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Q13185

- CBX3_HUMAN

UniProt

Q13185 - CBX3_HUMAN

Protein

Chromobox protein homolog 3

Gene

CBX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the mehtyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1.

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. histone methyltransferase binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. protein binding Source: UniProtKB
    5. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. chromatin remodeling Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. rhythmic process Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_2204. RNA Polymerase I Chain Elongation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromobox protein homolog 3
    Alternative name(s):
    HECH
    Heterochromatin protein 1 homolog gamma
    Short name:
    HP1 gamma
    Modifier 2 protein
    Gene namesi
    Name:CBX3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1553. CBX3.

    Subcellular locationi

    Nucleus Curated
    Note: Associates with euchromatin and is largely excluded from constitutive heterochromatin. May be associated with microtubules and mitotic poles during mitosis Potential.Curated

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. condensed chromosome, centromeric region Source: UniProtKB
    3. nuclear envelope Source: UniProtKB
    4. nuclear euchromatin Source: UniProtKB
    5. nuclear heterochromatin Source: UniProtKB
    6. nuclear inner membrane Source: UniProtKB
    7. nuclear pericentric heterochromatin Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26128.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 183182Chromobox protein homolog 3PRO_0000080203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei5 – 51N6-acetyllysineBy similarity
    Modified residuei10 – 101N6-acetyllysine1 Publication
    Modified residuei44 – 441N6-acetyllysine1 Publication
    Modified residuei50 – 501N6-acetyllysine1 Publication
    Modified residuei93 – 931Phosphoserine3 Publications
    Modified residuei95 – 951Phosphoserine3 Publications
    Modified residuei97 – 971Phosphoserine1 Publication
    Modified residuei99 – 991Phosphoserine1 Publication
    Modified residuei176 – 1761Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13185.
    PaxDbiQ13185.
    PeptideAtlasiQ13185.
    PRIDEiQ13185.

    2D gel databases

    SWISS-2DPAGEQ13185.

    PTM databases

    PhosphoSiteiQ13185.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13185.
    BgeeiQ13185.
    CleanExiHS_CBX3.
    GenevestigatoriQ13185.

    Organism-specific databases

    HPAiCAB001973.
    HPA004902.

    Interactioni

    Subunit structurei

    Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9'. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with LBR, INCENP, TRIM28/TIF1B, SUV420H1, SUV420H2 and SP100. Interacts with TIF1A. Interacts with MIS12 and DSN1. Can interact directly with CBX5 via the chromoshadow domain. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-78176,EBI-78176
    ADNPQ9H2P02EBI-78176,EBI-1764854
    HIST1H3DP684315EBI-78176,EBI-79722
    LBRQ147394EBI-78176,EBI-1055147
    legAS4Q5ZUS42EBI-78176,EBI-8871796From a different organism.
    SUV420H2Q86Y972EBI-78176,EBI-7960569
    TRIM28Q132633EBI-78176,EBI-78139

    Protein-protein interaction databases

    BioGridi116463. 93 interactions.
    DIPiDIP-5985N.
    IntActiQ13185. 50 interactions.
    MINTiMINT-5002782.
    STRINGi9606.ENSP00000336687.

    Structurei

    Secondary structure

    1
    183
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 4113
    Beta strandi44 – 518
    Helixi56 – 583
    Beta strandi60 – 634
    Helixi64 – 663
    Helixi70 – 8011
    Helixi116 – 1194
    Beta strandi123 – 1308
    Beta strandi137 – 1426
    Beta strandi149 – 1524
    Helixi153 – 1597
    Helixi161 – 17111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L11NMR-A29-81[»]
    3DM1X-ray2.40A/C/E/G29-86[»]
    3KUPX-ray1.77A/B/C/D110-173[»]
    3TZDX-ray1.81A29-81[»]
    ProteinModelPortaliQ13185.
    SMRiQ13185. Positions 29-81, 112-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13185.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 8859Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini121 – 17959Chromo 2; shadow subtypePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 chromo domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG264487.
    HOGENOMiHOG000220852.
    HOVERGENiHBG000400.
    InParanoidiQ13185.
    KOiK11586.
    OMAiRESADKP.
    OrthoDBiEOG7QRQWW.
    PhylomeDBiQ13185.
    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.

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

    Q13185-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK    50
    WKGFTDADNT WEPEENLDCP ELIEAFLNSQ KAGKEKDGTK RKSLSDSESD 100
    DSKSKKKRDA ADKPRGFARG LDPERIIGAT DSSGELMFLM KWKDSDEADL 150
    VLAKEANMKC PQIVIAFYEE RLTWHSCPED EAQ 183
    Length:183
    Mass (Da):20,811
    Last modified:October 17, 2006 - v4
    Checksum:i5928C63E0C93A76A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111A → G in AAH14380. (PubMed:15489334)Curated
    Sequence conflicti111 – 1111A → V in AAF62370. 1 PublicationCurated
    Sequence conflicti130 – 1301T → I in AAB48101. (PubMed:8663349)Curated
    Sequence conflicti130 – 1301T → I in BAA83340. (PubMed:10664448)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26312 mRNA. Translation: AAB48101.1.
    AB030905 mRNA. Translation: BAA83340.1.
    AF136630 mRNA. Translation: AAF62370.1.
    BC000954 mRNA. Translation: AAH00954.1.
    BC014380 mRNA. Translation: AAH14380.1.
    CCDSiCCDS5398.1.
    RefSeqiNP_009207.2. NM_007276.4.
    NP_057671.2. NM_016587.3.
    XP_005249668.1. XM_005249611.1.
    UniGeneiHs.381189.

    Genome annotation databases

    EnsembliENST00000337620; ENSP00000336687; ENSG00000122565.
    ENST00000396386; ENSP00000379670; ENSG00000122565.
    GeneIDi11335.
    KEGGihsa:11335.
    UCSCiuc003sxt.3. human.

    Polymorphism databases

    DMDMi116241284.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26312 mRNA. Translation: AAB48101.1 .
    AB030905 mRNA. Translation: BAA83340.1 .
    AF136630 mRNA. Translation: AAF62370.1 .
    BC000954 mRNA. Translation: AAH00954.1 .
    BC014380 mRNA. Translation: AAH14380.1 .
    CCDSi CCDS5398.1.
    RefSeqi NP_009207.2. NM_007276.4.
    NP_057671.2. NM_016587.3.
    XP_005249668.1. XM_005249611.1.
    UniGenei Hs.381189.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L11 NMR - A 29-81 [» ]
    3DM1 X-ray 2.40 A/C/E/G 29-86 [» ]
    3KUP X-ray 1.77 A/B/C/D 110-173 [» ]
    3TZD X-ray 1.81 A 29-81 [» ]
    ProteinModelPortali Q13185.
    SMRi Q13185. Positions 29-81, 112-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116463. 93 interactions.
    DIPi DIP-5985N.
    IntActi Q13185. 50 interactions.
    MINTi MINT-5002782.
    STRINGi 9606.ENSP00000336687.

    PTM databases

    PhosphoSitei Q13185.

    Polymorphism databases

    DMDMi 116241284.

    2D gel databases

    SWISS-2DPAGE Q13185.

    Proteomic databases

    MaxQBi Q13185.
    PaxDbi Q13185.
    PeptideAtlasi Q13185.
    PRIDEi Q13185.

    Protocols and materials databases

    DNASUi 11335.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337620 ; ENSP00000336687 ; ENSG00000122565 .
    ENST00000396386 ; ENSP00000379670 ; ENSG00000122565 .
    GeneIDi 11335.
    KEGGi hsa:11335.
    UCSCi uc003sxt.3. human.

    Organism-specific databases

    CTDi 11335.
    GeneCardsi GC07P026207.
    HGNCi HGNC:1553. CBX3.
    HPAi CAB001973.
    HPA004902.
    MIMi 604477. gene.
    neXtProti NX_Q13185.
    PharmGKBi PA26128.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264487.
    HOGENOMi HOG000220852.
    HOVERGENi HBG000400.
    InParanoidi Q13185.
    KOi K11586.
    OMAi RESADKP.
    OrthoDBi EOG7QRQWW.
    PhylomeDBi Q13185.
    TreeFami TF350503.

    Enzyme and pathway databases

    Reactomei REACT_2204. RNA Polymerase I Chain Elongation.

    Miscellaneous databases

    ChiTaRSi CBX3. human.
    EvolutionaryTracei Q13185.
    GeneWikii CBX3.
    GenomeRNAii 11335.
    NextBioi 43065.
    PROi Q13185.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13185.
    Bgeei Q13185.
    CleanExi HS_CBX3.
    Genevestigatori Q13185.

    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. "Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1."
      Ye Q., Worman H.J.
      J. Biol. Chem. 271:14653-14656(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-183.
    2. Ye Q., Worman H.J.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1."
      Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.
      FEBS Lett. 467:17-21(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-183, PHOSPHORYLATION BY PIM1.
    4. Chen J.H., Luo W.Q., Hu S.N., Zhou H.J., Huang X.W., Zhou Y., Yuan J.G., Qiang B.Q.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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].
      Tissue: Bone marrow and Placenta.
    6. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 160-171, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    7. "Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR."
      Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.
      J. Biol. Chem. 272:14983-14989(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LBR AND CBX5.
    8. "INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1."
      Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C.
      J. Cell Biol. 143:1763-1774(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INCENP.
    9. "Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment."
      Seeler J.-S., Marchio A., Sitterlin D., Transy C., Dejean A.
      Proc. Natl. Acad. Sci. U.S.A. 95:7316-7321(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SP100.
    10. "Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells."
      Minc E., Allory Y., Worman H.J., Courvalin J.-C., Buendia B.
      Chromosoma 108:220-234(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    11. "KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Kruppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing."
      Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R., Fredericks W.J., Rauscher F.J. III
      Mol. Cell. Biol. 19:4366-4378(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM28.
    12. "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.
    13. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
      Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
      Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; EUHMTASE1; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
    14. "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1."
      Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.
      Nat. Cell Biol. 6:1135-1141(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIS12 AND DSN1.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-44 AND LYS-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
      Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
      Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHAMP1 AND POGZ.
    22. "ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1."
      Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.
      J. Biol. Chem. 285:18-29(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASXL1.
    23. "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
      Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
      Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POGZ.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; SER-97 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Crystal structure of the complex of chromobox homolog 3 (CBX3) [Homo sapiens] and peptide."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-86 IN COMPLEX WITH PEPTIDE.

    Entry informationi

    Entry nameiCBX3_HUMAN
    AccessioniPrimary (citable) accession number: Q13185
    Secondary accession number(s): Q96CD7
    , Q99409, Q9BVS3, Q9P0Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3