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Q9VVR1

- NOT_DROME

UniProt

Q9VVR1 - NOT_DROME

Protein

Ubiquitin carboxyl-terminal hydrolase nonstop

Gene

not

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 114 (01 Oct 2014)
      Sequence version 3 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of histone H2B, thereby acting as a coactivator in a large subset of genes. Required to counteract heterochromatin silencing. Controls the development of neuronal connectivity in visual system by being required for accurate axon targeting in the optic lobe. Required for expression of ecdysone-induced genes such as br/broad.3 Publications

    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 sitei406 – 4061NucleophilePROSITE-ProRule annotation
    Active sitei689 – 6891Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri283 – 34260UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. protein binding Source: FlyBase
    3. ubiquitinyl hydrolase activity Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. axon guidance Source: FlyBase
    2. axon target recognition Source: FlyBase
    3. chromatin modification Source: UniProtKB
    4. chromatin organization Source: FlyBase
    5. glial cell development Source: FlyBase
    6. glial cell migration Source: FlyBase
    7. histone deubiquitination Source: FlyBase
    8. positive regulation of transcription, DNA-templated Source: UniProtKB
    9. protein deubiquitination Source: FlyBase
    10. regulation of transcription, DNA-templated Source: FlyBase
    11. transcription, DNA-templated Source: UniProtKB-KW
    12. ubiquitin-dependent protein catabolic process Source: FlyBase

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.095.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase nonstop (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme nonstop
    Ubiquitin thioesterase nonstop
    Ubiquitin-specific-processing protease nonstop
    Gene namesi
    Name:not
    ORF Names:CG4166
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0013717. not.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: FlyBase
    2. SAGA complex Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Defects in the number and migration of glial cells located within the lamina plexus of the developing eye; the lack of glial cells causing mistargeting of the R1-R6 axons in the optic lobe. Lamina neuron development is normal.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 735735Ubiquitin carboxyl-terminal hydrolase nonstopPRO_0000367514Add
    BLAST

    Proteomic databases

    PaxDbiQ9VVR1.
    PRIDEiQ9VVR1.

    Expressioni

    Tissue specificityi

    Expressed in the optic lobe and central brain. Highly expressed in the lamina precursor cells but not in differentiated lamina neurons. Also expressed in marginal, epithelial and medulla glial cells adjacent to the lamina plexus.1 Publication

    Gene expression databases

    BgeeiQ9VVR1.

    Interactioni

    Subunit structurei

    Component of the SAGA transcription coactivator-HAT complex, at least composed of Ada2b, not/nonstop, Pcaf/Gcn5, Sgf11 and Spt3.1 Publication

    Protein-protein interaction databases

    BioGridi65311. 5 interactions.
    IntActiQ9VVR1. 4 interactions.
    MINTiMINT-6179419.
    STRINGi7227.FBpp0288698.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VVR1.
    SMRiQ9VVR1. Positions 296-727.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini397 – 730334USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. UBP8 subfamily.Curated
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri283 – 34260UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5533.
    InParanoidiQ9U6Q9.
    KOiK11366.
    OrthoDBiEOG7FR7G7.
    PhylomeDBiQ9VVR1.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR015880. Znf_C2H2-like.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 2 hits.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VVR1-1 [UniParc]FASTAAdd to Basket

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    MFQYSYIRKI PMPTSEYDFA TGHTDSCLLP THMRACVCVC VQCEIETRKA    50
    SEKSQKFTKK KPNYFQNWAA RRRTAKVAKI RRKQRKCDKA FVPLQSSAKR 100
    AKTKENSVDS NTSVFSSSSS SSSGRSFGRG TERWAVGAEA GRGTAENETL 150
    AVAAAAATTT NAGRFITADL IKTVNSDKQR DRVAKGHRDA KNPLDATKHL 200
    RLSDCLRTVQ KLAIELESAD AGSDASAQAN ASADASSAVM SETGCRHYQS 250
    YVKEHSYDTF RVIDAYFAAC VNRDARERKA IHCNCFECGS YGIQLYACLH 300
    CIYFGCRGAH ITSHLRSKKH NVALELSHGT LYCYACRDFI YDARSREYAL 350
    INRKLEAKDL QKSIGWVPWV PTTKETNLLL ANARRRLVRP NQTIGLRGLL 400
    NLGATCFMNC IVQALVHTPL LSDYFMSDRH DCGSKSSHKC LVCEVSRLFQ 450
    EFYSGSRSPL SLHRLLHLIW NHAKHLAGYE QQDAHEFFIA TLDVLHRHCV 500
    KAKAEHESKS NSSGSGSGTN SSNSSSSHCY GQCNCIIDQI FTGMLQSDVV 550
    CQACNGVSTT YDPFWDISLD LGETTTHGGV TPKTLIDCLE RYTRAEHLGS 600
    AAKIKCSTCK SYQESTKQFS LRTLPSVVSF HLKRFEHSAL IDRKISSFIQ 650
    FPVEFDMTPF MSEKKNAYGD FRFSLYAVVN HVGTIDTGHY TAYVRHQKDT 700
    WVKCDDHVIT MASLKQVLDS EGYLLFYHKN VLEYE 735
    Length:735
    Mass (Da):82,458
    Last modified:April 14, 2009 - v3
    Checksum:iEAE3F4B1DBFF850F
    GO

    Sequence cautioni

    The sequence AAL13936.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAF49249.2 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901A → T in AAD53181. (PubMed:11182084)Curated
    Sequence conflicti199 – 1991H → N in AAD53181. (PubMed:11182084)Curated
    Sequence conflicti235 – 2351A → D in AAD53181. (PubMed:11182084)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF179590 Genomic DNA. Translation: AAD53181.1.
    AE014296 Genomic DNA. Translation: AAF49249.2. Sequence problems.
    AY058707 mRNA. Translation: AAL13936.1. Different initiation.
    RefSeqiNP_524140.2. NM_079416.4.
    UniGeneiDm.2731.

    Genome annotation databases

    GeneIDi40030.
    KEGGidme:Dmel_CG4166.
    UCSCiCG4166-RB. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF179590 Genomic DNA. Translation: AAD53181.1 .
    AE014296 Genomic DNA. Translation: AAF49249.2 . Sequence problems.
    AY058707 mRNA. Translation: AAL13936.1 . Different initiation.
    RefSeqi NP_524140.2. NM_079416.4.
    UniGenei Dm.2731.

    3D structure databases

    ProteinModelPortali Q9VVR1.
    SMRi Q9VVR1. Positions 296-727.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65311. 5 interactions.
    IntActi Q9VVR1. 4 interactions.
    MINTi MINT-6179419.
    STRINGi 7227.FBpp0288698.

    Protein family/group databases

    MEROPSi C19.095.

    Proteomic databases

    PaxDbi Q9VVR1.
    PRIDEi Q9VVR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 40030.
    KEGGi dme:Dmel_CG4166.
    UCSCi CG4166-RB. d. melanogaster.

    Organism-specific databases

    CTDi 40030.
    FlyBasei FBgn0013717. not.

    Phylogenomic databases

    eggNOGi COG5533.
    InParanoidi Q9U6Q9.
    KOi K11366.
    OrthoDBi EOG7FR7G7.
    PhylomeDBi Q9VVR1.

    Miscellaneous databases

    GenomeRNAii 40030.
    NextBioi 816633.

    Gene expression databases

    Bgeei Q9VVR1.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR015880. Znf_C2H2-like.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 2 hits.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Glial cells mediate target layer selection of retinal axons in the developing visual system of Drosophila."
      Poeck B., Fischer S., Gunning D., Zipursky S.L., Salecker I.
      Neuron 29:99-113(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-735.
      Strain: Berkeley.
      Tissue: Embryo.
    5. "SAGA-mediated H2B deubiquitination controls the development of neuronal connectivity in the Drosophila visual system."
      Weake V.M., Lee K.K., Guelman S., Lin C.-H., Seidel C., Abmayr S.M., Workman J.L.
      EMBO J. 27:394-405(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN THE SAGA COMPLEX, INTERACTION WITH SGF11.
    6. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
      Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
      Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiNOT_DROME
    AccessioniPrimary (citable) accession number: Q9VVR1
    Secondary accession number(s): Q95TK9, Q9U6Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 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