RBL1_RAT
ID RBL1_RAT Reviewed; 1049 AA.
AC D3ZS28;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 4.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Retinoblastoma-like protein 1 {ECO:0000305};
DE AltName: Full=107 kDa retinoblastoma-associated protein {ECO:0000305};
DE Short=p107 {ECO:0000305};
DE AltName: Full=pRb1 {ECO:0000305};
GN Name=Rbl1 {ECO:0000312|RGD:1595511};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP INTERACTION WITH RBBP9.
RX PubMed=9697699; DOI=10.1038/1258;
RA Woitach J.T., Zhang M., Niu C.-H., Thorgeirsson S.S.;
RT "A retinoblastoma-binding protein that affects cell-cycle control and
RT confers transforming ability.";
RL Nat. Genet. 19:371-374(1998).
RN [3] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Recruits and
CC targets histone methyltransferases KMT5B and KMT5C, leading to
CC epigenetic transcriptional repression. Controls histone H4 'Lys-20'
CC trimethylation. Probably acts as a transcription repressor by
CC recruiting chromatin-modifying enzymes to promoters (By similarity).
CC Potent inhibitor of E2F-mediated trans-activation. May act as a tumor
CC suppressor (By similarity). {ECO:0000250|UniProtKB:P28749,
CC ECO:0000250|UniProtKB:Q64701}.
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. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2. Interacts with AATF. Interacts with KDM5A (By similarity).
CC Interacts with KMT5B and KMT5C. Interacts with USP4 (By similarity).
CC Interacts with RBBP9 (PubMed:9697699). {ECO:0000250|UniProtKB:P28749,
CC ECO:0000250|UniProtKB:Q64701, ECO:0000269|PubMed:9697699}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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; AABR07054428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07054429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001177995.1; NM_001191066.1.
DR AlphaFoldDB; D3ZS28; -.
DR SMR; D3ZS28; -.
DR MINT; D3ZS28; -.
DR STRING; 10116.ENSRNOP00000063017; -.
DR PaxDb; D3ZS28; -.
DR GeneID; 680111; -.
DR KEGG; rno:680111; -.
DR CTD; 5933; -.
DR RGD; 1595511; Rbl1.
DR eggNOG; KOG1010; Eukaryota.
DR HOGENOM; CLU_008943_0_1_1; -.
DR InParanoid; D3ZS28; -.
DR TreeFam; TF105568; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR PRO; PR:D3ZS28; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
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:RGD.
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:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
DR GO; GO:0043550; P:regulation of lipid kinase activity; ISO:RGD.
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 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 Cell cycle; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor.
FT CHAIN 1..1049
FT /note="Retinoblastoma-like protein 1"
FT /id="PRO_0000447676"
FT REGION 385..944
FT /note="Pocket; binds T and E1A"
FT /evidence="ECO:0000250|UniProtKB:P28749"
FT REGION 385..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:0000250|UniProtKB:P28749"
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:0000250|UniProtKB:P28749"
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 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28749"
SQ SEQUENCE 1049 AA; 117818 MW; 68F2C046818BB277 CRC64;
MFEDEPHAEG AAAVAAAREA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVIHWLA
CSLYVACRKS IIPTVGKGVM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE
RIERLERNFE VSTVIFKKFE PIFLDIFQNP YEELPKLPRS RKQRRIPCSV KDLFNFCWTL
FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRR DLLNPSFKGL PSDFHAVNFK
AAEEPPCIIA VLCDLHDGLL VEAKGIKEHY FKPYISKLFD KKILKGECLL DLSSFTDNSK
AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFAADT QFGKLTSQAS VDCNLQQHFE
KKRSFAPSTP LTGRRYLQEK EAVTTPVASA TQSVSRLQSI VAGLKSAPSE QLLTIFESCM
RNPMGNIVKI VKGIGETFCQ HYTQSTDKQP GSHIDFAVNR LKLAEILYYK ILETIMVQET
RRLHGMDMSV LLEQDIFHRS LLACCLEIVL FAYSSPRTFP WIIDVLGLQP FYFYKVIEVV
IRSEEGLSRD MVKHLNSIEE QILESLAWTN NSALWEALRA SANKVPSCEE VIFPNNFEIG
NGGSVQGHLP MMPMSPIIHP RVKEVRTDSG SLRKDMQPLS PISVHERYSS PAAGSAKRRL
FGDDPPKETL MEKIMAEGTQ LKIAPSSVTA ESLSISPGQA LLTMATTTVT GTTGRKVTVP
LHGIANDAGE ITLVPISMNT TQDSTAESLV SLTAQSLIGA SPKQTHLTKT QDAPLTGISK
PKRTGSLALF YRKVYHLASV RLRDLCLKLD VSNELRRKIW TCFEFTLVHC PDLMKDRHLD
QLLLCAFYIM AKVTKEERTF QEIMKSYRNQ PQANSHVYRS VLLKSIPGEV VAYNGDYEMT
DGDIEDATKT PNCSSEPVKE ERGDLIKFYN AIYVGRVKSF ALKYDLSNQD HIMDAPPLSP
FPHIKQQPGS PRRISQQHSI YVSPHKNASG LTPRSALLYK FNGSPSKKAK KRVIAISGDA
ESPAKRLCQE NDDVLLKRLQ DVVSERANH
