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O43063

- PSB1_SCHPO

UniProt

O43063 - PSB1_SCHPO

Protein

Probable proteasome subunit beta type-1

Gene

pre3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei25 – 251NucleophileBy similarity

    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

    MEROPSiT01.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable proteasome subunit beta type-1 (EC:3.4.25.1)
    Gene namesi
    Name:pre3
    ORF Names:SPBC4C3.10c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC4C3.10c.

    Subcellular locationi

    Cytoplasm 1 PublicationPROSITE-ProRule annotation. Nucleus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 2424Removed in mature formBy similarityPRO_0000026641Add
    BLAST
    Chaini25 – 226202Probable proteasome subunit beta type-1PRO_0000026642Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiO43063.
    PaxDbiO43063.

    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

    BioGridi277395. 5 interactions.
    MINTiMINT-4675013.
    STRINGi4896.SPBC4C3.10c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO43063.
    SMRiO43063. Positions 16-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091079.
    KOiK02738.
    OMAiTSIMAVQ.
    OrthoDBiEOG7XDBSV.
    PhylomeDBiO43063.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O43063-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATTVKDTMN VDINAIKKGE IRMGTTITAL RYKDGVILAA DSRTTMGAYI    50
    ANRVTDKLTQ LTDNIWCCRS GSAADTQTVA DLLKYYLSMY RIQFGHDPSV 100
    HTAATLASEM CYQNKNMLSA GLIVAGYDEK TGGDVYSIPL GGSLHKQPLA 150
    IGGSGSAFIY GFCDANFREN MTQEEAVEFL KNAVALAMER DGSSGGTIRM 200
    VILNKDGMER KFFAIDTANP IPVFTH 226
    Length:226
    Mass (Da):24,564
    Last modified:June 1, 1998 - v1
    Checksum:i88AEEF4B2A87093A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA16832.1.
    PIRiT40487.
    RefSeqiNP_596295.1. NM_001022216.2.

    Genome annotation databases

    EnsemblFungiiSPBC4C3.10c.1; SPBC4C3.10c.1:pep; SPBC4C3.10c.
    GeneIDi2540878.
    KEGGispo:SPBC4C3.10c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA16832.1 .
    PIRi T40487.
    RefSeqi NP_596295.1. NM_001022216.2.

    3D structure databases

    ProteinModelPortali O43063.
    SMRi O43063. Positions 16-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277395. 5 interactions.
    MINTi MINT-4675013.
    STRINGi 4896.SPBC4C3.10c-1.

    Protein family/group databases

    MEROPSi T01.010.

    Proteomic databases

    MaxQBi O43063.
    PaxDbi O43063.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC4C3.10c.1 ; SPBC4C3.10c.1:pep ; SPBC4C3.10c .
    GeneIDi 2540878.
    KEGGi spo:SPBC4C3.10c.

    Organism-specific databases

    PomBasei SPBC4C3.10c.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091079.
    KOi K02738.
    OMAi TSIMAVQ.
    OrthoDBi EOG7XDBSV.
    PhylomeDBi O43063.

    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 20801994.
    PROi O43063.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    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 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 nameiPSB1_SCHPO
    AccessioniPrimary (citable) accession number: O43063
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 111 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