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P38624

- PSB1_YEAST

UniProt

P38624 - PSB1_YEAST

Protein

Proteasome subunit beta type-1

Gene

PRE3

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 147 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      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. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.
    This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei20 – 201Nucleophile1 Publication

    GO - Molecular functioni

    1. endopeptidase activity Source: SGD
    2. 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-31481-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

    MEROPSiT01.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-1 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PRE3
    Multicatalytic endopeptidase complex subunit PRE3
    Proteasome component PRE3
    Proteinase YSCE subunit PRE3
    Gene namesi
    Name:PRE3
    Ordered Locus Names:YJL001W
    ORF Names:J1407
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL001w.
    SGDiS000003538. PRE3.

    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 – 1919Removed in mature formPRO_0000026643Add
    BLAST
    Chaini20 – 215196Proteasome subunit beta type-1PRO_0000026644Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    MaxQBiP38624.
    PaxDbiP38624.
    PeptideAtlasiP38624.

    2D gel databases

    UCD-2DPAGEP38624.

    Expressioni

    Gene expression databases

    GenevestigatoriP38624.

    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

    BioGridi33756. 75 interactions.
    DIPiDIP-1527N.
    IntActiP38624. 20 interactions.
    MINTiMINT-401012.
    STRINGi4932.YJL001W.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 276
    Beta strandi30 – 356
    Beta strandi39 – 413
    Beta strandi44 – 496
    Beta strandi53 – 575
    Beta strandi60 – 678
    Helixi68 – 8922
    Helixi94 – 10714
    Turni108 – 1114
    Beta strandi114 – 1229
    Turni123 – 1253
    Beta strandi126 – 1327
    Turni134 – 1363
    Beta strandi139 – 1479
    Helixi148 – 1536
    Helixi154 – 1607
    Helixi167 – 18418
    Beta strandi185 – 1873
    Beta strandi192 – 1987
    Beta strandi201 – 2077
    Helixi209 – 2124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20H/V20-215[»]
    1G0UX-ray2.402/N20-215[»]
    1G65X-ray2.252/N20-215[»]
    1JD2X-ray3.00N/U20-215[»]
    1RYPX-ray1.90H/V11-215[»]
    1VSYX-ray3.00H/V21-215[»]
    1Z7QX-ray3.22H/V20-215[»]
    2F16X-ray2.802/N20-215[»]
    2FAKX-ray2.802/N20-205[»]
    2GPLX-ray2.812/N20-215[»]
    2ZCYX-ray2.901/N20-215[»]
    3BDMX-ray2.701/N20-215[»]
    3D29X-ray2.602/N20-215[»]
    3DY3X-ray2.812/N20-215[»]
    3DY4X-ray2.802/N20-215[»]
    3E47X-ray3.002/N20-215[»]
    3GPJX-ray2.702/N20-215[»]
    3GPTX-ray2.412/N20-215[»]
    3GPWX-ray2.502/N20-215[»]
    3HYEX-ray2.502/N20-215[»]
    3L5QX-ray3.00B/D21-215[»]
    3MG0X-ray2.682/N20-215[»]
    3MG4X-ray3.112/N20-215[»]
    3MG6X-ray2.602/N20-215[»]
    3MG7X-ray2.782/N20-215[»]
    3MG8X-ray2.592/N20-215[»]
    3NZJX-ray2.402/N1-215[»]
    3NZWX-ray2.502/N1-215[»]
    3NZXX-ray2.702/N1-215[»]
    3OEUX-ray2.602/N20-215[»]
    3OEVX-ray2.852/N20-215[»]
    3OKJX-ray2.702/N20-215[»]
    3SDIX-ray2.652/N20-215[»]
    3SDKX-ray2.702/N20-215[»]
    3SHJX-ray2.802/N20-215[»]
    3TDDX-ray2.702/N20-215[»]
    3UN4X-ray3.40N/b20-215[»]
    3UN8X-ray2.70N/b20-215[»]
    4CR2electron microscopy7.7011-215[»]
    4CR3electron microscopy9.3011-215[»]
    4CR4electron microscopy8.8011-215[»]
    4EU2X-ray2.51H/V20-215[»]
    4FZCX-ray2.80N/b20-215[»]
    4FZGX-ray3.00N/b20-215[»]
    4G4SX-ray2.49H20-215[»]
    4GK7X-ray2.80N/b20-215[»]
    4HNPX-ray2.80N/b20-215[»]
    4HRCX-ray2.80N/b20-215[»]
    4HRDX-ray2.80N/b20-215[»]
    4INRX-ray2.70N/b20-215[»]
    4INTX-ray2.90N/b20-215[»]
    4INUX-ray3.10N/b20-215[»]
    4J70X-ray2.80N/b20-215[»]
    4JSQX-ray2.80N/b20-215[»]
    4JSUX-ray2.90N/b20-215[»]
    4JT0X-ray3.10N/b20-215[»]
    4LQIX-ray2.70N/b20-215[»]
    4NNNX-ray2.50N/b20-215[»]
    4NNWX-ray2.60N/b20-215[»]
    4NO1X-ray2.50N/b20-215[»]
    4NO6X-ray3.00N/b20-215[»]
    4NO8X-ray2.70N/b20-215[»]
    4NO9X-ray2.90N/b20-215[»]
    4QBYX-ray3.00N/b20-215[»]
    ProteinModelPortaliP38624.
    SMRiP38624. Positions 20-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38624.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046484.
    HOGENOMiHOG000091079.
    KOiK02738.
    OMAiTSIMAVQ.
    OrthoDBiEOG7XDBSV.

    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.

    P38624-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT    50
    DKLTRVHDKI WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV 100
    FKELCYENKD NLTAGIIVAG YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS 150
    TFIYGYCDKN FRENMSKEET VDFIKHSLSQ AIKWDGSSGG VIRMVVLTAA 200
    GVERLIFYPD EYEQL 215
    Length:215
    Mass (Da):23,548
    Last modified:November 1, 1995 - v2
    Checksum:iBD1FCE649678D86B
    GO

    Sequence cautioni

    The sequence CAA55591.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA60921.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78991 Genomic DNA. Translation: CAA55591.1. Different initiation.
    Z49276 Genomic DNA. Translation: CAA89290.1.
    Z49277 Genomic DNA. Translation: CAA89292.1.
    X87611 Genomic DNA. Translation: CAA60921.1. Different initiation.
    X86020 mRNA. Translation: CAA60015.1.
    S78566 mRNA. Translation: AAB34629.1.
    BK006943 Genomic DNA. Translation: DAA08790.1.
    PIRiS61337.
    RefSeqiNP_012533.1. NM_001181435.1.

    Genome annotation databases

    EnsemblFungiiYJL001W; YJL001W; YJL001W.
    GeneIDi853456.
    KEGGisce:YJL001W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78991 Genomic DNA. Translation: CAA55591.1 . Different initiation.
    Z49276 Genomic DNA. Translation: CAA89290.1 .
    Z49277 Genomic DNA. Translation: CAA89292.1 .
    X87611 Genomic DNA. Translation: CAA60921.1 . Different initiation.
    X86020 mRNA. Translation: CAA60015.1 .
    S78566 mRNA. Translation: AAB34629.1 .
    BK006943 Genomic DNA. Translation: DAA08790.1 .
    PIRi S61337.
    RefSeqi NP_012533.1. NM_001181435.1.

    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 H/V 20-215 [» ]
    1G0U X-ray 2.40 2/N 20-215 [» ]
    1G65 X-ray 2.25 2/N 20-215 [» ]
    1JD2 X-ray 3.00 N/U 20-215 [» ]
    1RYP X-ray 1.90 H/V 11-215 [» ]
    1VSY X-ray 3.00 H/V 21-215 [» ]
    1Z7Q X-ray 3.22 H/V 20-215 [» ]
    2F16 X-ray 2.80 2/N 20-215 [» ]
    2FAK X-ray 2.80 2/N 20-205 [» ]
    2GPL X-ray 2.81 2/N 20-215 [» ]
    2ZCY X-ray 2.90 1/N 20-215 [» ]
    3BDM X-ray 2.70 1/N 20-215 [» ]
    3D29 X-ray 2.60 2/N 20-215 [» ]
    3DY3 X-ray 2.81 2/N 20-215 [» ]
    3DY4 X-ray 2.80 2/N 20-215 [» ]
    3E47 X-ray 3.00 2/N 20-215 [» ]
    3GPJ X-ray 2.70 2/N 20-215 [» ]
    3GPT X-ray 2.41 2/N 20-215 [» ]
    3GPW X-ray 2.50 2/N 20-215 [» ]
    3HYE X-ray 2.50 2/N 20-215 [» ]
    3L5Q X-ray 3.00 B/D 21-215 [» ]
    3MG0 X-ray 2.68 2/N 20-215 [» ]
    3MG4 X-ray 3.11 2/N 20-215 [» ]
    3MG6 X-ray 2.60 2/N 20-215 [» ]
    3MG7 X-ray 2.78 2/N 20-215 [» ]
    3MG8 X-ray 2.59 2/N 20-215 [» ]
    3NZJ X-ray 2.40 2/N 1-215 [» ]
    3NZW X-ray 2.50 2/N 1-215 [» ]
    3NZX X-ray 2.70 2/N 1-215 [» ]
    3OEU X-ray 2.60 2/N 20-215 [» ]
    3OEV X-ray 2.85 2/N 20-215 [» ]
    3OKJ X-ray 2.70 2/N 20-215 [» ]
    3SDI X-ray 2.65 2/N 20-215 [» ]
    3SDK X-ray 2.70 2/N 20-215 [» ]
    3SHJ X-ray 2.80 2/N 20-215 [» ]
    3TDD X-ray 2.70 2/N 20-215 [» ]
    3UN4 X-ray 3.40 N/b 20-215 [» ]
    3UN8 X-ray 2.70 N/b 20-215 [» ]
    4CR2 electron microscopy 7.70 1 1-215 [» ]
    4CR3 electron microscopy 9.30 1 1-215 [» ]
    4CR4 electron microscopy 8.80 1 1-215 [» ]
    4EU2 X-ray 2.51 H/V 20-215 [» ]
    4FZC X-ray 2.80 N/b 20-215 [» ]
    4FZG X-ray 3.00 N/b 20-215 [» ]
    4G4S X-ray 2.49 H 20-215 [» ]
    4GK7 X-ray 2.80 N/b 20-215 [» ]
    4HNP X-ray 2.80 N/b 20-215 [» ]
    4HRC X-ray 2.80 N/b 20-215 [» ]
    4HRD X-ray 2.80 N/b 20-215 [» ]
    4INR X-ray 2.70 N/b 20-215 [» ]
    4INT X-ray 2.90 N/b 20-215 [» ]
    4INU X-ray 3.10 N/b 20-215 [» ]
    4J70 X-ray 2.80 N/b 20-215 [» ]
    4JSQ X-ray 2.80 N/b 20-215 [» ]
    4JSU X-ray 2.90 N/b 20-215 [» ]
    4JT0 X-ray 3.10 N/b 20-215 [» ]
    4LQI X-ray 2.70 N/b 20-215 [» ]
    4NNN X-ray 2.50 N/b 20-215 [» ]
    4NNW X-ray 2.60 N/b 20-215 [» ]
    4NO1 X-ray 2.50 N/b 20-215 [» ]
    4NO6 X-ray 3.00 N/b 20-215 [» ]
    4NO8 X-ray 2.70 N/b 20-215 [» ]
    4NO9 X-ray 2.90 N/b 20-215 [» ]
    4QBY X-ray 3.00 N/b 20-215 [» ]
    ProteinModelPortali P38624.
    SMRi P38624. Positions 20-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33756. 75 interactions.
    DIPi DIP-1527N.
    IntActi P38624. 20 interactions.
    MINTi MINT-401012.
    STRINGi 4932.YJL001W.

    Protein family/group databases

    MEROPSi T01.010.

    2D gel databases

    UCD-2DPAGE P38624.

    Proteomic databases

    MaxQBi P38624.
    PaxDbi P38624.
    PeptideAtlasi P38624.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL001W ; YJL001W ; YJL001W .
    GeneIDi 853456.
    KEGGi sce:YJL001W.

    Organism-specific databases

    CYGDi YJL001w.
    SGDi S000003538. PRE3.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046484.
    HOGENOMi HOG000091079.
    KOi K02738.
    OMAi TSIMAVQ.
    OrthoDBi EOG7XDBSV.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31481-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 P38624.
    NextBioi 974026.
    PROi P38624.

    Gene expression databases

    Genevestigatori P38624.

    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. "PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity."
      Enenkel C., Lehmann H., Kipper J., Gueckel R., Hilt W., Wolf D.H.
      FEBS Lett. 341:193-196(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Biogenesis, structure and function of the yeast 20S proteasome."
      Chen P., Hochstrasser M.
      EMBO J. 14:2620-2630(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO N-TERMINUS.
    3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 11-215 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING, ACTIVE SITE.
    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 20-215 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-215 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 20-215 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 20-215 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 20-215 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 21-215 IN COMPLEX WITH THE PROTEASOME.
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSB1_YEAST
    AccessioniPrimary (citable) accession number: P38624
    Secondary accession number(s): D6VWH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The side chain of Thr-20 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
    Present with 7250 molecules/cell in log phase SD medium.1 Publication

    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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3