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Protein

Retinoblastoma-like protein 2

Gene

Rbl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

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

Enzyme and pathway databases

ReactomeiR-MMU-1538133. G0 and Early G1.
R-MMU-69231. Cyclin D associated events in G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-like protein 2
Alternative name(s):
130 kDa retinoblastoma-associated protein
Short name:
p130
Retinoblastoma-related protein 2
Short name:
RBR-2
pRb2
Gene namesi
Name:Rbl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:105085. Rbl2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001678421 – 1135Retinoblastoma-like protein 2Add BLAST1135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei410PhosphoserineCombined sources1
Modified residuei414PhosphothreonineCombined sources1
Modified residuei636PhosphoserineCombined sources1
Modified residuei639PhosphothreonineCombined sources1
Modified residuei659PhosphoserineBy similarity1
Modified residuei669PhosphoserineBy similarity1
Modified residuei684PhosphoserineBy similarity1
Modified residuei942PhosphoserineCombined sources1
Modified residuei946PhosphoserineBy similarity1
Modified residuei960PhosphoserineBy similarity1
Modified residuei965PhosphoserineCombined sources1
Modified residuei976PhosphoserineCombined sources1
Modified residuei980PhosphothreonineCombined sources1
Modified residuei1031PhosphoserineBy similarity1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1076PhosphoserineBy similarity1
Modified residuei1108PhosphoserineBy similarity1

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

EPDiQ64700.
MaxQBiQ64700.
PaxDbiQ64700.
PeptideAtlasiQ64700.
PRIDEiQ64700.

PTM databases

iPTMnetiQ64700.
PhosphoSitePlusiQ64700.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031666.
CleanExiMM_RBL2.
GenevisibleiQ64700. MM.

Interactioni

Subunit structurei

Interacts with AATF and RINT1. 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). Interacts with KMT5B, KMT5C and USP4. Interacts with PML (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CenpfQ155P73EBI-2271232,EBI-2211248

Protein-protein interaction databases

BioGridi202820. 5 interactors.
IntActiQ64700. 4 interactors.
MINTiMINT-5181879.
STRINGi10090.ENSMUSP00000034091.

Structurei

3D structure databases

ProteinModelPortaliQ64700.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni414 – 1021Pocket; binds E1AAdd BLAST608
Regioni414 – 613Domain AAdd BLAST200
Regioni614 – 824SpacerAdd BLAST211
Regioni825 – 1021Domain BAdd BLAST197

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi9 – 13Poly-Pro5
Compositional biasi14 – 17Poly-Ala4
Compositional biasi20 – 24Poly-Glu5
Compositional biasi992 – 995Poly-Glu4

Sequence similaritiesi

Belongs to the retinoblastoma protein (RB) family.Curated

Phylogenomic databases

eggNOGiKOG1010. Eukaryota.
ENOG410XQF7. LUCA.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiQ64700.
KOiK16332.
OMAiPPGNFPF.
OrthoDBiEOG091G0398.
TreeFamiTF105568.

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. 2 hits.

Sequencei

Sequence statusi: Complete.

Q64700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGGNQSPP PPPAAAASSE EEEEDGDAAD 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
FKGLSEDCHP KDSKASSDPP CVIEKLCSLH DGLVLEAKGI KEHFWKPYIR
310 320 330 340 350
KLFEKKLLKG KEENLTGFLE PGNFGESFKA VNKAYEEYVL AAGNLDERVF
360 370 380 390 400
LGEDAEEEVG TLSRCLSAAS GTESAERTQM RDILQQHLDK SKALRVCTPL
410 420 430 440 450
TGVRYVQENS PCVTPVSTAA HSLSRLHTML SGLRNAPSEK LERILRSCSR
460 470 480 490 500
DPTQAIADRL KEMYEIYSQH FQPDENFSNC AKEIANKHFR FAEMLYYKVL
510 520 530 540 550
ESVIEQEQKR LGDMDLSGVL EHDAFHRSLL ACCLEVVAFS HKPPGNFPFI
560 570 580 590 600
AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS
610 620 630 640 650
PLWDRIRDNE NRVPTCEEVM PPQNLERTDE IYIAGSPLTP RRVGEVRADA
660 670 680 690 700
GGLGRSITSP TTLYDRYSSP TVSTTRRRLF ENDSPSEGST SGRIPPQPLV
710 720 730 740 750
NAVPVQNVPG ETVSVTPVPG QTLVTMATAT VTANNGQTVT IPVQGIANEN
760 770 780 790 800
GGITFFPVQV NVGGQAQAVA GSIQPLSAQA LAGSLSSQQV TGTTLQVPGP
810 820 830 840 850
VAIQQISPGG QQQNPGQPLT SSSIRPRKTS SLALFFRKVY YLAGVRLRDL
860 870 880 890 900
CIKLDISDEL RKKIWTCFEF SIIQCTELMM DRHLDQLLMC AIYVMAKVTK
910 920 930 940 950
EDRSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSSES RSHQNSPTEL
960 970 980 990 1000
NTDRASRDSS PVMRSNSTLP VPQPSSAPPT PTRLTGASSD VEEEERGDLI
1010 1020 1030 1040 1050
QFYNNIYRKQ IQAFAMKYSQ ANAQTDTPPL SPYPFVRTGS PRRVQLSQSH
1060 1070 1080 1090 1100
PIYISPHNNE AMPSPREKIF YYFSNSPSKR LREINSMIRT GETPTKKRGI
1110 1120 1130
LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ
Length:1,135
Mass (Da):127,485
Last modified:July 27, 2011 - v3
Checksum:iF509E68A156929B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209 – 251Missing in AAC52555 (PubMed:8622859).CuratedAdd BLAST43
Sequence conflicti341A → P in AAB48991 (PubMed:8621630).Curated1
Sequence conflicti342A → P in AAC52555 (PubMed:8622859).Curated1
Sequence conflicti381R → T in AAC52598 (PubMed:9019172).Curated1
Sequence conflicti428T → S in AAC52598 (PubMed:9019172).Curated1
Sequence conflicti431S → T in AAC52598 (PubMed:9019172).Curated1
Sequence conflicti443R → Q in AAC52598 (PubMed:9019172).Curated1
Sequence conflicti483 – 492Missing in AAB48991 (PubMed:8621630).Curated10
Sequence conflicti768A → R in AAC52598 (PubMed:9019172).Curated1
Sequence conflicti826P → A in AAC52555 (PubMed:8622859).Curated1
Sequence conflicti947 – 948PT → RA in AAC52555 (PubMed:8622859).Curated2
Sequence conflicti1023A → S in AAC52598 (PubMed:9019172).Curated1
Sequence conflicti1044V → I in AAC52598 (PubMed:9019172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36799 mRNA. Translation: AAB48991.1.
U50850 mRNA. Translation: AAC52598.1.
U47333 mRNA. Translation: AAC52555.1.
AK160027 mRNA. Translation: BAE35570.1.
CCDSiCCDS22518.1.
RefSeqiNP_001268929.1. NM_001282000.1.
NP_001268930.1. NM_001282001.1.
NP_035380.3. NM_011250.4.
UniGeneiMm.235580.

Genome annotation databases

EnsembliENSMUST00000034091; ENSMUSP00000034091; ENSMUSG00000031666.
GeneIDi19651.
KEGGimmu:19651.
UCSCiuc012gid.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36799 mRNA. Translation: AAB48991.1.
U50850 mRNA. Translation: AAC52598.1.
U47333 mRNA. Translation: AAC52555.1.
AK160027 mRNA. Translation: BAE35570.1.
CCDSiCCDS22518.1.
RefSeqiNP_001268929.1. NM_001282000.1.
NP_001268930.1. NM_001282001.1.
NP_035380.3. NM_011250.4.
UniGeneiMm.235580.

3D structure databases

ProteinModelPortaliQ64700.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202820. 5 interactors.
IntActiQ64700. 4 interactors.
MINTiMINT-5181879.
STRINGi10090.ENSMUSP00000034091.

PTM databases

iPTMnetiQ64700.
PhosphoSitePlusiQ64700.

Proteomic databases

EPDiQ64700.
MaxQBiQ64700.
PaxDbiQ64700.
PeptideAtlasiQ64700.
PRIDEiQ64700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034091; ENSMUSP00000034091; ENSMUSG00000031666.
GeneIDi19651.
KEGGimmu:19651.
UCSCiuc012gid.2. mouse.

Organism-specific databases

CTDi5934.
MGIiMGI:105085. Rbl2.

Phylogenomic databases

eggNOGiKOG1010. Eukaryota.
ENOG410XQF7. LUCA.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiQ64700.
KOiK16332.
OMAiPPGNFPF.
OrthoDBiEOG091G0398.
TreeFamiTF105568.

Enzyme and pathway databases

ReactomeiR-MMU-1538133. G0 and Early G1.
R-MMU-69231. Cyclin D associated events in G1.

Miscellaneous databases

PROiQ64700.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031666.
CleanExiMM_RBL2.
GenevisibleiQ64700. MM.

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. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRBL2_MOUSE
AccessioniPrimary (citable) accession number: Q64700
Secondary accession number(s): Q3TVP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.