move through G1.";
RL Cell 98:859-869(1999).
RN [26]
RP INTERACTION WITH NDC80.
RX PubMed=10409732; DOI=10.1128/mcb.19.8.5417;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
RN [27]
RP INTERACTION WITH NDC80.
RX PubMed=10779342; DOI=10.1128/mcb.20.10.3529-3537.2000;
RA Zheng L., Chen Y., Riley D.J., Chen P.-L., Lee W.-H.;
RT "Retinoblastoma protein enhances the fidelity of chromosome segregation
RT mediated by hsHec1p.";
RL Mol. Cell. Biol. 20:3529-3537(2000).
RN [28]
RP INTERACTION WITH TAF1.
RX PubMed=9858607; DOI=10.1128/mcb.19.1.846;
RA Siegert J.L., Robbins P.D.;
RT "Rb inhibits the intrinsic kinase activity of TATA-binding protein-
RT associated factor TAFII250.";
RL Mol. Cell. Biol. 19:846-854(1999).
RN [29]
RP INTERACTION WITH PAX5.
RX PubMed=10197586;
RA Eberhard D., Busslinger M.;
RT "The partial homeodomain of the transcription factor Pax-5 (BSAP) is an
RT interaction motif for the retinoblastoma and TATA-binding proteins.";
RL Cancer Res. 59:1716-1724(1999).
RN [30]
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 [31]
RP INTERACTION WITH EID1.
RX PubMed=11223246; DOI=10.1016/s0378-1119(00)00585-0;
RA Wen H., Ao S.;
RT "Identification and characterization of a novel human cDNA encoding a 21
RT kDa pRb-associated protein.";
RL Gene 263:85-92(2001).
RN [32]
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 [33]
RP INTERACTION WITH SUV39H1.
RX PubMed=11484059; DOI=10.1038/35087620;
RA Nielsen S.J., Schneider R., Bauer U.-M., Bannister A.J., Morrison A.,
RA O'Carroll D., Firestein R., Cleary M.L., Jenuwein T., Herrera R.E.,
RA Kouzarides T.;
RT "Rb targets histone H3 methylation and HP1 to promoters.";
RL Nature 412:561-565(2001).
RN [34]
RP INTERACTION WITH USP4.
RX PubMed=11571652; DOI=10.1038/sj.onc.1204824;
RA DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T.,
RA Pagano M., Loda M.;
RT "The de-ubiquitinating enzyme Unp interacts with the retinoblastoma
RT protein.";
RL Oncogene 20:5538-5542(2001).
RN [35]
RP INTERACTION WITH AATF.
RX PubMed=12450794; DOI=10.1016/s1535-6108(02)00182-4;
RA Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M., Corbi N.,
RA Libri V., Benassi B., Mattei E., Chersi A., Soddu S., Floridi A.,
RA Passananti C., Fanciulli M.;
RT "Che-1 affects cell growth by interfering with the recruitment of HDAC1 by
RT Rb.";
RL Cancer Cell 2:387-399(2002).
RN [36]
RP INTERACTION WITH TMPO-ALPHA AND LMNA.
RX PubMed=12475961; DOI=10.1091/mbc.e02-07-0450;
RA Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.;
RT "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of
RT retinoblastoma protein.";
RL Mol. Biol. Cell 13:4401-4413(2002).
RN [37]
RP INTERACTION WITH SNW1.
RX PubMed=12466551; DOI=10.1093/nar/gkf658;
RA Prathapam T., Kuhne C., Banks L.;
RT "Skip interacts with the retinoblastoma tumor suppressor and inhibits its
RT transcriptional repression activity.";
RL Nucleic Acids Res. 30:5261-5268(2002).
RN [38]
RP INTERACTION WITH P-TEFB COMPLEX.
RX PubMed=12037672; DOI=10.1038/sj.onc.1205511;
RA Simone C., Bagella L., Bellan C., Giordano A.;
RT "Physical interaction between pRb and cdk9/cyclinT2 complex.";
RL Oncogene 21:4158-4165(2002).
RN [39]
RP INTERACTION WITH PELP1.
RX PubMed=12682072; DOI=10.1074/jbc.m212822200;
RA Balasenthil S., Vadlamudi R.K.;
RT "Functional interactions between the estrogen receptor coactivator
RT PELP1/MNAR and retinoblastoma protein.";
RL J. Biol. Chem. 278:22119-22127(2003).
RN [40]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL82 (MICROBIAL INFECTION).
RX PubMed=12626766; DOI=10.1073/pnas.0538058100;
RA Kalejta R.F., Shenk T.;
RT "Proteasome-dependent, ubiquitin-independent degradation of the Rb family
RT of tumor suppressors by the human cytomegalovirus pp71 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3263-3268(2003).
RN [41]
RP FUNCTION IN G0-G1 TRANSITION, AND PHOSPHORYLATION AT SER-807 AND SER-811 BY
RP CDK3.
RX PubMed=15084261; DOI=10.1016/s0092-8674(04)00300-9;
RA Ren S., Rollins B.J.;
RT "Cyclin C/cdk3 promotes Rb-dependent G0 exit.";
RL Cell 117:239-251(2004).
RN [42]
RP INTERACTION WITH LIN9.
RX PubMed=15538385; DOI=10.1038/sj.emboj.7600470;
RA Gagrica S., Hauser S., Kolfschoten I., Osterloh L., Agami R., Gaubatz S.;
RT "Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-
RT associated protein.";
RL EMBO J. 23:4627-4638(2004).
RN [43]
RP INTERACTION WITH CEBPA.
RX PubMed=15107404; DOI=10.1101/gad.1183304;
RA Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
RT "Liver tumors escape negative control of proliferation via PI3K/Akt-
RT mediated block of C/EBP alpha growth inhibitory activity.";
RL Genes Dev. 18:912-925(2004).
RN [44]
RP INTERACTION WITH LIMD1.
RX PubMed=15542589; DOI=10.1073/pnas.0407123101;
RA Sharp T.V., Munoz F., Bourboulia D., Presneau N., Darai E., Wang H.-W.,
RA Cannon M., Butcher D.N., Nicholson A.G., Klein G., Imreh S., Boshoff C.;
RT "LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at
RT chromosome 3p21.3, binds pRB and represses E2F-driven transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16531-16536(2004).
RN [45]
RP PHOSPHORYLATION AT THR-821 AND THR-826.
RX PubMed=15809340; DOI=10.1093/jb/mvi050;
RA Takaki T., Fukasawa K., Suzuki-Takahashi I., Semba K., Kitagawa M.,
RA Taya Y., Hirai H.;
RT "Preferences for phosphorylation sites in the retinoblastoma protein of D-
RT type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro.";
RL J. Biochem. 137:381-386(2005).
RN [46]
RP INTERACTION WITH KDM4A.
RX PubMed=15927959; DOI=10.1074/jbc.m413687200;
RA Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H.,
RA Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
RT "Functional characterization of JMJD2A, a histone deacetylase- and
RT retinoblastoma-binding protein.";
RL J. Biol. Chem. 280:28507-28518(2005).
RN [47]
RP INTERACTION WITH KDM5B.
RX PubMed=15803180; DOI=10.1038/modpathol.3800413;
RA Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M., Vogt T.;
RT "Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding
RT protein downregulated in malignant melanomas.";
RL Mod. Pathol. 18:1249-1257(2005).
RN [48]
RP INTERACTION WITH KDM5A.
RX PubMed=15949438; DOI=10.1016/j.molcel.2005.05.012;
RA Benevolenskaya E.V., Murray H.L., Branton P., Young R.A., Kaelin W.G. Jr.;
RT "Binding of pRB to the PHD protein RBP2 promotes cellular
RT differentiation.";
RL Mol. Cell 18:623-635(2005).
RN [49]
RP INTERACTION WITH PSMA3.
RX PubMed=16337594; DOI=10.1016/j.molcel.2005.10.017;
RA Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J.,
RA Xiao Z.X.;
RT "MDM2 promotes proteasome-dependent ubiquitin-independent degradation of
RT retinoblastoma protein.";
RL Mol. Cell 20:699-708(2005).
RN [50]
RP INTERACTION WITH ZUBR1.
RX PubMed=16214886; DOI=10.1073/pnas.0507458102;
RA Nakatani Y., Konishi H., Vassilev A., Kurooka H., Ishiguro K., Sawada J.,
RA Ikura T., Korsmeyer S.J., Qin J., Herlitz A.M.;
RT "p600, a unique protein required for membrane morphogenesis and cell
RT survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15093-15098(2005).
RN [51]
RP INTERACTION WITH KDM5B.
RX PubMed=16645588; DOI=10.1038/sj.jid.5700324;
RA Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M.,
RA Vogt T.;
RT "Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals
RT tumor-suppressive functions in highly metastatic melanoma cells.";
RL J. Invest. Dermatol. 126:1850-1859(2006).
RN [52]
RP PHOSPHORYLATION AT SER-612 BY CHEK2, AND INTERACTION WITH CHEK2.
RX PubMed=17380128; DOI=10.1038/sj.emboj.7601652;
RA Inoue Y., Kitagawa M., Taya Y.;
RT "Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between pRB
RT and E2F-1 after DNA damage.";
RL EMBO J. 26:2083-2093(2007).
RN [53]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-252 AND THR-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [54]
RP INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC007 (MICROBIAL
RP FUNCTION).
RX PubMed=18701596; DOI=10.1128/jvi.01187-08;
RA Mohr S., Grandemange S., Massimi P., Darai G., Banks L., Martinou J.C.,
RA Zeier M., Muranyi W.;
RT "Targeting the retinoblastoma protein by MC007L, gene product of the
RT molluscum contagiosum virus: detection of a novel virus-cell interaction by
RT a member of the poxviruses.";
RL J. Virol. 82:10625-10633(2008).
RN [55]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-252;
RP SER-612; SER-807; SER-811; THR-823 AND THR-826, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [56]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [57]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-373; SER-807
RP AND THR-841, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [58]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [59]
RP METHYLATION AT LYS-860, INTERACTION WITH L3MBTL1, AND MUTAGENESIS OF
RP LYS-860; LYS-870 AND 873-LYS-LYS-874.
RX PubMed=20870719; DOI=10.1074/jbc.m110.137612;
RA Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M., Gozani O.,
RA Sage J.;
RT "Methylation of the retinoblastoma tumor suppressor by SMYD2.";
RL J. Biol. Chem. 285:37733-37740(2010).
RN [60]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACETYLATION AT LYS-873 AND
RP LYS-874, AND MUTAGENESIS OF 873-LYS--LYS-874.
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 [61]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-821 AND THR-826, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [62]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [63]
RP INTERACTION WITH UHRF2.
RX PubMed=21952639; DOI=10.4161/cc.10.19.17176;
RA Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.;
RT "NIRF constitutes a nodal point in the cell cycle network and is a
RT candidate tumor suppressor.";
RL Cell Cycle 10:3284-3299(2011).
RN [64]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [65]
RP METHYLATION AT LYS-810 BY SMYD2.
RX PubMed=22787429; DOI=10.1593/neo.12656;
RA Cho H.S., Hayami S., Toyokawa G., Maejima K., Yamane Y., Suzuki T.,
RA Dohmae N., Kogure M., Kang D., Neal D.E., Ponder B.A., Yamaue H.,
RA Nakamura Y., Hamamoto R.;
RT "RB1 methylation by SMYD2 enhances cell cycle progression through an
RT increase of RB1 phosphorylation.";
RL Neoplasia 14:476-486(2012).
RN [66]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-252; THR-356;
RP THR-373; SER-624; SER-780; SER-788; SER-795; SER-807; SER-811; THR-821;
RP THR-823; THR-826 AND SER-855, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [67]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [68]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 378-562.
RX PubMed=9145110; DOI=10.1038/nsb0597-390;
RA Kim H.Y., Cho Y.;
RT "Structural similarity between the pocket region of retinoblastoma tumour
RT suppressor and the cyclin-box.";
RL Nat. Struct. Biol. 4:390-395(1997).
RN [69]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 380-785.
RX PubMed=9495340; DOI=10.1038/36038;
RA Lee J.O., Russo A.A., Pavletich N.P.;
RT "Structure of the retinoblastoma tumour-suppressor pocket domain bound to a
RT peptide from HPV E7.";
RL Nature 391:859-865(1998).
RN [70]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 860-876 IN COMPLEX WITH KPNA2.
RX PubMed=12695505; DOI=10.1074/jbc.m303275200;
RA Fontes M.R.M., Teh T., Jans D., Brinkworth R.I., Kobe B.;
RT "Structural basis for the specificity of bipartite nuclear localization
RT sequence binding by importin-alpha.";
RL J. Biol. Chem. 278:27981-27987(2003).
RN [71]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 829-874 IN COMPLEX WITH E2F1 AND
RP TFDP1, INTERACTION WITH HETERODIMERIC COMPLEXES CONTAINING TFDP1 AND EITHER
RP E2F1; E2F3; E2F4 OR E2F5, MUTAGENESIS OF THR-821 AND THR-826, AND
RP PHOSPHORYLATION AT THR-821 AND THR-826.
RX PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
RA Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
RT "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for
RT phosphorylation-induced E2F release.";
RL Cell 123:1093-1106(2005).
RN [72]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 380-787 IN COMPLEX WITH HUMAN
RP ADENOVIRUS E1A PROTEIN (MICROBIAL INFECTION).
RX PubMed=17974914; DOI=10.1101/gad.1590607;
RA Liu X., Marmorstein R.;
RT "Structure of the retinoblastoma protein bound to adenovirus E1A reveals
RT the molecular basis for viral oncoprotein inactivation of a tumor
RT suppressor.";
RL Genes Dev. 21:2711-2716(2007).
RN [73]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-355, PARTIAL PROTEIN SEQUENCE,
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THOC1 AND GRIP1, AND
RP INTERACTION OF THE UNPHOSPHORYLATED PROTEIN WITH EID1.
RX PubMed=17996702; DOI=10.1016/j.molcel.2007.08.023;
RA Hassler M., Singh S., Yue W.W., Luczynski M., Lakbir R.,
RA Sanchez-Sanchez F., Bader T., Pearl L.H., Mittnacht S.;
RT "Crystal structure of the retinoblastoma protein N domain provides insight
RT into tumor suppression, ligand interaction, and holoprotein architecture.";
RL Mol. Cell 28:371-385(2007).
RN [74]
RP VARIANT RB LEU-567.
RX PubMed=2594029; DOI=10.1056/nejm198912213212501;
RA Yandell D.W., Campbell T.A., Dayton S.H., Petersen R., Walton D.,
RA Little J.B., McConkie-Rosell A., Buckley E., Dryja T.P.;
RT "Oncogenic point mutations in the human retinoblastoma gene: their
RT application to genetic counseling.";
RL N. Engl. J. Med. 321:1689-1695(1989).
RN [75]
RP VARIANT RB TRP-661.
RX PubMed=1352883; DOI=10.1073/pnas.89.13.6177;
RA Onadim Z., Hogg A., Baird P.N., Cowell J.K.;
RT "Oncogenic point mutations in exon 20 of the RB1 gene in families showing
RT incomplete penetrance and mild expression of the retinoblastoma
RT phenotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6177-6181(1992).
RN [76]
RP VARIANT RB ARG-457.
RX PubMed=8346255; DOI=10.1073/pnas.90.15.7351;
RA Hogg A., Bia B., Onadim Z., Cowell J.K.;
RT "Molecular mechanisms of oncogenic mutations in tumors from patients with
RT bilateral and unilateral retinoblastoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7351-7355(1993).
RN [77]
RP VARIANT RB ARG-530.
RX PubMed=7704558; DOI=10.1159/000472372;
RA Cowell J.K., Smith T., Bia B.;
RT "Frequent constitutional C to T mutations in CGA-arginine codons in the RB1
RT gene produce premature stop codons in patients with bilateral (hereditary)
RT retinoblastoma.";
RL Eur. J. Hum. Genet. 2:281-290(1994).
RN [78]
RP VARIANTS RB ASN-480 DEL AND TRP-661.
RX PubMed=7927327; DOI=10.1007/bf00201591;
RA Lohmann D.R., Brandt B., Hoepping W., Passarge E., Horsthemke B.;
RT "Distinct RB1 gene mutations with low penetrance in hereditary
RT retinoblastoma.";
RL Hum. Genet. 94:349-354(1994).
RN [79]
RP VARIANTS RB GLN-72; TYR-549 AND LYS-803.
RX PubMed=8605116; DOI=10.1002/gcc.2870140406;
RA Liu Z., Song Y., Bia B., Cowell J.K.;
RT "Germline mutations in the RB1 gene in patients with hereditary
RT retinoblastoma.";
RL Genes Chromosomes Cancer 14:277-284(1995).
RN [80]
RP VARIANTS RB THR-185; PRO-635; GLU-654 AND PRO-685.
RX PubMed=7795591; DOI=10.1093/hmg/4.3.383;
RA Blanquet V., Turleau C., Gross-Morand M.S., Senamaud-Beaufort C., Doz F.,
RA Besmond C.;
RT "Spectrum of germline mutations in the RB1 gene: a study of 232 patients
RT with hereditary and non hereditary retinoblastoma.";
RL Hum. Mol. Genet. 4:383-388(1995).
RN [81]
RP VARIANTS RB GLY-358; PRO-657 AND TRP-661.
RX PubMed=8776589; DOI=10.1093/hmg/5.6.755;
RA Van Orsouw N.J., Li D., van der Vlies P., Scheffer H., Eng C.,
RA Buys C.H.C.M., Li F.P., Vijg J.;
RT "Mutational scanning of large genes by extensive PCR multiplexing and two-
RT dimensional electrophoresis: application to the RB1 gene.";
RL Hum. Mol. Genet. 5:755-761(1996).
RN [82]
RP VARIANTS RB ASP-137 AND TRP-661.
RX PubMed=9311732; DOI=10.1086/514845;
RA Lohmann D.R., Gerick M., Brandt B., Oelschlaeger U., Lorenz B.,
RA Passarge E., Horsthemke B.;
RT "Constitutional RB1-gene mutations in patients with isolated unilateral
RT retinoblastoma.";
RL Am. J. Hum. Genet. 61:282-294(1997).
RN [83]
RP VARIANT RB GLN-447.
RX PubMed=9140452; DOI=10.1016/s0165-4608(96)00387-1;
RA Mateu E., Sanchez F., Najera C., Beneyto M., Castell V., Hernandez M.,
RA Serra I., Prieto F.;
RT "Genetics of retinoblastoma: a study.";
RL Cancer Genet. Cytogenet. 95:40-50(1997).
RN [84]
RP VARIANTS RB LEU-567; PRO-662 AND ARG-712.
RX PubMed=10671068;
RX DOI=10.1002/(sici)1098-1004(1998)12:6<434::aid-humu16>3.0.co;2-7;
RA Yilmaz S., Horsthemke B., Lohmann D.R.;
RT "Twelve novel RB1 gene mutations in patients with hereditary
RT retinoblastoma.";
RL Hum. Mutat. 12:434-434(1998).
RN [85]
RP VARIANT RB GLU-310.
RX PubMed=9973307; DOI=10.1086/302254;
RA Klutz M., Horsthemke B., Lohmann D.R.;
RT "RB1 gene mutations in peripheral blood DNA of patients with isolated
RT unilateral retinoblastoma.";
RL Am. J. Hum. Genet. 64:667-668(1999).
RN [86]
RP VARIANTS RB GLY-500 AND GLU-616.
RX PubMed=11524739; DOI=10.1002/humu.1184;
RA Yu Y.S., Kim I.-J., Ku J.-L., Park J.-G.;
RT "Identification of four novel RB1 germline mutations in Korean
RT retinoblastoma patients.";
RL Hum. Mutat. 18:252-252(2001).
RN [87]
RP VARIANT HIS-173.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Tumor suppressor that is a key regulator of the G1/S
CC transition of the cell cycle (PubMed:10499802). The hypophosphorylated
CC form binds transcription regulators of the E2F family, preventing
CC transcription of E2F-responsive genes (PubMed:10499802). Both
CC physically blocks E2Fs transactivating domain and recruits chromatin-
CC modifying enzymes that actively repress transcription
CC (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1
CC induces its dissociation from E2Fs, thereby activating transcription of
CC E2F responsive genes and triggering entry into S phase
CC (PubMed:10499802). RB1 also promotes the G0-G1 transition upon
CC phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261).
CC Directly involved in heterochromatin formation by maintaining overall
CC chromatin structure and, in particular, that of constitutive
CC heterochromatin by stabilizing histone methylation. Recruits and
CC targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to
CC epigenetic transcriptional repression. Controls histone H4 'Lys-20'
CC trimethylation. 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).
CC {ECO:0000250|UniProtKB:P13405, ECO:0000250|UniProtKB:P33568,
CC ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:15084261}.
CC -!- FUNCTION: (Microbial infection) In case of viral infections,
CC interactions with SV40 large T antigen, HPV E7 protein or adenovirus
CC E1A protein induce the disassembly of RB1-E2F1 complex thereby
CC disrupting RB1's activity. {ECO:0000269|PubMed:1316611,
CC ECO:0000269|PubMed:17974914, ECO:0000269|PubMed:18701596,
CC ECO:0000269|PubMed:2839300, ECO:0000269|PubMed:8892909}.
CC -!- SUBUNIT: Interacts with ATAD5. Interacts with PRMT2, CDK1 and CDK2 (By
CC similarity). The hypophosphorylated form interacts with and sequesters
CC the E2F1 transcription factor (PubMed:8336704, PubMed:20940255).
CC Interacts with heterodimeric E2F/DP transcription factor complexes
CC containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and
CC E2F4. The unphosphorylated form interacts with EID1, ARID3B, KDM5A,
CC SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain
CC of TAF1. Interacts with SNW1, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C,
CC PELP1, UHRF2 and TMPO-alpha. May interact with NDC80. Interacts with
CC GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts with E4F1
CC and LIMD1. Interacts with SMARCA4/BRG1 and HDAC1 (By similarity).
CC Interacts with PSMA3 and USP4. Interacts (when methylated at Lys-860)
CC with L3MBTL1. Interacts with CHEK2; phosphorylates RB1. Interacts with
CC CEBPA (PubMed:15107404). P-TEFB complex interacts with RB1; promotes
CC phosphorylation of RB1 (PubMed:12037672). Interacts with RBBP9; the
CC interaction disrupts RB1 binding to E2F1 (By similarity). Interacts
CC with KAT2B/PCAF and EP300/P300 (By similarity). Interacts with PAX5
CC (PubMed:10197586). {ECO:0000250|UniProtKB:P13405,
CC ECO:0000250|UniProtKB:P33568, ECO:0000269|PubMed:10197586,
CC ECO:0000269|PubMed:10409732, ECO:0000269|PubMed:10446990,
CC ECO:0000269|PubMed:10779342, ECO:0000269|PubMed:10869426,
CC ECO:0000269|PubMed:10888886, ECO:0000269|PubMed:11223246,
CC ECO:0000269|PubMed:11484059, ECO:0000269|PubMed:11571652,
CC ECO:0000269|PubMed:12037672, ECO:0000269|PubMed:12450794,
CC ECO:0000269|PubMed:12466551, ECO:0000269|PubMed:12475961,
CC ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:12695505,
CC ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:15538385,
CC ECO:0000269|PubMed:15542589, ECO:0000269|PubMed:15803180,
CC ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:15949438,
CC ECO:0000269|PubMed:16214886, ECO:0000269|PubMed:16337594,
CC ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:16645588,
CC ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:17996702,
CC ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:20940255,
CC ECO:0000269|PubMed:21952639, ECO:0000269|PubMed:7525595,
CC ECO:0000269|PubMed:7935440, ECO:0000269|PubMed:8336704,
CC ECO:0000269|PubMed:8414517, ECO:0000269|PubMed:9858607}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1A protein.
CC {ECO:0000269|PubMed:17974914}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HPV E7 protein.
CC {ECO:0000269|PubMed:1316611}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 large T antigen.
CC {ECO:0000269|PubMed:1316611, ECO:0000269|PubMed:2839300}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 proteins UL82 and UL123.
CC {ECO:0000269|PubMed:12626766, ECO:0000269|PubMed:8892909}.
CC -!- SUBUNIT: (Microbial infection) Interacts with molluscum contagiosum
CC virus protein MC007. {ECO:0000269|PubMed:18701596}.
CC -!- INTERACTION:
CC P06400; Q9UKV8: AGO2; NbExp=3; IntAct=EBI-491274, EBI-528269;
CC P06400; P24863: CCNC; NbExp=4; IntAct=EBI-491274, EBI-395261;
CC P06400; P24941: CDK2; NbExp=3; IntAct=EBI-491274, EBI-375096;
CC P06400; O14757: CHEK1; NbExp=3; IntAct=EBI-491274, EBI-974488;
CC P06400; O96017: CHEK2; NbExp=3; IntAct=EBI-491274, EBI-1180783;
CC P06400; Q13574-2: DGKZ; NbExp=6; IntAct=EBI-491274, EBI-715527;
CC P06400; Q13627: DYRK1A; NbExp=4; IntAct=EBI-491274, EBI-1053596;
CC P06400; Q9Y463: DYRK1B; NbExp=4; IntAct=EBI-491274, EBI-634187;
CC P06400; Q01094: E2F1; NbExp=29; IntAct=EBI-491274, EBI-448924;
CC P06400; Q14209: E2F2; NbExp=5; IntAct=EBI-491274, EBI-718476;
CC P06400; O00716: E2F3; NbExp=5; IntAct=EBI-491274, EBI-765551;
CC P06400; Q16254: E2F4; NbExp=6; IntAct=EBI-491274, EBI-448943;
CC P06400; Q15329: E2F5; NbExp=2; IntAct=EBI-491274, EBI-1389773;
CC P06400; O43524: FOXO3; NbExp=2; IntAct=EBI-491274, EBI-1644164;
CC P06400; P42685: FRK; NbExp=3; IntAct=EBI-491274, EBI-1383583;
CC P06400; P15976: GATA1; NbExp=2; IntAct=EBI-491274, EBI-3909284;
CC P06400; P62993: GRB2; NbExp=4; IntAct=EBI-491274, EBI-401755;
CC P06400; O60381: HBP1; NbExp=2; IntAct=EBI-491274, EBI-954175;
CC P06400; Q13547: HDAC1; NbExp=16; IntAct=EBI-491274, EBI-301834;
CC P06400; Q14653: IRF3; NbExp=2; IntAct=EBI-491274, EBI-2650369;
CC P06400; P29375: KDM5A; NbExp=2; IntAct=EBI-491274, EBI-1560836;
CC P06400; Q16539: MAPK14; NbExp=4; IntAct=EBI-491274, EBI-73946;
CC P06400; Q00987: MDM2; NbExp=5; IntAct=EBI-491274, EBI-389668;
CC P06400; O15151: MDM4; NbExp=4; IntAct=EBI-491274, EBI-398437;
CC P06400; Q9Y676: MRPS18B; NbExp=2; IntAct=EBI-491274, EBI-750085;
CC P06400; Q14686: NCOA6; NbExp=3; IntAct=EBI-491274, EBI-78670;
CC P06400; P07197: NEFM; NbExp=2; IntAct=EBI-491274, EBI-1105035;
CC P06400; Q9UQ80: PA2G4; NbExp=4; IntAct=EBI-491274, EBI-924893;
CC P06400; P62136: PPP1CA; NbExp=2; IntAct=EBI-491274, EBI-357253;
CC P06400; P55345: PRMT2; NbExp=3; IntAct=EBI-491274, EBI-78458;
CC P06400; Q00577: PURA; NbExp=6; IntAct=EBI-491274, EBI-1045860;
CC P06400; P04049: RAF1; NbExp=3; IntAct=EBI-491274, EBI-365996;
CC P06400; P06400: RB1; NbExp=3; IntAct=EBI-491274, EBI-491274;
CC P06400; Q99708: RBBP8; NbExp=2; IntAct=EBI-491274, EBI-745715;
CC P06400; O75150: RNF40; NbExp=3; IntAct=EBI-491274, EBI-744408;
CC P06400; Q8WTS6: SETD7; NbExp=4; IntAct=EBI-491274, EBI-1268586;
CC P06400; Q96PU4: UHRF2; NbExp=4; IntAct=EBI-491274, EBI-625304;
CC P06400; Q93009: USP7; NbExp=8; IntAct=EBI-491274, EBI-302474;
CC P06400; P30285: Cdk4; Xeno; NbExp=2; IntAct=EBI-491274, EBI-847225;
CC P06400; Q155P7: Cenpf; Xeno; NbExp=4; IntAct=EBI-491274, EBI-2211248;
CC P06400; A0MPS7: E7; Xeno; NbExp=2; IntAct=EBI-491274, EBI-7014709;
CC P06400; P03129: E7; Xeno; NbExp=23; IntAct=EBI-491274, EBI-866453;
CC P06400; P04020: E7; Xeno; NbExp=3; IntAct=EBI-491274, EBI-7005254;
CC P06400; P06464: E7; Xeno; NbExp=3; IntAct=EBI-491274, EBI-6944797;
CC P06400; P06465: E7; Xeno; NbExp=3; IntAct=EBI-491274, EBI-963841;
CC P06400; P06788: E7; Xeno; NbExp=4; IntAct=EBI-491274, EBI-1776887;
CC P06400; P52927: Hmga2; Xeno; NbExp=5; IntAct=EBI-491274, EBI-912574;
CC P06400; Q9R002: Ifi202; Xeno; NbExp=5; IntAct=EBI-491274, EBI-3043899;
CC P06400; Q8VSP9: ospF; Xeno; NbExp=2; IntAct=EBI-491274, EBI-6506625;
CC P06400; Q9Z2X2: Psmd10; Xeno; NbExp=3; IntAct=EBI-491274, EBI-8377084;
CC P06400; PRO_0000037321 [P0C6X7]: rep; Xeno; NbExp=3; IntAct=EBI-491274, EBI-25487301;
CC P06400; Q923E4: Sirt1; Xeno; NbExp=4; IntAct=EBI-491274, EBI-1802585;
CC P06400; Q3TKT4: Smarca4; Xeno; NbExp=4; IntAct=EBI-491274, EBI-1210244;
CC P06400; P03070; Xeno; NbExp=6; IntAct=EBI-491274, EBI-617698;
CC P06400; P03254; Xeno; NbExp=3; IntAct=EBI-491274, EBI-8599077;
CC P06400; P03255; Xeno; NbExp=10; IntAct=EBI-491274, EBI-2603114;
CC P06400; P03255-1; Xeno; NbExp=2; IntAct=EBI-491274, EBI-6692439;
CC P06400; P03255-2; Xeno; NbExp=3; IntAct=EBI-491274, EBI-6859460;
CC P06400; PRO_0000041225 [Q86500]; Xeno; NbExp=3; IntAct=EBI-491274, EBI-2568719;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255}.
CC Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is
CC required for nuclear localization. {ECO:0000269|PubMed:20940255}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina. Expressed in foreskin
CC keratinocytes (at protein level) (PubMed:20940255).
CC {ECO:0000269|PubMed:20940255}.
CC -!- DOMAIN: The Pocket domain binds to the threonine-phosphorylated domain
CC C, thereby preventing interaction with heterodimeric E2F/DP
CC transcription factor complexes.
CC -!- PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-
CC 567 in G1, thereby releasing E2F1 which is then able to activate cell
CC growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV
CC E7 and adenovirus E1A bind to the underphosphorylated, active form of
CC pRb. Phosphorylation at Thr-821 and Thr-826 promotes interaction
CC between the C-terminal domain C and the Pocket domain, and thereby
CC inhibits interactions with heterodimeric E2F/DP transcription factor
CC complexes. Dephosphorylated at Ser-795 by calcineruin upon calcium
CC stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-
CC 811 is required for G0-G1 transition. Phosphorylated by CDK1 and CDK2
CC upon TGFB1-mediated apoptosis. {ECO:0000269|PubMed:10499802,
CC ECO:0000269|PubMed:8114739}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1 (By similarity).
CC Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807
CC and Ser-811, and promotes cell cycle progression. Monomethylation at
CC Lys-860 by SMYD2 promotes interaction with L3MBTL1. {ECO:0000250,
CC ECO:0000269|PubMed:15084261, ECO:0000269|PubMed:15809340,
CC ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17380128,
CC ECO:0000269|PubMed:1756735, ECO:0000269|PubMed:20870719,
CC ECO:0000269|PubMed:22787429}.
CC -!- PTM: Acetylated during keratinocyte differentiation. Acetylation at
CC Lys-873 and Lys-874 regulates subcellular localization. Can be
CC deacetylated by SIRT1. {ECO:0000269|PubMed:20940255}.
CC -!- DISEASE: Childhood cancer retinoblastoma (RB) [MIM:180200]: Congenital
CC malignant tumor that arises from the nuclear layers of the retina. It
CC occurs in about 1:20'000 live births and represents about 2% of
CC childhood malignancies. It is bilateral in about 30% of cases. Although
CC most RB appear sporadically, about 20% are transmitted as an autosomal
CC dominant trait with incomplete penetrance. The diagnosis is usually
CC made before the age of 2 years when strabismus or a gray to yellow
CC reflex from pupil ('cat eye') is investigated.
CC {ECO:0000269|PubMed:10671068, ECO:0000269|PubMed:11524739,
CC ECO:0000269|PubMed:1352883, ECO:0000269|PubMed:2594029,
CC ECO:0000269|PubMed:7704558, ECO:0000269|PubMed:7795591,
CC ECO:0000269|PubMed:7927327, ECO:0000269|PubMed:8346255,
CC ECO:0000269|PubMed:8605116, ECO:0000269|PubMed:8776589,
CC ECO:0000269|PubMed:9140452, ECO:0000269|PubMed:9311732,
CC ECO:0000269|PubMed:9973307}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy originating in
CC tissues of the urinary bladder. It often presents with multiple tumors
CC appearing at different times and at different sites in the bladder.
CC Most bladder cancers are transitional cell carcinomas that begin in
CC cells that normally make up the inner lining of the bladder. Other
CC types of bladder cancer include squamous cell carcinoma (cancer that
CC begins in thin, flat cells) and adenocarcinoma (cancer that begins in
CC cells that make and release mucus and other fluids). Bladder cancer is
CC a complex disorder with both genetic and environmental influences.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Osteogenic sarcoma (OSRC) [MIM:259500]: A sarcoma originating
CC in bone-forming cells, affecting the ends of long bones. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=RB1base; Note=RB1 mutation db;
CC URL="http://rb1-lsdb.d-lohmann.de/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/90/RB1";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rb1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Retinoblastoma protein entry;
CC URL="https://en.wikipedia.org/wiki/Retinoblastoma_protein";
CC ---------------------------------------------------------------------------
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DR EMBL; M15400; AAA69807.1; ALT_SEQ; mRNA.
DR EMBL; M28419; AAA69808.1; -; mRNA.
DR EMBL; M33647; AAA69806.1; -; mRNA.
DR EMBL; L41870; AAB59465.1; -; mRNA.
DR EMBL; M27866; AAA53484.1; -; Genomic_DNA.
DR EMBL; M27845; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27846; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27847; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27849; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27850; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27851; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; L35146; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27852; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27853; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27854; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27855; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27856; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27857; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27858; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27859; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27860; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; L35147; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27862; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27863; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27864; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; M27865; AAA53484.1; JOINED; Genomic_DNA.
DR EMBL; L41889; AAB59467.1; -; Genomic_DNA.
DR EMBL; L41890; AAA65735.1; -; Genomic_DNA.
DR EMBL; L41891; AAA65736.1; -; Genomic_DNA.
DR EMBL; L41893; AAA65737.1; -; Genomic_DNA.
DR EMBL; L41894; AAA65738.1; -; Genomic_DNA.
DR EMBL; L41895; AAA65739.1; -; Genomic_DNA.
DR EMBL; L41896; AAA65740.1; -; Genomic_DNA.
DR EMBL; L41897; AAA65741.1; -; Genomic_DNA.
DR EMBL; L41898; AAB59471.1; -; Genomic_DNA.
DR EMBL; L41899; AAB59473.1; -; Genomic_DNA.
DR EMBL; L41997; AAB59482.1; -; Genomic_DNA.
DR EMBL; X16439; CAA34462.1; -; Genomic_DNA.
DR EMBL; AF551763; AAN64133.1; -; Genomic_DNA.
DR EMBL; AK291258; BAF83947.1; -; mRNA.
DR EMBL; AL136960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08793.1; -; Genomic_DNA.
DR EMBL; BC039060; AAH39060.1; -; mRNA.
DR EMBL; BC040540; AAH40540.1; -; mRNA.
DR EMBL; L11910; AAA53483.1; -; Genomic_DNA.
DR CCDS; CCDS31973.1; -.
DR PIR; JS0276; RBHU.
DR RefSeq; NP_000312.2; NM_000321.2.
DR PDB; 1AD6; X-ray; 2.30 A; A=378-562.
DR PDB; 1GH6; X-ray; 3.20 A; B=379-577, B=645-772.
DR PDB; 1GUX; X-ray; 1.85 A; A=372-589, B=636-787.
DR PDB; 1H25; X-ray; 2.50 A; E=868-878.
DR PDB; 1N4M; X-ray; 2.20 A; A/B=380-785.
DR PDB; 1O9K; X-ray; 2.60 A; A/C/E/G=372-589, B/D/F/H=636-787.
DR PDB; 1PJM; X-ray; 2.50 A; A=858-881.
DR PDB; 2AZE; X-ray; 2.55 A; C=829-874.
DR PDB; 2QDJ; X-ray; 2.00 A; A=52-355.
DR PDB; 2R7G; X-ray; 1.67 A; A/C=380-787.
DR PDB; 3N5U; X-ray; 3.20 A; C=870-882.
DR PDB; 3POM; X-ray; 2.50 A; A/B=380-577, A/B=643-783.
DR PDB; 4CRI; X-ray; 2.35 A; C/D=802-817.
DR PDB; 4ELJ; X-ray; 2.70 A; A=53-787.
DR PDB; 4ELL; X-ray; 1.98 A; A/B=380-787.
DR PDBsum; 1AD6; -.
DR PDBsum; 1GH6; -.
DR PDBsum; 1GUX; -.
DR PDBsum; 1H25; -.
DR PDBsum; 1N4M; -.
DR PDBsum; 1O9K; -.
DR PDBsum; 1PJM; -.
DR PDBsum; 2AZE; -.
DR PDBsum; 2QDJ; -.
DR PDBsum; 2R7G; -.
DR PDBsum; 3N5U; -.
DR PDBsum; 3POM; -.
DR PDBsum; 4CRI; -.
DR PDBsum; 4ELJ; -.
DR PDBsum; 4ELL; -.
DR AlphaFoldDB; P06400; -.
DR SMR; P06400; -.
DR BioGRID; 111860; 368.
DR ComplexPortal; CPX-155; RB1-E2F1-DP1 transcriptional repressor complex.
DR ComplexPortal; CPX-175; RB1-E2F2-DP1 transcriptional repressor complex.
DR ComplexPortal; CPX-469; L3MBTL1 complex.
DR ComplexPortal; CPX-7728; RB1-E2F3-DP1 transcriptioal repressor complex.
DR CORUM; P06400; -.
DR DIP; DIP-582N; -.
DR IntAct; P06400; 185.
DR MINT; P06400; -.
DR STRING; 9606.ENSP00000267163; -.
DR BindingDB; P06400; -.
DR ChEMBL; CHEMBL5288; -.
DR GlyGen; P06400; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P06400; -.
DR PhosphoSitePlus; P06400; -.
DR BioMuta; RB1; -.
DR DMDM; 132164; -.
DR CPTAC; CPTAC-1328; -.
DR CPTAC; CPTAC-3251; -.
DR CPTAC; CPTAC-3288; -.
DR CPTAC; CPTAC-898; -.
DR CPTAC; CPTAC-941; -.
DR CPTAC; CPTAC-942; -.
DR EPD; P06400; -.
DR jPOST; P06400; -.
DR MassIVE; P06400; -.
DR MaxQB; P06400; -.
DR PaxDb; 9606-ENSP00000267163; -.
DR PeptideAtlas; P06400; -.
DR ProteomicsDB; 51900; -.
DR Pumba; P06400; -.
DR Antibodypedia; 3758; 3917 antibodies from 52 providers.
DR CPTC; P06400; 6 antibodies.
DR DNASU; 5925; -.
DR Ensembl; ENST00000267163.6; ENSP00000267163.4; ENSG00000139687.16.
DR GeneID; 5925; -.
DR KEGG; hsa:5925; -.
DR MANE-Select; ENST00000267163.6; ENSP00000267163.4; NM_000321.3; NP_000312.2.
DR UCSC; uc001vcb.4; human.
DR AGR; HGNC:9884; -.
DR CTD; 5925; -.
DR DisGeNET; 5925; -.
DR GeneCards; RB1; -.
DR GeneReviews; RB1; -.
DR HGNC; HGNC:9884; RB1.
DR HPA; ENSG00000139687; Low tissue specificity.
DR MalaCards; RB1; -.
DR MIM; 109800; phenotype.
DR MIM; 180200; phenotype.
DR MIM; 259500; phenotype.
DR MIM; 614041; gene.
DR neXtProt; NX_P06400; -.
DR OpenTargets; ENSG00000139687; -.
DR Orphanet; 357027; Hereditary retinoblastoma.
DR Orphanet; 1587; Monosomy 13q14.
DR Orphanet; 357034; Non-hereditary retinoblastoma.
DR Orphanet; 668; Osteosarcoma.
DR Orphanet; 70573; Small cell lung cancer.
DR PharmGKB; PA295; -.
DR VEuPathDB; HostDB:ENSG00000139687; -.
DR eggNOG; KOG1010; Eukaryota.
DR GeneTree; ENSGT00950000183202; -.
DR HOGENOM; CLU_015754_0_0_1; -.
DR InParanoid; P06400; -.
DR OMA; VKDIGCI; -.
DR OrthoDB; 519973at2759; -.
DR PhylomeDB; P06400; -.
DR TreeFam; TF105568; -.
DR PathwayCommons; P06400; -.
DR Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR Reactome; R-HSA-9661069; Defective binding of RB1 mutants to E2F1,(E2F2, E2F3).
DR Reactome; R-HSA-9661070; Defective translocation of RB1 mutants to the nucleus.
DR Reactome; R-HSA-9682706; Replication of the SARS-CoV-1 genome.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-9694686; Replication of the SARS-CoV-2 genome.
DR SignaLink; P06400; -.
DR SIGNOR; P06400; -.
DR BioGRID-ORCS; 5925; 32 hits in 1194 CRISPR screens.
DR ChiTaRS; RB1; human.
DR EvolutionaryTrace; P06400; -.
DR GeneWiki; Retinoblastoma_protein; -.
DR GenomeRNAi; 5925; -.
DR Pharos; P06400; Tchem.
DR PRO; PR:P06400; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P06400; Protein.
DR Bgee; ENSG00000139687; Expressed in epithelium of nasopharynx and 200 other cell types or tissues.
DR ExpressionAtlas; P06400; baseline and differential.
DR Genevisible; P06400; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0061793; C:chromatin lock complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0035189; C:Rb-E2F complex; IDA:CAFA.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0016514; C:SWI/SNF complex; TAS:BHF-UCL.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:CAFA.
DR GO; GO:0019900; F:kinase binding; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:Ensembl.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
DR GO; GO:0051276; P:chromosome organization; IMP:BHF-UCL.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0031507; P:heterochromatin formation; IDA:ComplexPortal.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IMP:BHF-UCL.
DR GO; GO:0045445; P:myoblast differentiation; IMP:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:ARUK-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
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; TAS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:BHF-UCL.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; ISS:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IPI:UniProtKB.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISS:ARUK-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:1902948; P:negative regulation of tau-protein kinase activity; ISS:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:BHF-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1904028; P:positive regulation of collagen fibril organization; ISS:BHF-UCL.
DR GO; GO:1903055; P:positive regulation of extracellular matrix organization; ISS:BHF-UCL.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:MGI.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:BHF-UCL.
DR GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:BHF-UCL.
DR GO; GO:0090230; P:regulation of centromere complex assembly; TAS:BHF-UCL.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal.
DR GO; GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:BHF-UCL.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:BHF-UCL.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd20599; CYCLIN_RB; 1.
DR DisProt; DP01426; -.
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 IDEAL; IID00017; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Chromatin regulator;
KW Direct protein sequencing; Disease variant; DNA-binding;
KW Host-virus interaction; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT CHAIN 2..928
FT /note="Retinoblastoma-associated protein"
FT /id="PRO_0000167836"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..771
FT /note="Pocket; binds T and E1A"
FT REGION 373..579
FT /note="Domain A"
FT REGION 580..639
FT /note="Spacer"
FT REGION 610..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..771
FT /note="Domain B"
FT REGION 763..928
FT /note="Interaction with LIMD1"
FT /evidence="ECO:0000269|PubMed:15542589"
FT REGION 771..928
FT /note="Domain C; mediates interaction with E4F1"
FT /evidence="ECO:0000269|PubMed:10869426"
FT REGION 860..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 860..876
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT COMPBIAS 18..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..918
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 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 249
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:1756735,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:1756735,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:1756735,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 567
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|PubMed:10499802"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13405"
FT MOD_RES 612
FT /note="Phosphoserine; by CHEK2 and CHEK1"
FT /evidence="ECO:0000269|PubMed:17380128,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 807
FT /note="Phosphoserine; by CDK1 and CDK3"
FT /evidence="ECO:0000269|PubMed:15084261,
FT ECO:0000269|PubMed:1756735, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 810
FT /note="N6-methyllysine; by SMYD2"
FT /evidence="ECO:0000269|PubMed:22787429"
FT MOD_RES 811
FT /note="Phosphoserine; by CDK1 and CDK3"
FT /evidence="ECO:0000269|PubMed:15084261,
FT ECO:0000269|PubMed:1756735, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 821
FT /note="Phosphothreonine; by CDK6"
FT /evidence="ECO:0000269|PubMed:15809340,
FT ECO:0000269|PubMed:16360038, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 823
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 826
FT /note="Phosphothreonine; by CDK4"
FT /evidence="ECO:0000269|PubMed:15809340,
FT ECO:0000269|PubMed:16360038, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 841
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 860
FT /note="N6-methyllysine; by SMYD2"
FT /evidence="ECO:0000269|PubMed:20870719"
FT MOD_RES 873
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:20940255"
FT MOD_RES 874
FT /note="N6-acetyllysine; by PCAF"
FT /evidence="ECO:0000269|PubMed:20940255"
FT VARIANT 72
FT /note="E -> Q (in RB)"
FT /evidence="ECO:0000269|PubMed:8605116"
FT /id="VAR_005572"
FT VARIANT 133
FT /note="N -> H (in dbSNP:rs3092900)"
FT /id="VAR_051909"
FT VARIANT 137
FT /note="E -> D (in RB; unilateral form; dbSNP:rs3092902)"
FT /evidence="ECO:0000269|PubMed:9311732"
FT /id="VAR_005573"
FT VARIANT 173
FT /note="Y -> H"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069376"
FT VARIANT 185
FT /note="I -> T (in RB)"
FT /evidence="ECO:0000269|PubMed:7795591"
FT /id="VAR_005574"
FT VARIANT 310
FT /note="G -> E (in RB; uncertain significance;
FT dbSNP:rs200844292)"
FT /evidence="ECO:0000269|PubMed:9973307"
FT /id="VAR_010045"
FT VARIANT 358
FT /note="R -> G (in RB)"
FT /evidence="ECO:0000269|PubMed:8776589"
FT /id="VAR_010046"
FT VARIANT 358
FT /note="R -> Q (in RB; dbSNP:rs767011440)"
FT /id="VAR_005575"
FT VARIANT 436
FT /note="Q -> K (in dbSNP:rs4151534)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019379"
FT VARIANT 447
FT /note="K -> Q (in RB)"
FT /evidence="ECO:0000269|PubMed:9140452"
FT /id="VAR_010048"
FT VARIANT 457
FT /note="M -> R (in RB)"
FT /evidence="ECO:0000269|PubMed:8346255"
FT /id="VAR_005576"
FT VARIANT 480
FT /note="Missing (in RB; mild form)"
FT /evidence="ECO:0000269|PubMed:7927327"
FT /id="VAR_005577"
FT VARIANT 500
FT /note="R -> G (in RB)"
FT /evidence="ECO:0000269|PubMed:11524739"
FT /id="VAR_011580"
FT VARIANT 525
FT /note="A -> G (in dbSNP:rs4151539)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019380"
FT VARIANT 530
FT /note="K -> R (in RB; dbSNP:rs1948534047)"
FT /evidence="ECO:0000269|PubMed:7704558"
FT /id="VAR_010049"
FT VARIANT 549
FT /note="H -> Y (in RB; dbSNP:rs1050717570)"
FT /evidence="ECO:0000269|PubMed:8605116"
FT /id="VAR_005578"
FT VARIANT 567
FT /note="S -> L (in RB; dbSNP:rs137853292)"
FT /evidence="ECO:0000269|PubMed:10671068,
FT ECO:0000269|PubMed:2594029"
FT /id="VAR_005579"
FT VARIANT 569
FT /note="L -> F (in dbSNP:rs3092895)"
FT /id="VAR_051910"
FT VARIANT 616
FT /note="K -> E (in RB)"
FT /evidence="ECO:0000269|PubMed:11524739"
FT /id="VAR_011581"
FT VARIANT 635
FT /note="A -> P (in RB)"
FT /evidence="ECO:0000269|PubMed:7795591"
FT /id="VAR_005580"
FT VARIANT 654
FT /note="V -> E (in RB)"
FT /evidence="ECO:0000269|PubMed:7795591"
FT /id="VAR_005581"
FT VARIANT 657
FT /note="L -> P (in RB)"
FT /evidence="ECO:0000269|PubMed:8776589"
FT /id="VAR_010050"
FT VARIANT 661
FT /note="R -> W (in RB; mild form; dbSNP:rs137853294)"
FT /evidence="ECO:0000269|PubMed:1352883,
FT ECO:0000269|PubMed:7927327, ECO:0000269|PubMed:8776589,
FT ECO:0000269|PubMed:9311732"
FT /id="VAR_005582"
FT VARIANT 662
FT /note="L -> P (in RB)"
FT /evidence="ECO:0000269|PubMed:10671068"
FT /id="VAR_005583"
FT VARIANT 673
FT /note="H -> P (in RB)"
FT /id="VAR_005584"
FT VARIANT 685
FT /note="Q -> P (in RB)"
FT /evidence="ECO:0000269|PubMed:7795591"
FT /id="VAR_005585"
FT VARIANT 697
FT /note="D -> E (in dbSNP:rs3092903)"
FT /id="VAR_051911"
FT VARIANT 706
FT /note="C -> Y (in RB)"
FT /id="VAR_005586"
FT VARIANT 712
FT /note="C -> R (in RB; dbSNP:rs137853296)"
FT /evidence="ECO:0000269|PubMed:10671068"
FT /id="VAR_005587"
FT VARIANT 746
FT /note="E -> G (in dbSNP:rs3092905)"
FT /id="VAR_034442"
FT VARIANT 803
FT /note="N -> K (in RB)"
FT /evidence="ECO:0000269|PubMed:8605116"
FT /id="VAR_005588"
FT MUTAGEN 821
FT /note="T->A: Abolishes interaction with Pocket domain; when
FT associated with A-826."
FT /evidence="ECO:0000269|PubMed:16360038"
FT MUTAGEN 826
FT /note="T->A: Abolishes interaction with Pocket domain; when
FT associated with A-821."
FT /evidence="ECO:0000269|PubMed:16360038"
FT MUTAGEN 860
FT /note="K->R: Abolishes monomethylation by SMYD2 and
FT subsequent interaction with L3MBTL1."
FT /evidence="ECO:0000269|PubMed:20870719"
FT MUTAGEN 870
FT /note="K->R: Does not affect the ability to be methylated
FT by SMYD2; when associated with 873-R-R-874."
FT /evidence="ECO:0000269|PubMed:20870719"
FT MUTAGEN 873..874
FT /note="KK->R: Does not affect the ability to be methylated
FT by SMYD2; when associated with 873-R-R-874."
FT /evidence="ECO:0000269|PubMed:20870719,
FT ECO:0000269|PubMed:20940255"
FT MUTAGEN 873..874
FT /note="KK->RR: Does not alter Rb localization in cycling
FT cells, but mislocalizes to the cytoplasm during
FT keratinocyte differentiation. Does not affect the ability
FT to arrest cell growth. Probable loss of acetylation by
FT PCAF."
FT /evidence="ECO:0000269|PubMed:20870719,
FT ECO:0000269|PubMed:20940255"
FT CONFLICT 500..501
FT /note="RS -> SN (in Ref. 7; AAN64133)"
FT /evidence="ECO:0000305"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 142..172
FT /evidence="ECO:0007829|PDB:2QDJ"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:2QDJ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4ELJ"
FT HELIX 212..228
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2QDJ"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:4ELJ"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:2QDJ"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 412..434
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 439..468
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 480..501
FT /evidence="ECO:0007829|PDB:2R7G"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:1N4M"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:4ELJ"
FT HELIX 516..521
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 532..538
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 544..559
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:4ELJ"
FT HELIX 569..577
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 582..586
FT /evidence="ECO:0007829|PDB:4ELL"
FT HELIX 602..607
FT /evidence="ECO:0007829|PDB:4ELL"
FT HELIX 645..669
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 676..690
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 692..695
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 700..714
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:1N4M"
FT HELIX 737..740
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:4ELJ"
FT HELIX 752..758
FT /evidence="ECO:0007829|PDB:2R7G"
FT HELIX 760..770
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 773..775
FT /evidence="ECO:0007829|PDB:2R7G"
FT STRAND 830..836
FT /evidence="ECO:0007829|PDB:2AZE"
FT TURN 838..840
FT /evidence="ECO:0007829|PDB:2AZE"
FT HELIX 841..853
FT /evidence="ECO:0007829|PDB:2AZE"
SQ SEQUENCE 928 AA; 106159 MW; C8E746111E19CC32 CRC64;
MPPKTPRKTA ATAAAAAAEP PAPPPPPPPE EDPEQDSGPE DLPLVRLEFE ETEEPDFTAL
CQKLKIPDHV RERAWLTWEK VSSVDGVLGG YIQKKKELWG ICIFIAAVDL DEMSFTFTEL
QKNIEISVHK FFNLLKEIDT STKVDNAMSR LLKKYDVLFA LFSKLERTCE LIYLTQPSSS
ISTEINSALV LKVSWITFLL AKGEVLQMED DLVISFQLML CVLDYFIKLS PPMLLKEPYK
TAVIPINGSP RTPRRGQNRS ARIAKQLEND TRIIEVLCKE HECNIDEVKN VYFKNFIPFM
NSLGLVTSNG LPEVENLSKR YEEIYLKNKD LDARLFLDHD KTLQTDSIDS FETQRTPRKS
NLDEEVNVIP PHTPVRTVMN TIQQLMMILN SASDQPSENL ISYFNNCTVN PKESILKRVK
DIGYIFKEKF AKAVGQGCVE IGSQRYKLGV RLYYRVMESM LKSEEERLSI QNFSKLLNDN
IFHMSLLACA LEVVMATYSR STSQNLDSGT DLSFPWILNV LNLKAFDFYK VIESFIKAEG
NLTREMIKHL ERCEHRIMES LAWLSDSPLF DLIKQSKDRE GPTDHLESAC PLNLPLQNNH
TAADMYLSPV RSPKKKGSTT RVNSTANAET QATSAFQTQK PLKSTSLSLF YKKVYRLAYL
RLNTLCERLL SEHPELEHII WTLFQHTLQN EYELMRDRHL DQIMMCSMYG ICKVKNIDLK
FKIIVTAYKD LPHAVQETFK RVLIKEEEYD SIIVFYNSVF MQRLKTNILQ YASTRPPTLS
PIPHIPRSPY KFPSSPLRIP GGNIYISPLK SPYKISEGLP TPTKMTPRSR ILVSIGESFG
TSEKFQKINQ MVCNSDRVLK RSAEGSNPPK PLKKLRFDIE GSDEADGSKH LPGESKFQQK
LAEMTSTRTR MQKQKMNDSM DTSNKEEK
//
