RBL2_RAT
ID RBL2_RAT Reviewed; 1135 AA.
AC O55081;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Retinoblastoma-like protein 2;
DE AltName: Full=130 kDa retinoblastoma-associated protein;
DE Short=p130;
DE AltName: Full=PPAR-alpha-interacting complex protein 128;
DE Short=PRIC128;
DE AltName: Full=Retinoblastoma-related protein 2;
DE Short=RBR-2;
DE AltName: Full=pRb2;
GN Name=Rbl2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RX PubMed=9247086; DOI=10.1016/s0925-4439(97)00037-9;
RA Sawada Y., Nomura H., Endo Y., Umeki K., Fujita T., Ohtaki S., Fujinaga K.;
RT "Cloning and characterization of the rat p130, a member of the
RT retinoblastoma gene family.";
RL Biochim. Biophys. Acta 1361:20-27(1997).
RN [2]
RP PROTEIN SEQUENCE OF 276-288 AND 829-838, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=12189208; DOI=10.1073/pnas.182426699;
RA Surapureddi S., Yu S., Bu H., Hashimoto T., Yeldandi A.V., Kashireddy P.,
RA Cherkaoui-Malki M., Qi C., Zhu Y.-J., Rao M.S., Reddy J.K.;
RT "Identification of a transcriptionally active peroxisome proliferator-
RT activated receptor alpha-interacting cofactor complex in rat liver and
RT characterization of PRIC285 as a coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11836-11841(2002).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; THR-639; SER-946;
RP SER-1064 AND SER-1108, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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. 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AATF, KMT5B and KMT5C. Component of the DREAM
CC complex (also named LINC complex) at least composed of E2F4, E2F5,
CC LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and
CC TFDP2. The complex exists in quiescent cells where it represses cell
CC cycle-dependent genes. It dissociates in S phase when LIN9, LIN37,
CC LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with
CC USP4 (By similarity). Part of the peroxisome proliferator activated
CC receptor alpha (PPAR-alpha) interacting complex (PRIC). Interacts with
CC RINT1 (By similarity). Interacts with PML (By similarity). Interacts
CC with RBBP9 (PubMed:9697699). {ECO:0000250, ECO:0000269|PubMed:9697699}.
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}.
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; D55627; BAA24196.1; -; mRNA.
DR RefSeq; NP_112356.1; NM_031094.1.
DR AlphaFoldDB; O55081; -.
DR SMR; O55081; -.
DR BioGRID; 249630; 5.
DR IntAct; O55081; 1.
DR STRING; 10116.ENSRNOP00000017361; -.
DR iPTMnet; O55081; -.
DR PhosphoSitePlus; O55081; -.
DR PaxDb; O55081; -.
DR PRIDE; O55081; -.
DR GeneID; 81758; -.
DR KEGG; rno:81758; -.
DR CTD; 5934; -.
DR RGD; 3541; Rbl2.
DR eggNOG; KOG1010; Eukaryota.
DR InParanoid; O55081; -.
DR OrthoDB; 113612at2759; -.
DR PhylomeDB; O55081; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR PRO; PR:O55081; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
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: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:0051302; P:regulation of cell division; IEA:InterPro.
DR GO; GO:0043550; P:regulation of lipid kinase activity; ISO:RGD.
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; 3.
PE 1: Evidence at protein level;
KW Cell cycle; Chromatin regulator; Direct protein sequencing; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..1135
FT /note="Retinoblastoma-like protein 2"
FT /id="PRO_0000167843"
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 649..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..1021
FT /note="Domain B"
FT REGION 932..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..691
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:0000250|UniProtKB:Q08999"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64700"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 639
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000250|UniProtKB:Q64700"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
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:0000250|UniProtKB:Q08999"
FT MOD_RES 980
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08999"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1135 AA; 127818 MW; 6C42A87E163B4298 CRC64;
MASGGNQSSP PPPAAAASSE EEEEDGDTAD RAQPAGSPSH QIQQRFEELC SRLNMDEAAR
AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS KGTAEGNYVS LTRILRCSEQ
SLIEFFNKMK KWEDMANLPP HFRERTERLE RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR
QQRGRKQRRQ PCTTSEIFHF CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC
SNRKELVNPN FKGVSEDGHP RDSHPSSDPP CVIEKLCSLH DGLVLEAKGI KQHFWKPYIR
KLFEKKLLRG KEENLTGFLE PGNFAESFKA VNKAYEEYVL ATGSLDERIF LGEDAEEEVG
TFSRCVSAAS GTESAERTQM RDILQQHLDK SKTLRVCNPL TGVRYVQENS PCVTPVSTAT
HSLNRLHTML AGLRNAPSEK LEQILRSCSR DPTRAIADRL REMYEIYSQH FQPDENVSNC
AKEMANKHFR FAEMLYYKVL ESVIEQEQKR LGDMDLSGVL EQDAFHKSLL ACCLEVVAFS
YKPPGNFPFI AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS
PLWDRIRDNE NRVPTCEEVT PPHNLERTDE IYIAGSPLTP RRVGEVRTDA GGLGRSVTSP
TTLYDRYSSP TVSTTRRRLF ESDSPSEGST AGRIPPQPLV NAVPVQNVSG ETVSVTPVPG
QTLVTMATAT VTANNGQTVT IPVQGIANEN GGITFFPVQV NVGGQAQAVT GSIQPLSAQA
LAGSLSSQQV TGTTLQVPGP VAIQQISPGG QQQNQGQPLT SSSIRPRKTS SLSLFFRKVY
YLAGVRLRDL CTKLDISDEL RKKIWTCFEF SIVQCPELMM DRHLDQLLMC AIYVMAKVTK
EDKSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSCEN RSHQNSPTEL NTDRASRDSS
PVMRSNSTLP VPQPSSAPPT PTRLTGANSD IEEEERGDLI QFYNNIYRKQ IQTFAMKYSQ
ANSQMDTPPL SPYPFVRTGS PRRVQLSQSH PIYISPHKNE AMLSPREKIF YYFSNSPSKR
LREINSMIRT GETPTKKRGI LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSH
