RBL1_HUMAN
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 03-AUG-2022, entry version 219.
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 PDBsum; 1H28; -.
DR PDBsum; 4YOO; -.
DR PDBsum; 4YOS; -.
DR PDBsum; 4YOZ; -.
DR PDBsum; 5TUV; -.
DR AlphaFoldDB; P28749; -.
DR SMR; P28749; -.
DR BioGRID; 111868; 93.
DR CORUM; P28749; -.
DR DIP; DIP-148N; -.
DR ELM; P28749; -.
DR IntAct; P28749; 56.
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; P28749; -.
DR PeptideAtlas; P28749; -.
DR PRIDE; P28749; -.
DR ProteomicsDB; 54497; -. [P28749-1]
DR ProteomicsDB; 54498; -. [P28749-2]
DR Antibodypedia; 11876; 439 antibodies from 35 providers.
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 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; 113612at2759; -.
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; 22 hits in 1085 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 154 other tissues.
DR ExpressionAtlas; P28749; baseline and differential.
DR Genevisible; P28749; HS.
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:0051302; P:regulation of cell division; IEA:InterPro.
DR GO; GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB.
DR CDD; cd00043; CYCLIN; 1.
DR IDEAL; IID00130; -.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR015030; RB_C.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR InterPro; IPR028310; RBL1.
DR PANTHER; PTHR13742; PTHR13742; 1.
DR PANTHER; PTHR13742:SF20; PTHR13742:SF20; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR Pfam; PF08934; Rb_C; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 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..400
FT /evidence="ECO:0007829|PDB:4YOZ"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 410..417
FT /evidence="ECO:0007829|PDB:4YOZ"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 424..442
FT /evidence="ECO:0007829|PDB:4YOZ"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 454..477
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 495..512
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 535..543
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 549..564
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 573..580
FT /evidence="ECO:0007829|PDB:4YOZ"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 785..809
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 814..830
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 840..854
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 861..868
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 877..880
FT /evidence="ECO:0007829|PDB:4YOZ"
FT STRAND 881..883
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 930..936
FT /evidence="ECO:0007829|PDB:4YOZ"
FT HELIX 938..946
FT /evidence="ECO:0007829|PDB:4YOZ"
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
