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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 SUV420H1 and SUV420H2, 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

ReactomeiREACT_274086. G0 and Early G1.
REACT_289448. 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
ProteomesiUP000000589 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11351135Retinoblastoma-like protein 2PRO_0000167842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei636 – 6361Phosphoserine1 Publication
Modified residuei639 – 6391Phosphothreonine1 Publication
Modified residuei659 – 6591PhosphoserineBy similarity
Modified residuei669 – 6691PhosphoserineBy similarity
Modified residuei942 – 9421Phosphoserine1 Publication
Modified residuei946 – 9461PhosphoserineBy similarity
Modified residuei960 – 9601PhosphoserineBy similarity
Modified residuei976 – 9761PhosphoserineBy similarity
Modified residuei980 – 9801PhosphothreonineBy similarity
Modified residuei1031 – 10311PhosphoserineBy similarity

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

MaxQBiQ64700.
PaxDbiQ64700.
PRIDEiQ64700.

PTM databases

PhosphoSiteiQ64700.

Expressioni

Gene expression databases

BgeeiQ64700.
CleanExiMM_RBL2.
ExpressionAtlasiQ64700. baseline and differential.
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 SUV420H1, SUV420H2 and USP4. Interacts with PML (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ64700.
SMRiQ64700. Positions 425-612, 828-935.
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 biasi9 – 135Poly-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

eggNOGiNOG296920.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiQ64700.
KOiK16332.
OMAiPPGNFPF.
OrthoDBiEOG7P5T04.
TreeFamiTF105568.

Family and domain databases

Gene3Di1.10.472.10. 3 hits.
InterProiIPR013763. Cyclin-like.
IPR028308. RB2.
IPR002720. RB_A.
IPR002719. RB_B.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF8. PTHR13742:SF8. 1 hit.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 2 hits.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 25143Missing in AAC52555 (PubMed:8622859).CuratedAdd
BLAST
Sequence conflicti341 – 3411A → P in AAB48991 (PubMed:8621630).Curated
Sequence conflicti342 – 3421A → P in AAC52555 (PubMed:8622859).Curated
Sequence conflicti381 – 3811R → T in AAC52598 (PubMed:9019172).Curated
Sequence conflicti428 – 4281T → S in AAC52598 (PubMed:9019172).Curated
Sequence conflicti431 – 4311S → T in AAC52598 (PubMed:9019172).Curated
Sequence conflicti443 – 4431R → Q in AAC52598 (PubMed:9019172).Curated
Sequence conflicti483 – 49210Missing in AAB48991 (PubMed:8621630).Curated
Sequence conflicti768 – 7681A → R in AAC52598 (PubMed:9019172).Curated
Sequence conflicti826 – 8261P → A in AAC52555 (PubMed:8622859).Curated
Sequence conflicti947 – 9482PT → RA in AAC52555 (PubMed:8622859).Curated
Sequence conflicti1023 – 10231A → S in AAC52598 (PubMed:9019172).Curated
Sequence conflicti1044 – 10441V → I in AAC52598 (PubMed:9019172).Curated

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.
SMRiQ64700. Positions 425-612, 828-935.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ64700.

Proteomic databases

MaxQBiQ64700.
PaxDbiQ64700.
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

eggNOGiNOG296920.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiQ64700.
KOiK16332.
OMAiPPGNFPF.
OrthoDBiEOG7P5T04.
TreeFamiTF105568.

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.
REACT_289448. Cyclin D associated events in G1.

Miscellaneous databases

NextBioi296912.
PROiQ64700.
SOURCEiSearch...

Gene expression databases

BgeeiQ64700.
CleanExiMM_RBL2.
ExpressionAtlasiQ64700. baseline and differential.
GenevisibleiQ64700. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and developmental expression of mouse p130, a member of the retinoblastoma gene family."
    Chen G., Guy C.T., Chen H.W., Hu N., Lee E.Y.H.P., Lee W.H.
    J. Biol. Chem. 271:9567-9572(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning, expression, and developmental characterization of the murine retinoblastoma-related gene Rb2/p130."
    Pertile P., Baldi A., de Luca A., Virgilio L., Pisano M.M., Giordano A.
    Cell Growth Differ. 6:1659-1664(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and expression of the Rb-related mouse p130 mRNA."
    Lecouter J.E., Whyte P.F.M., Rudnicki M.A.
    Oncogene 12:1433-1440(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  5. "Association of UNP, a ubiquitin-specific protease, with the pocket proteins pRb, p107 and p130."
    Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.
    Oncogene 20:5533-5537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP4.
  6. "Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin."
    Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.
    Nat. Cell Biol. 7:420-428(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; THR-639 AND SER-942, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 22, 2015
This is version 129 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

External Data

Dasty 3

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 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.