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P23724

- PSB6_YEAST

UniProt

P23724 - PSB6_YEAST

Protein

Proteasome subunit beta type-6

Gene

PRE7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It has an ATP-dependent proteolytic activity.

    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. proteasomal ubiquitin-independent protein catabolic process Source: SGD
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28942-MONOMER.
    ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_189025. ER-Phagosome pathway.
    REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_83036. Orc1 removal from chromatin.

    Protein family/group databases

    MEROPSiT01.A12.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-6 (EC:3.4.25.1)
    Alternative name(s):
    Multicatalytic endopeptidase complex subunit C5
    Proteasome component C5
    Gene namesi
    Name:PRE7
    Synonyms:PRS3, PTS1
    Ordered Locus Names:YBL041W
    ORF Names:YBL0407
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL041w.
    SGDiS000000137. PRE7.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: SGD
    2. nucleus Source: SGD
    3. proteasome core complex, beta-subunit complex Source: SGD
    4. proteasome storage granule Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1919PRO_0000331489Add
    BLAST
    Chaini20 – 241222Proteasome subunit beta type-6PRO_0000148042Add
    BLAST

    Proteomic databases

    MaxQBiP23724.
    PaxDbiP23724.
    PeptideAtlasiP23724.

    2D gel databases

    UCD-2DPAGEP23724.

    Expressioni

    Gene expression databases

    GenevestigatoriP23724.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi32656. 41 interactions.
    DIPiDIP-2821N.
    IntActiP23724. 16 interactions.
    MINTiMINT-592611.
    STRINGi4932.YBL041W.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 356
    Beta strandi40 – 456
    Beta strandi48 – 503
    Beta strandi53 – 575
    Beta strandi62 – 643
    Beta strandi70 – 767
    Helixi77 – 9721
    Turni98 – 1003
    Helixi105 – 11713
    Turni118 – 1214
    Beta strandi126 – 1338
    Beta strandi139 – 1446
    Beta strandi146 – 1483
    Beta strandi150 – 15910
    Helixi162 – 17211
    Turni181 – 1855
    Beta strandi186 – 1883
    Helixi196 – 21318
    Beta strandi214 – 2174
    Beta strandi219 – 2279
    Beta strandi230 – 2378

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20M/a20-240[»]
    1G0UX-ray2.40L/Z1-241[»]
    1G65X-ray2.25L/Z20-241[»]
    1JD2X-ray3.00L/S20-241[»]
    1RYPX-ray1.901/M20-241[»]
    1VSYX-ray3.001/M20-241[»]
    1Z7QX-ray3.22M/a20-241[»]
    2F16X-ray2.80L/Z20-241[»]
    2FAKX-ray2.80L/Z20-241[»]
    2GPLX-ray2.81L/Z20-241[»]
    2ZCYX-ray2.90L/Z1-241[»]
    3BDMX-ray2.70L/Z1-241[»]
    3D29X-ray2.60L/Z20-241[»]
    3DY3X-ray2.81L/Z20-241[»]
    3DY4X-ray2.80L/Z20-241[»]
    3E47X-ray3.00L/Z20-241[»]
    3GPJX-ray2.70L/Z20-241[»]
    3GPTX-ray2.41L/Z20-241[»]
    3GPWX-ray2.50L/Z20-241[»]
    3HYEX-ray2.50L/Z20-241[»]
    3L5QX-ray3.003/Q20-241[»]
    3MG0X-ray2.68L/Z20-241[»]
    3MG4X-ray3.11L/Z20-241[»]
    3MG6X-ray2.60L/Z1-241[»]
    3MG7X-ray2.78L/Z1-241[»]
    3MG8X-ray2.59L/Z1-241[»]
    3NZJX-ray2.40L/Z1-241[»]
    3NZWX-ray2.50L/Z1-241[»]
    3NZXX-ray2.70L/Z1-241[»]
    3OEUX-ray2.60L/Z20-241[»]
    3OEVX-ray2.85L/Z20-241[»]
    3OKJX-ray2.70L/Z20-241[»]
    3SDIX-ray2.65L/Z20-241[»]
    3SDKX-ray2.70L/Z20-241[»]
    3SHJX-ray2.80L/Z20-241[»]
    3TDDX-ray2.70L/Z20-241[»]
    3UN4X-ray3.40L/Z20-241[»]
    3UN8X-ray2.70L/Z20-241[»]
    4CR2electron microscopy7.7061-241[»]
    4CR3electron microscopy9.3061-241[»]
    4CR4electron microscopy8.8061-241[»]
    4EU2X-ray2.511/M20-241[»]
    4FZCX-ray2.80L/Z20-241[»]
    4FZGX-ray3.00L/Z20-241[»]
    4G4SX-ray2.49M20-241[»]
    4GK7X-ray2.80L/Z20-241[»]
    4HNPX-ray2.80L/Z20-241[»]
    4HRCX-ray2.80L/Z20-241[»]
    4HRDX-ray2.80L/Z20-241[»]
    4INRX-ray2.70L/Z20-241[»]
    4INTX-ray2.90L/Z20-241[»]
    4INUX-ray3.10L/Z20-241[»]
    4J70X-ray2.80L/Z20-241[»]
    4JSQX-ray2.80L/Z20-241[»]
    4JSUX-ray2.90L/Z20-241[»]
    4JT0X-ray3.10L/Z20-241[»]
    4LQIX-ray2.70L/Z20-241[»]
    4NNNX-ray2.50L/Z20-241[»]
    4NNWX-ray2.60L/Z20-241[»]
    4NO1X-ray2.50L/Z20-241[»]
    4NO6X-ray3.00L/Z20-241[»]
    4NO8X-ray2.70L/Z20-241[»]
    4NO9X-ray2.90L/Z20-241[»]
    4QBYX-ray3.00L/Z20-241[»]
    ProteinModelPortaliP23724.
    SMRiP23724. Positions 20-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23724.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000075035.
    HOGENOMiHOG000091081.
    KOiK02732.
    OMAiQCRAGGA.
    OrthoDBiEOG7VMPGM.

    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.

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

    P23724-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATIASEYSS EASNTPIEHQ FNPYGDNGGT ILGIAGEDFA VLAGDTRNIT    50
    DYSINSRYEP KVFDCGDNIV MSANGFAADG DALVKRFKNS VKWYHFDHND 100
    KKLSINSAAR NIQHLLYGKR FFPYYVHTII AGLDEDGKGA VYSFDPVGSY 150
    EREQCRAGGA AASLIMPFLD NQVNFKNQYE PGTNGKVKKP LKYLSVEEVI 200
    KLVRDSFTSA TERHIQVGDG LEILIVTKDG VRKEFYELKR D 241
    Length:241
    Mass (Da):26,871
    Last modified:November 1, 1991 - v1
    Checksum:i770A4DF1DF0A0F0E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34777 Genomic DNA. Translation: AAA68908.1.
    D00845 Genomic DNA. Translation: BAA00725.1.
    X78214 Genomic DNA. Translation: CAA55053.1.
    Z35802 Genomic DNA. Translation: CAA84861.1.
    AY558462 Genomic DNA. Translation: AAS56788.1.
    BK006936 Genomic DNA. Translation: DAA07077.1.
    PIRiS42436.
    RefSeqiNP_009512.1. NM_001178281.1.

    Genome annotation databases

    EnsemblFungiiYBL041W; YBL041W; YBL041W.
    GeneIDi852239.
    KEGGisce:YBL041W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34777 Genomic DNA. Translation: AAA68908.1 .
    D00845 Genomic DNA. Translation: BAA00725.1 .
    X78214 Genomic DNA. Translation: CAA55053.1 .
    Z35802 Genomic DNA. Translation: CAA84861.1 .
    AY558462 Genomic DNA. Translation: AAS56788.1 .
    BK006936 Genomic DNA. Translation: DAA07077.1 .
    PIRi S42436.
    RefSeqi NP_009512.1. NM_001178281.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FNT X-ray 3.20 M/a 20-240 [» ]
    1G0U X-ray 2.40 L/Z 1-241 [» ]
    1G65 X-ray 2.25 L/Z 20-241 [» ]
    1JD2 X-ray 3.00 L/S 20-241 [» ]
    1RYP X-ray 1.90 1/M 20-241 [» ]
    1VSY X-ray 3.00 1/M 20-241 [» ]
    1Z7Q X-ray 3.22 M/a 20-241 [» ]
    2F16 X-ray 2.80 L/Z 20-241 [» ]
    2FAK X-ray 2.80 L/Z 20-241 [» ]
    2GPL X-ray 2.81 L/Z 20-241 [» ]
    2ZCY X-ray 2.90 L/Z 1-241 [» ]
    3BDM X-ray 2.70 L/Z 1-241 [» ]
    3D29 X-ray 2.60 L/Z 20-241 [» ]
    3DY3 X-ray 2.81 L/Z 20-241 [» ]
    3DY4 X-ray 2.80 L/Z 20-241 [» ]
    3E47 X-ray 3.00 L/Z 20-241 [» ]
    3GPJ X-ray 2.70 L/Z 20-241 [» ]
    3GPT X-ray 2.41 L/Z 20-241 [» ]
    3GPW X-ray 2.50 L/Z 20-241 [» ]
    3HYE X-ray 2.50 L/Z 20-241 [» ]
    3L5Q X-ray 3.00 3/Q 20-241 [» ]
    3MG0 X-ray 2.68 L/Z 20-241 [» ]
    3MG4 X-ray 3.11 L/Z 20-241 [» ]
    3MG6 X-ray 2.60 L/Z 1-241 [» ]
    3MG7 X-ray 2.78 L/Z 1-241 [» ]
    3MG8 X-ray 2.59 L/Z 1-241 [» ]
    3NZJ X-ray 2.40 L/Z 1-241 [» ]
    3NZW X-ray 2.50 L/Z 1-241 [» ]
    3NZX X-ray 2.70 L/Z 1-241 [» ]
    3OEU X-ray 2.60 L/Z 20-241 [» ]
    3OEV X-ray 2.85 L/Z 20-241 [» ]
    3OKJ X-ray 2.70 L/Z 20-241 [» ]
    3SDI X-ray 2.65 L/Z 20-241 [» ]
    3SDK X-ray 2.70 L/Z 20-241 [» ]
    3SHJ X-ray 2.80 L/Z 20-241 [» ]
    3TDD X-ray 2.70 L/Z 20-241 [» ]
    3UN4 X-ray 3.40 L/Z 20-241 [» ]
    3UN8 X-ray 2.70 L/Z 20-241 [» ]
    4CR2 electron microscopy 7.70 6 1-241 [» ]
    4CR3 electron microscopy 9.30 6 1-241 [» ]
    4CR4 electron microscopy 8.80 6 1-241 [» ]
    4EU2 X-ray 2.51 1/M 20-241 [» ]
    4FZC X-ray 2.80 L/Z 20-241 [» ]
    4FZG X-ray 3.00 L/Z 20-241 [» ]
    4G4S X-ray 2.49 M 20-241 [» ]
    4GK7 X-ray 2.80 L/Z 20-241 [» ]
    4HNP X-ray 2.80 L/Z 20-241 [» ]
    4HRC X-ray 2.80 L/Z 20-241 [» ]
    4HRD X-ray 2.80 L/Z 20-241 [» ]
    4INR X-ray 2.70 L/Z 20-241 [» ]
    4INT X-ray 2.90 L/Z 20-241 [» ]
    4INU X-ray 3.10 L/Z 20-241 [» ]
    4J70 X-ray 2.80 L/Z 20-241 [» ]
    4JSQ X-ray 2.80 L/Z 20-241 [» ]
    4JSU X-ray 2.90 L/Z 20-241 [» ]
    4JT0 X-ray 3.10 L/Z 20-241 [» ]
    4LQI X-ray 2.70 L/Z 20-241 [» ]
    4NNN X-ray 2.50 L/Z 20-241 [» ]
    4NNW X-ray 2.60 L/Z 20-241 [» ]
    4NO1 X-ray 2.50 L/Z 20-241 [» ]
    4NO6 X-ray 3.00 L/Z 20-241 [» ]
    4NO8 X-ray 2.70 L/Z 20-241 [» ]
    4NO9 X-ray 2.90 L/Z 20-241 [» ]
    4QBY X-ray 3.00 L/Z 20-241 [» ]
    ProteinModelPortali P23724.
    SMRi P23724. Positions 20-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32656. 41 interactions.
    DIPi DIP-2821N.
    IntActi P23724. 16 interactions.
    MINTi MINT-592611.
    STRINGi 4932.YBL041W.

    Chemistry

    BindingDBi P23724.
    ChEMBLi CHEMBL4904.

    Protein family/group databases

    MEROPSi T01.A12.

    2D gel databases

    UCD-2DPAGE P23724.

    Proteomic databases

    MaxQBi P23724.
    PaxDbi P23724.
    PeptideAtlasi P23724.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL041W ; YBL041W ; YBL041W .
    GeneIDi 852239.
    KEGGi sce:YBL041W.

    Organism-specific databases

    CYGDi YBL041w.
    SGDi S000000137. PRE7.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000075035.
    HOGENOMi HOG000091081.
    KOi K02732.
    OMAi QCRAGGA.
    OrthoDBi EOG7VMPGM.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28942-MONOMER.
    Reactomei REACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_189025. ER-Phagosome pathway.
    REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_83036. Orc1 removal from chromatin.

    Miscellaneous databases

    EvolutionaryTracei P23724.
    NextBioi 970787.
    PROi P23724.

    Gene expression databases

    Genevestigatori P23724.

    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. "ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway."
      Semenza J.C., Hardwick K.G., Dean N., Pelham H.R.B.
      Cell 61:1349-1357(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A yeast homologue of a proteasome subunit."
      Semenza J.C., Pelham H.R.
      DNA Seq. 1:219-219(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "PRS3 encoding an essential subunit of yeast proteasomes homologous to mammalian proteasome subunit C5."
      Lee D.H., Tanaka K., Tamura T., Chung C.H., Ichihara A.
      Biochem. Biophys. Res. Commun. 182:452-460(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein."
      de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J., Goffeau A.
      Yeast 10:1489-1496(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    8. "Structure of 20S proteasome from yeast at 2.4-A resolution."
      Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
      Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING.
    9. "Structural basis for the activation of 20S proteasomes by 11S regulators."
      Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
      Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
    11. "TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
      Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
      Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
    12. "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
      Groll M., Huber R., Potts B.C.M.
      J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
    13. "Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
      Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
      Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-241 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
    14. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
      Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
      Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 20-241 IN COMPLEX WITH THE PROTEASOME.
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSB6_YEAST
    AccessioniPrimary (citable) accession number: P23724
    Secondary accession number(s): D6VPV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 160 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3