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P35122

- UCHL_DROME

UniProt

P35122 - UCHL_DROME

Protein

Ubiquitin carboxyl-terminal hydrolase

Gene

Uch

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin.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 sitei93 – 931NucleophilePROSITE-ProRule annotation
    Active sitei164 – 1641Proton donorPROSITE-ProRule annotation
    Sitei179 – 1791Important for enzyme activityBy similarity

    GO - Molecular functioni

    1. ubiquitin-specific protease activity Source: FlyBase

    GO - Biological processi

    1. protein deubiquitination Source: FlyBase
    2. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC12.008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase (EC:3.4.19.12)
    Alternative name(s):
    Ubiquitin thioesterase
    Gene namesi
    Name:Uch
    Synonyms:ubc-D
    ORF Names:CG4265
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0010288. Uch.

    Subcellular locationi

    GO - Cellular componenti

    1. microtubule associated complex Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 227227Ubiquitin carboxyl-terminal hydrolasePRO_0000211072Add
    BLAST

    Proteomic databases

    PaxDbiP35122.

    Expressioni

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiP35122.

    Interactioni

    Protein-protein interaction databases

    BioGridi59626. 62 interactions.
    MINTiMINT-1599795.

    Structurei

    3D structure databases

    ProteinModelPortaliP35122.
    SMRiP35122. Positions 4-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C12 family.Curated

    Phylogenomic databases

    eggNOGiNOG327708.
    GeneTreeiENSGT00510000046640.
    InParanoidiP35122.
    KOiK05609.
    OMAiYVCFVKG.
    OrthoDBiEOG7S7SFK.
    PhylomeDBiP35122.

    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.
    PROSITEiPS00140. UCH_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P35122-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTWTPLESN PEVLTKYIHK LGVSPAWSVT DVIGLEDDTL EWIPRPVKAF    50
    ILLFPCSETY EKHRAEEHDR IKEVEEQHPE DLFYMRQFTH NACGTVALIH 100
    SVANNKEVDI DRGVLKDFLE KTASLSPEER GRALEKDEKF TADHEALAQE 150
    GQTNAANHEK VIHHFIALVN KEGTLYELDG RKSFPIKHGP TSEETFVKDA 200
    AKVCKEFMAR DPNEVRFTVL ALTAAQQ 227
    Length:227
    Mass (Da):25,850
    Last modified:August 30, 2005 - v2
    Checksum:i298A025569C3D409
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221G → A in AAA15411. (PubMed:7683284)Curated
    Sequence conflicti22 – 221G → A in CAA49358. (PubMed:7683284)Curated
    Sequence conflicti22 – 221G → A in CAA49359. (PubMed:7683284)Curated
    Sequence conflicti65 – 651A → T(PubMed:1426603)Curated
    Sequence conflicti65 – 651A → T(PubMed:7683284)Curated
    Sequence conflicti107 – 1071E → G(PubMed:1426603)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S60346 Genomic DNA. Translation: AAA15411.1.
    X69678 mRNA. Translation: CAA49358.1.
    X69679 Genomic DNA. Translation: CAA49359.1.
    AE014134 Genomic DNA. Translation: AAF51291.1.
    AF145600 mRNA. Translation: AAD38575.1.
    PIRiS33956.
    RefSeqiNP_001188681.1. NM_001201752.2.
    NP_476940.1. NM_057592.4.
    UniGeneiDm.4794.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077844; FBpp0077516; FBgn0010288.
    FBtr0303459; FBpp0292511; FBgn0010288.
    GeneIDi33397.
    KEGGidme:Dmel_CG4265.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S60346 Genomic DNA. Translation: AAA15411.1 .
    X69678 mRNA. Translation: CAA49358.1 .
    X69679 Genomic DNA. Translation: CAA49359.1 .
    AE014134 Genomic DNA. Translation: AAF51291.1 .
    AF145600 mRNA. Translation: AAD38575.1 .
    PIRi S33956.
    RefSeqi NP_001188681.1. NM_001201752.2.
    NP_476940.1. NM_057592.4.
    UniGenei Dm.4794.

    3D structure databases

    ProteinModelPortali P35122.
    SMRi P35122. Positions 4-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59626. 62 interactions.
    MINTi MINT-1599795.

    Protein family/group databases

    MEROPSi C12.008.

    Proteomic databases

    PaxDbi P35122.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077844 ; FBpp0077516 ; FBgn0010288 .
    FBtr0303459 ; FBpp0292511 ; FBgn0010288 .
    GeneIDi 33397.
    KEGGi dme:Dmel_CG4265.

    Organism-specific databases

    CTDi 33397.
    FlyBasei FBgn0010288. Uch.

    Phylogenomic databases

    eggNOGi NOG327708.
    GeneTreei ENSGT00510000046640.
    InParanoidi P35122.
    KOi K05609.
    OMAi YVCFVKG.
    OrthoDBi EOG7S7SFK.
    PhylomeDBi P35122.

    Miscellaneous databases

    GenomeRNAii 33397.
    NextBioi 783351.

    Gene expression databases

    Bgeei P35122.

    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.
    PROSITEi PS00140. UCH_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases."
      Wilkinson K.D., Deshpande S., Larsen C.N.
      Biochem. Soc. Trans. 20:631-637(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and analysis of expression of a ubiquitin carboxyl terminal hydrolase expressed during oogenesis in Drosophila melanogaster."
      Zhang N., Wilkinson K., Bownes M.
      Dev. Biol. 157:214-223(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE.
      Strain: Oregon-R.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiUCHL_DROME
    AccessioniPrimary (citable) accession number: P35122
    Secondary accession number(s): Q4PIX7, Q9TWA0, Q9V417
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 105 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