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P45973

- CBX5_HUMAN

UniProt

P45973 - CBX5_HUMAN

Protein

Chromobox protein homolog 5

Gene

CBX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins.1 Publication

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. methylated histone binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein binding, bridging Source: BHF-UCL
    5. repressing transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromobox protein homolog 5
    Alternative name(s):
    Antigen p25
    Heterochromatin protein 1 homolog alpha
    Short name:
    HP1 alpha
    Gene namesi
    Name:CBX5
    Synonyms:HP1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1555. CBX5.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication. Chromosomecentromere 1 Publication
    Note: Component of centromeric and pericentromeric heterochromatin. Associates with chromosomes during mitosis. Associates specifically with chromatin during metaphase and anaphase.

    GO - Cellular componenti

    1. chromocenter Source: Ensembl
    2. histone deacetylase complex Source: BHF-UCL
    3. histone methyltransferase complex Source: BHF-UCL
    4. kinetochore Source: Ensembl
    5. nuclear envelope Source: ProtInc
    6. nuclear heterochromatin Source: ProtInc
    7. nuclear pericentric heterochromatin Source: BHF-UCL
    8. nucleolus Source: BHF-UCL
    9. nucleoplasm Source: Reactome
    10. nucleus Source: UniProtKB
    11. transcriptional repressor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651I → E: No effect on interaction with POGZ. Abolishes interaction with TRIM28, CHAF1A and NIPBL. 1 Publication
    Mutagenesisi174 – 1741W → A: Abolishes interaction with TRIM28, CHAF1A and NIPBL. 1 Publication

    Organism-specific databases

    PharmGKBiPA26130.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 191191Chromobox protein homolog 5PRO_0000080208Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine4 Publications
    Modified residuei12 – 121Phosphoserine3 Publications
    Modified residuei13 – 131Phosphoserine5 Publications
    Modified residuei14 – 141Phosphoserine5 Publications
    Modified residuei92 – 921Phosphoserine5 Publications
    Modified residuei95 – 951Phosphoserine2 Publications
    Modified residuei97 – 971Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylation of HP1 and LBR may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle By similarity. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis.By similarity6 Publications
    Ubiquitinated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP45973.
    PaxDbiP45973.
    PeptideAtlasiP45973.
    PRIDEiP45973.

    PTM databases

    PhosphoSiteiP45973.

    Expressioni

    Gene expression databases

    ArrayExpressiP45973.
    BgeeiP45973.
    CleanExiHS_CBX5.
    GenevestigatoriP45973.

    Organism-specific databases

    HPAiCAB017548.
    HPA016699.

    Interactioni

    Subunit structurei

    Interacts with SUV420H1 and SUV420H2 By similarity. Interacts with HP1BP3 By similarity. Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100, STAM2 and TRIM28 via the chromoshadow domain. Can interact directly with CBX3 via the chromoshadow domain. Interacts with histone H3 methylated at 'Lys-9'. Interacts with BAHD1, MIS12 and DSN1. Interacts with POGZ; POGZ and PXVXL motif-containing proteins such as INCENP and TRIM28 compete for interaction with CBX5. Interacts with INCENP and TRIM24. Interacts with JC virus agnoprotein; this interaction induces the dissociation of CBX5 from LBR, resulting in destabilization of the nuclear envelope. Interacts with CHAMP1. Interacts with ASXL1.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADNPQ9H2P02EBI-78219,EBI-1764854
    ASXL1Q8IXJ92EBI-78219,EBI-1646500
    Asxl1P595985EBI-78219,EBI-5743705From a different organism.
    ATRXP461002EBI-78219,EBI-396461
    CHAF1AQ131117EBI-78219,EBI-1020839
    H3F3BP842432EBI-78219,EBI-120658
    HIST1H3DP684319EBI-78219,EBI-79722
    INCENPQ9NQS76EBI-78219,EBI-307907
    LBRQ147394EBI-78219,EBI-1055147
    legAS4Q5ZUS46EBI-78219,EBI-8871796From a different organism.
    MBD1Q9UIS96EBI-78219,EBI-867196
    POGZQ7Z3K36EBI-78219,EBI-1389308
    SENP7Q9BQF62EBI-78219,EBI-766251
    SUV39H1O434633EBI-78219,EBI-349968
    TRIM28Q132639EBI-78219,EBI-78139

    Protein-protein interaction databases

    BioGridi117030. 147 interactions.
    DIPiDIP-5986N.
    IntActiP45973. 125 interactions.
    MINTiMINT-1178082.
    STRINGi9606.ENSP00000209875.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 3113
    Beta strandi34 – 418
    Helixi46 – 483
    Beta strandi50 – 534
    Helixi54 – 563
    Helixi60 – 678
    Helixi116 – 1194
    Beta strandi123 – 1308
    Beta strandi137 – 1426
    Beta strandi148 – 1525
    Helixi153 – 1597
    Helixi161 – 1688

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FDTX-ray2.00A18-75[»]
    3I3CX-ray2.48A/B/C/D110-173[»]
    ProteinModelPortaliP45973.
    SMRiP45973. Positions 18-68, 112-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45973.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 7859Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini121 – 17959Chromo 2; shadow subtypePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni116 – 19176Interaction with ASXL1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 144Poly-Ser

    Sequence similaritiesi

    Contains 2 chromo domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG132879.
    HOGENOMiHOG000220852.
    HOVERGENiHBG000400.
    InParanoidiP45973.
    KOiK11587.
    OMAiSEFMKTY.
    OrthoDBiEOG7QRQWW.
    PhylomeDBiP45973.
    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.

    P45973-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT    50
    WEPEKNLDCP ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD 100
    IKSKKKREQS NDIARGFERG LEPEKIIGAT DSCGDLMFLM KWKDTDEADL 150
    VLAKEANVKC PQIVIAFYEE RLTWHAYPED AENKEKETAK S 191
    Length:191
    Mass (Da):22,225
    Last modified:November 1, 1995 - v1
    Checksum:i16FFC476367093B1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S62077 mRNA. Translation: AAB26994.1.
    L07515 mRNA. Translation: AAA72327.1.
    AK313506 mRNA. Translation: BAG36286.1.
    CH471054 Genomic DNA. Translation: EAW96759.1.
    BC006821 mRNA. Translation: AAH06821.1.
    U26311 mRNA. Translation: AAC50553.1.
    CCDSiCCDS8875.1.
    PIRiG01808.
    RefSeqiNP_001120793.1. NM_001127321.1.
    NP_001120794.1. NM_001127322.1.
    NP_036249.1. NM_012117.2.
    UniGeneiHs.349283.

    Genome annotation databases

    EnsembliENST00000209875; ENSP00000209875; ENSG00000094916.
    ENST00000439541; ENSP00000401009; ENSG00000094916.
    ENST00000550411; ENSP00000449207; ENSG00000094916.
    GeneIDi23468.
    KEGGihsa:23468.
    UCSCiuc001sfh.4. human.

    Polymorphism databases

    DMDMi1170338.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S62077 mRNA. Translation: AAB26994.1 .
    L07515 mRNA. Translation: AAA72327.1 .
    AK313506 mRNA. Translation: BAG36286.1 .
    CH471054 Genomic DNA. Translation: EAW96759.1 .
    BC006821 mRNA. Translation: AAH06821.1 .
    U26311 mRNA. Translation: AAC50553.1 .
    CCDSi CCDS8875.1.
    PIRi G01808.
    RefSeqi NP_001120793.1. NM_001127321.1.
    NP_001120794.1. NM_001127322.1.
    NP_036249.1. NM_012117.2.
    UniGenei Hs.349283.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FDT X-ray 2.00 A 18-75 [» ]
    3I3C X-ray 2.48 A/B/C/D 110-173 [» ]
    ProteinModelPortali P45973.
    SMRi P45973. Positions 18-68, 112-170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117030. 147 interactions.
    DIPi DIP-5986N.
    IntActi P45973. 125 interactions.
    MINTi MINT-1178082.
    STRINGi 9606.ENSP00000209875.

    PTM databases

    PhosphoSitei P45973.

    Polymorphism databases

    DMDMi 1170338.

    Proteomic databases

    MaxQBi P45973.
    PaxDbi P45973.
    PeptideAtlasi P45973.
    PRIDEi P45973.

    Protocols and materials databases

    DNASUi 23468.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000209875 ; ENSP00000209875 ; ENSG00000094916 .
    ENST00000439541 ; ENSP00000401009 ; ENSG00000094916 .
    ENST00000550411 ; ENSP00000449207 ; ENSG00000094916 .
    GeneIDi 23468.
    KEGGi hsa:23468.
    UCSCi uc001sfh.4. human.

    Organism-specific databases

    CTDi 23468.
    GeneCardsi GC12M054624.
    HGNCi HGNC:1555. CBX5.
    HPAi CAB017548.
    HPA016699.
    MIMi 604478. gene.
    neXtProti NX_P45973.
    PharmGKBi PA26130.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG132879.
    HOGENOMi HOG000220852.
    HOVERGENi HBG000400.
    InParanoidi P45973.
    KOi K11587.
    OMAi SEFMKTY.
    OrthoDBi EOG7QRQWW.
    PhylomeDBi P45973.
    TreeFami TF350503.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi CBX5. human.
    EvolutionaryTracei P45973.
    GeneWikii CBX5_(gene).
    GenomeRNAii 23468.
    NextBioi 45793.
    PROi P45973.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45973.
    Bgeei P45973.
    CleanExi HS_CBX5.
    Genevestigatori P45973.

    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. "Molecular cloning of a human homologue of Drosophila heterochromatin protein HP1 using anti-centromere autoantibodies with anti-chromo specificity."
      Saunders W.S., Chue C., Goebl M., Craig C., Clark R.F., Powers J.A., Eissenberg J.C., Elgin S.C.R., Rothfield N.F., Earnshaw W.C.
      J. Cell Sci. 104:573-582(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Placenta.
    5. "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 2-191.
    6. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-40; 56-68; 126-154 AND 160-184, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    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 CBX3.
    8. "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.
    9. "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor: role of SUMO modification."
      Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P., Dejean A.
      Mol. Cell. Biol. 21:3314-3324(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM24.
    10. "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.
    11. "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.
    12. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
      Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
      Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATRX; CHAF1A; LBR; NIPBL; SP100; STAM2 AND TRIM28.
    13. "Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: role in nuclear egress of viral particles."
      Okada Y., Suzuki T., Sunden Y., Orba Y., Kose S., Imamoto N., Takahashi H., Tanaka S., Hall W.W., Nagashima K., Sawa H.
      EMBO Rep. 6:452-457(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH JC VIRUS AGNOPROTEIN.
    14. "In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation."
      Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., Carpenter A.E., Belmont A.S., van Driel R.
      Mol. Cell. Biol. 25:4552-4564(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1.
    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. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin."
      Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.
      Nature 461:819-822(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HISTONE-BINDING.
    19. Cited for: INTERACTION WITH BAHD1.
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-14; SER-92 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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; TRIM28; CHAF1A; NIPBL AND INCENP, MUTAGENESIS OF ILE-165 AND TRP-174.
    24. "Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein, FBXW10."
      Chaturvedi P., Parnaik V.K.
      PLoS ONE 5:E10620-E10620(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    25. "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-11; SER-12; SER-13; SER-14; SER-92 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-13; SER-14; SER-95 AND SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-75 IN COMPLEX WITH TRIMETHYLATED HISTONE H3 PEPTIDE, SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 110-173.

    Entry informationi

    Entry nameiCBX5_HUMAN
    AccessioniPrimary (citable) accession number: P45973
    Secondary accession number(s): B2R8T9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 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 12
      Human chromosome 12: 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