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Q9UT97

- PSA5_SCHPO

UniProt

Q9UT97 - PSA5_SCHPO

Protein

Probable proteasome subunit alpha type-5

Gene

pup2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (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.PROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: PomBase
    2. regulation of mitotic cell cycle Source: PomBase

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    ReactomeiREACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_188566. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_188568. ER-Phagosome pathway.
    REACT_188587. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_208775. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_215140. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_215320. Orc1 removal from chromatin.
    REACT_218991. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_81558. Regulation of activated PAK-2p34 by proteasome mediated degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable proteasome subunit alpha type-5 (EC:3.4.25.1)
    Gene namesi
    Name:pup2
    ORF Names:SPAC323.02c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC323.02c.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. nucleus Source: PomBase
    3. proteasome core complex, alpha-subunit complex Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 247247Probable proteasome subunit alpha type-5PRO_0000124128Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UT97.
    PaxDbiQ9UT97.
    PRIDEiQ9UT97.

    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

    BioGridi279634. 9 interactions.
    IntActiQ9UT97. 3 interactions.
    MINTiMINT-4709913.
    STRINGi4896.SPAC323.02c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UT97.
    SMRiQ9UT97. Positions 6-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091085.
    KOiK02729.
    OMAiCAMSGLT.
    OrthoDBiEOG7SBP0C.
    PhylomeDBiQ9UT97.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view]
    SMARTiSM00948. Proteasome_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UT97-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFMTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKDAVVLGV    50
    EKRLTSPLME SHSVEKLFEI DSHIGCAISG LTADARTIIE HARVQTQNHR 100
    FTYDEPQGIE STTQSICDLA LRFGEGEDGE ERIMSRPFGV ALLIAGIDEH 150
    GPQLYHSEPS GTYFRYEAKA IGSGSEPAKS ELVKEFHKDM TLEEAEVLIL 200
    KVLRQVMEEK LDSKNVQLAK VTAEGGFHIY NDEEMADAVA REQQRMD 247
    Length:247
    Mass (Da):27,573
    Last modified:May 1, 2000 - v1
    Checksum:i713E1AB3A3ADE658
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB53405.1.
    PIRiT38639.
    RefSeqiNP_594372.1. NM_001019793.2.

    Genome annotation databases

    EnsemblFungiiSPAC323.02c.1; SPAC323.02c.1:pep; SPAC323.02c.
    GeneIDi2543205.
    KEGGispo:SPAC323.02c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB53405.1 .
    PIRi T38639.
    RefSeqi NP_594372.1. NM_001019793.2.

    3D structure databases

    ProteinModelPortali Q9UT97.
    SMRi Q9UT97. Positions 6-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279634. 9 interactions.
    IntActi Q9UT97. 3 interactions.
    MINTi MINT-4709913.
    STRINGi 4896.SPAC323.02c-1.

    Proteomic databases

    MaxQBi Q9UT97.
    PaxDbi Q9UT97.
    PRIDEi Q9UT97.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC323.02c.1 ; SPAC323.02c.1:pep ; SPAC323.02c .
    GeneIDi 2543205.
    KEGGi spo:SPAC323.02c.

    Organism-specific databases

    PomBasei SPAC323.02c.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091085.
    KOi K02729.
    OMAi CAMSGLT.
    OrthoDBi EOG7SBP0C.
    PhylomeDBi Q9UT97.

    Enzyme and pathway databases

    Reactomei REACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_188566. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_188568. ER-Phagosome pathway.
    REACT_188587. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_208775. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_215140. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_215320. Orc1 removal from chromatin.
    REACT_218991. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_81558. Regulation of activated PAK-2p34 by proteasome mediated degradation.

    Miscellaneous databases

    NextBioi 20804228.
    PROi Q9UT97.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPSA5_SCHPO
    AccessioniPrimary (citable) accession number: Q9UT97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3