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Q64700

- RBL2_MOUSE

UniProt

Q64700 - RBL2_MOUSE

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Protein
Retinoblastoma-like protein 2
Gene
Rbl2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. chromatin modification Source: UniProtKB-KW
  3. regulation of cell cycle Source: InterPro
  4. regulation of lipid kinase activity Source: Ensembl
  5. regulation of transcription from RNA polymerase II promoter Source: InterPro
  6. transcription, DNA-templated Source: UniProtKB-KW
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_199110. G0 and Early 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: Chromosome 8

Organism-specific databases

MGIiMGI:105085. Rbl2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleolus Source: Ensembl
  3. nucleus Source: MGI
  4. 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 2
PRO_0000167842Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ64700.
PRIDEiQ64700.

PTM databases

PhosphoSiteiQ64700.

Expressioni

Gene expression databases

ArrayExpressiQ64700.
BgeeiQ64700.
CleanExiMM_RBL2.
GenevestigatoriQ64700.

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.2 Publications

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni414 – 1021608Pocket; binds E1A
Add
BLAST
Regioni414 – 613200Domain A
Add
BLAST
Regioni614 – 824211Spacer
Add
BLAST
Regioni825 – 1021197Domain B
Add
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

Phylogenomic databases

eggNOGiNOG296920.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000273892.
HOVERGENiHBG017710.
InParanoidiQ3TVP8.
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

MASGGNQSPP PPPAAAASSE EEEEDGDAAD RAQPAGSPSH QIQQRFEELC     50
SRLNMDEAAR AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS 100
KGTAEGNYVS LTRILRCSEQ SLIEFFNKMK KWEDMANLPP HFRERTERLE 150
RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR QQRGRKQRRQ PCTTSEIFHF 200
CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC SNRKELVNPN 250
FKGLSEDCHP KDSKASSDPP CVIEKLCSLH DGLVLEAKGI KEHFWKPYIR 300
KLFEKKLLKG KEENLTGFLE PGNFGESFKA VNKAYEEYVL AAGNLDERVF 350
LGEDAEEEVG TLSRCLSAAS GTESAERTQM RDILQQHLDK SKALRVCTPL 400
TGVRYVQENS PCVTPVSTAA HSLSRLHTML SGLRNAPSEK LERILRSCSR 450
DPTQAIADRL KEMYEIYSQH FQPDENFSNC AKEIANKHFR FAEMLYYKVL 500
ESVIEQEQKR LGDMDLSGVL EHDAFHRSLL ACCLEVVAFS HKPPGNFPFI 550
AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS 600
PLWDRIRDNE NRVPTCEEVM PPQNLERTDE IYIAGSPLTP RRVGEVRADA 650
GGLGRSITSP TTLYDRYSSP TVSTTRRRLF ENDSPSEGST SGRIPPQPLV 700
NAVPVQNVPG ETVSVTPVPG QTLVTMATAT VTANNGQTVT IPVQGIANEN 750
GGITFFPVQV NVGGQAQAVA GSIQPLSAQA LAGSLSSQQV TGTTLQVPGP 800
VAIQQISPGG QQQNPGQPLT SSSIRPRKTS SLALFFRKVY YLAGVRLRDL 850
CIKLDISDEL RKKIWTCFEF SIIQCTELMM DRHLDQLLMC AIYVMAKVTK 900
EDRSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSSES RSHQNSPTEL 950
NTDRASRDSS PVMRSNSTLP VPQPSSAPPT PTRLTGASSD VEEEERGDLI 1000
QFYNNIYRKQ IQAFAMKYSQ ANAQTDTPPL SPYPFVRTGS PRRVQLSQSH 1050
PIYISPHNNE AMPSPREKIF YYFSNSPSKR LREINSMIRT GETPTKKRGI 1100
LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ 1135
Length:1,135
Mass (Da):127,485
Last modified:July 27, 2011 - v3
Checksum:iF509E68A156929B2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 25143Missing in AAC52555. 1 Publication
Add
BLAST
Sequence conflicti341 – 3411A → P in AAB48991. 1 Publication
Sequence conflicti342 – 3421A → P in AAC52555. 1 Publication
Sequence conflicti381 – 3811R → T in AAC52598. 1 Publication
Sequence conflicti428 – 4281T → S in AAC52598. 1 Publication
Sequence conflicti431 – 4311S → T in AAC52598. 1 Publication
Sequence conflicti443 – 4431R → Q in AAC52598. 1 Publication
Sequence conflicti483 – 49210Missing in AAB48991. 1 Publication
Sequence conflicti768 – 7681A → R in AAC52598. 1 Publication
Sequence conflicti826 – 8261P → A in AAC52555. 1 Publication
Sequence conflicti947 – 9482PT → RA in AAC52555. 1 Publication
Sequence conflicti1023 – 10231A → S in AAC52598. 1 Publication
Sequence conflicti1044 – 10441V → I in AAC52598. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U36799 mRNA. Translation: AAB48991.1 .
U50850 mRNA. Translation: AAC52598.1 .
U47333 mRNA. Translation: AAC52555.1 .
AK160027 mRNA. Translation: BAE35570.1 .
CCDSi CCDS22518.1.
RefSeqi NP_001268929.1. NM_001282000.1.
NP_001268930.1. NM_001282001.1.
NP_035380.3. NM_011250.4.
UniGenei Mm.235580.

3D structure databases

ProteinModelPortali Q64700.
SMRi Q64700. Positions 425-612, 828-935.
ModBasei Search...

Protein-protein interaction databases

BioGridi 202820. 5 interactions.
IntActi Q64700. 4 interactions.
MINTi MINT-5181879.
STRINGi 10090.ENSMUSP00000034091.

PTM databases

PhosphoSitei Q64700.

Proteomic databases

PaxDbi Q64700.
PRIDEi Q64700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034091 ; ENSMUSP00000034091 ; ENSMUSG00000031666 .
GeneIDi 19651.
KEGGi mmu:19651.
UCSCi uc012gid.1. mouse.

Organism-specific databases

CTDi 5934.
MGIi MGI:105085. Rbl2.

Phylogenomic databases

eggNOGi NOG296920.
GeneTreei ENSGT00530000063235.
HOGENOMi HOG000273892.
HOVERGENi HBG017710.
InParanoidi Q3TVP8.
KOi K16332.
OMAi PPGNFPF.
OrthoDBi EOG7P5T04.
TreeFami TF105568.

Enzyme and pathway databases

Reactomei REACT_199110. G0 and Early G1.

Miscellaneous databases

NextBioi 296912.
PROi Q64700.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q64700.
Bgeei Q64700.
CleanExi MM_RBL2.
Genevestigatori Q64700.

Family and domain databases

Gene3Di 1.10.472.10. 3 hits.
InterProi IPR013763. Cyclin-like.
IPR028308. RB2.
IPR002720. RB_A.
IPR002719. RB_B.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view ]
PANTHERi PTHR13742. PTHR13742. 1 hit.
PTHR13742:SF8. PTHR13742:SF8. 1 hit.
Pfami PF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
[Graphical view ]
SMARTi SM00385. CYCLIN. 2 hits.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
ProtoNeti Search...

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: September 3, 2014
This is version 119 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

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