RBL2_MOUSE
ID RBL2_MOUSE Reviewed; 1135 AA.
AC Q64700; Q3TVP8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 177.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8621630; DOI=10.1074/jbc.271.16.9567;
RA Chen G., Guy C.T., Chen H.W., Hu N., Lee E.Y.H.P., Lee W.H.;
RT "Molecular cloning and developmental expression of mouse p130, a member of
RT the retinoblastoma gene family.";
RL J. Biol. Chem. 271:9567-9572(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9019172;
RA Pertile P., Baldi A., de Luca A., Virgilio L., Pisano M.M., Giordano A.;
RT "Molecular cloning, expression, and developmental characterization of the
RT murine retinoblastoma-related gene Rb2/p130.";
RL Cell Growth Differ. 6:1659-1664(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8622859;
RA Lecouter J.E., Whyte P.F.M., Rudnicki M.A.;
RT "Cloning and expression of the Rb-related mouse p130 mRNA.";
RL Oncogene 12:1433-1440(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH USP4.
RX PubMed=11571651; DOI=10.1038/sj.onc.1204823;
RA Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.;
RT "Association of UNP, a ubiquitin-specific protease, with the pocket
RT proteins pRb, p107 and p130.";
RL Oncogene 20:5533-5537(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH KMT5B AND KMT5C.
RX PubMed=15750587; DOI=10.1038/ncb1235;
RA Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
RA Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.;
RT "Role of the RB1 family in stabilizing histone methylation at constitutive
RT heterochromatin.";
RL Nat. Cell Biol. 7:420-428(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; THR-639 AND SER-942, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; THR-414; SER-636;
RP THR-639; SER-942; SER-965; SER-976 AND THR-980, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:15750587}.
CC -!- SUBUNIT: Interacts with AATF and RINT1. Component of the DREAM complex
CC (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37,
CC LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The
CC complex exists in quiescent cells where it represses cell cycle-
CC dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and
CC LIN54 form a subcomplex that binds to MYBL2. Interacts with USP4 (By
CC similarity). Interacts with KMT5B, KMT5C and USP4. Interacts with PML
CC (By similarity). Interacts with RBBP9 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O55081}.
CC -!- INTERACTION:
CC Q64700; Q155P7: Cenpf; NbExp=3; IntAct=EBI-2271232, EBI-2211248;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: During G0 and early G1 phase of the cell cycle, phosphorylated on
CC Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669
CC in G1 leads to its ubiquitin-dependent proteolysis (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
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DR EMBL; U36799; AAB48991.1; -; mRNA.
DR EMBL; U50850; AAC52598.1; -; mRNA.
DR EMBL; U47333; AAC52555.1; -; mRNA.
DR EMBL; AK160027; BAE35570.1; -; mRNA.
DR CCDS; CCDS22518.1; -.
DR RefSeq; NP_001268929.1; NM_001282000.1.
DR RefSeq; NP_001268930.1; NM_001282001.1.
DR RefSeq; NP_035380.3; NM_011250.4.
DR AlphaFoldDB; Q64700; -.
DR SMR; Q64700; -.
DR BioGRID; 202820; 19.
DR CORUM; Q64700; -.
DR IntAct; Q64700; 5.
DR MINT; Q64700; -.
DR STRING; 10090.ENSMUSP00000034091; -.
DR iPTMnet; Q64700; -.
DR PhosphoSitePlus; Q64700; -.
DR EPD; Q64700; -.
DR jPOST; Q64700; -.
DR MaxQB; Q64700; -.
DR PaxDb; Q64700; -.
DR PeptideAtlas; Q64700; -.
DR PRIDE; Q64700; -.
DR ProteomicsDB; 254996; -.
DR Antibodypedia; 4299; 474 antibodies from 39 providers.
DR DNASU; 19651; -.
DR Ensembl; ENSMUST00000034091; ENSMUSP00000034091; ENSMUSG00000031666.
DR GeneID; 19651; -.
DR KEGG; mmu:19651; -.
DR UCSC; uc012gid.2; mouse.
DR CTD; 5934; -.
DR MGI; MGI:105085; Rbl2.
DR VEuPathDB; HostDB:ENSMUSG00000031666; -.
DR eggNOG; KOG1010; Eukaryota.
DR GeneTree; ENSGT00950000183202; -.
DR HOGENOM; CLU_008943_0_0_1; -.
DR InParanoid; Q64700; -.
DR OMA; VYCQSTQ; -.
DR OrthoDB; 113612at2759; -.
DR PhylomeDB; Q64700; -.
DR TreeFam; TF105568; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR BioGRID-ORCS; 19651; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rbl2; mouse.
DR PRO; PR:Q64700; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q64700; protein.
DR Bgee; ENSMUSG00000031666; Expressed in parotid gland and 243 other tissues.
DR ExpressionAtlas; Q64700; baseline and differential.
DR Genevisible; Q64700; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO: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; ISO:MGI.
DR GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
DR GO; GO:0043550; P:regulation of lipid kinase activity; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
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; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor.
FT CHAIN 1..1135
FT /note="Retinoblastoma-like protein 2"
FT /id="PRO_0000167842"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..1021
FT /note="Pocket; binds E1A"
FT REGION 414..613
FT /note="Domain A"
FT REGION 614..824
FT /note="Spacer"
FT REGION 661..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..1021
FT /note="Domain B"
FT REGION 930..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 639
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 968
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 980
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT CONFLICT 209..251
FT /note="Missing (in Ref. 3; AAC52555)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="A -> P (in Ref. 1; AAB48991)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="A -> P (in Ref. 3; AAC52555)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="R -> T (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="T -> S (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> T (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="R -> Q (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
FT CONFLICT 483..492
FT /note="Missing (in Ref. 1; AAB48991)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="A -> R (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="P -> A (in Ref. 3; AAC52555)"
FT /evidence="ECO:0000305"
FT CONFLICT 947..948
FT /note="PT -> RA (in Ref. 3; AAC52555)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="A -> S (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="V -> I (in Ref. 2; AAC52598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 127485 MW; F509E68A156929B2 CRC64;
MASGGNQSPP PPPAAAASSE EEEEDGDAAD RAQPAGSPSH QIQQRFEELC SRLNMDEAAR
AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS KGTAEGNYVS LTRILRCSEQ
SLIEFFNKMK KWEDMANLPP HFRERTERLE RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR
QQRGRKQRRQ PCTTSEIFHF CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC
SNRKELVNPN FKGLSEDCHP KDSKASSDPP CVIEKLCSLH DGLVLEAKGI KEHFWKPYIR
KLFEKKLLKG KEENLTGFLE PGNFGESFKA VNKAYEEYVL AAGNLDERVF LGEDAEEEVG
TLSRCLSAAS GTESAERTQM RDILQQHLDK SKALRVCTPL TGVRYVQENS PCVTPVSTAA
HSLSRLHTML SGLRNAPSEK LERILRSCSR DPTQAIADRL KEMYEIYSQH FQPDENFSNC
AKEIANKHFR FAEMLYYKVL ESVIEQEQKR LGDMDLSGVL EHDAFHRSLL ACCLEVVAFS
HKPPGNFPFI AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS
PLWDRIRDNE NRVPTCEEVM PPQNLERTDE IYIAGSPLTP RRVGEVRADA GGLGRSITSP
TTLYDRYSSP TVSTTRRRLF ENDSPSEGST SGRIPPQPLV NAVPVQNVPG ETVSVTPVPG
QTLVTMATAT VTANNGQTVT IPVQGIANEN GGITFFPVQV NVGGQAQAVA GSIQPLSAQA
LAGSLSSQQV TGTTLQVPGP VAIQQISPGG QQQNPGQPLT SSSIRPRKTS SLALFFRKVY
YLAGVRLRDL CIKLDISDEL RKKIWTCFEF SIIQCTELMM DRHLDQLLMC AIYVMAKVTK
EDRSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSSES RSHQNSPTEL NTDRASRDSS
PVMRSNSTLP VPQPSSAPPT PTRLTGASSD VEEEERGDLI QFYNNIYRKQ IQAFAMKYSQ
ANAQTDTPPL SPYPFVRTGS PRRVQLSQSH PIYISPHNNE AMPSPREKIF YYFSNSPSKR
LREINSMIRT GETPTKKRGI LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ
