Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O94579

- PSA2_SCHPO

UniProt

O94579 - PSA2_SCHPO

Protein

Probable proteasome subunit alpha type-2

Gene

pre8

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Protein family/group databases

    MEROPSiT01.A11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable proteasome subunit alpha type-2 (EC:3.4.25.1)
    Gene namesi
    Name:pre8
    ORF Names:SPCC1442.06
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome III

    Organism-specific databases

    PomBaseiSPCC1442.06.

    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 – 245245Probable proteasome subunit alpha type-2PRO_0000124089Add
    BLAST

    Proteomic databases

    MaxQBiO94579.
    PaxDbiO94579.

    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

    BioGridi275599. 9 interactions.
    MINTiMINT-4685310.
    STRINGi4896.SPCC1442.06-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO94579.
    SMRiO94579. Positions 1-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091085.
    KOiK02726.
    OMAiWKATALG.
    OrthoDBiEOG7SBP0C.
    PhylomeDBiO94579.

    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.

    O94579-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDKYAFSLT TFSPNGKLVQ IEYALNAVNA GVTSVGIKAT DGVVLATEKK    50
    PTSELAIGAS LEKVCAITPD IGMVYSGMGP DFRVLVDKSR KVAQTTYKKI 100
    YNEYPPTKIL VQEIASVMQE STQSGGVRPF GVSLLVAGMD EKGPSLYQVD 150
    PSGTYFAWKA TAIGKSSTAA KTFLEKRYND ELELDDAVHT AILALKETFE 200
    GELTEDNIEI AVVSTKPTDS GIVGVPGGHF CRLSQSEIRD YLDQV 245
    Length:245
    Mass (Da):26,404
    Last modified:May 1, 1999 - v1
    Checksum:iCFCCA93537D2464A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329672 Genomic DNA. Translation: CAA21440.1.
    PIRiT40971.
    RefSeqiNP_588320.1. NM_001023311.2.

    Genome annotation databases

    EnsemblFungiiSPCC1442.06.1; SPCC1442.06.1:pep; SPCC1442.06.
    GeneIDi2539026.
    KEGGispo:SPCC1442.06.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329672 Genomic DNA. Translation: CAA21440.1 .
    PIRi T40971.
    RefSeqi NP_588320.1. NM_001023311.2.

    3D structure databases

    ProteinModelPortali O94579.
    SMRi O94579. Positions 1-243.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 275599. 9 interactions.
    MINTi MINT-4685310.
    STRINGi 4896.SPCC1442.06-1.

    Protein family/group databases

    MEROPSi T01.A11.

    Proteomic databases

    MaxQBi O94579.
    PaxDbi O94579.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPCC1442.06.1 ; SPCC1442.06.1:pep ; SPCC1442.06 .
    GeneIDi 2539026.
    KEGGi spo:SPCC1442.06.

    Organism-specific databases

    PomBasei SPCC1442.06.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091085.
    KOi K02726.
    OMAi WKATALG.
    OrthoDBi EOG7SBP0C.
    PhylomeDBi O94579.

    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 20800200.
    PROi O94579.

    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].

    Entry informationi

    Entry nameiPSA2_SCHPO
    AccessioniPrimary (citable) accession number: O94579
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 1, 1999
    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