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Q24574

- UBPE_DROME

UniProt

Q24574 - UBPE_DROME

Protein

Ubiquitin carboxyl-terminal hydrolase 64E

Gene

Ubp64E

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 108 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    Has an effect on position-effect variegation.

    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 sitei405 – 4051NucleophilePROSITE-ProRule annotation
    Active sitei720 – 7201Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ubiquitin-specific protease activity Source: FlyBase

    GO - Biological processi

    1. compound eye cone cell differentiation Source: FlyBase
    2. protein deubiquitination Source: FlyBase
    3. protein stabilization Source: FlyBase
    4. regulation of chromatin silencing Source: FlyBase
    5. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.105.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 64E (EC:3.4.19.12)
    Alternative name(s):
    Ubiquitin thioesterase 64E
    Ubiquitin-specific-processing protease 64E
    Short name:
    Deubiquitinating enzyme 64E
    Gene namesi
    Name:Ubp64E
    Synonyms:D-UBP-64E
    ORF Names:CG5486
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0016756. Ubp64E.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. nucleus Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15561556Ubiquitin carboxyl-terminal hydrolase 64EPRO_0000080687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphoserine1 Publication
    Modified residuei173 – 1731Phosphoserine1 Publication
    Modified residuei238 – 2381Phosphoserine1 Publication
    Modified residuei1131 – 11311Phosphoserine1 Publication
    Modified residuei1132 – 11321Phosphoserine1 Publication
    Modified residuei1140 – 11401Phosphoserine1 Publication
    Modified residuei1141 – 11411Phosphoserine1 Publication
    Modified residuei1199 – 11991Phosphoserine1 Publication
    Modified residuei1201 – 12011Phosphoserine1 Publication
    Modified residuei1205 – 12051Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ24574.

    Expressioni

    Gene expression databases

    BgeeiQ24574.

    Interactioni

    Protein-protein interaction databases

    BioGridi64105. 7 interactions.
    IntActiQ24574. 4 interactions.
    MINTiMINT-971166.

    Structurei

    3D structure databases

    ProteinModelPortaliQ24574.
    SMRiQ24574. Positions 394-812.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini396 – 779384USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5077.
    GeneTreeiENSGT00740000115066.
    InParanoidiQ24574.
    KOiK11857.
    OMAiLECNTEK.
    OrthoDBiEOG7M3HZD.
    PhylomeDBiQ24574.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q24574-1) [UniParc]FASTAAdd to Basket

    Also known as: B

    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

    MTDKESEQCT VSVFDQTPGS EQKKINVVVR SHFTVKRVID LIGTQFSYEK     50
    FELLLQPHDN KDLVNLNALE SQLMYEVAGF EPQLKNHLIL LPSGSWDGDV 100
    TKRFELPIKR VVVKKVMKSD GEKAKSPATG EKKKRVVGEK TKKKPASGSS 150
    SPSKAKTTSE DSLAKTSISS ESSPEKTSKI KTTAAKISKP GSEKAPRASP 200
    EECPELSTEI NSKNTSSESP VAKKTAKVTS KPTLELLSPI KPSSPIKELD 250
    CEPVDTLSKQ QLSEQLQLYP QGRNLISPVD DAPSDLFISD AEQLSDDDLA 300
    LGASASPTML GPGYDYGAPT GDSDVEGVTG VTDPSTIGTD DGTYPALSNF 350
    YRRKYGGDEL RAWQRVNTTG ADFVSSATTE TEAEARQASL GPRGYVGLVN 400
    QAMTCYLNSL LQALFMTPEF RNALYRWEFD NDNEAKNIPY QLQKLFLNLQ 450
    TSPKAAVETT DLTRSFGWDS TEAWQQHDIQ ELCRVMFDAL EHKFKNTKQA 500
    NLISNLYEGK MNDYVKCLEC NTEKTREDTF LDIPLPVRPF GSSSAYGSIE 550
    EALRAFVQPE TLDGNNQYLC EKCKKKCDAH KGLHFKSFPY ILTLHLKRFD 600
    FDYQTMHRIK LNDRVTFPQT LNLNTFINRS GNSGEQNSQL NGTVDDCSTA 650
    DSGSAMEDDN LSSGVVTTAS SSQHENDLND EDEGIDMSSS TSKSAKQGSG 700
    PYLYELFAIM IHSGSASGGH YYAYIKDFDN NEWFCFNDQN VTSITQEDIQ 750
    RSFGGPNGSY YSSAYTSSTN AYMLMYRQVD AKRNELVAKV ADFPEHIKTL 800
    LPKLHSEEET RVSRLGRHIT VTDLALPDLY KPRVYFYNPS LKKMKITRVY 850
    VSQSFNINLV LMSAYEMLNV EQFAPLSRCR LVAYNSSMDT IIQSLESCTD 900
    PALTELRAAQ NYSLDFLLEY RAEDQEFEVY PPNGITWYVF KVDLSTMAMD 950
    GPFLVYSAAR EREASDVLRR SIALRLHISE QQFLLATVRA TVPKAFVSYD 1000
    PHPTPEALQH LQNMANTQFK SITYFYLNVP NTDAATLEML GVPTVESVEC 1050
    ASGGDVVDAA MMNGVAPGHM SSSNDYDWRR YKRDLVEPMS QPSPSHGHES 1100
    NSEDSSLSDG DRTLVETDNM AHRGGGDSQV SSTSHSPQLS SPEDEAASHD 1150
    AMMRVHAYCN GNGSYAAADV VDPLLLPTST NHFFYATKVE CVDVVGTGSS 1200
    SGHQSDEEAQ LRKPTRAYKL LVGTHMRMGA FKKHIEQLIQ VPAAHFKLQR 1250
    KHDNNLSNNQ NNSLVHLIEG ETLTVELGKT LEPDEFKAKI HFLRLADIDN 1300
    ETSKLPCVCE WVYNANTTAE QAKKELVAKL HRIDAKYATL SVQNCRIWLK 1350
    GGRIPIKILS DDETLYCDMR SSIAAEFIVQ ECEEEVDPQP KDDSLTLFVR 1400
    RWCPAKLEFG KFQEITLDQD SEIRLSLSQI SDIPIDKLSY MKLNSNFPCT 1450
    SISALSVNES SSWYSVPTTL DKYPLNSTQT GNIYLYKDRT VPARELTLEE 1500
    RRLMNAREKA RLDRVGCVST TRYAQRRERA LKIYLDSPEK SSNVTASAPM 1550
    DVHVNN 1556
    Length:1,556
    Mass (Da):173,794
    Last modified:September 13, 2005 - v2
    Checksum:iF70AE5BB2914E8BE
    GO
    Isoform D (identifier: Q24574-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         272-289: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,538
    Mass (Da):171,896
    Checksum:i497CFA02811B7D18
    GO

    Sequence cautioni

    The sequence CAA67601.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAL13901.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA67601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti437 – 4393NIP → KS in CAA67601. (PubMed:8816485)Curated
    Sequence conflicti513 – 5131D → A in CAA67601. (PubMed:8816485)Curated
    Sequence conflicti519 – 5191E → G in CAA67601. (PubMed:8816485)Curated
    Sequence conflicti525 – 5262TR → NDC in CAA67601. (PubMed:8816485)Curated
    Sequence conflicti645 – 6451D → DS in AAL13901. (PubMed:12537569)Curated
    Sequence conflicti791 – 7911A → R in CAA67601. (PubMed:8816485)Curated
    Sequence conflicti910 – 9101Missing in CAA67601. (PubMed:8816485)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei272 – 28918Missing in isoform D. CuratedVSP_054033Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF50752.2.
    AE014296 Genomic DNA. Translation: AAN12105.1.
    AE014296 Genomic DNA. Translation: AAS65076.2.
    BT003784 mRNA. Translation: AAO41467.1.
    X99211 mRNA. Translation: CAA67601.1. Sequence problems.
    AY058672 mRNA. Translation: AAL13901.1. Different initiation.
    RefSeqiNP_523937.2. NM_079213.4. [Q24574-1]
    NP_729087.1. NM_168129.3. [Q24574-1]
    NP_996001.2. NM_206279.3. [Q24574-2]
    UniGeneiDm.3704.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077095; FBpp0076802; FBgn0016756. [Q24574-1]
    FBtr0077096; FBpp0076803; FBgn0016756. [Q24574-1]
    GeneIDi38644.
    KEGGidme:Dmel_CG5486.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF50752.2 .
    AE014296 Genomic DNA. Translation: AAN12105.1 .
    AE014296 Genomic DNA. Translation: AAS65076.2 .
    BT003784 mRNA. Translation: AAO41467.1 .
    X99211 mRNA. Translation: CAA67601.1 . Sequence problems.
    AY058672 mRNA. Translation: AAL13901.1 . Different initiation.
    RefSeqi NP_523937.2. NM_079213.4. [Q24574-1 ]
    NP_729087.1. NM_168129.3. [Q24574-1 ]
    NP_996001.2. NM_206279.3. [Q24574-2 ]
    UniGenei Dm.3704.

    3D structure databases

    ProteinModelPortali Q24574.
    SMRi Q24574. Positions 394-812.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 64105. 7 interactions.
    IntActi Q24574. 4 interactions.
    MINTi MINT-971166.

    Protein family/group databases

    MEROPSi C19.105.

    Proteomic databases

    PaxDbi Q24574.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077095 ; FBpp0076802 ; FBgn0016756 . [Q24574-1 ]
    FBtr0077096 ; FBpp0076803 ; FBgn0016756 . [Q24574-1 ]
    GeneIDi 38644.
    KEGGi dme:Dmel_CG5486.

    Organism-specific databases

    CTDi 38644.
    FlyBasei FBgn0016756. Ubp64E.

    Phylogenomic databases

    eggNOGi COG5077.
    GeneTreei ENSGT00740000115066.
    InParanoidi Q24574.
    KOi K11857.
    OMAi LECNTEK.
    OrthoDBi EOG7M3HZD.
    PhylomeDBi Q24574.

    Miscellaneous databases

    ChiTaRSi Ubp64E. drosophila.
    GenomeRNAii 38644.
    NextBioi 809673.
    PROi Q24574.

    Gene expression databases

    Bgeei Q24574.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    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, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Embryo.
    4. "The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster."
      Henchoz S., de Rubertis F., Pauli D., Spierer P.
      Mol. Cell. Biol. 16:5717-5725(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 318-1556 (ISOFORMS A/D).
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-1556 (ISOFORMS A/D).
      Strain: Berkeley.
      Tissue: Embryo.
    6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-173; SER-238; SER-1131; SER-1132; SER-1140; SER-1141; SER-1199; SER-1201 AND SER-1205, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiUBPE_DROME
    AccessioniPrimary (citable) accession number: Q24574
    Secondary accession number(s): A4V1I7, Q95TM9, Q9VRP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 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