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P83917

- CBX1_MOUSE

UniProt

P83917 - CBX1_MOUSE

Protein

Chromobox protein homolog 1

Gene

Cbx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211Histone H3K9me2
    Binding sitei23 – 231Histone H3A7
    Binding sitei40 – 401Histone H3A7
    Binding sitei42 – 421Histone H3A7
    Binding sitei42 – 421Histone H3K9me2
    Binding sitei45 – 451Histone H3K9me2
    Binding sitei58 – 581Histone H3A7
    Binding sitei60 – 601Histone H3A7
    Binding sitei125 – 1251PxVxL motif
    Binding sitei126 – 1261PxVxL motif
    Binding sitei135 – 1351PxVxL motif
    Binding sitei146 – 1461PxVxL motif
    Binding sitei163 – 1631PxVxL motif
    Binding sitei167 – 1671PxVxL motif
    Binding sitei168 – 1681PxVxL motif
    Binding sitei170 – 1701PxVxL motif

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromobox protein homolog 1
    Alternative name(s):
    Heterochromatin protein 1 homolog beta
    Short name:
    HP1 beta
    Heterochromatin protein p25
    M31
    Modifier 1 protein
    Gene namesi
    Name:Cbx1
    Synonyms:Cbx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:105369. Cbx1.

    Subcellular locationi

    Nucleus By similarity
    Note: Unassociated with chromosomes during mitosis.By similarity

    GO - Cellular componenti

    1. chromatin Source: MGI
    2. chromocenter Source: MGI
    3. female pronucleus Source: MGI
    4. male pronucleus Source: MGI
    5. pericentric heterochromatin Source: MGI
    6. spindle Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231V → M: Abolishes interaction with SUV39H1. 2 Publications
    Mutagenesisi26 – 261V → R: Abolishes interaction with SUV39H1. 2 Publications
    Mutagenesisi161 – 1611I → E: Abolishes homodimer formation. 1 Publication
    Mutagenesisi164 – 1641Y → E: Abolishes homodimer formation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185Chromobox protein homolog 1PRO_0000080200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei89 – 891PhosphoserineBy similarity
    Modified residuei91 – 911PhosphoserineBy similarity
    Modified residuei175 – 1751PhosphoserineBy similarity

    Post-translational modificationi

    Not phosphorylated.By similarity
    Ubiquitinated.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP83917.
    PaxDbiP83917.
    PRIDEiP83917.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00129466.

    PTM databases

    PhosphoSiteiP83917.

    Expressioni

    Tissue specificityi

    In all adult and embryonic tissues.1 Publication

    Gene expression databases

    ArrayExpressiP83917.
    BgeeiP83917.
    CleanExiMM_CBX1.
    GenevestigatoriP83917.

    Interactioni

    Subunit structurei

    Homodimer. Interacts directly with CHAF1A, EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the chromoshadow domain. Interacts directly with histone H3 methylated at 'Lys-9' via the chromo domain. Interacts with SUV39H1, SETDB1, SUV420H1 and SUV420H2. Interacts with PRDM6. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-78119,EBI-78119
    Chaf1aQ9QWF03EBI-78119,EBI-639217
    Hist1h3iP684336EBI-78119,EBI-79743
    Trim24Q641274EBI-78119,EBI-307947

    Protein-protein interaction databases

    BioGridi198534. 38 interactions.
    DIPiDIP-30892N.
    IntActiP83917. 37 interactions.
    MINTiMINT-191134.

    Structurei

    Secondary structure

    1
    185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 133
    Beta strandi22 – 3110
    Beta strandi33 – 4715
    Beta strandi51 – 544
    Turni55 – 573
    Helixi61 – 677
    Turni68 – 725
    Turni75 – 773
    Beta strandi104 – 1074
    Helixi112 – 1154
    Beta strandi125 – 13410
    Beta strandi141 – 1433
    Beta strandi145 – 1484
    Helixi149 – 1557
    Helixi157 – 16610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AP0NMR-A10-80[»]
    1DZ1NMR-A/B104-171[»]
    1GUWNMR-A10-80[»]
    1S4ZNMR-A/B104-176[»]
    ProteinModelPortaliP83917.
    SMRiP83917. Positions 27-80, 110-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP83917.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 7959Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini117 – 17559Chromo 2; shadow subtypePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 chromo domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG264487.
    GeneTreeiENSGT00510000046310.
    HOGENOMiHOG000220852.
    HOVERGENiHBG000400.
    InParanoidiP83917.
    KOiK11585.
    OMAiCEVIRAC.
    OrthoDBiEOG7QRQWW.
    PhylomeDBiP83917.
    TreeFamiTF350503.

    Family and domain databases

    InterProiIPR017984. Chromo_dom_subgr.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR008251. Chromo_shadow_dom.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    [Graphical view]
    PfamiPF00385. Chromo. 1 hit.
    PF01393. Chromo_shadow. 1 hit.
    [Graphical view]
    PRINTSiPR00504. CHROMODOMAIN.
    SMARTiSM00298. CHROMO. 2 hits.
    SM00300. ChSh. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 2 hits.
    PROSITEiPS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P83917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN    50
    TWEPEENLDC PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP 100
    KKKKEESEKP RGFARGLEPE RIIGATDSSG ELMFLMKWKN SDEADLVPAK 150
    EANVKCPQVV ISFYEERLTW HSYPSEDDDK KDDKN 185
    Length:185
    Mass (Da):21,418
    Last modified:June 7, 2004 - v1
    Checksum:iBE687AF9C66E48E3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56690 mRNA. Translation: CAA40018.1.
    AK014215 mRNA. Translation: BAB29211.1.
    CCDSiCCDS25303.1.
    PIRiS26847.
    RefSeqiNP_031648.1. NM_007622.3.
    XP_006532162.1. XM_006532099.1.
    XP_006532163.1. XM_006532100.1.
    UniGeneiMm.29055.

    Genome annotation databases

    EnsembliENSMUST00000093943; ENSMUSP00000091475; ENSMUSG00000018666.
    GeneIDi12412.
    KEGGimmu:12412.
    UCSCiuc007lck.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56690 mRNA. Translation: CAA40018.1 .
    AK014215 mRNA. Translation: BAB29211.1 .
    CCDSi CCDS25303.1.
    PIRi S26847.
    RefSeqi NP_031648.1. NM_007622.3.
    XP_006532162.1. XM_006532099.1.
    XP_006532163.1. XM_006532100.1.
    UniGenei Mm.29055.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AP0 NMR - A 10-80 [» ]
    1DZ1 NMR - A/B 104-171 [» ]
    1GUW NMR - A 10-80 [» ]
    1S4Z NMR - A/B 104-176 [» ]
    ProteinModelPortali P83917.
    SMRi P83917. Positions 27-80, 110-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198534. 38 interactions.
    DIPi DIP-30892N.
    IntActi P83917. 37 interactions.
    MINTi MINT-191134.

    PTM databases

    PhosphoSitei P83917.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00129466.

    Proteomic databases

    MaxQBi P83917.
    PaxDbi P83917.
    PRIDEi P83917.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000093943 ; ENSMUSP00000091475 ; ENSMUSG00000018666 .
    GeneIDi 12412.
    KEGGi mmu:12412.
    UCSCi uc007lck.1. mouse.

    Organism-specific databases

    CTDi 10951.
    MGIi MGI:105369. Cbx1.

    Phylogenomic databases

    eggNOGi NOG264487.
    GeneTreei ENSGT00510000046310.
    HOGENOMi HOG000220852.
    HOVERGENi HBG000400.
    InParanoidi P83917.
    KOi K11585.
    OMAi CEVIRAC.
    OrthoDBi EOG7QRQWW.
    PhylomeDBi P83917.
    TreeFami TF350503.

    Miscellaneous databases

    ChiTaRSi CBX1. mouse.
    EvolutionaryTracei P83917.
    NextBioi 281200.
    PROi P83917.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P83917.
    Bgeei P83917.
    CleanExi MM_CBX1.
    Genevestigatori P83917.

    Family and domain databases

    InterProi IPR017984. Chromo_dom_subgr.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR008251. Chromo_shadow_dom.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    [Graphical view ]
    Pfami PF00385. Chromo. 1 hit.
    PF01393. Chromo_shadow. 1 hit.
    [Graphical view ]
    PRINTSi PR00504. CHROMODOMAIN.
    SMARTi SM00298. CHROMO. 2 hits.
    SM00300. ChSh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 2 hits.
    PROSITEi PS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants."
      Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R., James T.C., Gaunt S.J.
      Nucleic Acids Res. 19:789-794(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DOMAIN.
      Strain: C57BL/6.
      Tissue: Embryo.
    2. "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.
      Tissue: Head.
    3. "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
      le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
      EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIF1A.
    4. "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31."
      Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.
      EMBO J. 18:1923-1938(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUV39H1.
    5. "Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family."
      Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R., Gansmuller A., Chambon P., Losson R.
      EMBO J. 18:6385-6395(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM28.
    6. "Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1."
      Polioudaki H., Kourmouli N., Drosou V., Bakou A., Theodoropoulos P.A., Singh P.B., Giannakouros T., Georgatos S.D.
      EMBO Rep. 2:920-925(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HISTONE H3 AND LBR.
    7. "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins."
      Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.
      Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HISTONE H3 LYS-9, MUTAGENESIS OF VAL-23 AND VAL-26.
    8. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
      Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
      Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUV420H1 AND SUV420H2.
    9. "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells."
      Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.
      Mol. Cell. Biol. 26:2626-2636(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRDM6.
    10. "Structure of the chromatin binding (chromo) domain from mouse modifier protein 1."
      Ball L.J., Murzina N.V., Broadhurst R.W., Raine A.R., Archer S.J., Stott F.J., Murzin A.G., Singh P.B., Domaille P.J., Laue E.D.
      EMBO J. 16:2473-2481(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 10-80.
    11. "The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer."
      Brasher S.V., Smith B.O., Fogh R.H., Nietlispach D., Thiru A., Nielsen P.R., Broadhurst R.W., Ball L.J., Murzina N.V., Laue E.D.
      EMBO J. 19:1587-1597(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 104-171, SUBUNIT, INTERACTION WITH CHAF1A AND TRIM28, MUTAGENESIS.
    12. "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9."
      Nielsen P.R., Nietlispach D., Mott H.R., Callaghan J., Bannister A., Kouzarides T., Murzin A.G., Murzina N.V., Laue E.D.
      Nature 416:103-107(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 10-80.
    13. "Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin."
      Thiru A., Nietlispach D., Mott H.R., Okuwaki M., Lyon D., Nielsen P.R., Hirshberg M., Verreault A., Murzina N.V., Laue E.D.
      EMBO J. 23:489-499(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 104-175, SUBUNIT, INTERACTION WITH CHAF1A.

    Entry informationi

    Entry nameiCBX1_MOUSE
    AccessioniPrimary (citable) accession number: P83917
    Secondary accession number(s): P23197
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3