RBL2_HUMAN
ID RBL2_HUMAN Reviewed; 1139 AA.
AC Q08999; B7Z913; Q15073; Q16084; Q8NE70; Q92812;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Retinoblastoma-like protein 2;
DE AltName: Full=130 kDa retinoblastoma-associated protein;
DE Short=p130;
DE AltName: Full=Retinoblastoma-related protein 2;
DE Short=RBR-2;
DE AltName: Full=pRb2;
GN Name=RBL2; Synonyms=RB2;
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).
RC TISSUE=Placenta, and Spleen;
RX PubMed=8253383; DOI=10.1101/gad.7.12a.2366;
RA Li Y., Graham C., Lacy S., Duncan A.M.V., Whyte P.;
RT "The adenovirus E1A-associated 130-kD protein is encoded by a member of the
RT retinoblastoma gene family and physically interacts with cyclins A and E.";
RL Genes Dev. 7:2366-2377(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8253384; DOI=10.1101/gad.7.12a.2378;
RA Hannon G.J., Demetrick D., Beach D.;
RT "Isolation of the Rb-related p130 through its interaction with CDK2 and
RT cyclins.";
RL Genes Dev. 7:2378-2391(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 58-1139 (ISOFORM 1).
RX PubMed=8361765;
RA Mayol X., Grana X., Baldi A., Sang N., Hu Q., Giordano A.;
RT "Cloning of a new member of the retinoblastoma gene family (pRb2) which
RT binds to the E1A transforming domain.";
RL Oncogene 8:2561-2566(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC TISSUE=Placenta;
RX PubMed=8643454; DOI=10.1073/pnas.93.10.4629;
RA Baldi A., Boccia V., Claudio P.P., de Luca A., Giordano A.;
RT "Genomic structure of the human retinoblastoma-related Rb2/p130 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4629-4632(1996).
RN [8]
RP PHOSPHORYLATION AT SER-639; SER-952; SER-966; SER-971; SER-972; SER-973;
RP THR-974; SER-981; SER-982 AND THR-986, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11042701; DOI=10.1038/sj.onc.1203893;
RA Canhoto A.J., Chestukhin A., Litovchick L., DeCaprio J.A.;
RT "Phosphorylation of the retinoblastoma-related protein p130 in growth-
RT arrested cells.";
RL Oncogene 19:5116-5122(2000).
RN [9]
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 [10]
RP PHOSPHORYLATION AT SER-672.
RX PubMed=12435635; DOI=10.1101/gad.1011202;
RA Tedesco D., Lukas J., Reed S.I.;
RT "The pRb-related protein p130 is regulated by phosphorylation-dependent
RT proteolysis via the protein-ubiquitin ligase SCF(Skp2).";
RL Genes Dev. 16:2946-2957(2002).
RN [11]
RP INTERACTION WITH RINT1.
RX PubMed=16600870; DOI=10.1016/j.molcel.2006.02.016;
RA Kong L.-J., Meloni A.R., Nevins J.R.;
RT "The Rb-related p130 protein controls telomere lengthening through an
RT interaction with a Rad50-interacting protein, RINT-1.";
RL Mol. Cell 22:63-71(2006).
RN [12]
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-672 AND SER-1035,
RP AND 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 INTERACTION WITH PML.
RX PubMed=22002537; DOI=10.1038/emboj.2011.370;
RA Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
RA Dejean A., Bischof O.;
RT "Physical and functional interaction between PML and TBX2 in the
RT establishment of cellular senescence.";
RL EMBO J. 31:95-109(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-662; SER-688;
RP SER-1068; SER-1080 AND SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP VARIANT PHE-99.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Key regulator of entry into cell division. Directly involved
CC in heterochromatin formation by maintaining overall chromatin structure
CC and, in particular, that of constitutive heterochromatin by stabilizing
CC histone methylation. Recruits and targets histone methyltransferases
CC KMT5B and KMT5C, leading to epigenetic transcriptional repression.
CC Controls histone H4 'Lys-20' trimethylation. Probably acts as a
CC transcription repressor by recruiting chromatin-modifying enzymes to
CC promoters. Potent inhibitor of E2F-mediated trans-activation,
CC associates preferentially with E2F5. Binds to cyclins A and E. Binds to
CC and may be involved in the transforming capacity of the adenovirus E1A
CC protein. May act as a tumor suppressor.
CC -!- SUBUNIT: Interacts with AATF. Interacts with KMT5B, KMT5C and USP4 (By
CC similarity). Component of the DREAM complex (also named LINC complex)
CC at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1,
CC MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in
CC quiescent cells where it represses cell cycle-dependent genes. It
CC dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a
CC subcomplex that binds to MYBL2. Interacts with RINT1. Interacts with
CC PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and
CC isoform PML-5). Interacts with RBBP9 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O55081, ECO:0000269|PubMed:12450794,
CC ECO:0000269|PubMed:16600870, ECO:0000269|PubMed:17671431,
CC ECO:0000269|PubMed:22002537}.
CC -!- SUBUNIT: (Microbial infection) Interacts with JC virus small t antigen.
CC {ECO:0000269|PubMed:20485545}.
CC -!- INTERACTION:
CC Q08999; Q13574-2: DGKZ; NbExp=2; IntAct=EBI-971439, EBI-715527;
CC Q08999; Q16254: E2F4; NbExp=7; IntAct=EBI-971439, EBI-448943;
CC Q08999; Q6MZP7: LIN54; NbExp=10; IntAct=EBI-971439, EBI-1389411;
CC Q08999; P67775: PPP2CA; NbExp=2; IntAct=EBI-971439, EBI-712311;
CC Q08999; I6L8A6: RBBP8; NbExp=3; IntAct=EBI-971439, EBI-11525639;
CC Q08999; Q99708-2: RBBP8; NbExp=3; IntAct=EBI-971439, EBI-10203615;
CC Q08999; P24610: Pax3; Xeno; NbExp=3; IntAct=EBI-971439, EBI-1208116;
CC Q08999; Q923E4: Sirt1; Xeno; NbExp=2; IntAct=EBI-971439, EBI-1802585;
CC Q08999; Q61412: Vsx2; Xeno; NbExp=4; IntAct=EBI-971439, EBI-1208174;
CC Q08999; P03255; Xeno; NbExp=2; IntAct=EBI-971439, EBI-2603114;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08999-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08999-2; Sequence=VSP_054328, VSP_054329;
CC -!- DEVELOPMENTAL STAGE: G0-restricted expression.
CC -!- PTM: During G0 and early G1 phase of the cell cycle, phosphorylated on
CC Ser-639 and on 5 sites within the domain B. Phosphorylation on Ser-672
CC in G1 leads to its ubiquitin-dependent proteolysis.
CC {ECO:0000269|PubMed:11042701, ECO:0000269|PubMed:12435635}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBL2ID443.html";
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DR EMBL; X76061; CAA53661.1; -; mRNA.
DR EMBL; S67171; AAB29227.1; -; mRNA.
DR EMBL; AK304283; BAH14149.1; -; mRNA.
DR EMBL; AC007342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034490; AAH34490.1; -; mRNA.
DR EMBL; X74594; CAA52671.1; -; mRNA.
DR EMBL; U53220; AAC50479.1; -; Genomic_DNA.
DR CCDS; CCDS10748.1; -. [Q08999-1]
DR PIR; A49370; A49370.
DR RefSeq; NP_001310537.1; NM_001323608.1. [Q08999-1]
DR RefSeq; NP_005602.3; NM_005611.3. [Q08999-1]
DR PDB; 4XI9; X-ray; 3.10 A; E/F/G/H=416-422.
DR PDB; 5C1D; X-ray; 2.05 A; C=416-422.
DR PDBsum; 4XI9; -.
DR PDBsum; 5C1D; -.
DR AlphaFoldDB; Q08999; -.
DR SMR; Q08999; -.
DR BioGRID; 111869; 75.
DR CORUM; Q08999; -.
DR DIP; DIP-425N; -.
DR ELM; Q08999; -.
DR IntAct; Q08999; 48.
DR MINT; Q08999; -.
DR STRING; 9606.ENSP00000262133; -.
DR GlyGen; Q08999; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08999; -.
DR PhosphoSitePlus; Q08999; -.
DR BioMuta; RBL2; -.
DR DMDM; 116242746; -.
DR EPD; Q08999; -.
DR jPOST; Q08999; -.
DR MassIVE; Q08999; -.
DR MaxQB; Q08999; -.
DR PaxDb; Q08999; -.
DR PeptideAtlas; Q08999; -.
DR PRIDE; Q08999; -.
DR ProteomicsDB; 58652; -. [Q08999-1]
DR ProteomicsDB; 6997; -.
DR Antibodypedia; 4299; 474 antibodies from 39 providers.
DR DNASU; 5934; -.
DR Ensembl; ENST00000262133.11; ENSP00000262133.6; ENSG00000103479.17. [Q08999-1]
DR GeneID; 5934; -.
DR KEGG; hsa:5934; -.
DR MANE-Select; ENST00000262133.11; ENSP00000262133.6; NM_005611.4; NP_005602.3.
DR UCSC; uc002ehi.5; human. [Q08999-1]
DR CTD; 5934; -.
DR DisGeNET; 5934; -.
DR GeneCards; RBL2; -.
DR HGNC; HGNC:9894; RBL2.
DR HPA; ENSG00000103479; Low tissue specificity.
DR MIM; 180203; gene.
DR neXtProt; NX_Q08999; -.
DR OpenTargets; ENSG00000103479; -.
DR PharmGKB; PA34258; -.
DR VEuPathDB; HostDB:ENSG00000103479; -.
DR eggNOG; KOG1010; Eukaryota.
DR GeneTree; ENSGT00950000183202; -.
DR HOGENOM; CLU_008943_0_0_1; -.
DR InParanoid; Q08999; -.
DR OMA; VYCQSTQ; -.
DR OrthoDB; 113612at2759; -.
DR PhylomeDB; Q08999; -.
DR TreeFam; TF105568; -.
DR PathwayCommons; Q08999; -.
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-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-HSA-9617828; FOXO-mediated transcription of cell cycle genes.
DR SignaLink; Q08999; -.
DR SIGNOR; Q08999; -.
DR BioGRID-ORCS; 5934; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; RBL2; human.
DR GeneWiki; Retinoblastoma-like_protein_2; -.
DR GenomeRNAi; 5934; -.
DR Pharos; Q08999; Tbio.
DR PRO; PR:Q08999; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q08999; protein.
DR Bgee; ENSG00000103479; Expressed in germinal epithelium of ovary and 203 other tissues.
DR ExpressionAtlas; Q08999; baseline and differential.
DR Genevisible; Q08999; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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: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:0051302; P:regulation of cell division; IEA:InterPro.
DR GO; GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
DR IDEAL; IID00663; -.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR028308; RB2.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR015030; RB_C.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742; PTHR13742; 1.
DR PANTHER; PTHR13742:SF8; PTHR13742:SF8; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; SSF47954; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Chromatin regulator;
KW DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor.
FT CHAIN 1..1139
FT /note="Retinoblastoma-like protein 2"
FT /id="PRO_0000167841"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..1024
FT /note="Pocket; binds E1A"
FT REGION 417..616
FT /note="Domain A"
FT REGION 617..827
FT /note="Spacer"
FT REGION 654..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1024
FT /note="Domain B"
FT REGION 933..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64700"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11042701"
FT MOD_RES 642
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64700"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12435635,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64700"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11042701"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11042701"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11042701"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11042701"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11042701"
FT MOD_RES 974
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:11042701"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11042701"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11042701"
FT MOD_RES 986
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11042701"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054328"
FT VAR_SEQ 638..1042
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054329"
FT VARIANT 99
FT /note="V -> F"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069377"
FT VARIANT 210
FT /note="Y -> C (in dbSNP:rs17800727)"
FT /id="VAR_028437"
FT CONFLICT 37
FT /note="P -> S (in Ref. 1; CAA53661 and 7; AAC50479)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> P (in Ref. 1 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="V -> M (in Ref. 6; CAA52671)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="R -> H (in Ref. 5; AAH34490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1139 AA; 128367 MW; D129032FB1F383D4 CRC64;
MPSGGDQSPP PPPPPPAAAA SDEEEEDDGE AEDAAPPAES PTPQIQQRFD ELCSRLNMDE
AARAEAWDSY RSMSESYTLE GNDLHWLACA LYVACRKSVP TVSKGTVEGN YVSLTRILKC
SEQSLIEFFN KMKKWEDMAN LPPHFRERTE RLERNFTVSA VIFKKYEPIF QDIFKYPQEE
QPRQQRGRKQ RRQPCTVSEI FHFCWVLFIY AKGNFPMISD DLVNSYHLLL CALDLVYGNA
LQCSNRKELV NPNFKGLSED FHAKDSKPSS DPPCIIEKLC SLHDGLVLEA KGIKEHFWKP
YIRKLYEKKL LKGKEENLTG FLEPGNFGES FKAINKAYEE YVLSVGNLDE RIFLGEDAEE
EIGTLSRCLN AGSGTETAER VQMKNILQQH FDKSKALRIS TPLTGVRYIK ENSPCVTPVS
TATHSLSRLH TMLTGLRNAP SEKLEQILRT CSRDPTQAIA NRLKEMFEIY SQHFQPDEDF
SNCAKEIASK HFRFAEMLYY KVLESVIEQE QKRLGDMDLS GILEQDAFHR SLLACCLEVV
TFSYKPPGNF PFITEIFDVP LYHFYKVIEV FIRAEDGLCR EVVKHLNQIE EQILDHLAWK
PESPLWEKIR DNENRVPTCE EVMPPQNLER ADEICIAGSP LTPRRVTEVR ADTGGLGRSI
TSPTTLYDRY SSPPASTTRR RLFVENDSPS DGGTPGRMPP QPLVNAVPVQ NVSGETVSVT
PVPGQTLVTM ATATVTANNG QTVTIPVQGI ANENGGITFF PVQVNVGGQA QAVTGSIQPL
SAQALAGSLS SQQVTGTTLQ VPGQVAIQQI SPGGQQQKQG QSVTSSSNRP RKTSSLSLFF
RKVYHLAAVR LRDLCAKLDI SDELRKKIWT CFEFSIIQCP ELMMDRHLDQ LLMCAIYVMA
KVTKEDKSFQ NIMRCYRTQP QARSQVYRSV LIKGKRKRRN SGSSDSRSHQ NSPTELNKDR
TSRDSSPVMR SSSTLPVPQP SSAPPTPTRL TGANSDMEEE ERGDLIQFYN NIYIKQIKTF
AMKYSQANMD APPLSPYPFV RTGSPRRIQL SQNHPVYISP HKNETMLSPR EKIFYYFSNS
PSKRLREINS MIRTGETPTK KRGILLEDGS ESPAKRICPE NHSALLRRLQ DVANDRGSH
