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Q64701

- RBL1_MOUSE

UniProt

Q64701 - RBL1_MOUSE

Protein

Retinoblastoma-like protein 1

Gene

Rbl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (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. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_199110. G0 and Early G1.
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoblastoma-like protein 1
    Alternative name(s):
    107 kDa retinoblastoma-associated protein
    Short name:
    p107
    pRb1
    Gene namesi
    Name:Rbl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:103300. Rbl1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: MGI
    2. 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 – 10631063Retinoblastoma-like protein 1PRO_0000167840Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei332 – 3321PhosphothreonineBy similarity
    Modified residuei369 – 3691PhosphothreonineBy similarity
    Modified residuei385 – 3851PhosphothreonineBy similarity
    Modified residuei640 – 6401PhosphoserineBy similarity
    Modified residuei650 – 6501PhosphoserineBy similarity
    Modified residuei748 – 7481PhosphoserineBy similarity
    Modified residuei761 – 7611PhosphoserineBy similarity
    Modified residuei959 – 9591PhosphoserineBy similarity
    Modified residuei970 – 9701PhosphoserineBy similarity
    Modified residuei983 – 9831PhosphoserineBy similarity
    Modified residuei992 – 9921PhosphothreonineBy similarity
    Modified residuei1004 – 10041PhosphoserineBy similarity
    Modified residuei1036 – 10361Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated. SV40 large T antigen binds only to the unphosphorylated form, whereas the adenovirus E1A binds to both forms. Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ64701.
    PaxDbiQ64701.
    PRIDEiQ64701.

    PTM databases

    PhosphoSiteiQ64701.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal heart and liver. Expressed at low levels in all other fetal tissues except skeletal muscle. High levels in neonatal spleen and thymus with low levels in other tissues. In adult, highly expressed in testis. Barely detectable in other tissues.

    Developmental stagei

    Highly expressed in fetal tissues. Expression markedly decreased in adult.

    Gene expression databases

    BgeeiQ64701.
    CleanExiMM_RBL1.
    GenevestigatoriQ64701.

    Interactioni

    Subunit structurei

    Interacts with AATF. Interacts with KDM5A. 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 By similarity. Interacts with SUV420H1, SUV420H2 and USP4.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CenpfQ155P73EBI-1213109,EBI-2211248

    Protein-protein interaction databases

    BioGridi202819. 6 interactions.
    IntActiQ64701. 3 interactions.
    STRINGi10090.ENSMUSP00000029170.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64701.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni383 – 944562Pocket; binds T and E1AAdd
    BLAST
    Regioni383 – 584202Domain AAdd
    BLAST
    Regioni585 – 779195SpacerAdd
    BLAST
    Regioni780 – 944165Domain BAdd
    BLAST

    Sequence similaritiesi

    Belongs to the retinoblastoma protein (RB) family.Curated

    Phylogenomic databases

    eggNOGiNOG296920.
    GeneTreeiENSGT00530000063235.
    HOGENOMiHOG000273892.
    HOVERGENiHBG017710.
    InParanoidiQ3U1D4.
    KOiK04681.
    OMAiRRDMQPL.
    OrthoDBiEOG7P5T04.
    TreeFamiTF105568.

    Family and domain databases

    Gene3Di1.10.472.10. 3 hits.
    InterProiIPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    IPR028310. RBL1.
    [Graphical view]
    PANTHERiPTHR13742. PTHR13742. 1 hit.
    PTHR13742:SF20. PTHR13742:SF20. 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. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q64701-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFEDEPHAEG AAAVAAAREA LQALCQELNL DEGSAAEALD DFTAIRGNYS     50
    LEGEVIHWLA CSLYVACRKS IIPTVGKGVM EGNCVSLTRI LRSAKLSLIQ 100
    FFSKMKKWMD MSNLPQEFRE RIERLERNFE VSTVIFKKFE PIFLDIFQNP 150
    YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL FVYTKGNFRM IGDDLVNSYH 200
    LLLCCLDLIF ANAIMCPNRR DLLNPSFKGL PSDFHAPDFK AAEEPPCIIA 250
    VLCDLHDGLL VEAKGIKEHY FKPYISKLFD KKILKGECLL DLSSFTDNSK 300
    AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTADT PFGKLTSQAS 350
    VECNLQQHFE KKRSFAPSTP LTGRRYLQEK EAVTTPVASA TQSVSRLQSI 400
    VAGLKSAPSE QLLNIFESCM RNPMGNIIKI VKGIGETFCQ HYTQSTDKQP 450
    GSHIDFAVNR LKLAEILYYK ILETIMVQET RRLHGMDMSV LLEQDIFHKS 500
    LMACCLEIVL FAYSSPRTFP WIIEVLDLQP FYFYKVIEVV IRSEEGLSRD 550
    MVKHLNSIEE QILESLAWTN NSALWEALHA SANRVPSCEE VIFPNNFEIG 600
    NGGNVQGHLP MMPMSPIIHP RVKEVRTDSG SLRQDMQPLS PISVHERYSS 650
    PAAGSAKRRL FGDDPPKDTL MDKIMAEGTK LKIAPSSVTA ESLSISPGQA 700
    LLTMATTTVT GTTGRKVTVP LHGIANDAGE ITLVPISMNP TQESTAESPV 750
    SLTAQSLIGT SPKQTHLTKA QDAHLTGVSK PKRTGSLALF YRKVYHLASV 800
    RLRDLCLKLD VSNELRRKIW TCFEFTLVHC PDLMKDRHLD QLLLCAFYIM 850
    AKVTKEERTF QEIMKSYRNQ PQANSHVYRS VLLKSIPGGV VVYNGDCEMT 900
    DGDIEDATKT PNCSSEPVKE ERGDLIKFYN TVYVGRVKSF ALKYDLSNQD 950
    HIMDAPPLSP FPHIKQQPGS PRRISQQHSL YVSPHKNGAG LTPRSALLYK 1000
    FNGSPSKSLK DINNMIRQGE QKTKKRVIAI SGDADSPAKR LCQENDDVLL 1050
    KRLQDVVSER ANH 1063
    Length:1,063
    Mass (Da):119,456
    Last modified:July 27, 2011 - v3
    Checksum:i85BEA8EC064EC06E
    GO
    Isoform Short (identifier: Q64701-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         592-594: IFP → SQG
         595-1063: Missing.

    Show »
    Length:594
    Mass (Da):67,497
    Checksum:i264EAF692D791D03
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261Q → P in AAB18279. (PubMed:8661722)Curated
    Sequence conflicti430 – 4301I → T in AAB18279. (PubMed:8661722)Curated
    Sequence conflicti863 – 8631I → R in AAB53235. (PubMed:7490090)Curated
    Sequence conflicti989 – 9891A → C in AAB18279. (PubMed:8661722)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei592 – 5943IFP → SQG in isoform Short. 1 PublicationVSP_005537
    Alternative sequencei595 – 1063469Missing in isoform Short. 1 PublicationVSP_005538Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33320 mRNA. Translation: AAB18279.1.
    U27177 mRNA. Translation: AAB53235.1.
    U27178 mRNA. Translation: AAB53236.1.
    AK156055 mRNA. Translation: BAE33564.1.
    AL669828 Genomic DNA. Translation: CAM15973.1.
    CCDSiCCDS16974.1. [Q64701-1]
    PIRiI49328.
    RefSeqiNP_001132988.1. NM_001139516.1. [Q64701-2]
    NP_035379.2. NM_011249.2. [Q64701-1]
    UniGeneiMm.244671.

    Genome annotation databases

    EnsembliENSMUST00000029170; ENSMUSP00000029170; ENSMUSG00000027641. [Q64701-1]
    GeneIDi19650.
    KEGGimmu:19650.
    UCSCiuc008noq.2. mouse. [Q64701-1]
    uc008nos.2. mouse. [Q64701-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33320 mRNA. Translation: AAB18279.1 .
    U27177 mRNA. Translation: AAB53235.1 .
    U27178 mRNA. Translation: AAB53236.1 .
    AK156055 mRNA. Translation: BAE33564.1 .
    AL669828 Genomic DNA. Translation: CAM15973.1 .
    CCDSi CCDS16974.1. [Q64701-1 ]
    PIRi I49328.
    RefSeqi NP_001132988.1. NM_001139516.1. [Q64701-2 ]
    NP_035379.2. NM_011249.2. [Q64701-1 ]
    UniGenei Mm.244671.

    3D structure databases

    ProteinModelPortali Q64701.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202819. 6 interactions.
    IntActi Q64701. 3 interactions.
    STRINGi 10090.ENSMUSP00000029170.

    PTM databases

    PhosphoSitei Q64701.

    Proteomic databases

    MaxQBi Q64701.
    PaxDbi Q64701.
    PRIDEi Q64701.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029170 ; ENSMUSP00000029170 ; ENSMUSG00000027641 . [Q64701-1 ]
    GeneIDi 19650.
    KEGGi mmu:19650.
    UCSCi uc008noq.2. mouse. [Q64701-1 ]
    uc008nos.2. mouse. [Q64701-2 ]

    Organism-specific databases

    CTDi 5933.
    MGIi MGI:103300. Rbl1.

    Phylogenomic databases

    eggNOGi NOG296920.
    GeneTreei ENSGT00530000063235.
    HOGENOMi HOG000273892.
    HOVERGENi HBG017710.
    InParanoidi Q3U1D4.
    KOi K04681.
    OMAi RRDMQPL.
    OrthoDBi EOG7P5T04.
    TreeFami TF105568.

    Enzyme and pathway databases

    Reactomei REACT_199110. G0 and Early G1.
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

    Miscellaneous databases

    NextBioi 296908.
    PROi Q64701.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q64701.
    CleanExi MM_RBL1.
    Genevestigatori Q64701.

    Family and domain databases

    Gene3Di 1.10.472.10. 3 hits.
    InterProi IPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    IPR028310. RBL1.
    [Graphical view ]
    PANTHERi PTHR13742. PTHR13742. 1 hit.
    PTHR13742:SF20. PTHR13742:SF20. 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. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, chromosomal mapping, and expression of the mouse p107 gene."
      Huppi K., Siwarski D., Mock B.A., Dosik J., Hamel P.A.
      Mamm. Genome 7:353-355(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. "Developmental expression of p107 mRNA and evidence for alternative splicing of the p107 (RBL1) gene product."
      Kim K.K., Soonpaa M.H., Wang H., Field L.J.
      Genomics 28:520-529(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    3. Kim K.K., Soonpaa M.H., Wang H., Field L.J.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    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: NOD.
      Tissue: Spleen.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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. "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.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiRBL1_MOUSE
    AccessioniPrimary (citable) accession number: Q64701
    Secondary accession number(s): Q3U1D4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 127 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