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Q7K5N4

- CALYP_DROME

UniProt

Q7K5N4 - CALYP_DROME

Protein

Ubiquitin carboxyl-terminal hydrolase calypso

Gene

calypso

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    Polycomb group (PcG) protein. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-118' (H2AK118ub1). Does not deubiquitinate monoubiquitinated histone H2B. Required to maintain the transcriptionally repressive state of homeotic genes throughout development. The PR-DUB complex has weak or no activity toward 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei131 – 1311NucleophileCurated
    Active sitei213 – 2131Proton donorBy similarity
    Sitei228 – 2281Important for enzyme activityBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. ubiquitin-specific protease activity Source: UniProtKB
    3. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. chromatin silencing Source: UniProtKB
    2. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
    3. specification of segmental identity, abdomen Source: FlyBase
    4. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC12.A09.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase calypso (EC:3.4.19.12)
    Alternative name(s):
    BAP1 homolog
    Gene namesi
    Name:calypso
    ORF Names:CG8445
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0262166. calypso.

    Subcellular locationi

    Nucleus
    Note: Localizes to PcG response elements (PREs).

    GO - Cellular componenti

    1. nuclear chromatin Source: UniProtKB
    2. nucleus Source: FlyBase
    3. PR-DUB complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Polycomb phenotype leading to lethality, probably due to misexpression of homeotic genes.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311C → S: Abolishes deubiquitinase activity without affecting the interaction with Asx. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Ubiquitin carboxyl-terminal hydrolase calypsoPRO_0000395823Add
    BLAST

    Proteomic databases

    PaxDbiQ7K5N4.
    PRIDEiQ7K5N4.

    Expressioni

    Gene expression databases

    BgeeiQ7K5N4.

    Interactioni

    Subunit structurei

    Component of the PR-DUB complex, at least composed of calypso and Asx.1 Publication

    Protein-protein interaction databases

    DIPiDIP-59274N.
    STRINGi7227.FBpp0086383.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7K5N4.
    SMRiQ7K5N4. Positions 46-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi440 – 4434Poly-Gln
    Compositional biasi444 – 4474Poly-Ala

    Sequence similaritiesi

    Belongs to the peptidase C12 family. BAP1 subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG249036.
    GeneTreeiENSGT00510000046560.
    InParanoidiQ7K5N4.
    KOiK08588.
    OMAiTDKFRRV.
    OrthoDBiEOG7GN2M2.
    PhylomeDBiQ7K5N4.

    Family and domain databases

    Gene3Di3.40.532.10. 1 hit.
    InterProiIPR001578. Peptidase_C12_UCH.
    [Graphical view]
    PANTHERiPTHR10589. PTHR10589. 1 hit.
    PfamiPF01088. Peptidase_C12. 1 hit.
    [Graphical view]
    PRINTSiPR00707. UBCTHYDRLASE.

    Sequencei

    Sequence statusi: Complete.

    Q7K5N4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAAGGGSGA QAAAVAAGNN SLSHNALLST ASGATTMPMA QLADGWLELE    50
    SDPGLFTLLL KDFGCHDVQV EEVYDLQKPI ESPYGFIFLF RWIEERRARR 100
    KIVETTAEIF VKDEEAISSI FFAQQVVPNS CATHALLSVL LNCNENNLQL 150
    GDTLSRLKTH TKGMSPENKG LAIGNTPELA CAHNSHAMPQ ARRRLERTGA 200
    GVSSCRFTGE AFHFVSFVPI NGQLFELDGL KPYPMNHGGW EDSEDWTDKF 250
    RRVMAERLGI ATGEQDIRFN LMAVVPDRRI AITHKLKMLR TNQAIVSGTL 300
    QKLLKADEQG ESGNGDSQRP DTPTTLLEPS AFTARDLQSL LKNLDTEIAI 350
    NEQHLADEND RRHMFKVDAS RRTHNYDKFI CTFLSMLAHQ GVLGELVSQH 400
    LLPSKKVSGQ GAANRISKQS TTASAGGSTA AGTASTPKTQ QQQAAAAKNG 450
    KSPSKTPGRR RKGRNKCRKR K 471
    Length:471
    Mass (Da):51,507
    Last modified:October 3, 2006 - v1
    Checksum:iB7C90121EF7716E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF58046.1.
    AE013599 Genomic DNA. Translation: AAO41384.1.
    AY047515 mRNA. Translation: AAK77247.1.
    RefSeqiNP_611096.1. NM_137252.2.
    NP_788374.1. NM_176194.1.
    UniGeneiDm.19939.

    Genome annotation databases

    EnsemblMetazoaiFBtr0087245; FBpp0086383; FBgn0262166.
    FBtr0087246; FBpp0086384; FBgn0262166.
    GeneIDi36794.
    KEGGidme:Dmel_CG8445.
    UCSCiCG8445-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF58046.1 .
    AE013599 Genomic DNA. Translation: AAO41384.1 .
    AY047515 mRNA. Translation: AAK77247.1 .
    RefSeqi NP_611096.1. NM_137252.2.
    NP_788374.1. NM_176194.1.
    UniGenei Dm.19939.

    3D structure databases

    ProteinModelPortali Q7K5N4.
    SMRi Q7K5N4. Positions 46-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59274N.
    STRINGi 7227.FBpp0086383.

    Protein family/group databases

    MEROPSi C12.A09.

    Proteomic databases

    PaxDbi Q7K5N4.
    PRIDEi Q7K5N4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087245 ; FBpp0086383 ; FBgn0262166 .
    FBtr0087246 ; FBpp0086384 ; FBgn0262166 .
    GeneIDi 36794.
    KEGGi dme:Dmel_CG8445.
    UCSCi CG8445-RA. d. melanogaster.

    Organism-specific databases

    CTDi 36794.
    FlyBasei FBgn0262166. calypso.

    Phylogenomic databases

    eggNOGi NOG249036.
    GeneTreei ENSGT00510000046560.
    InParanoidi Q7K5N4.
    KOi K08588.
    OMAi TDKFRRV.
    OrthoDBi EOG7GN2M2.
    PhylomeDBi Q7K5N4.

    Miscellaneous databases

    GenomeRNAii 36794.
    NextBioi 800424.
    PROi Q7K5N4.

    Gene expression databases

    Bgeei Q7K5N4.

    Family and domain databases

    Gene3Di 3.40.532.10. 1 hit.
    InterProi IPR001578. Peptidase_C12_UCH.
    [Graphical view ]
    PANTHERi PTHR10589. PTHR10589. 1 hit.
    Pfami PF01088. Peptidase_C12. 1 hit.
    [Graphical view ]
    PRINTSi PR00707. UBCTHYDRLASE.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    4. "A genetic screen identifies novel polycomb group genes in Drosophila."
      Gaytan de Ayala Alonso A., Gutierrez L., Fritsch C., Papp B., Beuchle D., Muller J.
      Genetics 176:2099-2108(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    5. "Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB."
      Scheuermann J.C., de Ayala Alonso A.G., Oktaba K., Ly-Hartig N., McGinty R.K., Fraterman S., Wilm M., Muir T.W., Muller J.
      Nature 465:243-247(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, INTERACTION WITH ASX, MUTAGENESIS OF CYS-131, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiCALYP_DROME
    AccessioniPrimary (citable) accession number: Q7K5N4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3