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Q9VQE5

- PSB2_DROME

UniProt

Q9VQE5 - PSB2_DROME

Protein

Probable proteasome subunit beta type-2

Gene

Prosbeta4R2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (25 Jul 2003)
      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. proteolysis involved in cellular protein catabolic process Source: InterPro

    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

    MEROPSiT01.984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable proteasome subunit beta type-2 (EC:3.4.25.1)
    Gene namesi
    Name:Prosbeta4R2
    ORF Names:CG17302
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0031443. Prosbeta4R2.

    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: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 210210Probable proteasome subunit beta type-2PRO_0000148047Add
    BLAST

    Proteomic databases

    PaxDbiQ9VQE5.
    PRIDEiQ9VQE5.

    Expressioni

    Gene expression databases

    BgeeiQ9VQE5.

    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

    BioGridi59678. 13 interactions.
    IntActiQ9VQE5. 1 interaction.
    MINTiMINT-1573384.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VQE5.
    SMRiQ9VQE5. Positions 3-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00640000091536.
    InParanoidiQ9VQE5.
    KOiK02734.
    OMAiNTRYQVA.
    OrthoDBiEOG7N63NQ.
    PhylomeDBiQ9VQE5.

    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.

    Q9VQE5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMETILGIK GPDFVMLASD TMQAKSLVFM KDDQSKIHRL SDFNMMATVG    50
    DGGDTIQFTD FISKNLHLYK ISHGYHLSAK SAAHFTRKTL ADYIRTNTRY 100
    QVAMLLAGYD AVEGPDLHYI DSYGAAQSIN HAGHGWGSMF CGSILQRYWN 150
    SKLSQEDAYS LMKKCVLEIQ RRLIINQRNF EVYVVDSKGM RKMEAINPGS 200
    LNKESISLSW 210
    Length:210
    Mass (Da):23,721
    Last modified:July 25, 2003 - v3
    Checksum:i1B568F3FFCC3C3EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF51229.3.
    AY119488 mRNA. Translation: AAM50142.1.
    RefSeqiNP_001259950.1. NM_001273021.1.
    NP_722823.2. NM_164491.3.
    UniGeneiDm.2603.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077699; FBpp0077383; FBgn0031443.
    FBtr0332513; FBpp0304788; FBgn0031443.
    GeneIDi33451.
    KEGGidme:Dmel_CG17302.
    UCSCiCG17302-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF51229.3 .
    AY119488 mRNA. Translation: AAM50142.1 .
    RefSeqi NP_001259950.1. NM_001273021.1.
    NP_722823.2. NM_164491.3.
    UniGenei Dm.2603.

    3D structure databases

    ProteinModelPortali Q9VQE5.
    SMRi Q9VQE5. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 59678. 13 interactions.
    IntActi Q9VQE5. 1 interaction.
    MINTi MINT-1573384.

    Protein family/group databases

    MEROPSi T01.984.

    Proteomic databases

    PaxDbi Q9VQE5.
    PRIDEi Q9VQE5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077699 ; FBpp0077383 ; FBgn0031443 .
    FBtr0332513 ; FBpp0304788 ; FBgn0031443 .
    GeneIDi 33451.
    KEGGi dme:Dmel_CG17302.
    UCSCi CG17302-RA. d. melanogaster.

    Organism-specific databases

    CTDi 33451.
    FlyBasei FBgn0031443. Prosbeta4R2.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00640000091536.
    InParanoidi Q9VQE5.
    KOi K02734.
    OMAi NTRYQVA.
    OrthoDBi EOG7N63NQ.
    PhylomeDBi Q9VQE5.

    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 33451.
    NextBioi 783640.

    Gene expression databases

    Bgeei Q9VQE5.

    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 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: Head.
    4. "Expression of proteasome subunit isoforms during spermatogenesis in Drosophila melanogaster."
      Ma J., Katz E., Belote J.M.
      Insect Mol. Biol. 11:627-639(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiPSB2_DROME
    AccessioniPrimary (citable) accession number: Q9VQE5
    Secondary accession number(s): Q8MRP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: July 25, 2003
    Last modified: October 1, 2014
    This is version 105 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