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P13405

- RB_MOUSE

UniProt

P13405 - RB_MOUSE

Protein

Retinoblastoma-associated protein

Gene

Rb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. 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 SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex By similarity.By similarity

    GO - Molecular functioni

    1. core promoter binding Source: Ensembl
    2. enzyme binding Source: UniProtKB
    3. kinase binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: MGI
    2. cell division Source: MGI
    3. cell morphogenesis involved in neuron differentiation Source: MGI
    4. chromatin modification Source: UniProtKB-KW
    5. digestive tract development Source: MGI
    6. enucleate erythrocyte differentiation Source: MGI
    7. G1/S transition of mitotic cell cycle Source: MGI
    8. glial cell apoptotic process Source: MGI
    9. hepatocyte apoptotic process Source: MGI
    10. maintenance of mitotic sister chromatid cohesion Source: Ensembl
    11. myoblast differentiation Source: UniProtKB
    12. negative regulation of cell cycle Source: MGI
    13. negative regulation of cell proliferation Source: MGI
    14. negative regulation of epithelial cell proliferation Source: MGI
    15. negative regulation of G1/S transition of mitotic cell cycle Source: MGI
    16. negative regulation of protein kinase activity Source: UniProtKB
    17. negative regulation of smoothened signaling pathway Source: MGI
    18. negative regulation of transcription, DNA-templated Source: MGI
    19. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    20. negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
    21. neuron apoptotic process Source: MGI
    22. neuron differentiation Source: MGI
    23. neuron maturation Source: MGI
    24. neuron projection development Source: MGI
    25. positive regulation of macrophage differentiation Source: MGI
    26. positive regulation of mitotic metaphase/anaphase transition Source: Ensembl
    27. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    28. protein localization to chromosome, centromeric region Source: Ensembl
    29. Ras protein signal transduction Source: Ensembl
    30. regulation of cell cycle Source: MGI
    31. regulation of cohesin localization to chromatin Source: Ensembl
    32. regulation of lipid kinase activity Source: UniProtKB
    33. sister chromatid biorientation Source: Ensembl
    34. skeletal muscle cell differentiation Source: MGI
    35. striated muscle cell differentiation Source: MGI
    36. 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_196580. Condensation of Prophase Chromosomes.
    REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_219010. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoblastoma-associated protein
    Alternative name(s):
    pRb
    Short name:
    Rb
    pp105
    Gene namesi
    Name:Rb1
    Synonyms:Rb-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:97874. Rb1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. PML body Source: UniProtKB
    3. Rb-E2F complex Source: BHF-UCL
    4. spindle Source: MGI
    5. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi746 – 7461I → A: Abolishes the interaction with many chromatin regulators but not that with SUV420H1 and SUV420H2; when associated with A-750 and A-754. 1 Publication
    Mutagenesisi750 – 7501N → A: Abolishes the interaction with many chromatin regulators but not that with SUV420H1 and SUV420H2; when associated with A-746 and A-754. 1 Publication
    Mutagenesisi754 – 7541M → A: Abolishes the interaction with many chromatin regulators but not that with SUV420H1 and SUV420H2; when associated with A-746 and A-750. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 921920Retinoblastoma-associated proteinPRO_0000167837Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N-dimethylproline; by NTM11 Publication
    Modified residuei31 – 311PhosphoserineBy similarity
    Modified residuei243 – 2431Phosphoserine; by CDK1By similarity
    Modified residuei246 – 2461Phosphothreonine; by CDK1By similarity
    Modified residuei350 – 3501PhosphothreonineBy similarity
    Modified residuei367 – 3671Phosphothreonine; by CDK1By similarity
    Modified residuei561 – 5611Phosphoserine; by CDK2By similarity
    Modified residuei605 – 6051Phosphoserine; by CHEK2 and CHEK1By similarity
    Modified residuei788 – 7881PhosphoserineBy similarity
    Modified residuei800 – 8001Phosphoserine; by CDK1 and CDK3By similarity
    Modified residuei803 – 8031N6-methyllysine; by SMYD2By similarity
    Modified residuei804 – 8041Phosphoserine; by CDK1 and CDK3By similarity
    Modified residuei814 – 8141Phosphothreonine; by CDK6By similarity
    Modified residuei816 – 8161PhosphothreonineBy similarity
    Modified residuei819 – 8191Phosphothreonine; by CDK4
    Modified residuei834 – 8341PhosphothreonineBy similarity
    Modified residuei853 – 8531N6-methyllysine; by SMYD2By similarity
    Modified residuei866 – 8661N6-acetyllysine; by PCAFBy similarity
    Modified residuei867 – 8671N6-acetyllysine; by PCAFBy similarity

    Post-translational modificationi

    Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of threonine residues in domain C promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-788 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition By similarity. Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis By similarity.By similarity
    Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression. Monomethylation at Lys-853 by SMYD2 promotes interaction with L3MBTL1 By similarity. N-terminus is methylated by METTL11A/NTM1.By similarity1 Publication
    Acetylation at Lys-866 and Lys-867 regulates subcellular localization, at least during keratinocytes differentiation.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP13405.
    PRIDEiP13405.

    PTM databases

    PhosphoSiteiP13405.

    Expressioni

    Tissue specificityi

    Expressed in the cell nuclei of renal tubules, hepathocytes and skeletal muscles. Colocalizes with RB1CC1 in various tissues.1 Publication

    Gene expression databases

    ArrayExpressiP13405.
    BgeeiP13405.
    CleanExiMM_RB1.
    GenevestigatoriP13405.

    Interactioni

    Subunit structurei

    The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor. Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain of TAF1. Interacts with SNW1, ATAD5, AATF, DNMT1, LIN9, LMNA, SUV420H1, SUV420H2, PELP1, UHRF2, TMPO-alpha and USP4. May interact with NDC80. Interacts with GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 and HDAC1. Interacts with USP4. Interacts (when methylated at Lys-853) with L3MBTL1. Binds to CDK1 and CDK2. Interacts with CHEK2; phosphorylates RB1 By similarity. Interacts with PRMT2.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CenpfQ155P74EBI-971782,EBI-2211248
    DgkzQ80UP32EBI-971782,EBI-971774
    Ifi202Q9R0027EBI-971782,EBI-3043899
    Pax3P246103EBI-971782,EBI-1208116
    Pdx1P529462EBI-971782,EBI-7128945
    Smarca4Q3TKT43EBI-971782,EBI-1210244
    Vsx2Q614122EBI-971782,EBI-1208174

    Protein-protein interaction databases

    BioGridi202815. 37 interactions.
    DIPiDIP-37637N.
    IntActiP13405. 16 interactions.
    MINTiMINT-225292.

    Structurei

    3D structure databases

    ProteinModelPortaliP13405.
    SMRiP13405. Positions 47-779, 822-865.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni367 – 764398Pocket; binds T and E1ABy similarityAdd
    BLAST
    Regioni367 – 573207Domain ABy similarityAdd
    BLAST
    Regioni574 – 63259SpacerBy similarityAdd
    BLAST
    Regioni633 – 764132Domain BBy similarityAdd
    BLAST
    Regioni756 – 921166Interaction with LIMD1By similarityAdd
    BLAST
    Regioni764 – 921158Domain; mediates interaction with E4F1By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi863 – 8697Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 124Poly-Ala
    Compositional biasi14 – 229Poly-Pro

    Sequence similaritiesi

    Belongs to the retinoblastoma protein (RB) family.Curated

    Phylogenomic databases

    eggNOGiNOG296920.
    GeneTreeiENSGT00530000063235.
    HOGENOMiHOG000136539.
    HOVERGENiHBG008967.
    InParanoidiQ4VA62.
    KOiK06618.
    OMAiTNILQYA.
    OrthoDBiEOG7P5T04.
    TreeFamiTF105568.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    [Graphical view]
    PANTHERiPTHR13742. PTHR13742. 1 hit.
    PfamiPF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    PF08934. Rb_C. 1 hit.
    [Graphical view]
    SMARTiSM00385. CYCLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13405-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE    50
    FIALCQKLKV PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA 100
    AVDLDEMPFT FTELQKSIET SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN 150
    VLCALYSKLE RTCELIYLTQ PSSALSTEIN SMLVLKISWI TFLLAKGEVL 200
    QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI NGSPRTPRRG 250
    QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV 300
    SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT 350
    PRKNNPDEEA NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN 400
    CTVNPKENIL KRVKDVGHIF KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV 450
    MESMLKSEEE RLSIQNFSKL LNDNIFHMSL LACALEVVMA TYSRSTLQHL 500
    DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM IKHLERCEHR 550
    IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL 600
    SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL 650
    AYLRLNTLCA RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS 700
    MYGICKVKNI DLKFKIIVTA YKDLPHAAQE TFKRVLIREE EFDSIIVFYN 750
    SVFMQRLKTN ILQYASTRPP TLSPIPHIPR SPYKFSSSPL RIPGGNIYIS 800
    PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK INQMVCNSDR 850
    VLKRSAEGGN PPKPLKKLRF DIEGADEADG SKHLPAESKF QQKLAEMTST 900
    RTRMQKQRMN ESKDVSNKEE K 921
    Length:921
    Mass (Da):105,367
    Last modified:July 27, 2011 - v2
    Checksum:iAE81D35A07ADB493
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti867 – 8682KL → NV in AAA39964. (PubMed:2671991)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26391 mRNA. Translation: AAA39964.1.
    DQ400415 mRNA. Translation: ABD72475.1.
    BC096525 mRNA. Translation: AAH96525.1.
    CCDSiCCDS27267.1.
    PIRiA33718.
    RefSeqiNP_033055.2. NM_009029.2.
    UniGeneiMm.273862.

    Genome annotation databases

    EnsembliENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105.
    GeneIDi19645.
    KEGGimmu:19645.
    UCSCiuc007upp.2. mouse.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Retinoblastoma protein entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26391 mRNA. Translation: AAA39964.1 .
    DQ400415 mRNA. Translation: ABD72475.1 .
    BC096525 mRNA. Translation: AAH96525.1 .
    CCDSi CCDS27267.1.
    PIRi A33718.
    RefSeqi NP_033055.2. NM_009029.2.
    UniGenei Mm.273862.

    3D structure databases

    ProteinModelPortali P13405.
    SMRi P13405. Positions 47-779, 822-865.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202815. 37 interactions.
    DIPi DIP-37637N.
    IntActi P13405. 16 interactions.
    MINTi MINT-225292.

    PTM databases

    PhosphoSitei P13405.

    Proteomic databases

    PaxDbi P13405.
    PRIDEi P13405.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022701 ; ENSMUSP00000022701 ; ENSMUSG00000022105 .
    GeneIDi 19645.
    KEGGi mmu:19645.
    UCSCi uc007upp.2. mouse.

    Organism-specific databases

    CTDi 5925.
    MGIi MGI:97874. Rb1.

    Phylogenomic databases

    eggNOGi NOG296920.
    GeneTreei ENSGT00530000063235.
    HOGENOMi HOG000136539.
    HOVERGENi HBG008967.
    InParanoidi Q4VA62.
    KOi K06618.
    OMAi TNILQYA.
    OrthoDBi EOG7P5T04.
    TreeFami TF105568.

    Enzyme and pathway databases

    Reactomei REACT_196580. Condensation of Prophase Chromosomes.
    REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_219010. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    NextBioi 296890.
    PROi P13405.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13405.
    Bgeei P13405.
    CleanExi MM_RB1.
    Genevestigatori P13405.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    [Graphical view ]
    PANTHERi PTHR13742. PTHR13742. 1 hit.
    Pfami PF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    PF08934. Rb_C. 1 hit.
    [Graphical view ]
    SMARTi SM00385. CYCLIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the murine retinoblastoma gene and characterization of its encoded protein."
      Bernards R., Schackleford G.M., Gerber M.R., Horowitz J.M., Friend S.H., Schartl M., Bogenmann E., Rapaport J., McGee T., Dryja T.P., Weinberg R.A.
      Proc. Natl. Acad. Sci. U.S.A. 86:6474-6478(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequencing of the full-length cDNA sequence of the murine retinoblastoma gene."
      Wu J., Liao J.D.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    4. "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters."
      Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P.
      Nat. Genet. 25:338-342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMT1.
    5. "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F."
      Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E., Medema R., Vignais M.-L., Sardet C.
      Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH E4F1.
    6. "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.
    7. "Isolation, characterization and mapping of the mouse and human RB1CC1 genes."
      Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A., Saeki Y., Okabe H.
      Gene 291:29-34(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, COLOCALIZATION WITH RB1CC1.
      Strain: C57BL/6.
      Tissue: Skeletal muscle.
    8. "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.
    9. "Frag1, a homolog of alternative replication factor C subunits, links replication stress surveillance with apoptosis."
      Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.
      Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATAD5.
    10. "The arginine methyltransferase PRMT2 binds RB and regulates E2F function."
      Yoshimoto T., Boehm M., Olive M., Crook M.F., San H., Langenickel T., Nabel E.G.
      Exp. Cell Res. 312:2040-2053(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT2.
    11. Cited for: FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2, MUTAGENESIS OF ILE-746; ASN-750 AND MET-754.
    12. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
      Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.
      Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT PRO-2.

    Entry informationi

    Entry nameiRB_MOUSE
    AccessioniPrimary (citable) accession number: P13405
    Secondary accession number(s): Q4VA62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 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