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Q64700

- RBL2_MOUSE

UniProt

Q64700 - RBL2_MOUSE

Protein

Retinoblastoma-like protein 2

Gene

Rbl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    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

    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.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.
    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

    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 120 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