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O00257

- CBX4_HUMAN

UniProt

O00257 - CBX4_HUMAN

Protein

E3 SUMO-protein ligase CBX4

Gene

CBX4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131.
    Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.

    Pathwayi

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. enzyme binding Source: UniProtKB
    3. ligase activity Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. single-stranded RNA binding Source: Ensembl
    6. SUMO binding Source: MGI
    7. transcription corepressor activity Source: ProtInc
    8. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. negative regulation of apoptotic process Source: ProtInc
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. protein sumoylation Source: UniProtKB-UniPathway
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Ligase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 SUMO-protein ligase CBX4 (EC:6.3.2.-)
    Alternative name(s):
    Chromobox protein homolog 4
    Polycomb 2 homolog
    Short name:
    Pc2
    Short name:
    hPc2
    Gene namesi
    Name:CBX4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:1554. CBX4.

    Subcellular locationi

    Nucleus. Nucleus speckle
    Note: Localization to nuclear polycomb bodies is required for ZNF131 sumoylation.

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. PcG protein complex Source: UniProtKB
    5. PRC1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi434 – 4341S → A: Abolishes interaction with YWHAZ and YWHAE; impairs interaction with PCGF6 and BMI1; no effect on interaction with RNF2. 1 Publication
    Mutagenesisi494 – 4941K → R: No effect on ZNF131 sumoylation. 1 Publication
    Mutagenesisi497 – 4971T → A: Small decrease in ZNF131 sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA26129.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 560560E3 SUMO-protein ligase CBX4PRO_0000080206Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei149 – 1491N6-acetyllysine1 Publication
    Cross-linki494 – 494Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei497 – 4971Phosphothreonine; by HIPK21 Publication

    Post-translational modificationi

    Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK.3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO00257.
    PaxDbiO00257.
    PRIDEiO00257.

    PTM databases

    PhosphoSiteiO00257.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO00257.
    BgeeiO00257.
    CleanExiHS_CBX4.
    GenevestigatoriO00257.

    Organism-specific databases

    HPAiHPA008228.

    Interactioni

    Subunit structurei

    Interacts with histone H3-K9Me3. Interacts with CHTOP By similarity. Component of a PRC1-like complex. Self-associates. Interacts with SUV39H1 and HIPK2. Interacts with CSNK2B.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMI1P352264EBI-722425,EBI-2341576
    CSNK2A1P684002EBI-4392727,EBI-347804
    CSNK2BP678702EBI-4392727,EBI-348169
    HIF1AQ1666515EBI-722425,EBI-447269
    PCGF6Q9BYE72EBI-4392727,EBI-1048026
    RNF2Q994962EBI-4392727,EBI-722416
    YWHABP319462EBI-722425,EBI-359815
    YWHAEP622582EBI-4392727,EBI-356498
    YWHAZP631042EBI-4392727,EBI-347088

    Protein-protein interaction databases

    BioGridi114105. 74 interactions.
    DIPiDIP-42042N.
    IntActiO00257. 49 interactions.
    MINTiMINT-1196265.
    STRINGi9606.ENSP00000269397.

    Structurei

    Secondary structure

    1
    560
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 2210
    Beta strandi25 – 328
    Helixi37 – 393
    Beta strandi41 – 444
    Helixi45 – 484
    Helixi51 – 533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K28NMR-A8-65[»]
    3I8ZX-ray1.51A8-62[»]
    ProteinModelPortaliO00257.
    SMRiO00257. Positions 11-60.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00257.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 6959ChromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 539539Interaction with BMI1Add
    BLAST
    Regioni540 – 56021Interaction with RNF2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi378 – 40023His-richAdd
    BLAST
    Compositional biasi389 – 40012Poly-HisAdd
    BLAST
    Compositional biasi499 – 51012Poly-AlaAdd
    BLAST

    Domaini

    The polyhistidine repeat may act as a targeting signal to nuclear speckles.1 Publication

    Sequence similaritiesi

    Contains 1 chromo domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG281109.
    HOGENOMiHOG000206923.
    HOVERGENiHBG005257.
    InParanoidiO00257.
    KOiK11452.
    OMAiKWAHGAG.
    OrthoDBiEOG7PCJGP.
    PhylomeDBiO00257.
    TreeFamiTF106456.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00257-1) [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

    MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD    50
    PRLLIAFQNR ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS 100
    TDNRAKLDLG AQGKGQGHQY ELNSKKHHQY QPHSKERAGK PPPPGKSGKY 150
    YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA PSPTCPDLGA KSHPPDKWAQ 200
    GAGAKGYLGA VKPLAGAAGA PGKGSEKGPP NGMMPAPKEA VTGNGIGGKM 250
    KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEVAEGEAR SPSHKKRAAD 300
    ERHPPADRTF KKAAGAEEKK VEAPPKRREE EVSGVSDPQP QDAGSRKLSP 350
    TKEAFGEQPL QLTTKPDLLA WDPARNTHPP SHHPHPHPHH HHHHHHHHHH 400
    AVGLNLSHVR KRCLSETHGE REPCKKRLTA RSISTPTCLG GSPAAERPAD 450
    LPPAAALPQP EVILLDSDLD EPIDLRCVKT RSEAGEPPSS LQVKPETPAS 500
    AAVAVAAAAA PTTTAEKPPA EAQDEPAESL SEFKPFFGNI IITDVTANCL 550
    TVTFKEYVTV 560
    Length:560
    Mass (Da):61,368
    Last modified:July 28, 2009 - v3
    Checksum:iDF5C8C4C0CCB1F31
    GO
    Isoform 2 (identifier: O00257-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         127-396: Missing.

    Show »
    Length:290
    Mass (Da):31,987
    Checksum:iB1E71D5122A7B7FA
    GO

    Sequence cautioni

    The sequence AAH14967.1 differs from that shown. Reason: Aberrant splicing.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1382Missing in AAB80718. (PubMed:9315667)Curated
    Sequence conflicti142 – 1421P → R in AAB80718. (PubMed:9315667)Curated
    Sequence conflicti458 – 4581P → R in AAB80718. (PubMed:9315667)Curated
    Sequence conflicti458 – 4581P → R in AAB62734. (PubMed:15489334)Curated
    Sequence conflicti477 – 4771C → S in AAB80718. (PubMed:9315667)Curated
    Sequence conflicti477 – 4771C → S in AAB62734. (PubMed:15489334)Curated
    Sequence conflicti480 – 4801T → S in AAB80718. (PubMed:9315667)Curated
    Sequence conflicti480 – 4801T → S in AAB62734. (PubMed:15489334)Curated
    Sequence conflicti505 – 5051V → VAA in ACA49234. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei127 – 396270Missing in isoform 2. 1 PublicationVSP_041599Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013956 mRNA. Translation: AAB80718.1.
    EU439707 mRNA. Translation: ACA49234.1.
    AY390430 mRNA. Translation: AAQ97596.1.
    AC100791 Genomic DNA. No translation available.
    BC014967 mRNA. Translation: AAH14967.1. Sequence problems.
    U94344 mRNA. Translation: AAB62734.1.
    CCDSiCCDS32758.1. [O00257-1]
    RefSeqiNP_003646.2. NM_003655.2. [O00257-1]
    UniGeneiHs.405046.

    Genome annotation databases

    EnsembliENST00000269397; ENSP00000269397; ENSG00000141582. [O00257-1]
    GeneIDi8535.
    KEGGihsa:8535.
    UCSCiuc002jxe.3. human. [O00257-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF013956 mRNA. Translation: AAB80718.1 .
    EU439707 mRNA. Translation: ACA49234.1 .
    AY390430 mRNA. Translation: AAQ97596.1 .
    AC100791 Genomic DNA. No translation available.
    BC014967 mRNA. Translation: AAH14967.1 . Sequence problems.
    U94344 mRNA. Translation: AAB62734.1 .
    CCDSi CCDS32758.1. [O00257-1 ]
    RefSeqi NP_003646.2. NM_003655.2. [O00257-1 ]
    UniGenei Hs.405046.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K28 NMR - A 8-65 [» ]
    3I8Z X-ray 1.51 A 8-62 [» ]
    ProteinModelPortali O00257.
    SMRi O00257. Positions 11-60.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114105. 74 interactions.
    DIPi DIP-42042N.
    IntActi O00257. 49 interactions.
    MINTi MINT-1196265.
    STRINGi 9606.ENSP00000269397.

    PTM databases

    PhosphoSitei O00257.

    Proteomic databases

    MaxQBi O00257.
    PaxDbi O00257.
    PRIDEi O00257.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269397 ; ENSP00000269397 ; ENSG00000141582 . [O00257-1 ]
    GeneIDi 8535.
    KEGGi hsa:8535.
    UCSCi uc002jxe.3. human. [O00257-1 ]

    Organism-specific databases

    CTDi 8535.
    GeneCardsi GC17M077806.
    H-InvDB HIX0014237.
    HGNCi HGNC:1554. CBX4.
    HPAi HPA008228.
    MIMi 603079. gene.
    neXtProti NX_O00257.
    PharmGKBi PA26129.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG281109.
    HOGENOMi HOG000206923.
    HOVERGENi HBG005257.
    InParanoidi O00257.
    KOi K11452.
    OMAi KWAHGAG.
    OrthoDBi EOG7PCJGP.
    PhylomeDBi O00257.
    TreeFami TF106456.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_169436. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    ChiTaRSi CBX4. human.
    EvolutionaryTracei O00257.
    GenomeRNAii 8535.
    NextBioi 31968.
    PROi O00257.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00257.
    Bgeei O00257.
    CleanExi HS_CBX4.
    Genevestigatori O00257.

    Family and domain databases

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

    Publicationsi

    1. "Interference with the expression of a novel human polycomb protein, hPc2, results in cellular transformation and apoptosis."
      Satijn D.P.E., Olson D.J., van der Vlag J., Hamer K.M., Lambrechts C., Masselink H., Gunster M.J., Sewalt R.G.A.B., van Driel R., Otte A.P.
      Mol. Cell. Biol. 17:6076-6086(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Genome-wide analysis of histidine repeats reveals their role in the localization of human proteins to the nuclear speckles compartment."
      Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.
      PLoS Genet. 5:E1000397-E1000397(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    3. "Cloning and identification of NS5ATP1-binding protein 16."
      Liu M., Cheng J., Wang L.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Colon.
    6. "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor."
      Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.
      Mol. Cell. Biol. 17:4105-4113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 457-560 (ISOFORM 1).
    7. "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins."
      Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.
      Mol. Cell. Biol. 22:5539-5553(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUV39H1.
    8. "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans."
      Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E.
      Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX WITH BMI1; CBX2; CBX8; PHC1; PHC2; PHC3; RING1 AND RNF2.
    9. "The polycomb protein Pc2 is a SUMO E3."
      Kagey M.H., Melhuish T.A., Wotton D.
      Cell 113:127-137(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUMOYLATION, SUBCELLULAR LOCATION.
    10. "Multiple activities contribute to Pc2 E3 function."
      Kagey M.H., Melhuish T.A., Powers S.E., Wotton D.
      EMBO J. 24:108-119(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-494.
    11. "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin."
      Long J., Zuo D., Park M.
      J. Biol. Chem. 280:35477-35489(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2."
      Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C., Gresko E., Luedi K.S., Schmitz M.L.
      Mol. Cell 24:77-89(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIPK2, SUMOYLATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-497.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
      Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
      PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX.
    15. "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-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
      Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), IDENTIFICATION IN A PRC1-LIKE COMPLEX, SELF-ASSOCIATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-434.
    17. "Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signaling."
      Oh Y., Chung K.C.
      J. Biol. Chem. 287:17517-17529(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ZNF131 SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-494 AND THR-497.
    18. "DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation."
      Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.
      J. Biol. Chem. 287:30789-30799(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Solution NMR structure of the chromo domain of the chromobox protein homolog 4."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 8-65.
    20. "Crystal structure of human chromobox homolog 4 (cbx4)."
      Structural genomics consortium (SGC)
      Submitted (SEP-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 8-62.

    Entry informationi

    Entry nameiCBX4_HUMAN
    AccessioniPrimary (citable) accession number: O00257
    Secondary accession number(s): B1PJR7, Q6TPI8, Q96C04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 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

    Miscellaneous

    The human orthologs of the Drosophila Polycomb group protein Pc are CBX2, CBX4, CBX6, CBX7 and CBX8. These show distinct nuclear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. The hPRC-H complex purified in PubMed:12167701 probably presents a mixture of different complexes containing different Polycomb group proteins.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3