ID RBL1_HUMAN Reviewed; 1068 AA. AC P28749; A8K2W5; Q4VXA0; Q8N5K6; Q9H1L5; Q9H1M1; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 3. DT 27-MAR-2024, entry version 228. DE RecName: Full=Retinoblastoma-like protein 1; DE AltName: Full=107 kDa retinoblastoma-associated protein; DE Short=p107; DE AltName: Full=pRb1; GN Name=RBL1; 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] (ISOFORM 1), AND FUNCTION. RX PubMed=8319904; DOI=10.1101/gad.7.7a.1111; RA Zhu L., van den Heuvel S., Helin K., Fattaey A., Ewen M., Livingston D., RA Dyson N., Harlow E.; RT "Inhibition of cell proliferation by p107, a relative of the retinoblastoma RT protein."; RL Genes Dev. 7:1111-1125(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Tongue; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-1068 (ISOFORM 1), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=1833063; DOI=10.1016/0092-8674(91)90038-z; RA Ewen M.E., Xing Y., Lawrence J.B., Livingston D.M.; RT "Molecular cloning, chromosomal mapping, and expression of the cDNA for RT p107, a retinoblastoma gene product-related protein."; RL Cell 66:1155-1164(1991). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52. RX PubMed=7791762; DOI=10.1128/mcb.15.7.3552; RA Zhu L., Zhu L., Xie E., Chang L.S.; RT "Differential roles of two tandem E2F sites in repression of the human p107 RT promoter by retinoblastoma and p107 proteins."; RL Mol. Cell. Biol. 15:3552-3562(1995). RN [8] RP PROTEIN SEQUENCE OF 320-334; 364-374; 635-657; 949-977 AND 1006-1012, RP PHOSPHORYLATION AT THR-332; THR-369; THR-385; SER-640; SER-762; SER-964; RP SER-975; SER-988; THR-997 AND SER-1009, MUTAGENESIS OF SER-640; SER-643; RP SER-650 AND 657-LYS--LEU-660, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11884610; DOI=10.1128/mcb.22.7.2242-2254.2002; RA Leng X., Noble M., Adams P.D., Qin J., Harper J.W.; RT "Reversal of growth suppression by p107 via direct phosphorylation by RT cyclin D1/cyclin-dependent kinase 4."; RL Mol. Cell. Biol. 22:2242-2254(2002). RN [9] RP INTERACTION WITH SV40 AND JC VIRUS LARGE T ANTIGEN (MICROBIAL INFECTION). RX PubMed=2546678; DOI=10.1016/0092-8674(89)90839-8; RA Dyson N., Buchkovich K., Whyte P., Harlow E.; RT "The cellular 107K protein that binds to adenovirus E1A also associates RT with the large T antigens of SV40 and JC virus."; RL Cell 58:249-255(1989). RN [10] 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 [11] 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 [12] RP PHOSPHORYLATION AT THR-369 AND SER-650. RX PubMed=12006580; DOI=10.1074/jbc.m200381200; RA Farkas T., Hansen K., Holm K., Lukas J., Bartek J.; RT "Distinct phosphorylation events regulate p130- and p107-mediated RT repression of E2F-4."; RL J. Biol. Chem. 277:26741-26752(2002). RN [13] RP INTERACTION WITH E2F4 AND TFDP1. 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 [14] RP FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX. RX PubMed=17671431; DOI=10.4161/cc.6.15.4512; RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., RA Gagrica S., Haenel F., Brehm A., Gaubatz S.; RT "LINC, a human complex that is related to pRB-containing complexes in RT invertebrates regulates the expression of G2/M genes."; RL Cell Cycle 6:1903-1913(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385; SER-749 AND SER-762, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [16] RP INTERACTION WITH JC VIRUS SMALL T ANTIGEN (MICROBIAL INFECTION). RX PubMed=20485545; DOI=10.1371/journal.pone.0010606; RA Bollag B., Hofstetter C.A., Reviriego-Mendoza M.M., Frisque R.J.; RT "JC virus small T antigen binds phosphatase PP2A and Rb family proteins and RT is required for efficient viral DNA replication activity."; RL PLoS ONE 5:e10606-e10606(2010). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-332; THR-369; THR-385; RP SER-640; SER-749; SER-762; SER-988 AND SER-1041, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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). CC -!- FUNCTION: Key regulator of entry into cell division (PubMed:17671431). CC Directly involved in heterochromatin formation by maintaining overall CC chromatin structure and, in particular, that of constitutive CC heterochromatin by stabilizing histone methylation (By similarity). CC Recruits and targets histone methyltransferases KMT5B and KMT5C, CC leading to epigenetic transcriptional repression (By similarity). CC Controls histone H4 'Lys-20' trimethylation (By similarity). Probably CC acts as a transcription repressor by recruiting chromatin-modifying CC enzymes to promoters (By similarity). Potent inhibitor of E2F-mediated CC trans-activation (PubMed:8319904). May act as a tumor suppressor CC (PubMed:8319904). {ECO:0000250|UniProtKB:Q64701, CC ECO:0000269|PubMed:17671431, ECO:0000269|PubMed:8319904}. CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2 (PubMed:17671431, PubMed:16360038). CC The complex exists in quiescent cells where it represses cell cycle- CC dependent genes (PubMed:17671431). It dissociates in S phase when LIN9, CC LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 CC (PubMed:17671431). Interacts with AATF (PubMed:12450794). Interacts CC with KDM5A (PubMed:7935440). Interacts with KMT5B and KMT5C (By CC similarity). Interacts with USP4 (By similarity). Interacts with RBBP9 CC (By similarity). {ECO:0000250|UniProtKB:D3ZS28, CC ECO:0000250|UniProtKB:Q64701, ECO:0000269|PubMed:12450794, CC ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17671431, CC ECO:0000269|PubMed:7935440}. CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 and JC virus large T CC antigens. Large T antigen, but not E1A, binds only to the CC unphosphorylated form. {ECO:0000269|PubMed:2546678}. CC -!- SUBUNIT: (Microbial infection) Interacts with JC virus small t antigen. CC {ECO:0000269|PubMed:20485545}. CC -!- INTERACTION: CC P28749; Q9BUH8: BEGAIN; NbExp=2; IntAct=EBI-971402, EBI-742722; CC P28749; P11802: CDK4; NbExp=2; IntAct=EBI-971402, EBI-295644; CC P28749; Q13574-2: DGKZ; NbExp=2; IntAct=EBI-971402, EBI-715527; CC P28749; Q13627: DYRK1A; NbExp=4; IntAct=EBI-971402, EBI-1053596; CC P28749; Q9Y463: DYRK1B; NbExp=4; IntAct=EBI-971402, EBI-634187; CC P28749; O43524: FOXO3; NbExp=3; IntAct=EBI-971402, EBI-1644164; CC P28749; Q14653: IRF3; NbExp=2; IntAct=EBI-971402, EBI-2650369; CC P28749; P67775: PPP2CA; NbExp=2; IntAct=EBI-971402, EBI-712311; CC P28749; P03129: E7; Xeno; NbExp=4; IntAct=EBI-971402, EBI-866453; CC P28749; P24610: Pax3; Xeno; NbExp=3; IntAct=EBI-971402, EBI-1208116; CC P28749; Q923E4: Sirt1; Xeno; NbExp=2; IntAct=EBI-971402, EBI-1802585; CC P28749; P03255; Xeno; NbExp=3; IntAct=EBI-971402, EBI-2603114; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P28749-1; Sequence=Displayed; CC Name=2; CC IsoId=P28749-2; Sequence=VSP_017496; CC -!- PTM: Cell-cycle arrest properties are inactivated by phosphorylation on CC Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4. CC {ECO:0000269|PubMed:11884610, ECO:0000269|PubMed:12006580}. CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L14812; AAA02489.1; -; mRNA. DR EMBL; AK290380; BAF83069.1; -; mRNA. DR EMBL; AL136172; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL365505; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW76088.1; -; Genomic_DNA. DR EMBL; BC032247; AAH32247.1; -; mRNA. DR EMBL; M74547; AAA36397.1; -; mRNA. DR EMBL; S78664; AAD14290.1; -; Genomic_DNA. DR CCDS; CCDS13289.1; -. [P28749-1] DR CCDS; CCDS13290.1; -. [P28749-2] DR PIR; A47319; A40265. DR RefSeq; NP_002886.2; NM_002895.4. [P28749-1] DR RefSeq; NP_899662.1; NM_183404.3. [P28749-2] DR PDB; 1H28; X-ray; 2.80 A; E/F=653-663. DR PDB; 4YOO; X-ray; 2.40 A; A=391-600, A=781-972. DR PDB; 4YOS; X-ray; 2.30 A; A=391-599. DR PDB; 4YOZ; X-ray; 2.25 A; A=391-593, A=777-972. DR PDB; 5TUV; X-ray; 2.90 A; C/F=994-1031. DR PDB; 7SMC; X-ray; 2.70 A; A/C=391-972. DR PDB; 7SMD; X-ray; 2.15 A; A=391-972. DR PDB; 7SME; X-ray; 2.64 A; A=391-972. DR PDB; 7SMF; X-ray; 3.00 A; A/C=391-972. DR PDBsum; 1H28; -. DR PDBsum; 4YOO; -. DR PDBsum; 4YOS; -. DR PDBsum; 4YOZ; -. DR PDBsum; 5TUV; -. DR PDBsum; 7SMC; -. DR PDBsum; 7SMD; -. DR PDBsum; 7SME; -. DR PDBsum; 7SMF; -. DR AlphaFoldDB; P28749; -. DR SMR; P28749; -. DR BioGRID; 111868; 102. DR ComplexPortal; CPX-2368; DREAM transcriptional repressor complex, RBL1 variant. DR CORUM; P28749; -. DR DIP; DIP-148N; -. DR ELM; P28749; -. DR IntAct; P28749; 57. DR MINT; P28749; -. DR STRING; 9606.ENSP00000362768; -. DR GlyGen; P28749; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P28749; -. DR PhosphoSitePlus; P28749; -. DR BioMuta; RBL1; -. DR DMDM; 90103515; -. DR EPD; P28749; -. DR jPOST; P28749; -. DR MassIVE; P28749; -. DR MaxQB; P28749; -. DR PaxDb; 9606-ENSP00000362768; -. DR PeptideAtlas; P28749; -. DR ProteomicsDB; 54497; -. [P28749-1] DR ProteomicsDB; 54498; -. [P28749-2] DR Pumba; P28749; -. DR Antibodypedia; 11876; 525 antibodies from 35 providers. DR CPTC; P28749; 1 antibody. DR DNASU; 5933; -. DR Ensembl; ENST00000344359.7; ENSP00000343646.3; ENSG00000080839.12. [P28749-2] DR Ensembl; ENST00000373664.8; ENSP00000362768.3; ENSG00000080839.12. [P28749-1] DR GeneID; 5933; -. DR KEGG; hsa:5933; -. DR MANE-Select; ENST00000373664.8; ENSP00000362768.3; NM_002895.5; NP_002886.2. DR UCSC; uc002xgi.5; human. [P28749-1] DR AGR; HGNC:9893; -. DR CTD; 5933; -. DR DisGeNET; 5933; -. DR GeneCards; RBL1; -. DR HGNC; HGNC:9893; RBL1. DR HPA; ENSG00000080839; Tissue enhanced (bone). DR MIM; 116957; gene. DR neXtProt; NX_P28749; -. DR OpenTargets; ENSG00000080839; -. DR PharmGKB; PA34257; -. DR VEuPathDB; HostDB:ENSG00000080839; -. DR eggNOG; KOG1010; Eukaryota. DR GeneTree; ENSGT00950000183202; -. DR HOGENOM; CLU_008943_0_1_1; -. DR InParanoid; P28749; -. DR OMA; AILCELH; -. DR OrthoDB; 519973at2759; -. DR PhylomeDB; P28749; -. DR TreeFam; TF105568; -. DR PathwayCommons; P28749; -. DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex. DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1. DR Reactome; R-HSA-1538133; G0 and Early G1. DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription. DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest. DR Reactome; R-HSA-69205; G1/S-Specific Transcription. DR Reactome; R-HSA-69231; Cyclin D associated events in G1. DR SignaLink; P28749; -. DR SIGNOR; P28749; -. DR BioGRID-ORCS; 5933; 27 hits in 1165 CRISPR screens. DR ChiTaRS; RBL1; human. DR EvolutionaryTrace; P28749; -. DR GeneWiki; Retinoblastoma-like_protein_1; -. DR GenomeRNAi; 5933; -. DR Pharos; P28749; Tbio. DR PRO; PR:P28749; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P28749; Protein. DR Bgee; ENSG00000080839; Expressed in buccal mucosa cell and 155 other cell types or tissues. DR ExpressionAtlas; P28749; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:BHF-UCL. 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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB. DR CDD; cd20605; CYCLIN_RBL1; 1. DR Gene3D; 1.10.472.140; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 3. DR IDEAL; IID00130; -. 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; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 1. DR PANTHER; PTHR13742:SF20; RETINOBLASTOMA-LIKE PROTEIN 1; 1. DR Pfam; PF11934; DUF3452; 1. DR Pfam; PF01858; RB_A; 1. DR Pfam; PF01857; RB_B; 1. DR Pfam; PF08934; Rb_C; 1. DR SMART; SM00385; CYCLIN; 1. DR SMART; SM01367; DUF3452; 1. DR SMART; SM01368; RB_A; 1. DR SMART; SM01369; Rb_C; 1. DR SUPFAM; SSF47954; Cyclin-like; 2. DR Genevisible; P28749; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Chromatin regulator; KW Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Transcription; Transcription regulation; KW Tumor suppressor. FT CHAIN 1..1068 FT /note="Retinoblastoma-like protein 1" FT /id="PRO_0000167839" FT REGION 385..949 FT /note="Pocket; binds T and E1A" FT /evidence="ECO:0000305|PubMed:7935440" FT REGION 385..584 FT /note="Domain A" FT /evidence="ECO:0000305" FT REGION 585..780 FT /note="Spacer" FT /evidence="ECO:0000305" FT REGION 781..949 FT /note="Domain B" FT /evidence="ECO:0000305" FT MOD_RES 332 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000269|PubMed:11884610, FT ECO:0007744|PubMed:23186163" FT MOD_RES 369 FT /note="Phosphothreonine; by CDK4" FT /evidence="ECO:0000269|PubMed:11884610, FT ECO:0000269|PubMed:12006580, ECO:0007744|PubMed:23186163" FT MOD_RES 385 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000269|PubMed:11884610, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 640 FT /note="Phosphoserine; by CDK2 and CDK4" FT /evidence="ECO:0000269|PubMed:11884610, FT ECO:0007744|PubMed:23186163" FT MOD_RES 650 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12006580" FT MOD_RES 749 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 762 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:11884610, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 964 FT /note="Phosphoserine; by CDK2 and CDK4" FT /evidence="ECO:0000269|PubMed:11884610" FT MOD_RES 975 FT /note="Phosphoserine; by CDK2 and CDK4" FT /evidence="ECO:0000269|PubMed:11884610" FT MOD_RES 988 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:11884610, FT ECO:0007744|PubMed:23186163" FT MOD_RES 997 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000269|PubMed:11884610" FT MOD_RES 1009 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:11884610" FT MOD_RES 1041 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1013..1068 FT /note="SLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSE FT RANH -> VR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017496" FT VARIANT 1035 FT /note="I -> M (in dbSNP:rs8114297)" FT /id="VAR_034443" FT MUTAGEN 640 FT /note="S->A: Strongly reduces phosphorylation by CDK2 and FT CDK4." FT /evidence="ECO:0000269|PubMed:11884610" FT MUTAGEN 643 FT /note="S->R: No effect on S-640 phosphorylation, but FT strongly increases S-640 phosphorylation; when associated FT with 657-A--A-660." FT /evidence="ECO:0000269|PubMed:11884610" FT MUTAGEN 650 FT /note="S->A: No effect on phosphorylation by CDK2." FT /evidence="ECO:0000269|PubMed:11884610" FT MUTAGEN 657..660 FT /note="KRRL->AAAA: Reduces S-640 phosphorylation by CDK2 FT and CDK4." FT /evidence="ECO:0000269|PubMed:11884610" FT CONFLICT 326 FT /note="Missing (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 928 FT /note="G -> S (in Ref. 1 and 6)" FT /evidence="ECO:0000305" FT HELIX 392..401 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 410..418 FT /evidence="ECO:0007829|PDB:7SMD" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 424..442 FT /evidence="ECO:0007829|PDB:7SMD" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 454..478 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 480..483 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 489..492 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 495..512 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 521..525 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 530..533 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 536..543 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 549..564 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 566..568 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 574..580 FT /evidence="ECO:0007829|PDB:7SMD" FT TURN 581..583 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 588..592 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 787..809 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 814..830 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 832..835 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 840..855 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 861..868 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 877..880 FT /evidence="ECO:0007829|PDB:7SMD" FT STRAND 881..885 FT /evidence="ECO:0007829|PDB:7SMD" FT STRAND 926..928 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 930..936 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 938..946 FT /evidence="ECO:0007829|PDB:7SMD" FT HELIX 947..949 FT /evidence="ECO:0007829|PDB:7SMD" FT STRAND 1001..1005 FT /evidence="ECO:0007829|PDB:5TUV" FT TURN 1006..1008 FT /evidence="ECO:0007829|PDB:5TUV" FT HELIX 1011..1023 FT /evidence="ECO:0007829|PDB:5TUV" SQ SEQUENCE 1068 AA; 120847 MW; 2BC4876EA04BDB31 CRC64; MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVTHWLA CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE RIERLERNFE VSTVIFKKYE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT ASEEPPCIIA VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN VEYNLQQHFE KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI VAGLKNAPSD QLINIFESCV RNPVENIMKI LKGIGETFCQ HYTQSTDEQP GSHIDFAVNR LKLAEILYYK ILETVMVQET RRLHGMDMSV LLEQDIFHRS LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV IRSEEGLSRD MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS PTAGSAKRRL FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ TLLTMATAPV TGTTGHKVTI PLHGVANDAG EITLIPLSMN TNQESKVKSP VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN RPKRTGSLAL FYRKVYHLAS VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL DQLLLCAFYI MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD LANQDHMMDA PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS ALLYKFNGSP SKSLKDINNM IRQGEQRTKK RVIAIDSDAE SPAKRVCQEN DDVLLKRLQD VVSERANH //