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Q9XYN7

- PSB3_DROME

UniProt

Q9XYN7 - PSB3_DROME

Protein

Proteasome subunit beta type-3

Gene

Prosbeta3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    GO - Molecular functioni

    1. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: FlyBase
    2. neurogenesis Source: FlyBase
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    ReactomeiREACT_180649. Activation of NF-kappaB in B cells.
    REACT_180655. ER-Phagosome pathway.
    REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_181662. Separation of Sister Chromatids.
    REACT_184330. Asymmetric localization of PCP proteins.
    REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_215026. degradation of AXIN.
    REACT_218589. Orc1 removal from chromatin.
    REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-3 (EC:3.4.25.1)
    Alternative name(s):
    20S proteasome subunit beta-3
    Gene namesi
    Name:Prosbeta3
    ORF Names:CG11980
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0026380. Prosbeta3.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205Proteasome subunit beta type-3PRO_0000148062Add
    BLAST

    Proteomic databases

    PaxDbiQ9XYN7.
    PRIDEiQ9XYN7.

    Expressioni

    Gene expression databases

    BgeeiQ9XYN7.

    Interactioni

    Subunit structurei

    The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel By similarity.By similarity

    Protein-protein interaction databases

    BioGridi66247. 57 interactions.
    DIPiDIP-18901N.
    IntActiQ9XYN7. 16 interactions.
    MINTiMINT-306832.
    STRINGi7227.FBpp0081488.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XYN7.
    SMRiQ9XYN7. Positions 2-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074820.
    InParanoidiQ9XYN7.
    KOiK02735.
    OMAiMDLIGCP.
    OrthoDBiEOG783MWB.
    PhylomeDBiQ9XYN7.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9XYN7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSILAYNGGC VVAMRGKDCV AIATDHRFGI QAQTISTDFK KVFHIGPRMF    50
    LGLTGLQTDI LTVRDRLMFR KNLYETRENR EMCPKPFSAM MSSFLYEHRF 100
    GPYFIEPVVA GLDPKTMEPF ICNMDLIGCP NAPDDFVVAG TCAEQLYGMC 150
    ETLWKPDLEP DQLFEVIAQS IVNAFDRDAM SGWGATVYII EKDKITERTL 200
    KTRMD 205
    Length:205
    Mass (Da):23,234
    Last modified:November 1, 1999 - v1
    Checksum:i3AE365887AF3A247
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF116898 Genomic DNA. Translation: AAD22968.1.
    AM294562 Genomic DNA. Translation: CAL26545.1.
    AM294563 Genomic DNA. Translation: CAL26546.1.
    AM294564 Genomic DNA. Translation: CAL26547.1.
    AM294565 Genomic DNA. Translation: CAL26548.1.
    AM294566 Genomic DNA. Translation: CAL26549.1.
    AM294567 Genomic DNA. Translation: CAL26550.1.
    AM294568 Genomic DNA. Translation: CAL26551.1.
    AM294569 Genomic DNA. Translation: CAL26552.1.
    AE014297 Genomic DNA. Translation: AAF54320.1.
    AY095029 mRNA. Translation: AAM11357.1.
    RefSeqiNP_649858.1. NM_141601.2.
    UniGeneiDm.6972.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082010; FBpp0081488; FBgn0026380.
    GeneIDi41079.
    KEGGidme:Dmel_CG11981.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF116898 Genomic DNA. Translation: AAD22968.1 .
    AM294562 Genomic DNA. Translation: CAL26545.1 .
    AM294563 Genomic DNA. Translation: CAL26546.1 .
    AM294564 Genomic DNA. Translation: CAL26547.1 .
    AM294565 Genomic DNA. Translation: CAL26548.1 .
    AM294566 Genomic DNA. Translation: CAL26549.1 .
    AM294567 Genomic DNA. Translation: CAL26550.1 .
    AM294568 Genomic DNA. Translation: CAL26551.1 .
    AM294569 Genomic DNA. Translation: CAL26552.1 .
    AE014297 Genomic DNA. Translation: AAF54320.1 .
    AY095029 mRNA. Translation: AAM11357.1 .
    RefSeqi NP_649858.1. NM_141601.2.
    UniGenei Dm.6972.

    3D structure databases

    ProteinModelPortali Q9XYN7.
    SMRi Q9XYN7. Positions 2-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66247. 57 interactions.
    DIPi DIP-18901N.
    IntActi Q9XYN7. 16 interactions.
    MINTi MINT-306832.
    STRINGi 7227.FBpp0081488.

    Proteomic databases

    PaxDbi Q9XYN7.
    PRIDEi Q9XYN7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082010 ; FBpp0081488 ; FBgn0026380 .
    GeneIDi 41079.
    KEGGi dme:Dmel_CG11981.

    Organism-specific databases

    CTDi 41079.
    FlyBasei FBgn0026380. Prosbeta3.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074820.
    InParanoidi Q9XYN7.
    KOi K02735.
    OMAi MDLIGCP.
    OrthoDBi EOG783MWB.
    PhylomeDBi Q9XYN7.

    Enzyme and pathway databases

    Reactomei REACT_180649. Activation of NF-kappaB in B cells.
    REACT_180655. ER-Phagosome pathway.
    REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_181662. Separation of Sister Chromatids.
    REACT_184330. Asymmetric localization of PCP proteins.
    REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_215026. degradation of AXIN.
    REACT_218589. Orc1 removal from chromatin.
    REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

    Miscellaneous databases

    GenomeRNAii 41079.
    NextBioi 822046.
    PROi Q9XYN7.

    Gene expression databases

    Bgeei Q9XYN7.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit."
      Smyth K.A., Belote J.M.
      Genetics 151:211-220(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: Samarkand.
    2. "Widespread adaptive evolution of Drosophila genes with sex-biased expression."
      Proeschel M., Zhang Z., Parsch J.
      Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL82, ZBMEL84 and ZBMEL95.
    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: Embryo.

    Entry informationi

    Entry nameiPSB3_DROME
    AccessioniPrimary (citable) accession number: Q9XYN7
    Secondary accession number(s): A0APH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 113 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