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Retinoblastoma-associated protein (p105-Rb) (pRb) (Rb) (pp110)

 RB_HUMAN                Reviewed;         928 AA.
P06400; A8K5E3; P78499; Q5VW46; Q8IZL4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
30-AUG-2017, entry version 231.
RecName: Full=Retinoblastoma-associated protein;
AltName: Full=p105-Rb;
AltName: Full=pRb;
Short=Rb;
AltName: Full=pp110;
Name=RB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3657987; DOI=10.1038/329642a0;
Lee W.-H., Shew J.-Y., Hong F.D., Sery T.W., Donoso L.A.,
Young L.-J.S., Bookstein R., Lee E.Y.-H.P.;
"The retinoblastoma susceptibility gene encodes a nuclear
phosphoprotein associated with DNA binding activity.";
Nature 329:642-645(1987).
[2]
SEQUENCE REVISION.
PubMed=3823889; DOI=10.1126/science.3823889;
Lee W.-H., Bookstein R., Hong F.D., Young L.-J., Shew J.-Y.,
Lee E.Y.-H.P.;
"Human retinoblastoma susceptibility gene: cloning, identification,
and sequence.";
Science 235:1394-1399(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3480530; DOI=10.1073/pnas.84.24.9059;
Friend S.H., Horowitz J.M., Gerber M.R., Wang X.-F., Bogenmann E.,
Li F.P., Weinberg R.A.;
"Deletions of a DNA sequence in retinoblastomas and mesenchymal
tumors: organization of the sequence and its encoded protein.";
Proc. Natl. Acad. Sci. U.S.A. 84:9059-9063(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2701949; DOI=10.1016/0378-1119(89)90256-4;
McGee T.L., Yandell D.W., Dryja T.P.;
"Structure and partial genomic sequence of the human retinoblastoma
susceptibility gene.";
Gene 80:119-128(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Carcinoma;
PubMed=1352398;
Hogg A., Onadim Z., Baird P.N., Cowell J.K.;
"Detection of heterozygous mutations in the RB1 gene in retinoblastoma
patients using single-strand conformation polymorphism analysis and
polymerase chain reaction sequencing.";
Oncogene 7:1445-1451(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7902321; DOI=10.1006/geno.1993.1368;
Toguchida J., McGee T.L., Paterson J.C., Eagle J.R., Tucker S.,
Yandell D.W., Dryja T.P.;
"Complete genomic sequence of the human retinoblastoma susceptibility
gene.";
Genomics 17:535-543(1993).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-436 AND GLY-525.
NIEHS SNPs program;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
PubMed=2717184;
T'Ang A., Wu K.J., Hashimoto T., Liu W.Y., Takahashi R., Shi X.H.,
Mihara K., Zhang F.H., Chen Y.Y., Du C., Qian J., Lin Y.G.,
Murphree A.L., Qiu W.R., Thompson T., Benedict W.F., Fung Y.K.T.;
"Genomic organization of the human retinoblastoma gene.";
Oncogene 4:401-407(1989).
[13]
INTERACTION WITH SV40 LARGE T ANTIGEN AND HPV E7 PROTEIN.
PubMed=1316611; DOI=10.1073/pnas.89.10.4549;
Chellappan S., Kraus V.B., Kroger B., Munger K., Howley P.M.,
Phelps W.C., Nevins J.R.;
"Adenovirus E1A, simian virus 40 tumor antigen, and human
papillomavirus E7 protein share the capacity to disrupt the
interaction between transcription factor E2F and the retinoblastoma
gene product.";
Proc. Natl. Acad. Sci. U.S.A. 89:4549-4553(1992).
[14]
PROTEIN SEQUENCE OF 47-65, AND INVOLVEMENT IN RETINOBLASTOMA.
PubMed=7881418; DOI=10.1093/hmg/3.12.2187;
Lohmann D.R., Brandt B., Hopping W., Passarge E., Horsthemke B.;
"Spectrum of small length germline mutations in the RB1 gene.";
Hum. Mol. Genet. 3:2187-2193(1994).
[15]
PHOSPHORYLATION BY CDK6.
PubMed=8114739; DOI=10.1128/MCB.14.3.2077;
Meyerson M., Harlow E.;
"Identification of G1 kinase activity for cdk6, a novel cyclin D
partner.";
Mol. Cell. Biol. 14:2077-2086(1994).
[16]
INTERACTION WITH SV40 LARGE T ANTIGEN.
PubMed=2839300; DOI=10.1016/0092-8674(88)90559-4;
Decaprio J.A., Ludlow J.W., Figge J., Shew J.-Y., Huang C.-M.,
Lee W.-H., Marsilio E., Paucha E., Livingston D.M.;
"SV40 large tumor antigen forms a specific complex with the product of
the retinoblastoma susceptibility gene.";
Cell 54:275-283(1988).
[17]
INVOLVEMENT IN RETINOBLASTOMA.
PubMed=3413073; DOI=10.1073/pnas.85.16.6017;
Lee E.Y.-H.P., Bookstein R., Young L.-J., Lin C.-J., Rosenfeld M.G.,
Lee W.-H.;
"Molecular mechanism of retinoblastoma gene inactivation in
retinoblastoma cell line Y79.";
Proc. Natl. Acad. Sci. U.S.A. 85:6017-6021(1988).
[18]
PHOSPHORYLATION AT SER-249; THR-252; THR-373; SER-807 AND SER-811.
PubMed=1756735;
Lees J.A., Buchkovich K.J., Marshak D.R., Anderson C.W., Harlow E.;
"The retinoblastoma protein is phosphorylated on multiple sites by
human cdc2.";
EMBO J. 10:4279-4290(1991).
[19]
INTERACTION WITH KDM5A AND ARID4A.
PubMed=8414517;
Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E.,
Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D.,
Jones R.E.;
"Characterization of the retinoblastoma binding proteins RBP1 and
RBP2.";
Oncogene 8:3149-3156(1993).
[20]
INTERACTION WITH THOC1.
PubMed=7525595; DOI=10.1083/jcb.127.3.609;
Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.;
"The amino-terminal region of the retinoblastoma gene product binds a
novel nuclear matrix protein that co-localizes to centers for RNA
processing.";
J. Cell Biol. 127:609-622(1994).
[21]
INTERACTION WITH KDM5A.
PubMed=7935440; DOI=10.1128/MCB.14.11.7256;
Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J.;
"Differential specificity for binding of retinoblastoma binding
protein 2 to RB, p107, and TATA-binding protein.";
Mol. Cell. Biol. 14:7256-7264(1994).
[22]
INTERACTION WITH HHV-5 PROTEIN UL123.
PubMed=8892909;
Poma E.E., Kowalik T.F., Zhu L., Sinclair J.H., Huang E.S.;
"The human cytomegalovirus IE1-72 protein interacts with the cellular
p107 protein and relieves p107-mediated transcriptional repression of
an E2F-responsive promoter.";
J. Virol. 70:7867-7877(1996).
[23]
INTERACTION WITH ARID3B.
PubMed=10446990;
Numata S., Claudio P.P., Dean C., Giordano A., Croce C.M.;
"Bdp, a new member of a family of DNA-binding proteins, associates
with the retinoblastoma gene product.";
Cancer Res. 59:3741-3747(1999).
[24]
PHOSPHORYLATION AT SER-567 BY CDK2, AND PHOSPHORYLATION BY CDK4 AND
CDK6.
PubMed=10499802; DOI=10.1016/S0092-8674(00)81519-6;
Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.;
"Cdk phosphorylation triggers sequential intramolecular interactions
that progressively block Rb functions as cells move through G1.";
Cell 98:859-869(1999).
[25]
INTERACTION WITH NDC80.
PubMed=10409732; DOI=10.1128/MCB.19.8.5417;
Zheng L., Chen Y., Lee W.-H.;
"Hec1p, an evolutionarily conserved coiled-coil protein, modulates
chromosome segregation through interaction with SMC proteins.";
Mol. Cell. Biol. 19:5417-5428(1999).
[26]
INTERACTION WITH NDC80.
PubMed=10779342; DOI=10.1128/MCB.20.10.3529-3537.2000;
Zheng L., Chen Y., Riley D.J., Chen P.-L., Lee W.-H.;
"Retinoblastoma protein enhances the fidelity of chromosome
segregation mediated by hsHec1p.";
Mol. Cell. Biol. 20:3529-3537(2000).
[27]
INTERACTION WITH TAF1.
PubMed=9858607; DOI=10.1128/MCB.19.1.846;
Siegert J.L., Robbins P.D.;
"Rb inhibits the intrinsic kinase activity of TATA-binding protein-
associated factor TAFII250.";
Mol. Cell. Biol. 19:846-854(1999).
[28]
INTERACTION WITH E4F1.
PubMed=10869426; DOI=10.1073/pnas.130198397;
Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
Medema R., Vignais M.-L., Sardet C.;
"pRB binds to and modulates the transrepressing activity of the E1A-
regulated transcription factor p120E4F.";
Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
[29]
INTERACTION WITH EID1.
PubMed=11223246; DOI=10.1016/S0378-1119(00)00585-0;
Wen H., Ao S.;
"Identification and characterization of a novel human cDNA encoding a
21 kDa pRb-associated protein.";
Gene 263:85-92(2001).
[30]
INTERACTION WITH DNMT1.
PubMed=10888886; DOI=10.1038/77124;
Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
Wolffe A.P.;
"DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses
transcription from E2F-responsive promoters.";
Nat. Genet. 25:338-342(2000).
[31]
INTERACTION WITH SUV39H1.
PubMed=11484059; DOI=10.1038/35087620;
Nielsen S.J., Schneider R., Bauer U.-M., Bannister A.J., Morrison A.,
O'Carroll D., Firestein R., Cleary M.L., Jenuwein T., Herrera R.E.,
Kouzarides T.;
"Rb targets histone H3 methylation and HP1 to promoters.";
Nature 412:561-565(2001).
[32]
INTERACTION WITH USP4.
PubMed=11571652; DOI=10.1038/sj.onc.1204824;
DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T.,
Pagano M., Loda M.;
"The de-ubiquitinating enzyme Unp interacts with the retinoblastoma
protein.";
Oncogene 20:5538-5542(2001).
[33]
INTERACTION WITH AATF.
PubMed=12450794; DOI=10.1016/S1535-6108(02)00182-4;
Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M.,
Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S.,
Floridi A., Passananti C., Fanciulli M.;
"Che-1 affects cell growth by interfering with the recruitment of
HDAC1 by Rb.";
Cancer Cell 2:387-399(2002).
[34]
INTERACTION WITH TMPO-ALPHA AND LMNA.
PubMed=12475961; DOI=10.1091/mbc.E02-07-0450;
Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.;
"Lamin A/C binding protein LAP2alpha is required for nuclear anchorage
of retinoblastoma protein.";
Mol. Biol. Cell 13:4401-4413(2002).
[35]
INTERACTION WITH SNW1.
PubMed=12466551; DOI=10.1093/nar/gkf658;
Prathapam T., Kuhne C., Banks L.;
"Skip interacts with the retinoblastoma tumor suppressor and inhibits
its transcriptional repression activity.";
Nucleic Acids Res. 30:5261-5268(2002).
[36]
INTERACTION WITH P-TEFB COMPLEX.
PubMed=12037672; DOI=10.1038/sj.onc.1205511;
Simone C., Bagella L., Bellan C., Giordano A.;
"Physical interaction between pRb and cdk9/cyclinT2 complex.";
Oncogene 21:4158-4165(2002).
[37]
INTERACTION WITH PELP1.
PubMed=12682072; DOI=10.1074/jbc.M212822200;
Balasenthil S., Vadlamudi R.K.;
"Functional interactions between the estrogen receptor coactivator
PELP1/MNAR and retinoblastoma protein.";
J. Biol. Chem. 278:22119-22127(2003).
[38]
FUNCTION IN G0-G1 TRANSITION, AND PHOSPHORYLATION AT SER-807 AND
SER-811 BY CDK3.
PubMed=15084261; DOI=10.1016/S0092-8674(04)00300-9;
Ren S., Rollins B.J.;
"Cyclin C/cdk3 promotes Rb-dependent G0 exit.";
Cell 117:239-251(2004).
[39]
INTERACTION WITH LIN9.
PubMed=15538385; DOI=10.1038/sj.emboj.7600470;
Gagrica S., Hauser S., Kolfschoten I., Osterloh L., Agami R.,
Gaubatz S.;
"Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-
associated protein.";
EMBO J. 23:4627-4638(2004).
[40]
INTERACTION WITH CEBPA.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[41]
INTERACTION WITH LIMD1.
PubMed=15542589; DOI=10.1073/pnas.0407123101;
Sharp T.V., Munoz F., Bourboulia D., Presneau N., Darai E.,
Wang H.-W., Cannon M., Butcher D.N., Nicholson A.G., Klein G.,
Imreh S., Boshoff C.;
"LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded
at chromosome 3p21.3, binds pRB and represses E2F-driven
transcription.";
Proc. Natl. Acad. Sci. U.S.A. 101:16531-16536(2004).
[42]
PHOSPHORYLATION AT THR-821 AND THR-826.
PubMed=15809340; DOI=10.1093/jb/mvi050;
Takaki T., Fukasawa K., Suzuki-Takahashi I., Semba K., Kitagawa M.,
Taya Y., Hirai H.;
"Preferences for phosphorylation sites in the retinoblastoma protein
of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro.";
J. Biochem. 137:381-386(2005).
[43]
INTERACTION WITH KDM4A.
PubMed=15927959; DOI=10.1074/jbc.M413687200;
Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S.,
Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
"Functional characterization of JMJD2A, a histone deacetylase- and
retinoblastoma-binding protein.";
J. Biol. Chem. 280:28507-28518(2005).
[44]
INTERACTION WITH KDM5B.
PubMed=15803180; DOI=10.1038/modpathol.3800413;
Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M.,
Vogt T.;
"Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding
protein downregulated in malignant melanomas.";
Mod. Pathol. 18:1249-1257(2005).
[45]
INTERACTION WITH KDM5A.
PubMed=15949438; DOI=10.1016/j.molcel.2005.05.012;
Benevolenskaya E.V., Murray H.L., Branton P., Young R.A.,
Kaelin W.G. Jr.;
"Binding of pRB to the PHD protein RBP2 promotes cellular
differentiation.";
Mol. Cell 18:623-635(2005).
[46]
INTERACTION WITH PSMA3.
PubMed=16337594; DOI=10.1016/j.molcel.2005.10.017;
Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R.,
Allday M.J., Xiao Z.X.;
"MDM2 promotes proteasome-dependent ubiquitin-independent degradation
of retinoblastoma protein.";
Mol. Cell 20:699-708(2005).
[47]
INTERACTION WITH ZUBR1.
PubMed=16214886; DOI=10.1073/pnas.0507458102;
Nakatani Y., Konishi H., Vassilev A., Kurooka H., Ishiguro K.,
Sawada J., Ikura T., Korsmeyer S.J., Qin J., Herlitz A.M.;
"p600, a unique protein required for membrane morphogenesis and cell
survival.";
Proc. Natl. Acad. Sci. U.S.A. 102:15093-15098(2005).
[48]
INTERACTION WITH KDM5B.
PubMed=16645588; DOI=10.1038/sj.jid.5700324;
Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M.,
Vogt T.;
"Re-expression of the retinoblastoma-binding protein 2-homolog 1
reveals tumor-suppressive functions in highly metastatic melanoma
cells.";
J. Invest. Dermatol. 126:1850-1859(2006).
[49]
PHOSPHORYLATION AT SER-612 BY CHEK2, AND INTERACTION WITH CHEK2.
PubMed=17380128; DOI=10.1038/sj.emboj.7601652;
Inoue Y., Kitagawa M., Taya Y.;
"Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between
pRB and E2F-1 after DNA damage.";
EMBO J. 26:2083-2093(2007).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-252 AND
THR-356, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-252;
SER-612; SER-807; SER-811; THR-823 AND THR-826, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[52]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-373;
SER-807 AND THR-841, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[54]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[55]
METHYLATION AT LYS-860, INTERACTION WITH L3MBTL1, AND MUTAGENESIS OF
LYS-860; LYS-870 AND 873-LYS-LYS-874.
PubMed=20870719; DOI=10.1074/jbc.M110.137612;
Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M.,
Gozani O., Sage J.;
"Methylation of the retinoblastoma tumor suppressor by SMYD2.";
J. Biol. Chem. 285:37733-37740(2010).
[56]
ACETYLATION AT LYS-873 AND LYS-874, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 873-LYS--LYS-874.
PubMed=20940255; DOI=10.1242/jcs.068924;
Pickard A., Wong P.P., McCance D.J.;
"Acetylation of Rb by PCAF is required for nuclear localization and
keratinocyte differentiation.";
J. Cell Sci. 123:3718-3726(2010).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-821 AND THR-826, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[58]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[59]
INTERACTION WITH UHRF2.
PubMed=21952639; DOI=10.4161/cc.10.19.17176;
Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.;
"NIRF constitutes a nodal point in the cell cycle network and is a
candidate tumor suppressor.";
Cell Cycle 10:3284-3299(2011).
[60]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[61]
METHYLATION AT LYS-810 BY SMYD2.
PubMed=22787429;
Cho H.S., Hayami S., Toyokawa G., Maejima K., Yamane Y., Suzuki T.,
Dohmae N., Kogure M., Kang D., Neal D.E., Ponder B.A., Yamaue H.,
Nakamura Y., Hamamoto R.;
"RB1 methylation by SMYD2 enhances cell cycle progression through an
increase of RB1 phosphorylation.";
Neoplasia 14:476-486(2012).
[62]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-252; THR-356;
THR-373; SER-624; SER-780; SER-788; SER-795; SER-807; SER-811;
THR-821; THR-823; THR-826 AND SER-855, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[63]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[64]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 378-562.
PubMed=9145110; DOI=10.1038/nsb0597-390;
Kim H.Y., Cho Y.;
"Structural similarity between the pocket region of retinoblastoma
tumour suppressor and the cyclin-box.";
Nat. Struct. Biol. 4:390-395(1997).
[65]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 380-785.
PubMed=9495340; DOI=10.1038/36038;
Lee J.O., Russo A.A., Pavletich N.P.;
"Structure of the retinoblastoma tumour-suppressor pocket domain bound
to a peptide from HPV E7.";
Nature 391:859-865(1998).
[66]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 860-876 IN COMPLEX WITH
KPNA2.
PubMed=12695505; DOI=10.1074/jbc.M303275200;
Fontes M.R.M., Teh T., Jans D., Brinkworth R.I., Kobe B.;
"Structural basis for the specificity of bipartite nuclear
localization sequence binding by importin-alpha.";
J. Biol. Chem. 278:27981-27987(2003).
[67]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 829-874 IN COMPLEX WITH E2F1
AND TFDP1, INTERACTION WITH HETERODIMERIC COMPLEXES CONTAINING TFDP1
AND EITHER E2F1; E2F3; E2F4 OR E2F5, MUTAGENESIS OF THR-821 AND
THR-826, AND PHOSPHORYLATION AT THR-821 AND THR-826.
PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism
for phosphorylation-induced E2F release.";
Cell 123:1093-1106(2005).
[68]
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 380-787 IN COMPLEX WITH
HUMAN ADENOVIRUS E1A PROTEIN.
PubMed=17974914; DOI=10.1101/gad.1590607;
Liu X., Marmorstein R.;
"Structure of the retinoblastoma protein bound to adenovirus E1A
reveals the molecular basis for viral oncoprotein inactivation of a
tumor suppressor.";
Genes Dev. 21:2711-2716(2007).
[69]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-355, PARTIAL PROTEIN
SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THOC1
AND GRIP1, AND INTERACTION OF THE UNPHOSPHORYLATED PROTEIN WITH EID1.
PubMed=17996702; DOI=10.1016/j.molcel.2007.08.023;
Hassler M., Singh S., Yue W.W., Luczynski M., Lakbir R.,
Sanchez-Sanchez F., Bader T., Pearl L.H., Mittnacht S.;
"Crystal structure of the retinoblastoma protein N domain provides
insight into tumor suppression, ligand interaction, and holoprotein
architecture.";
Mol. Cell 28:371-385(2007).
[70]
VARIANT RB LEU-567.
PubMed=2594029; DOI=10.1056/NEJM198912213212501;
Yandell D.W., Campbell T.A., Dayton S.H., Petersen R., Walton D.,
Little J.B., McConkie-Rosell A., Buckley E., Dryja T.P.;
"Oncogenic point mutations in the human retinoblastoma gene: their
application to genetic counseling.";
N. Engl. J. Med. 321:1689-1695(1989).
[71]
VARIANT RB TRP-661.
PubMed=1352883; DOI=10.1073/pnas.89.13.6177;
Onadim Z., Hogg A., Baird P.N., Cowell J.K.;
"Oncogenic point mutations in exon 20 of the RB1 gene in families
showing incomplete penetrance and mild expression of the
retinoblastoma phenotype.";
Proc. Natl. Acad. Sci. U.S.A. 89:6177-6181(1992).
[72]
VARIANT RB ARG-457.
PubMed=8346255; DOI=10.1073/pnas.90.15.7351;
Hogg A., Bia B., Onadim Z., Cowell J.K.;
"Molecular mechanisms of oncogenic mutations in tumors from patients
with bilateral and unilateral retinoblastoma.";
Proc. Natl. Acad. Sci. U.S.A. 90:7351-7355(1993).
[73]
VARIANT RB ARG-530.
PubMed=7704558;
Cowell J.K., Smith T., Bia B.;
"Frequent constitutional C to T mutations in CGA-arginine codons in
the RB1 gene produce premature stop codons in patients with bilateral
(hereditary) retinoblastoma.";
Eur. J. Hum. Genet. 2:281-290(1994).
[74]
VARIANTS RB ASN-480 DEL AND TRP-661.
PubMed=7927327; DOI=10.1007/BF00201591;
Lohmann D.R., Brandt B., Hoepping W., Passarge E., Horsthemke B.;
"Distinct RB1 gene mutations with low penetrance in hereditary
retinoblastoma.";
Hum. Genet. 94:349-354(1994).
[75]
VARIANTS RB GLN-72; TYR-549 AND LYS-803.
PubMed=8605116; DOI=10.1002/gcc.2870140406;
Liu Z., Song Y., Bia B., Cowell J.K.;
"Germline mutations in the RB1 gene in patients with hereditary
retinoblastoma.";
Genes Chromosomes Cancer 14:277-284(1995).
[76]
VARIANTS RB THR-185; PRO-635; GLU-654 AND PRO-685.
PubMed=7795591; DOI=10.1093/hmg/4.3.383;
Blanquet V., Turleau C., Gross-Morand M.S., Senamaud-Beaufort C.,
Doz F., Besmond C.;
"Spectrum of germline mutations in the RB1 gene: a study of 232
patients with hereditary and non hereditary retinoblastoma.";
Hum. Mol. Genet. 4:383-388(1995).
[77]
VARIANTS RB GLY-358; PRO-657 AND TRP-661.
PubMed=8776589; DOI=10.1093/hmg/5.6.755;
Van Orsouw N.J., Li D., van der Vlies P., Scheffer H., Eng C.,
Buys C.H.C.M., Li F.P., Vijg J.;
"Mutational scanning of large genes by extensive PCR multiplexing and
two-dimensional electrophoresis: application to the RB1 gene.";
Hum. Mol. Genet. 5:755-761(1996).
[78]
VARIANTS RB ASP-137 AND TRP-661.
PubMed=9311732; DOI=10.1086/514845;
Lohmann D.R., Gerick M., Brandt B., Oelschlaeger U., Lorenz B.,
Passarge E., Horsthemke B.;
"Constitutional RB1-gene mutations in patients with isolated
unilateral retinoblastoma.";
Am. J. Hum. Genet. 61:282-294(1997).
[79]
VARIANT RB GLN-447.
PubMed=9140452; DOI=10.1016/S0165-4608(96)00387-1;
Mateu E., Sanchez F., Najera C., Beneyto M., Castell V., Hernandez M.,
Serra I., Prieto F.;
"Genetics of retinoblastoma: a study.";
Cancer Genet. Cytogenet. 95:40-50(1997).
[80]
VARIANTS RB LEU-567; PRO-662 AND ARG-712.
PubMed=10671068;
DOI=10.1002/(SICI)1098-1004(1998)12:6<434::AID-HUMU16>3.3.CO;2-Z;
Yilmaz S., Horsthemke B., Lohmann D.R.;
"Twelve novel RB1 gene mutations in patients with hereditary
retinoblastoma.";
Hum. Mutat. 12:434-434(1998).
[81]
VARIANT RB GLU-310.
PubMed=9973307; DOI=10.1086/302254;
Klutz M., Horsthemke B., Lohmann D.R.;
"RB1 gene mutations in peripheral blood DNA of patients with isolated
unilateral retinoblastoma.";
Am. J. Hum. Genet. 64:667-668(1999).
[82]
VARIANTS RB GLY-500 AND GLU-616.
PubMed=11524739; DOI=10.1002/humu.1184;
Yu Y.S., Kim I.-J., Ku J.-L., Park J.-G.;
"Identification of four novel RB1 germline mutations in Korean
retinoblastoma patients.";
Hum. Mutat. 18:252-252(2001).
[83]
VARIANT HIS-173.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: Key regulator of entry into cell division that acts as a
tumor suppressor. Promotes G0-G1 transition when phosphorylated by
CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target
genes. The underphosphorylated, active form of RB1 interacts with
E2F1 and represses its transcription activity, leading to cell
cycle arrest. Directly involved in heterochromatin formation by
maintaining overall chromatin structure and, in particular, that
of constitutive heterochromatin by stabilizing histone
methylation. Recruits and targets histone methyltransferases
SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional
repression. Controls histone H4 'Lys-20' trimethylation. Inhibits
the intrinsic kinase activity of TAF1. Mediates transcriptional
repression by SMARCA4/BRG1 by recruiting a histone deacetylase
(HDAC) complex to the c-FOS promoter. In resting neurons,
transcription of the c-FOS promoter is inhibited by BRG1-dependent
recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium
influx, RB1 is dephosphorylated by calcineurin, which leads to
release of the repressor complex (By similarity). In case of viral
infections, interactions with SV40 large T antigen, HPV E7 protein
or adenovirus E1A protein induce the disassembly of RB1-E2F1
complex thereby disrupting RB1's activity. {ECO:0000250,
ECO:0000269|PubMed:15084261}.
-!- SUBUNIT: Interacts with ATAD5. Interacts with PRMT2, CDK1 and CDK2
(By similarity). The hypophosphorylated form interacts with and
sequesters the E2F1 transcription factor. Interacts with
heterodimeric E2F/DP transcription factor complexes containing
TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The
unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1,
MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain of
TAF1. Interacts with SNW1, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C,
PELP1, UHRF2 and TMPO-alpha. May interact with NDC80. Interacts
with GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts
with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 AND HDAC1 (By
similarity). Interacts with PSMA3 and USP4. Interacts (when
methylated at Lys-860) with L3MBTL1. Interacts with CHEK2;
phosphorylates RB1. Interacts with CEBPA (PubMed:15107404).
Interacts with adenovirus E1A protein, HPV E7 protein and SV40
large T antigen. Interacts with human cytomegalovirus/HHV-5
protein UL123. P-TEFB complex interacts with RB1; promotes
phosphorylation of RB1 (PubMed:12037672).
{ECO:0000250|UniProtKB:P13405, ECO:0000250|UniProtKB:P33568,
ECO:0000269|PubMed:10409732, ECO:0000269|PubMed:10446990,
ECO:0000269|PubMed:10779342, ECO:0000269|PubMed:10869426,
ECO:0000269|PubMed:10888886, ECO:0000269|PubMed:11223246,
ECO:0000269|PubMed:11484059, ECO:0000269|PubMed:11571652,
ECO:0000269|PubMed:12037672, ECO:0000269|PubMed:12450794,
ECO:0000269|PubMed:12466551, ECO:0000269|PubMed:12475961,
ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:12695505,
ECO:0000269|PubMed:1316611, ECO:0000269|PubMed:15107404,
ECO:0000269|PubMed:15538385, ECO:0000269|PubMed:15542589,
ECO:0000269|PubMed:15803180, ECO:0000269|PubMed:15927959,
ECO:0000269|PubMed:15949438, ECO:0000269|PubMed:16214886,
ECO:0000269|PubMed:16337594, ECO:0000269|PubMed:16360038,
ECO:0000269|PubMed:16645588, ECO:0000269|PubMed:17380128,
ECO:0000269|PubMed:17974914, ECO:0000269|PubMed:17996702,
ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:21952639,
ECO:0000269|PubMed:2839300, ECO:0000269|PubMed:7525595,
ECO:0000269|PubMed:7935440, ECO:0000269|PubMed:8414517,
ECO:0000269|PubMed:8892909, ECO:0000269|PubMed:9858607}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-491274, EBI-491274;
P03070:- (xeno); NbExp=6; IntAct=EBI-491274, EBI-617698;
P03255:- (xeno); NbExp=9; IntAct=EBI-491274, EBI-2603114;
P03255-1:- (xeno); NbExp=2; IntAct=EBI-491274, EBI-6692439;
P03255-2:- (xeno); NbExp=3; IntAct=EBI-491274, EBI-6859460;
P24941:CDK2; NbExp=3; IntAct=EBI-491274, EBI-375096;
P30285:Cdk4 (xeno); NbExp=2; IntAct=EBI-491274, EBI-847225;
Q155P7:Cenpf (xeno); NbExp=4; IntAct=EBI-491274, EBI-2211248;
O14757:CHEK1; NbExp=3; IntAct=EBI-491274, EBI-974488;
O96017:CHEK2; NbExp=3; IntAct=EBI-491274, EBI-1180783;
Q13574-2:DGKZ; NbExp=6; IntAct=EBI-491274, EBI-715527;
Q13627:DYRK1A; NbExp=3; IntAct=EBI-491274, EBI-1053596;
Q9Y463:DYRK1B; NbExp=3; IntAct=EBI-491274, EBI-634187;
Q01094:E2F1; NbExp=20; IntAct=EBI-491274, EBI-448924;
Q14209:E2F2; NbExp=3; IntAct=EBI-491274, EBI-718476;
O00716:E2F3; NbExp=4; IntAct=EBI-491274, EBI-765551;
A0MPS7:E7 (xeno); NbExp=2; IntAct=EBI-491274, EBI-7014709;
P03129:E7 (xeno); NbExp=22; IntAct=EBI-491274, EBI-866453;
P04020:E7 (xeno); NbExp=3; IntAct=EBI-491274, EBI-7005254;
P06464:E7 (xeno); NbExp=3; IntAct=EBI-491274, EBI-6944797;
P06465:E7 (xeno); NbExp=2; IntAct=EBI-491274, EBI-963841;
P06788:E7 (xeno); NbExp=3; IntAct=EBI-491274, EBI-1776887;
O43524:FOXO3; NbExp=2; IntAct=EBI-491274, EBI-1644164;
P42685:FRK; NbExp=3; IntAct=EBI-491274, EBI-1383583;
P62993:GRB2; NbExp=4; IntAct=EBI-491274, EBI-401755;
O60381:HBP1; NbExp=2; IntAct=EBI-491274, EBI-954175;
Q13547:HDAC1; NbExp=4; IntAct=EBI-491274, EBI-301834;
P52927:Hmga2 (xeno); NbExp=5; IntAct=EBI-491274, EBI-912574;
Q9R002:Ifi202 (xeno); NbExp=5; IntAct=EBI-491274, EBI-3043899;
Q14653:IRF3; NbExp=2; IntAct=EBI-491274, EBI-2650369;
Q16539:MAPK14; NbExp=4; IntAct=EBI-491274, EBI-73946;
Q00987:MDM2; NbExp=4; IntAct=EBI-491274, EBI-389668;
O15151:MDM4; NbExp=4; IntAct=EBI-491274, EBI-398437;
Q14686:NCOA6; NbExp=3; IntAct=EBI-491274, EBI-78670;
P07197:NEFM; NbExp=2; IntAct=EBI-491274, EBI-1105035;
Q8VSP9:ospF (xeno); NbExp=2; IntAct=EBI-491274, EBI-6506625;
Q9UQ80:PA2G4; NbExp=4; IntAct=EBI-491274, EBI-924893;
P62136:PPP1CA; NbExp=2; IntAct=EBI-491274, EBI-357253;
P55345:PRMT2; NbExp=3; IntAct=EBI-491274, EBI-78458;
Q00577:PURA; NbExp=6; IntAct=EBI-491274, EBI-1045860;
P04049:RAF1; NbExp=3; IntAct=EBI-491274, EBI-365996;
O75150:RNF40; NbExp=3; IntAct=EBI-491274, EBI-744408;
Q8WTS6:SETD7; NbExp=4; IntAct=EBI-491274, EBI-1268586;
Q923E4:Sirt1 (xeno); NbExp=4; IntAct=EBI-491274, EBI-1802585;
Q3TKT4:Smarca4 (xeno); NbExp=4; IntAct=EBI-491274, EBI-1210244;
Q96PU4:UHRF2; NbExp=4; IntAct=EBI-491274, EBI-625304;
Q93009:USP7; NbExp=8; IntAct=EBI-491274, EBI-302474;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255}.
-!- TISSUE SPECIFICITY: Expressed in the retina.
-!- DOMAIN: The Pocket domain binds to the threonine-phosphorylated
domain C, thereby preventing interaction with heterodimeric E2F/DP
transcription factor complexes.
-!- PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at
Ser-567 in G1, thereby releasing E2F1 which is then able to
activate cell growth. Dephosphorylated at the late M phase. SV40
large T antigen, HPV E7 and adenovirus E1A bind to the
underphosphorylated, active form of pRb. Phosphorylation at Thr-
821 and Thr-826 promotes interaction between the C-terminal domain
C and the Pocket domain, and thereby inhibits interactions with
heterodimeric E2F/DP transcription factor complexes.
Dephosphorylated at Ser-795 by calcineruin upon calcium
stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and
Ser-811 is required for G0-G1 transition. Phosphorylated by CDK1
and CDK2 upon TGFB1-mediated apoptosis (By similarity).
{ECO:0000250}.
-!- PTM: N-terminus is methylated by METTL11A/NTM1 (By similarity).
Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at
Ser-807 and Ser-811, and promotes cell cycle progression.
Monomethylation at Lys-860 by SMYD2 promotes interaction with
L3MBTL1. {ECO:0000250, ECO:0000269|PubMed:10499802,
ECO:0000269|PubMed:15084261, ECO:0000269|PubMed:15809340,
ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17380128,
ECO:0000269|PubMed:1756735, ECO:0000269|PubMed:20870719,
ECO:0000269|PubMed:22787429, ECO:0000269|PubMed:8114739}.
-!- PTM: Acetylation at Lys-873 and Lys-874 regulates subcellular
localization, at least during keratinocytes differentiation.
{ECO:0000269|PubMed:20940255}.
-!- DISEASE: Childhood cancer retinoblastoma (RB) [MIM:180200]:
Congenital malignant tumor that arises from the nuclear layers of
the retina. It occurs in about 1:20'000 live births and represents
about 2% of childhood malignancies. It is bilateral in about 30%
of cases. Although most RB appear sporadically, about 20% are
transmitted as an autosomal dominant trait with incomplete
penetrance. The diagnosis is usually made before the age of 2
years when strabismus or a gray to yellow reflex from pupil ('cat
eye') is investigated. {ECO:0000269|PubMed:10671068,
ECO:0000269|PubMed:11524739, ECO:0000269|PubMed:1352883,
ECO:0000269|PubMed:2594029, ECO:0000269|PubMed:7704558,
ECO:0000269|PubMed:7795591, ECO:0000269|PubMed:7927327,
ECO:0000269|PubMed:8346255, ECO:0000269|PubMed:8605116,
ECO:0000269|PubMed:8776589, ECO:0000269|PubMed:9140452,
ECO:0000269|PubMed:9311732, ECO:0000269|PubMed:9973307}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy
originating in tissues of the urinary bladder. It often presents
with multiple tumors appearing at different times and at different
sites in the bladder. Most bladder cancers are transitional cell
carcinomas that begin in cells that normally make up the inner
lining of the bladder. Other types of bladder cancer include
squamous cell carcinoma (cancer that begins in thin, flat cells)
and adenocarcinoma (cancer that begins in cells that make and
release mucus and other fluids). Bladder cancer is a complex
disorder with both genetic and environmental influences.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Osteogenic sarcoma (OSRC) [MIM:259500]: A sarcoma
originating in bone-forming cells, affecting the ends of long
bones. Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=RB1base; Note=RB1 mutation db;
URL="http://rb1-lsdb.d-lohmann.de/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RB1ID90.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rb1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Retinoblastoma protein entry;
URL="https://en.wikipedia.org/wiki/Retinoblastoma_protein";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M15400; AAA69807.1; ALT_SEQ; mRNA.
EMBL; M28419; AAA69808.1; -; mRNA.
EMBL; M33647; AAA69806.1; -; mRNA.
EMBL; L41870; AAB59465.1; -; mRNA.
EMBL; M27866; AAA53484.1; -; Genomic_DNA.
EMBL; M27845; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27846; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27847; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27849; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27850; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27851; AAA53484.1; JOINED; Genomic_DNA.
EMBL; L35146; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27852; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27853; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27854; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27855; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27856; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27857; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27858; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27859; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27860; AAA53484.1; JOINED; Genomic_DNA.
EMBL; L35147; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27862; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27863; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27864; AAA53484.1; JOINED; Genomic_DNA.
EMBL; M27865; AAA53484.1; JOINED; Genomic_DNA.
EMBL; L41889; AAB59467.1; -; Genomic_DNA.
EMBL; L41890; AAA65735.1; -; Genomic_DNA.
EMBL; L41891; AAA65736.1; -; Genomic_DNA.
EMBL; L41893; AAA65737.1; -; Genomic_DNA.
EMBL; L41894; AAA65738.1; -; Genomic_DNA.
EMBL; L41895; AAA65739.1; -; Genomic_DNA.
EMBL; L41896; AAA65740.1; -; Genomic_DNA.
EMBL; L41897; AAA65741.1; -; Genomic_DNA.
EMBL; L41898; AAB59471.1; -; Genomic_DNA.
EMBL; L41899; AAB59473.1; -; Genomic_DNA.
EMBL; L41997; AAB59482.1; -; Genomic_DNA.
EMBL; X16439; CAA34462.1; -; Genomic_DNA.
EMBL; AF551763; AAN64133.1; -; Genomic_DNA.
EMBL; AK291258; BAF83947.1; -; mRNA.
EMBL; AL136960; CAH70901.1; -; Genomic_DNA.
EMBL; AL392048; CAH70901.1; JOINED; Genomic_DNA.
EMBL; AL392048; CAH72243.1; -; Genomic_DNA.
EMBL; AL136960; CAH72243.1; JOINED; Genomic_DNA.
EMBL; CH471075; EAX08793.1; -; Genomic_DNA.
EMBL; BC039060; AAH39060.1; -; mRNA.
EMBL; BC040540; AAH40540.1; -; mRNA.
EMBL; L11910; AAA53483.1; -; Genomic_DNA.
CCDS; CCDS31973.1; -.
PIR; JS0276; RBHU.
RefSeq; NP_000312.2; NM_000321.2.
UniGene; Hs.408528; -.
PDB; 1AD6; X-ray; 2.30 A; A=378-562.
PDB; 1GH6; X-ray; 3.20 A; B=379-577, B=645-772.
PDB; 1GUX; X-ray; 1.85 A; A=372-589, B=636-787.
PDB; 1H25; X-ray; 2.50 A; E=868-878.
PDB; 1N4M; X-ray; 2.20 A; A/B=380-785.
PDB; 1O9K; X-ray; 2.60 A; A/C/E/G=372-589, B/D/F/H=636-787.
PDB; 1PJM; X-ray; 2.50 A; A=858-881.
PDB; 2AZE; X-ray; 2.55 A; C=829-874.
PDB; 2QDJ; X-ray; 2.00 A; A=52-355.
PDB; 2R7G; X-ray; 1.67 A; A/C=380-787.
PDB; 3N5U; X-ray; 3.20 A; C=870-882.
PDB; 3POM; X-ray; 2.50 A; A/B=380-577, A/B=643-783.
PDB; 4CRI; X-ray; 2.35 A; C/D=802-817.
PDB; 4ELJ; X-ray; 2.70 A; A=53-787.
PDB; 4ELL; X-ray; 1.98 A; A/B=380-787.
PDBsum; 1AD6; -.
PDBsum; 1GH6; -.
PDBsum; 1GUX; -.
PDBsum; 1H25; -.
PDBsum; 1N4M; -.
PDBsum; 1O9K; -.
PDBsum; 1PJM; -.
PDBsum; 2AZE; -.
PDBsum; 2QDJ; -.
PDBsum; 2R7G; -.
PDBsum; 3N5U; -.
PDBsum; 3POM; -.
PDBsum; 4CRI; -.
PDBsum; 4ELJ; -.
PDBsum; 4ELL; -.
ProteinModelPortal; P06400; -.
SMR; P06400; -.
BioGrid; 111860; 233.
DIP; DIP-582N; -.
ELM; P06400; -.
IntAct; P06400; 123.
MINT; MINT-98847; -.
STRING; 9606.ENSP00000267163; -.
BindingDB; P06400; -.
ChEMBL; CHEMBL5288; -.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00071; Insulin Pork.
iPTMnet; P06400; -.
PhosphoSitePlus; P06400; -.
BioMuta; RB1; -.
DMDM; 132164; -.
EPD; P06400; -.
MaxQB; P06400; -.
PaxDb; P06400; -.
PeptideAtlas; P06400; -.
PRIDE; P06400; -.
DNASU; 5925; -.
Ensembl; ENST00000267163; ENSP00000267163; ENSG00000139687.
GeneID; 5925; -.
KEGG; hsa:5925; -.
UCSC; uc001vcb.4; human.
CTD; 5925; -.
DisGeNET; 5925; -.
GeneCards; RB1; -.
GeneReviews; RB1; -.
HGNC; HGNC:9884; RB1.
HPA; CAB000095; -.
HPA; CAB016687; -.
HPA; HPA050082; -.
MalaCards; RB1; -.
MIM; 109800; phenotype.
MIM; 180200; phenotype.
MIM; 259500; phenotype.
MIM; 614041; gene.
neXtProt; NX_P06400; -.
OpenTargets; ENSG00000139687; -.
Orphanet; 357027; Familial retinoblastoma.
Orphanet; 1587; Monosomy 13q14.
Orphanet; 357034; Unilateral retinoblastoma.
PharmGKB; PA295; -.
eggNOG; KOG1010; Eukaryota.
eggNOG; ENOG410XQF7; LUCA.
GeneTree; ENSGT00530000063235; -.
HOVERGEN; HBG008967; -.
InParanoid; P06400; -.
KO; K06618; -.
OMA; TNILQYA; -.
OrthoDB; EOG091G0398; -.
PhylomeDB; P06400; -.
TreeFam; TF105568; -.
Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
SignaLink; P06400; -.
SIGNOR; P06400; -.
ChiTaRS; RB1; human.
EvolutionaryTrace; P06400; -.
GeneWiki; Retinoblastoma_protein; -.
GenomeRNAi; 5925; -.
PMAP-CutDB; P06400; -.
PRO; PR:P06400; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000139687; -.
CleanEx; HS_RB1; -.
ExpressionAtlas; P06400; baseline and differential.
Genevisible; P06400; HS.
GO; GO:0000785; C:chromatin; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:UniProtKB.
GO; GO:0035189; C:Rb-E2F complex; IDA:CAFA.
GO; GO:0005819; C:spindle; IEA:Ensembl.
GO; GO:0016514; C:SWI/SNF complex; TAS:BHF-UCL.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0061676; F:importin-alpha family protein binding; IPI:CAFA.
GO; GO:0019900; F:kinase binding; IDA:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:BHF-UCL.
GO; GO:0000075; P:cell cycle checkpoint; TAS:ProtInc.
GO; GO:0051301; P:cell division; IEA:Ensembl.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:Ensembl.
GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IMP:BHF-UCL.
GO; GO:0007093; P:mitotic cell cycle checkpoint; TAS:BHF-UCL.
GO; GO:0045445; P:myoblast differentiation; IMP:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; TAS:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; IPI:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; TAS:BHF-UCL.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0007070; P:negative regulation of transcription from RNA polymerase II promoter during mitotic cell cycle; TAS:BHF-UCL.
GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:BHF-UCL.
GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:0090230; P:regulation of centromere complex assembly; TAS:BHF-UCL.
GO; GO:0071922; P:regulation of cohesin loading; IMP:BHF-UCL.
GO; GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0031134; P:sister chromatid biorientation; IMP:BHF-UCL.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.472.10; -; 3.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR033057; RB1.
InterPro; IPR002720; RB_A.
InterPro; IPR002719; RB_B.
InterPro; IPR015030; RB_C.
InterPro; IPR028309; RB_fam.
InterPro; IPR024599; RB_N.
PANTHER; PTHR13742; PTHR13742; 1.
PANTHER; PTHR13742:SF26; PTHR13742:SF26; 1.
Pfam; PF11934; DUF3452; 1.
Pfam; PF01858; RB_A; 1.
Pfam; PF01857; RB_B; 1.
Pfam; PF08934; Rb_C; 1.
SMART; SM00385; CYCLIN; 1.
SMART; SM01367; DUF3452; 1.
SMART; SM01368; RB_A; 1.
SMART; SM01369; Rb_C; 1.
SUPFAM; SSF47954; SSF47954; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Chromatin regulator;
Complete proteome; Direct protein sequencing; Disease mutation;
DNA-binding; Host-virus interaction; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Tumor suppressor.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P13405}.
CHAIN 2 928 Retinoblastoma-associated protein.
/FTId=PRO_0000167836.
REGION 373 771 Pocket; binds T and E1A.
REGION 373 579 Domain A.
REGION 580 639 Spacer.
REGION 640 771 Domain B.
REGION 763 928 Interaction with LIMD1.
{ECO:0000269|PubMed:15542589}.
REGION 771 928 Domain C; mediates interaction with E4F1.
{ECO:0000269|PubMed:10869426}.
MOTIF 870 876 Nuclear localization signal.
{ECO:0000305}.
COMPBIAS 10 18 Poly-Ala.
COMPBIAS 20 29 Poly-Pro.
MOD_RES 2 2 N,N-dimethylproline.
{ECO:0000250|UniProtKB:P13405}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 249 249 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:1756735}.
MOD_RES 252 252 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:1756735}.
MOD_RES 356 356 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
MOD_RES 373 373 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:1756735}.
MOD_RES 567 567 Phosphoserine; by CDK2.
{ECO:0000269|PubMed:10499802}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000250|UniProtKB:P13405}.
MOD_RES 612 612 Phosphoserine; by CHEK2 and CHEK1.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17380128}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 788 788 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 807 807 Phosphoserine; by CDK1 and CDK3.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15084261,
ECO:0000269|PubMed:1756735}.
MOD_RES 810 810 N6-methyllysine; by SMYD2.
{ECO:0000269|PubMed:22787429}.
MOD_RES 811 811 Phosphoserine; by CDK1 and CDK3.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15084261,
ECO:0000269|PubMed:1756735}.
MOD_RES 821 821 Phosphothreonine; by CDK6.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15809340,
ECO:0000269|PubMed:16360038}.
MOD_RES 823 823 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 826 826 Phosphothreonine; by CDK4.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15809340,
ECO:0000269|PubMed:16360038}.
MOD_RES 841 841 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 860 860 N6-methyllysine; by SMYD2.
{ECO:0000269|PubMed:20870719}.
MOD_RES 873 873 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:20940255}.
MOD_RES 874 874 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:20940255}.
VARIANT 72 72 E -> Q (in RB).
{ECO:0000269|PubMed:8605116}.
/FTId=VAR_005572.
VARIANT 133 133 N -> H (in dbSNP:rs3092900).
/FTId=VAR_051909.
VARIANT 137 137 E -> D (in RB; unilateral form;
dbSNP:rs3092902).
{ECO:0000269|PubMed:9311732}.
/FTId=VAR_005573.
VARIANT 173 173 Y -> H. {ECO:0000269|PubMed:23033978}.
/FTId=VAR_069376.
VARIANT 185 185 I -> T (in RB).
{ECO:0000269|PubMed:7795591}.
/FTId=VAR_005574.
VARIANT 310 310 G -> E (in RB; unknown pathological
significance; dbSNP:rs200844292).
{ECO:0000269|PubMed:9973307}.
/FTId=VAR_010045.
VARIANT 358 358 R -> G (in RB).
{ECO:0000269|PubMed:8776589}.
/FTId=VAR_010046.
VARIANT 358 358 R -> Q (in RB; dbSNP:rs767011440).
/FTId=VAR_005575.
VARIANT 436 436 Q -> K (in dbSNP:rs4151534).
{ECO:0000269|Ref.7}.
/FTId=VAR_019379.
VARIANT 447 447 K -> Q (in RB).
{ECO:0000269|PubMed:9140452}.
/FTId=VAR_010048.
VARIANT 457 457 M -> R (in RB).
{ECO:0000269|PubMed:8346255}.
/FTId=VAR_005576.
VARIANT 480 480 Missing (in RB; mild form).
{ECO:0000269|PubMed:7927327}.
/FTId=VAR_005577.
VARIANT 500 500 R -> G (in RB).
{ECO:0000269|PubMed:11524739}.
/FTId=VAR_011580.
VARIANT 525 525 A -> G (in dbSNP:rs4151539).
{ECO:0000269|Ref.7}.
/FTId=VAR_019380.
VARIANT 530 530 K -> R (in RB).
{ECO:0000269|PubMed:7704558}.
/FTId=VAR_010049.
VARIANT 549 549 H -> Y (in RB).
{ECO:0000269|PubMed:8605116}.
/FTId=VAR_005578.
VARIANT 567 567 S -> L (in RB; dbSNP:rs137853292).
{ECO:0000269|PubMed:10671068,
ECO:0000269|PubMed:2594029}.
/FTId=VAR_005579.
VARIANT 569 569 L -> F (in dbSNP:rs3092895).
/FTId=VAR_051910.
VARIANT 616 616 K -> E (in RB).
{ECO:0000269|PubMed:11524739}.
/FTId=VAR_011581.
VARIANT 635 635 A -> P (in RB).
{ECO:0000269|PubMed:7795591}.
/FTId=VAR_005580.
VARIANT 654 654 V -> E (in RB).
{ECO:0000269|PubMed:7795591}.
/FTId=VAR_005581.
VARIANT 657 657 L -> P (in RB).
{ECO:0000269|PubMed:8776589}.
/FTId=VAR_010050.
VARIANT 661 661 R -> W (in RB; mild form;
dbSNP:rs137853294).
{ECO:0000269|PubMed:1352883,
ECO:0000269|PubMed:7927327,
ECO:0000269|PubMed:8776589,
ECO:0000269|PubMed:9311732}.
/FTId=VAR_005582.
VARIANT 662 662 L -> P (in RB).
{ECO:0000269|PubMed:10671068}.
/FTId=VAR_005583.
VARIANT 673 673 H -> P (in RB).
/FTId=VAR_005584.
VARIANT 685 685 Q -> P (in RB).
{ECO:0000269|PubMed:7795591}.
/FTId=VAR_005585.
VARIANT 697 697 D -> E (in dbSNP:rs3092903).
/FTId=VAR_051911.
VARIANT 706 706 C -> Y (in RB).
/FTId=VAR_005586.
VARIANT 712 712 C -> R (in RB; dbSNP:rs137853296).
{ECO:0000269|PubMed:10671068}.
/FTId=VAR_005587.
VARIANT 746 746 E -> G (in dbSNP:rs3092905).
/FTId=VAR_034442.
VARIANT 803 803 N -> K (in RB).
{ECO:0000269|PubMed:8605116}.
/FTId=VAR_005588.
MUTAGEN 821 821 T->A: Abolishes interaction with Pocket
domain; when associated with A-826.
{ECO:0000269|PubMed:16360038}.
MUTAGEN 826 826 T->A: Abolishes interaction with Pocket
domain; when associated with A-821.
{ECO:0000269|PubMed:16360038}.
MUTAGEN 860 860 K->R: Abolishes monomethylation by SMYD2
and subsequent interaction with L3MBTL1.
{ECO:0000269|PubMed:20870719}.
MUTAGEN 870 870 K->R: Does not affect the ability to be
methylated by SMYD2; when associated with
873-R-R-874.
{ECO:0000269|PubMed:20870719}.
MUTAGEN 873 874 KK->R: Does not affect the ability to be
methylated by SMYD2; when associated with
873-R-R-874.
{ECO:0000269|PubMed:20870719,
ECO:0000269|PubMed:20940255}.
MUTAGEN 873 874 KK->RR: Does not alter Rb localization in
cycling cells, but mislocalizes to the
cytoplasm during keratinocytes
differentiation.
{ECO:0000269|PubMed:20870719,
ECO:0000269|PubMed:20940255}.
CONFLICT 500 501 RS -> SN (in Ref. 7; AAN64133).
{ECO:0000305}.
HELIX 55 63 {ECO:0000244|PDB:2QDJ}.
HELIX 68 82 {ECO:0000244|PDB:2QDJ}.
HELIX 95 110 {ECO:0000244|PDB:2QDJ}.
HELIX 117 124 {ECO:0000244|PDB:2QDJ}.
HELIX 128 135 {ECO:0000244|PDB:2QDJ}.
HELIX 142 172 {ECO:0000244|PDB:2QDJ}.
STRAND 180 182 {ECO:0000244|PDB:2QDJ}.
HELIX 188 204 {ECO:0000244|PDB:2QDJ}.
STRAND 207 209 {ECO:0000244|PDB:4ELJ}.
HELIX 212 228 {ECO:0000244|PDB:2QDJ}.
HELIX 232 234 {ECO:0000244|PDB:2QDJ}.
TURN 237 240 {ECO:0000244|PDB:2QDJ}.
HELIX 241 243 {ECO:0000244|PDB:2QDJ}.
HELIX 272 281 {ECO:0000244|PDB:2QDJ}.
HELIX 285 294 {ECO:0000244|PDB:2QDJ}.
HELIX 296 299 {ECO:0000244|PDB:2QDJ}.
HELIX 302 306 {ECO:0000244|PDB:4ELJ}.
HELIX 314 328 {ECO:0000244|PDB:2QDJ}.
HELIX 333 338 {ECO:0000244|PDB:2QDJ}.
HELIX 341 343 {ECO:0000244|PDB:2QDJ}.
HELIX 347 353 {ECO:0000244|PDB:2QDJ}.
HELIX 382 391 {ECO:0000244|PDB:2R7G}.
HELIX 398 405 {ECO:0000244|PDB:2R7G}.
STRAND 407 409 {ECO:0000244|PDB:2R7G}.
HELIX 412 434 {ECO:0000244|PDB:2R7G}.
HELIX 436 438 {ECO:0000244|PDB:2R7G}.
HELIX 439 468 {ECO:0000244|PDB:2R7G}.
HELIX 474 477 {ECO:0000244|PDB:2R7G}.
HELIX 480 501 {ECO:0000244|PDB:2R7G}.
TURN 504 506 {ECO:0000244|PDB:1N4M}.
STRAND 511 513 {ECO:0000244|PDB:4ELJ}.
HELIX 516 521 {ECO:0000244|PDB:2R7G}.
HELIX 525 529 {ECO:0000244|PDB:2R7G}.
HELIX 532 538 {ECO:0000244|PDB:2R7G}.
HELIX 544 559 {ECO:0000244|PDB:2R7G}.
HELIX 561 563 {ECO:0000244|PDB:2R7G}.
STRAND 564 566 {ECO:0000244|PDB:4ELJ}.
HELIX 569 577 {ECO:0000244|PDB:2R7G}.
HELIX 582 586 {ECO:0000244|PDB:4ELL}.
HELIX 602 607 {ECO:0000244|PDB:4ELL}.
HELIX 645 669 {ECO:0000244|PDB:2R7G}.
HELIX 676 690 {ECO:0000244|PDB:2R7G}.
HELIX 692 695 {ECO:0000244|PDB:2R7G}.
HELIX 700 714 {ECO:0000244|PDB:2R7G}.
HELIX 721 728 {ECO:0000244|PDB:2R7G}.
STRAND 731 733 {ECO:0000244|PDB:1N4M}.
HELIX 737 740 {ECO:0000244|PDB:2R7G}.
STRAND 741 743 {ECO:0000244|PDB:2R7G}.
STRAND 745 747 {ECO:0000244|PDB:2R7G}.
STRAND 748 750 {ECO:0000244|PDB:4ELJ}.
HELIX 752 758 {ECO:0000244|PDB:2R7G}.
HELIX 760 770 {ECO:0000244|PDB:2R7G}.
STRAND 773 775 {ECO:0000244|PDB:2R7G}.
STRAND 830 836 {ECO:0000244|PDB:2AZE}.
TURN 838 840 {ECO:0000244|PDB:2AZE}.
HELIX 841 853 {ECO:0000244|PDB:2AZE}.
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


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