Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O95931

- CBX7_HUMAN

UniProt

O95931 - CBX7_HUMAN

Protein

Chromobox protein homolog 7

Gene

CBX7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity.4 Publications

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. protein binding Source: UniProtKB
    3. single-stranded RNA binding Source: Ensembl

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromobox protein homolog 7
    Gene namesi
    Name:CBX7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:1557. CBX7.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311K → A: Loss of cellular lifespan extension. 1 Publication
    Mutagenesisi32 – 321W → A: Loss of cellular lifespan extension. 1 Publication
    Mutagenesisi234 – 2341F → D: Loss of interaction with RNF2. 1 Publication
    Mutagenesisi244 – 2441F → D: Reduced interaction with RNF2. 1 Publication

    Organism-specific databases

    PharmGKBiPA26132.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Chromobox protein homolog 7PRO_0000080212Add
    BLAST

    Proteomic databases

    MaxQBiO95931.
    PaxDbiO95931.
    PRIDEiO95931.

    PTM databases

    PhosphoSiteiO95931.

    Expressioni

    Gene expression databases

    ArrayExpressiO95931.
    BgeeiO95931.
    CleanExiHS_CBX7.
    GenevestigatoriO95931.

    Organism-specific databases

    HPAiCAB011574.
    HPA056480.

    Interactioni

    Subunit structurei

    Component of a PRC1-like complex. Interacts with RING1 and RNF2/RING1B, but not with BMI1, EED or EZH2. Interacts with PCGF1, PCGF2, PCGF3, PCGF5 and PCGF6.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMI1P352267EBI-3923843,EBI-2341576
    PCGF2P352273EBI-3923843,EBI-2129767
    PCGF3Q3KNV82EBI-3923843,EBI-2339807
    PCGF6Q9BYE72EBI-3923843,EBI-1048026
    RING1Q065873EBI-3923843,EBI-752313
    RNF2Q994963EBI-3923843,EBI-722416

    Protein-protein interaction databases

    BioGridi117044. 28 interactions.
    DIPiDIP-44565N.
    IntActiO95931. 22 interactions.
    MINTiMINT-4543653.
    STRINGi9606.ENSP00000216133.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 2210
    Beta strandi25 – 328
    Helixi37 – 393
    Beta strandi41 – 444
    Helixi45 – 473
    Helixi51 – 6010
    Beta strandi221 – 2277
    Beta strandi230 – 2389
    Turni241 – 2433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K1BNMR-A7-62[»]
    2L12NMR-A7-62[»]
    2L1BNMR-A8-62[»]
    3GS2X-ray1.70B/D219-248[»]
    4MN3X-ray1.54A7-62[»]
    ProteinModelPortaliO95931.
    SMRiO95931. Positions 7-62, 219-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95931.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni223 – 23614Required for cellular lifespan extensionAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chromo domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG258927.
    HOGENOMiHOG000233642.
    HOVERGENiHBG019320.
    InParanoidiO95931.
    KOiK11454.
    OMAiPPPWTPV.
    OrthoDBiEOG77T15B.
    PhylomeDBiO95931.
    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]

    Sequencei

    Sequence statusi: Complete.

    O95931-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELSAIGEQV FAVESIRKKR VRKGKVEYLV KWKGWPPKYS TWEPEEHILD    50
    PRLVMAYEEK EERDRASGYR KRGPKPKRLL LQRLYSMDLR SSHKAKGKEK 100
    LCFSLTCPLG SGSPEGVVKA GAPELVDKGP LVPTLPFPLR KPRKAHKYLR 150
    LSRKKFPPRG PNLESHSHRR ELFLQEPPAP DVLQAAGEWE PAAQPPEEEA 200
    DADLAEGPPP WTPALPSSEV TVTDITANSI TVTFREAQAA EGFFRDRSGK 250
    F 251
    Length:251
    Mass (Da):28,341
    Last modified:May 1, 1999 - v1
    Checksum:iA90019C1D08812B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771K → R in AAH51773. (PubMed:15489334)Curated
    Sequence conflicti239 – 2391A → P in AAH51773. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL031846 Genomic DNA. Translation: CAB36555.1.
    BC051773 mRNA. Translation: AAH51773.1.
    CCDSiCCDS13986.1.
    RefSeqiNP_783640.1. NM_175709.3.
    UniGeneiHs.356416.

    Genome annotation databases

    EnsembliENST00000216133; ENSP00000216133; ENSG00000100307.
    GeneIDi23492.
    KEGGihsa:23492.
    UCSCiuc003axb.3. human.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL031846 Genomic DNA. Translation: CAB36555.1 .
    BC051773 mRNA. Translation: AAH51773.1 .
    CCDSi CCDS13986.1.
    RefSeqi NP_783640.1. NM_175709.3.
    UniGenei Hs.356416.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K1B NMR - A 7-62 [» ]
    2L12 NMR - A 7-62 [» ]
    2L1B NMR - A 8-62 [» ]
    3GS2 X-ray 1.70 B/D 219-248 [» ]
    4MN3 X-ray 1.54 A 7-62 [» ]
    ProteinModelPortali O95931.
    SMRi O95931. Positions 7-62, 219-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117044. 28 interactions.
    DIPi DIP-44565N.
    IntActi O95931. 22 interactions.
    MINTi MINT-4543653.
    STRINGi 9606.ENSP00000216133.

    Chemistry

    ChEMBLi CHEMBL1764946.

    PTM databases

    PhosphoSitei O95931.

    Proteomic databases

    MaxQBi O95931.
    PaxDbi O95931.
    PRIDEi O95931.

    Protocols and materials databases

    DNASUi 23492.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216133 ; ENSP00000216133 ; ENSG00000100307 .
    GeneIDi 23492.
    KEGGi hsa:23492.
    UCSCi uc003axb.3. human.

    Organism-specific databases

    CTDi 23492.
    GeneCardsi GC22M039605.
    HGNCi HGNC:1557. CBX7.
    HPAi CAB011574.
    HPA056480.
    MIMi 608457. gene.
    neXtProti NX_O95931.
    PharmGKBi PA26132.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258927.
    HOGENOMi HOG000233642.
    HOVERGENi HBG019320.
    InParanoidi O95931.
    KOi K11454.
    OMAi PPPWTPV.
    OrthoDBi EOG77T15B.
    PhylomeDBi O95931.
    TreeFami TF106456.

    Miscellaneous databases

    EvolutionaryTracei O95931.
    GenomeRNAii 23492.
    NextBioi 45855.
    PROi O95931.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95931.
    Bgeei O95931.
    CleanExi HS_CBX7.
    Genevestigatori O95931.

    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. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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: PNS.
    3. "Polycomb CBX7 has a unifying role in cellular lifespan."
      Gil J., Bernard D., Martinez D., Beach D.
      Nat. Cell Biol. 6:67-72(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RING1, MUTAGENESIS OF LYS-31 AND TRP-32.
    4. "Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins."
      Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S., Arrowsmith C.H.
      Biochemistry 48:10542-10548(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF2.
    5. "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: FUNCTION, IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH BMI1.
    6. "Polycomb CBX7 directly controls trimethylation of histone H3 at lysine 9 at the p16 locus."
      Li Q., Wang X., Lu Z., Zhang B., Guan Z., Liu Z., Zhong Q., Gu L., Zhou J., Zhu B., Ji J., Deng D.
      PLoS ONE 5:E13732-E13732(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "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.
    8. "Solution NMR structure of the chromobox protein homolog 7."
      Structural genomics consortium (SGC)
      Submitted (MAR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 7-62.
    9. "Polycomb group targeting through different binding partners of RING1B C-terminal domain."
      Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U., Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P., McEwen D.G., Kim C.A.
      Structure 18:966-975(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 219-248 IN COMPLEX WITH RNF2, INTERACTION WITH RNF2, MUTAGENESIS OF PHE-234 AND PHE-244.
    10. Cited for: STRUCTURE BY NMR OF 8-62, FUNCTION, INTERACTION WITH TRIMETHYLATED LYSINE RESIDUES.

    Entry informationi

    Entry nameiCBX7_HUMAN
    AccessioniPrimary (citable) accession number: O95931
    Secondary accession number(s): Q86T17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 122 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

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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