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Protein

Retinoblastoma-like protein 2

Gene

Rbl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-like protein 2
Alternative name(s):
130 kDa retinoblastoma-associated protein
Short name:
p130
PPAR-alpha-interacting complex protein 128
Short name:
PRIC128
Retinoblastoma-related protein 2
Short name:
RBR-2
pRb2
Gene namesi
Name:Rbl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3541. Rbl2.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11351135Retinoblastoma-like protein 2PRO_0000167843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei410 – 4101PhosphoserineBy similarity
Modified residuei414 – 4141PhosphothreonineBy similarity
Modified residuei636 – 6361PhosphoserineCombined sources
Modified residuei639 – 6391PhosphothreonineCombined sources
Modified residuei659 – 6591PhosphoserineBy similarity
Modified residuei669 – 6691PhosphoserineBy similarity
Modified residuei942 – 9421PhosphoserineBy similarity
Modified residuei946 – 9461PhosphoserineCombined sources
Modified residuei960 – 9601PhosphoserineBy similarity
Modified residuei965 – 9651PhosphoserineBy similarity
Modified residuei976 – 9761PhosphoserineBy similarity
Modified residuei980 – 9801PhosphothreonineBy similarity
Modified residuei1031 – 10311PhosphoserineBy similarity
Modified residuei1064 – 10641PhosphoserineCombined sources
Modified residuei1108 – 11081PhosphoserineCombined sources

Post-translational modificationi

During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO55081.
PRIDEiO55081.

PTM databases

PhosphoSiteiO55081.

Interactioni

Subunit structurei

Interacts with AATF, KMT5B and KMT5C. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with USP4 (By similarity). Part of the peroxisome proliferator activated receptor alpha (PPAR-alpha) interacting complex (PRIC). Interacts with RINT1 (By similarity). Interacts with PML (By similarity).By similarity

Protein-protein interaction databases

BioGridi249630. 5 interactions.
IntActiO55081. 1 interaction.
STRINGi10116.ENSRNOP00000017361.

Structurei

3D structure databases

ProteinModelPortaliO55081.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni414 – 1021608Pocket; binds E1AAdd
BLAST
Regioni414 – 613200Domain AAdd
BLAST
Regioni614 – 824211SpacerAdd
BLAST
Regioni825 – 1021197Domain BAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 134Poly-Pro
Compositional biasi14 – 174Poly-Ala
Compositional biasi20 – 245Poly-Glu
Compositional biasi992 – 9954Poly-Glu

Sequence similaritiesi

Belongs to the retinoblastoma protein (RB) family.Curated

Phylogenomic databases

eggNOGiKOG1010. Eukaryota.
ENOG410XQF7. LUCA.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiO55081.
KOiK16332.
PhylomeDBiO55081.

Family and domain databases

Gene3Di1.10.472.10. 3 hits.
InterProiIPR013763. Cyclin-like.
IPR028308. RB2.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 3 hits.
PTHR13742:SF8. PTHR13742:SF8. 3 hits.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01367. DUF3452. 1 hit.
SM01368. RB_A. 1 hit.
SM01369. Rb_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 3 hits.

Sequencei

Sequence statusi: Complete.

O55081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGGNQSSP PPPAAAASSE EEEEDGDTAD RAQPAGSPSH QIQQRFEELC
60 70 80 90 100
SRLNMDEAAR AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS
110 120 130 140 150
KGTAEGNYVS LTRILRCSEQ SLIEFFNKMK KWEDMANLPP HFRERTERLE
160 170 180 190 200
RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR QQRGRKQRRQ PCTTSEIFHF
210 220 230 240 250
CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC SNRKELVNPN
260 270 280 290 300
FKGVSEDGHP RDSHPSSDPP CVIEKLCSLH DGLVLEAKGI KQHFWKPYIR
310 320 330 340 350
KLFEKKLLRG KEENLTGFLE PGNFAESFKA VNKAYEEYVL ATGSLDERIF
360 370 380 390 400
LGEDAEEEVG TFSRCVSAAS GTESAERTQM RDILQQHLDK SKTLRVCNPL
410 420 430 440 450
TGVRYVQENS PCVTPVSTAT HSLNRLHTML AGLRNAPSEK LEQILRSCSR
460 470 480 490 500
DPTRAIADRL REMYEIYSQH FQPDENVSNC AKEMANKHFR FAEMLYYKVL
510 520 530 540 550
ESVIEQEQKR LGDMDLSGVL EQDAFHKSLL ACCLEVVAFS YKPPGNFPFI
560 570 580 590 600
AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS
610 620 630 640 650
PLWDRIRDNE NRVPTCEEVT PPHNLERTDE IYIAGSPLTP RRVGEVRTDA
660 670 680 690 700
GGLGRSVTSP TTLYDRYSSP TVSTTRRRLF ESDSPSEGST AGRIPPQPLV
710 720 730 740 750
NAVPVQNVSG ETVSVTPVPG QTLVTMATAT VTANNGQTVT IPVQGIANEN
760 770 780 790 800
GGITFFPVQV NVGGQAQAVT GSIQPLSAQA LAGSLSSQQV TGTTLQVPGP
810 820 830 840 850
VAIQQISPGG QQQNQGQPLT SSSIRPRKTS SLSLFFRKVY YLAGVRLRDL
860 870 880 890 900
CTKLDISDEL RKKIWTCFEF SIVQCPELMM DRHLDQLLMC AIYVMAKVTK
910 920 930 940 950
EDKSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSCEN RSHQNSPTEL
960 970 980 990 1000
NTDRASRDSS PVMRSNSTLP VPQPSSAPPT PTRLTGANSD IEEEERGDLI
1010 1020 1030 1040 1050
QFYNNIYRKQ IQTFAMKYSQ ANSQMDTPPL SPYPFVRTGS PRRVQLSQSH
1060 1070 1080 1090 1100
PIYISPHKNE AMLSPREKIF YYFSNSPSKR LREINSMIRT GETPTKKRGI
1110 1120 1130
LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSH
Length:1,135
Mass (Da):127,818
Last modified:June 1, 1998 - v1
Checksum:i6C42A87E163B4298
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55627 mRNA. Translation: BAA24196.1.
RefSeqiNP_112356.1. NM_031094.1.
UniGeneiRn.11020.

Genome annotation databases

GeneIDi81758.
KEGGirno:81758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55627 mRNA. Translation: BAA24196.1.
RefSeqiNP_112356.1. NM_031094.1.
UniGeneiRn.11020.

3D structure databases

ProteinModelPortaliO55081.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249630. 5 interactions.
IntActiO55081. 1 interaction.
STRINGi10116.ENSRNOP00000017361.

PTM databases

PhosphoSiteiO55081.

Proteomic databases

PaxDbiO55081.
PRIDEiO55081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81758.
KEGGirno:81758.

Organism-specific databases

CTDi5934.
RGDi3541. Rbl2.

Phylogenomic databases

eggNOGiKOG1010. Eukaryota.
ENOG410XQF7. LUCA.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiO55081.
KOiK16332.
PhylomeDBiO55081.

Miscellaneous databases

NextBioi615534.
PROiO55081.

Family and domain databases

Gene3Di1.10.472.10. 3 hits.
InterProiIPR013763. Cyclin-like.
IPR028308. RB2.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 3 hits.
PTHR13742:SF8. PTHR13742:SF8. 3 hits.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
SM01367. DUF3452. 1 hit.
SM01368. RB_A. 1 hit.
SM01369. Rb_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the rat p130, a member of the retinoblastoma gene family."
    Sawada Y., Nomura H., Endo Y., Umeki K., Fujita T., Ohtaki S., Fujinaga K.
    Biochim. Biophys. Acta 1361:20-27(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Spleen.
  2. "Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha-interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator."
    Surapureddi S., Yu S., Bu H., Hashimoto T., Yeldandi A.V., Kashireddy P., Cherkaoui-Malki M., Qi C., Zhu Y.-J., Rao M.S., Reddy J.K.
    Proc. Natl. Acad. Sci. U.S.A. 99:11836-11841(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 276-288 AND 829-838, SUBUNIT.
    Tissue: Liver.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; THR-639; SER-946; SER-1064 AND SER-1108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRBL2_RAT
AccessioniPrimary (citable) accession number: O55081
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.