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Q9HC52

- CBX8_HUMAN

UniProt

Q9HC52 - CBX8_HUMAN

Protein

Chromobox protein homolog 8

Gene

CBX8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (10 May 2005)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. single-stranded RNA binding Source: Ensembl
    4. ubiquitin-protein transferase activity Source: Ensembl

    GO - Biological processi

    1. histone ubiquitination Source: Ensembl
    2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromobox protein homolog 8
    Alternative name(s):
    Polycomb 3 homolog
    Short name:
    Pc3
    Short name:
    hPc3
    Rectachrome 1
    Gene namesi
    Name:CBX8
    Synonyms:PC3, RC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:15962. CBX8.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. heterochromatin Source: Ensembl
    2. nuclear chromatin Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. PcG protein complex Source: UniProtKB
    6. PRC1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26133.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 389389Chromobox protein homolog 8PRO_0000080215Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101Phosphoserine2 Publications
    Modified residuei130 – 1301Phosphoserine1 Publication
    Modified residuei191 – 1911Phosphoserine1 Publication
    Modified residuei256 – 2561Phosphoserine2 Publications
    Modified residuei265 – 2651Phosphoserine1 Publication
    Modified residuei311 – 3111PhosphoserineBy similarity
    Modified residuei352 – 3521Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HC52.
    PaxDbiQ9HC52.
    PeptideAtlasiQ9HC52.
    PRIDEiQ9HC52.

    PTM databases

    PhosphoSiteiQ9HC52.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HC52.
    BgeeiQ9HC52.
    CleanExiHS_CBX8.
    GenevestigatoriQ9HC52.

    Organism-specific databases

    HPAiHPA031462.

    Interactioni

    Subunit structurei

    Component of a PRC1-like complex. Interacts with RING1 RNF2, PCGF1, PCGF2, PCGF3, BMI1, PCGF5 AND PCGF6. Interacts with MLLT3 and histone H3. Interacts with PHC2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMI1P3522613EBI-712912,EBI-2341576
    KAT5Q929932EBI-712912,EBI-399080
    PCGF1Q9BSM12EBI-712912,EBI-749901
    PCGF2P352277EBI-712912,EBI-2129767
    PCGF3Q3KNV83EBI-712912,EBI-2339807
    PCGF5Q86SE92EBI-712912,EBI-2827999
    PCGF6Q9BYE72EBI-712912,EBI-1048026
    RING1Q065873EBI-712912,EBI-752313
    RNF2Q994965EBI-712912,EBI-722416
    USP11P517845EBI-712912,EBI-306876
    USP7Q930097EBI-712912,EBI-302474

    Protein-protein interaction databases

    BioGridi121487. 79 interactions.
    DIPiDIP-44566N.
    IntActiQ9HC52. 74 interactions.
    MINTiMINT-1372508.
    STRINGi9606.ENSP00000269385.

    Structurei

    Secondary structure

    1
    389
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 2213
    Beta strandi25 – 328
    Helixi37 – 393
    Beta strandi41 – 444
    Helixi45 – 473
    Helixi51 – 599

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I91X-ray1.55A/B8-61[»]
    ProteinModelPortaliQ9HC52.
    SMRiQ9HC52. Positions 9-60.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HC52.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 1 chromo domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG304493.
    HOGENOMiHOG000233642.
    HOVERGENiHBG003608.
    InParanoidiQ9HC52.
    KOiK11455.
    OMAiVQCGVTS.
    PhylomeDBiQ9HC52.
    TreeFamiTF106456.

    Family and domain databases

    InterProiIPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    [Graphical view]
    PfamiPF00385. Chromo. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    PROSITEiPS00598. CHROMO_1. 1 hit.
    PS50013. CHROMO_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9HC52-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELSAVGERV FAAEALLKRR IRKGRMEYLV KWKGWSQKYS TWEPEENILD    50
    ARLLAAFEER EREMELYGPK KRGPKPKTFL LKAQAKAKAK TYEFRSDSAR 100
    GIRIPYPGRS PQDLASTSRA REGLRNMGLS PPASSTSTSS TCRAEAPRDR 150
    DRDRDRDRER DRERERERER ERERERERER GTSRVDDKPS SPGDSSKKRG 200
    PKPRKELPDP SQRPLGEPSA GLGEYLKGRK LDDTPSGAGK FPAGHSVIQL 250
    ARRQDSDLVQ CGVTSPSSAE ATGKLAVDTF PARVIKHRAA FLEAKGQGAL 300
    DPNGTRVRHG SGPPSSGGGL YRDMGAQGGR PSLIARIPVA RILGDPEEES 350
    WSPSLTNLEK VVVTDVTSNF LTVTIKESNT DQGFFKEKR 389
    Length:389
    Mass (Da):43,396
    Last modified:May 10, 2005 - v3
    Checksum:i651263C85B0ECD93
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171G → V.2 Publications
    Corresponds to variant rs4889891 [ dbSNP | Ensembl ].
    VAR_014954

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF174482 mRNA. Translation: AAG09180.1.
    AF266479 mRNA. Translation: AAF76328.2.
    AK074560 mRNA. Translation: BAC11061.1.
    BC008937 mRNA. Translation: AAH08937.1.
    BC009376 mRNA. Translation: AAH09376.1.
    BC019289 mRNA. Translation: AAH19289.1.
    CCDSiCCDS11765.1.
    RefSeqiNP_065700.1. NM_020649.2.
    UniGeneiHs.387258.

    Genome annotation databases

    EnsembliENST00000269385; ENSP00000269385; ENSG00000141570.
    GeneIDi57332.
    KEGGihsa:57332.
    UCSCiuc002jxd.2. human.

    Polymorphism databases

    DMDMi78099843.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF174482 mRNA. Translation: AAG09180.1 .
    AF266479 mRNA. Translation: AAF76328.2 .
    AK074560 mRNA. Translation: BAC11061.1 .
    BC008937 mRNA. Translation: AAH08937.1 .
    BC009376 mRNA. Translation: AAH09376.1 .
    BC019289 mRNA. Translation: AAH19289.1 .
    CCDSi CCDS11765.1.
    RefSeqi NP_065700.1. NM_020649.2.
    UniGenei Hs.387258.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3I91 X-ray 1.55 A/B 8-61 [» ]
    ProteinModelPortali Q9HC52.
    SMRi Q9HC52. Positions 9-60.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121487. 79 interactions.
    DIPi DIP-44566N.
    IntActi Q9HC52. 74 interactions.
    MINTi MINT-1372508.
    STRINGi 9606.ENSP00000269385.

    PTM databases

    PhosphoSitei Q9HC52.

    Polymorphism databases

    DMDMi 78099843.

    Proteomic databases

    MaxQBi Q9HC52.
    PaxDbi Q9HC52.
    PeptideAtlasi Q9HC52.
    PRIDEi Q9HC52.

    Protocols and materials databases

    DNASUi 57332.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269385 ; ENSP00000269385 ; ENSG00000141570 .
    GeneIDi 57332.
    KEGGi hsa:57332.
    UCSCi uc002jxd.2. human.

    Organism-specific databases

    CTDi 57332.
    GeneCardsi GC17M077765.
    HGNCi HGNC:15962. CBX8.
    HPAi HPA031462.
    neXtProti NX_Q9HC52.
    PharmGKBi PA26133.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304493.
    HOGENOMi HOG000233642.
    HOVERGENi HBG003608.
    InParanoidi Q9HC52.
    KOi K11455.
    OMAi VQCGVTS.
    PhylomeDBi Q9HC52.
    TreeFami TF106456.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    EvolutionaryTracei Q9HC52.
    GeneWikii CBX8.
    GenomeRNAii 57332.
    NextBioi 63438.
    PROi Q9HC52.

    Gene expression databases

    ArrayExpressi Q9HC52.
    Bgeei Q9HC52.
    CleanExi HS_CBX8.
    Genevestigatori Q9HC52.

    Family and domain databases

    InterProi IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR023779. Chromodomain_CS.
    [Graphical view ]
    Pfami PF00385. Chromo. 1 hit.
    [Graphical view ]
    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. "HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties."
      Bardos J.I., Saurin A.J., Tissot C., Duprez E., Freemont P.S.
      J. Biol. Chem. 275:28785-28792(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Isolation of Polycomb and Trithorax-related genes that are expressed in human colorectal mucosa."
      Michael M.Z., James R.J.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-317.
      Tissue: Colon carcinoma.
    3. "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], VARIANT VAL-317.
      Tissue: Embryo.
    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: Lung and Muscle.
    5. "The ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein recruits human Polycomb 3."
      Garcia-Cuellar M.P., Zilles O., Schreiner S.A., Birke M., Winkler T.H., Slany R.K.
      Oncogene 20:411-419(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLLT3.
    6. "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; CBX4; PHC1; PHC2; PHC3; RING1 AND RNF2.
    7. "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.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-130; SER-256; SER-265 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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, INTERACTION WITH BMI1 AND PCGF2.
    10. "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-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-110; SER-191 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH RING1; RNF2; PCGF1; PCGF2; PCGF3; BMI1; PCGF5 AND PCGF6.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-61 IN COMPLEX WITH HISTONE H3 PEPTIDE.

    Entry informationi

    Entry nameiCBX8_HUMAN
    AccessioniPrimary (citable) accession number: Q9HC52
    Secondary accession number(s): Q96H39, Q9NR07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 124 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 orthologuous proteins of Drosphila Polycomb group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct nulear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different complexes.

    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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    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