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Q9VNA5

- PSB4_DROME

UniProt

Q9VNA5 - PSB4_DROME

Protein

Proteasome subunit beta type-4

Gene

Prosbeta7

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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 By similarity.By similarity

    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. cell proliferation Source: FlyBase
    2. cellular process Source: FlyBase
    3. cellular response to DNA damage stimulus Source: FlyBase
    4. centrosome organization Source: FlyBase
    5. mitotic spindle elongation Source: FlyBase
    6. mitotic spindle organization Source: FlyBase
    7. neurogenesis Source: FlyBase
    8. 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.

    Protein family/group databases

    MEROPSiT01.987.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-4 (EC:3.4.25.1)
    Alternative name(s):
    Proteasome subunit beta type-7
    Gene namesi
    Name:Prosbeta7
    Synonyms:Prosb4, Prosbeta4
    ORF Names:CG12000
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0250746. Prosbeta7.

    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 – 268268Proteasome subunit beta type-4PRO_0000148071Add
    BLAST

    Proteomic databases

    PaxDbiQ9VNA5.
    PRIDEiQ9VNA5.

    Expressioni

    Gene expression databases

    BgeeiQ9VNA5.

    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

    BioGridi65850. 41 interactions.
    DIPiDIP-19164N.
    IntActiQ9VNA5. 8 interactions.
    MINTiMINT-924269.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VNA5.
    SMRiQ9VNA5. Positions 56-265.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00390000000698.
    InParanoidiQ9VNA5.
    KOiK02736.
    OMAiRIMRVND.
    OrthoDBiEOG74FF1D.
    PhylomeDBiQ9VNA5.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9VNA5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNNYNSLAQ PMWQNGPAPG EFYNFTGGQT PVQQLPRELT TMGPYGTKHS    50
    TASSTTGTSV LGIRYDSGVM LAADTLVSYG SMARYQNIER VFKVNKNILL 100
    GGSGDFADIQ SIKRNIDQKM IEDQCCDDNI EMKPKSLASW MTRVLYNRRS 150
    RMNPLYIDVV VGGVDNEGTP YLANVDLRGR SYEDYVVATG FARHLAVPLV 200
    REKKPKDRDF TAVEASELIR TCMEVLYYRD TRNISQYTVG VCSVNGCGVE 250
    GPFQVNENWT FAETIKGY 268
    Length:268
    Mass (Da):29,986
    Last modified:May 1, 2000 - v1
    Checksum:i215433952659EAD0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF52041.1.
    AE014297 Genomic DNA. Translation: AAN13277.1.
    AY118936 mRNA. Translation: AAM50796.1.
    RefSeqiNP_649529.1. NM_141272.1.
    NP_730922.1. NM_169049.2.
    UniGeneiDm.11642.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078805; FBpp0078448; FBgn0250746.
    FBtr0078806; FBpp0078449; FBgn0250746.
    GeneIDi40639.
    KEGGidme:Dmel_CG12000.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF52041.1 .
    AE014297 Genomic DNA. Translation: AAN13277.1 .
    AY118936 mRNA. Translation: AAM50796.1 .
    RefSeqi NP_649529.1. NM_141272.1.
    NP_730922.1. NM_169049.2.
    UniGenei Dm.11642.

    3D structure databases

    ProteinModelPortali Q9VNA5.
    SMRi Q9VNA5. Positions 56-265.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65850. 41 interactions.
    DIPi DIP-19164N.
    IntActi Q9VNA5. 8 interactions.
    MINTi MINT-924269.

    Protein family/group databases

    MEROPSi T01.987.

    Proteomic databases

    PaxDbi Q9VNA5.
    PRIDEi Q9VNA5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078805 ; FBpp0078448 ; FBgn0250746 .
    FBtr0078806 ; FBpp0078449 ; FBgn0250746 .
    GeneIDi 40639.
    KEGGi dme:Dmel_CG12000.

    Organism-specific databases

    CTDi 40639.
    FlyBasei FBgn0250746. Prosbeta7.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00390000000698.
    InParanoidi Q9VNA5.
    KOi K02736.
    OMAi RIMRVND.
    OrthoDBi EOG74FF1D.
    PhylomeDBi Q9VNA5.

    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 40639.
    NextBioi 819792.
    PROi Q9VNA5.

    Gene expression databases

    Bgeei Q9VNA5.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
    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 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: Embryo.
    4. "Genes required for mitotic spindle assembly in Drosophila S2 cells."
      Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M., Vale R.D., Stuurman N.
      Science 316:417-421(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiPSB4_DROME
    AccessioniPrimary (citable) accession number: Q9VNA5
    Secondary accession number(s): A4V2F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 112 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