RBL1_MOUSE
ID RBL1_MOUSE Reviewed; 1063 AA.
AC Q64701; Q3U1D4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 184.
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 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].
RC STRAIN=BALB/cJ;
RX PubMed=8661722; DOI=10.1007/s003359900102;
RA Huppi K., Siwarski D., Mock B.A., Dosik J., Hamel P.A.;
RT "Molecular cloning, chromosomal mapping, and expression of the mouse p107
RT gene.";
RL Mamm. Genome 7:353-355(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=7490090; DOI=10.1006/geno.1995.1184;
RA Kim K.K., Soonpaa M.H., Wang H., Field L.J.;
RT "Developmental expression of p107 mRNA and evidence for alternative
RT splicing of the p107 (RBL1) gene product.";
RL Genomics 28:520-529(1995).
RN [3]
RP SEQUENCE REVISION.
RA Kim K.K., Soonpaa M.H., Wang H., Field L.J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-332; SER-959 AND SER-1036,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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 (By similarity).
CC Directly involved in heterochromatin formation by maintaining overall
CC chromatin structure and, in particular, that of constitutive
CC heterochromatin by stabilizing histone methylation (PubMed:15750587).
CC Recruits and targets histone methyltransferases KMT5B and KMT5C,
CC leading to epigenetic transcriptional repression (PubMed:15750587).
CC Controls histone H4 'Lys-20' trimethylation (PubMed:15750587). Probably
CC acts as a transcription repressor by recruiting chromatin-modifying
CC enzymes to promoters (PubMed:15750587). Potent inhibitor of E2F-
CC mediated trans-activation (By similarity). May act as a tumor
CC suppressor (By similarity). {ECO:0000250|UniProtKB:P28749,
CC ECO:0000269|PubMed:15750587}.
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 (By similarity). The complex exists
CC in quiescent cells where it represses cell cycle-dependent genes (By
CC similarity). It dissociates in S phase when LIN9, LIN37, LIN52 and
CC LIN54 form a subcomplex that binds to MYBL2 (By similarity). Interacts
CC with AATF (By similarity). Interacts with KDM5A (By similarity).
CC Interacts with KMT5B and KMT5C (PubMed:11571651). Interacts with USP4
CC (PubMed:15750587). Interacts with RBBP9 (By similarity).
CC {ECO:0000250|UniProtKB:D3ZS28, ECO:0000250|UniProtKB:P28749,
CC ECO:0000269|PubMed:11571651, ECO:0000269|PubMed:15750587}.
CC -!- INTERACTION:
CC Q64701; Q155P7: Cenpf; NbExp=3; IntAct=EBI-1213109, EBI-2211248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q64701-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q64701-2; Sequence=VSP_005537, VSP_005538;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal heart and liver.
CC Expressed at low levels in all other fetal tissues except skeletal
CC muscle. High levels in neonatal spleen and thymus with low levels in
CC other tissues. In adult, highly expressed in testis. Barely detectable
CC in other tissues.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in fetal tissues. Expression
CC markedly decreased in adult.
CC -!- PTM: Cell-cycle arrest properties are inactivated by phosphorylation on
CC Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4.
CC {ECO:0000250|UniProtKB:P28749}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
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DR EMBL; U33320; AAB18279.1; -; mRNA.
DR EMBL; U27177; AAB53235.1; -; mRNA.
DR EMBL; U27178; AAB53236.1; -; mRNA.
DR EMBL; AK156055; BAE33564.1; -; mRNA.
DR EMBL; AL669828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16974.1; -. [Q64701-1]
DR PIR; I49328; I49328.
DR RefSeq; NP_001132988.1; NM_001139516.1. [Q64701-2]
DR RefSeq; NP_035379.2; NM_011249.2. [Q64701-1]
DR AlphaFoldDB; Q64701; -.
DR SMR; Q64701; -.
DR BioGRID; 202819; 28.
DR CORUM; Q64701; -.
DR IntAct; Q64701; 4.
DR STRING; 10090.ENSMUSP00000029170; -.
DR iPTMnet; Q64701; -.
DR PhosphoSitePlus; Q64701; -.
DR EPD; Q64701; -.
DR jPOST; Q64701; -.
DR MaxQB; Q64701; -.
DR PaxDb; Q64701; -.
DR PeptideAtlas; Q64701; -.
DR PRIDE; Q64701; -.
DR ProteomicsDB; 300314; -. [Q64701-1]
DR ProteomicsDB; 300315; -. [Q64701-2]
DR Antibodypedia; 11876; 439 antibodies from 35 providers.
DR DNASU; 19650; -.
DR Ensembl; ENSMUST00000029170; ENSMUSP00000029170; ENSMUSG00000027641. [Q64701-1]
DR GeneID; 19650; -.
DR KEGG; mmu:19650; -.
DR UCSC; uc008noq.2; mouse. [Q64701-1]
DR UCSC; uc008nos.2; mouse. [Q64701-2]
DR CTD; 5933; -.
DR MGI; MGI:103300; Rbl1.
DR VEuPathDB; HostDB:ENSMUSG00000027641; -.
DR eggNOG; KOG1010; Eukaryota.
DR GeneTree; ENSGT00950000183202; -.
DR HOGENOM; CLU_008943_0_1_1; -.
DR InParanoid; Q64701; -.
DR OMA; AILCELH; -.
DR PhylomeDB; Q64701; -.
DR TreeFam; TF105568; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR BioGRID-ORCS; 19650; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Rbl1; mouse.
DR PRO; PR:Q64701; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64701; protein.
DR Bgee; ENSMUSG00000027641; Expressed in paneth cell and 199 other tissues.
DR Genevisible; Q64701; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
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:2000773; P:negative regulation of cellular senescence; ISO:MGI.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA: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 CDD; cd00043; CYCLIN; 1.
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 Alternative splicing; Cell cycle; Chromatin regulator; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..1063
FT /note="Retinoblastoma-like protein 1"
FT /id="PRO_0000167840"
FT REGION 383..944
FT /note="Pocket; binds T and E1A"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT REGION 383..584
FT /note="Domain A"
FT /evidence="ECO:0000305"
FT REGION 585..779
FT /note="Spacer"
FT /evidence="ECO:0000305"
FT REGION 780..944
FT /note="Domain B"
FT /evidence="ECO:0000305"
FT MOD_RES 332
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 992
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 592..594
FT /note="IFP -> SQG (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7490090"
FT /id="VSP_005537"
FT VAR_SEQ 595..1063
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7490090"
FT /id="VSP_005538"
FT CONFLICT 26
FT /note="Q -> P (in Ref. 1; AAB18279)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="I -> T (in Ref. 1; AAB18279)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="I -> R (in Ref. 2; AAB53235)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="A -> C (in Ref. 1; AAB18279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1063 AA; 119456 MW; 85BEA8EC064EC06E CRC64;
MFEDEPHAEG AAAVAAAREA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVIHWLA
CSLYVACRKS IIPTVGKGVM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE
RIERLERNFE VSTVIFKKFE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL
FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRR DLLNPSFKGL PSDFHAPDFK
AAEEPPCIIA VLCDLHDGLL VEAKGIKEHY FKPYISKLFD KKILKGECLL DLSSFTDNSK
AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTADT PFGKLTSQAS VECNLQQHFE
KKRSFAPSTP LTGRRYLQEK EAVTTPVASA TQSVSRLQSI VAGLKSAPSE QLLNIFESCM
RNPMGNIIKI VKGIGETFCQ HYTQSTDKQP GSHIDFAVNR LKLAEILYYK ILETIMVQET
RRLHGMDMSV LLEQDIFHKS LMACCLEIVL FAYSSPRTFP WIIEVLDLQP FYFYKVIEVV
IRSEEGLSRD MVKHLNSIEE QILESLAWTN NSALWEALHA SANRVPSCEE VIFPNNFEIG
NGGNVQGHLP MMPMSPIIHP RVKEVRTDSG SLRQDMQPLS PISVHERYSS PAAGSAKRRL
FGDDPPKDTL MDKIMAEGTK LKIAPSSVTA ESLSISPGQA LLTMATTTVT GTTGRKVTVP
LHGIANDAGE ITLVPISMNP TQESTAESPV SLTAQSLIGT SPKQTHLTKA QDAHLTGVSK
PKRTGSLALF YRKVYHLASV RLRDLCLKLD VSNELRRKIW TCFEFTLVHC PDLMKDRHLD
QLLLCAFYIM AKVTKEERTF QEIMKSYRNQ PQANSHVYRS VLLKSIPGGV VVYNGDCEMT
DGDIEDATKT PNCSSEPVKE ERGDLIKFYN TVYVGRVKSF ALKYDLSNQD HIMDAPPLSP
FPHIKQQPGS PRRISQQHSL YVSPHKNGAG LTPRSALLYK FNGSPSKSLK DINNMIRQGE
QKTKKRVIAI SGDADSPAKR LCQENDDVLL KRLQDVVSER ANH
