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Q09841

- PSB2_SCHPO

UniProt

Q09841 - PSB2_SCHPO

Protein

Probable proteasome subunit beta type-2

Gene

pup1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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 Potential.Curated

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361NucleophileBy 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

    MEROPSiT01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable proteasome subunit beta type-2 (EC:3.4.25.1)
    Gene namesi
    Name:pup1
    ORF Names:SPAC23D3.07
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC23D3.07.

    Subcellular locationi

    Cytoplasm 1 PublicationPROSITE-ProRule annotation. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. nuclear envelope Source: PomBase
    3. nucleus Source: PomBase
    4. 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 – 3535Removed in mature formBy similarityPRO_0000026655Add
    BLAST
    Chaini36 – 267232Probable proteasome subunit beta type-2PRO_0000026656Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiQ09841.
    PaxDbiQ09841.

    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

    BioGridi278296. 2 interactions.
    MINTiMINT-4695632.
    STRINGi4896.SPAC23D3.07-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ09841.
    SMRiQ09841. Positions 36-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000182856.
    KOiK02739.
    OMAiQIWCAGA.
    OrthoDBiEOG7TJ3V6.
    PhylomeDBiQ09841.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF12465. Pr_beta_C. 1 hit.
    PF00227. 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.

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

    Q09841-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMGINERKGF DFEYYQRNLL LQEKGFPTPK ATSTGTTIVG VIAKDCIVLG    50
    ADTRATAGPI IADKNCKKLH LISPNIWCAG AGTAADTEFV TSMISSNIEL 100
    HSLYTNRKPR VVTALTMLKQ HLFRYQGHIG AYLVLGGYDC KGPHLFTIAA 150
    HGSSDKLPYV ALGSGSLAAI SVLETKYQPD LERHEAMELV KEAIEAGIFN 200
    DLGSGSNCDL VVIDEEKATP YRGYSKPNER ATKQSKYTYD RGTTAVLKED 250
    IYKFVTVQDL DEMQVDV 267
    Length:267
    Mass (Da):29,337
    Last modified:February 1, 1996 - v1
    Checksum:i646764EBE1E3CFBF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA91242.1.
    AB000540 mRNA. Translation: BAA19146.1.
    PIRiT38282. S62498.
    RefSeqiNP_594544.1. NM_001019973.2.

    Genome annotation databases

    EnsemblFungiiSPAC23D3.07.1; SPAC23D3.07.1:pep; SPAC23D3.07.
    GeneIDi2541805.
    KEGGispo:SPAC23D3.07.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA91242.1 .
    AB000540 mRNA. Translation: BAA19146.1 .
    PIRi T38282. S62498.
    RefSeqi NP_594544.1. NM_001019973.2.

    3D structure databases

    ProteinModelPortali Q09841.
    SMRi Q09841. Positions 36-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278296. 2 interactions.
    MINTi MINT-4695632.
    STRINGi 4896.SPAC23D3.07-1.

    Protein family/group databases

    MEROPSi T01.011.

    Proteomic databases

    MaxQBi Q09841.
    PaxDbi Q09841.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC23D3.07.1 ; SPAC23D3.07.1:pep ; SPAC23D3.07 .
    GeneIDi 2541805.
    KEGGi spo:SPAC23D3.07.

    Organism-specific databases

    PomBasei SPAC23D3.07.

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000182856.
    KOi K02739.
    OMAi QIWCAGA.
    OrthoDBi EOG7TJ3V6.
    PhylomeDBi Q09841.

    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 20802893.
    PROi Q09841.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF12465. Pr_beta_C. 1 hit.
    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 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. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
      Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
      DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-267.
      Strain: PR745.
    3. "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 nameiPSB2_SCHPO
    AccessioniPrimary (citable) accession number: Q09841
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 116 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