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P40302

- PSA6_YEAST

UniProt

P40302 - PSA6_YEAST

Protein

Proteasome subunit alpha type-6

Gene

PRE5

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 154 (01 Oct 2014)
      Sequence version 1 (01 Feb 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.

    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. 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-32978-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

    MEROPSiT01.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-6 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PRE5
    Multicatalytic endopeptidase complex subunit PRE5
    Proteasome component PRE5
    Proteinase YSCE subunit PRE5
    Gene namesi
    Name:PRE5
    Ordered Locus Names:YMR314W
    ORF Names:YM9924.06
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR314w.
    SGDiS000004931. PRE5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
    3. nucleus Source: SGD
    4. proteasome core complex, alpha-subunit complex Source: SGD
    5. proteasome storage granule Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 234234Proteasome subunit alpha type-6PRO_0000124076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40302.
    PaxDbiP40302.
    PeptideAtlasiP40302.
    PRIDEiP40302.

    2D gel databases

    UCD-2DPAGEP40302.

    Expressioni

    Gene expression databases

    GenevestigatoriP40302.

    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

    BioGridi35494. 85 interactions.
    DIPiDIP-1528N.
    IntActiP40302. 33 interactions.
    MINTiMINT-400436.
    STRINGi4932.YMR314W.

    Structurei

    Secondary structure

    1
    234
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Beta strandi15 – 173
    Helixi20 – 3011
    Beta strandi35 – 395
    Beta strandi41 – 499
    Beta strandi53 – 575
    Beta strandi63 – 675
    Beta strandi70 – 767
    Helixi78 – 9922
    Helixi105 – 12117
    Beta strandi122 – 1243
    Beta strandi130 – 1389
    Beta strandi141 – 1477
    Turni149 – 1513
    Beta strandi153 – 16210
    Turni163 – 1653
    Helixi166 – 17914
    Helixi186 – 19712
    Helixi198 – 2003
    Beta strandi202 – 2043
    Turni208 – 2103
    Beta strandi211 – 2177
    Beta strandi220 – 2267
    Helixi227 – 2337

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20F/T1-234[»]
    1G0UX-ray2.40E/S1-234[»]
    1G65X-ray2.25E/S2-234[»]
    1JD2X-ray3.00E/Z2-234[»]
    1RYPX-ray1.90F/T2-234[»]
    1VSYX-ray3.00F/T1-234[»]
    1Z7QX-ray3.22F/T1-234[»]
    2F16X-ray2.80E/S2-234[»]
    2FAKX-ray2.80E/S2-234[»]
    2GPLX-ray2.81E/S2-234[»]
    2ZCYX-ray2.90E/S1-234[»]
    3BDMX-ray2.70E/S1-234[»]
    3D29X-ray2.60E/S2-234[»]
    3DY3X-ray2.81E/S2-234[»]
    3DY4X-ray2.80E/S2-234[»]
    3E47X-ray3.00E/S2-234[»]
    3GPJX-ray2.70E/S2-234[»]
    3GPTX-ray2.41E/S2-234[»]
    3GPWX-ray2.50E/S2-234[»]
    3HYEX-ray2.50E/S2-234[»]
    3L5QX-ray3.00K/W1-234[»]
    3MG0X-ray2.68E/S2-234[»]
    3MG4X-ray3.11E/S2-234[»]
    3MG6X-ray2.60E/S1-234[»]
    3MG7X-ray2.78E/S1-234[»]
    3MG8X-ray2.59E/S1-234[»]
    3NZJX-ray2.40E/S1-234[»]
    3NZWX-ray2.50E/S1-234[»]
    3NZXX-ray2.70E/S1-234[»]
    3OEUX-ray2.60E/S2-234[»]
    3OEVX-ray2.85E/S2-234[»]
    3OKJX-ray2.70E/S2-234[»]
    3SDIX-ray2.65E/S2-234[»]
    3SDKX-ray2.70E/S2-234[»]
    3SHJX-ray2.80E/S2-234[»]
    3TDDX-ray2.70E/S2-234[»]
    3UN4X-ray3.40E/S1-234[»]
    3UN8X-ray2.70E/S1-234[»]
    4CR2electron microscopy7.70F1-234[»]
    4CR3electron microscopy9.30F1-234[»]
    4CR4electron microscopy8.80F1-234[»]
    4EU2X-ray2.51F/T2-234[»]
    4FZCX-ray2.80E/S2-234[»]
    4FZGX-ray3.00E/S2-234[»]
    4G4SX-ray2.49F1-234[»]
    4GK7X-ray2.80E/S2-234[»]
    4HNPX-ray2.80E/S2-234[»]
    4HRCX-ray2.80E/S2-234[»]
    4HRDX-ray2.80E/S2-234[»]
    4INRX-ray2.70E/S1-234[»]
    4INTX-ray2.90E/S1-234[»]
    4INUX-ray3.10E/S1-234[»]
    4J70X-ray2.80E/S1-234[»]
    4JSQX-ray2.80E/S1-234[»]
    4JSUX-ray2.90E/S1-234[»]
    4JT0X-ray3.10E/S1-234[»]
    4LQIX-ray2.70E/S2-234[»]
    4NNNX-ray2.50E/S1-234[»]
    4NNWX-ray2.60E/S1-234[»]
    4NO1X-ray2.50E/S1-234[»]
    4NO6X-ray3.00E/S1-234[»]
    4NO8X-ray2.70E/S1-234[»]
    4NO9X-ray2.90E/S1-234[»]
    4QBYX-ray3.00E/S1-234[»]
    ProteinModelPortaliP40302.
    SMRiP40302. Positions 2-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40302.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074855.
    HOGENOMiHOG000091080.
    KOiK02725.
    OMAiFMKQQCL.
    OrthoDBiEOG7SBP0C.

    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.

    P40302-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFRNNYDGDT VTFSPTGRLF QVEYALEAIK QGSVTVGLRS NTHAVLVALK    50
    RNADELSSYQ KKIIKCDEHM GLSLAGLAPD ARVLSNYLRQ QCNYSSLVFN 100
    RKLAVERAGH LLCDKAQKNT QSYGGRPYGV GLLIIGYDKS GAHLLEFQPS 150
    GNVTELYGTA IGARSQGAKT YLERTLDTFI KIDGNPDELI KAGVEAISQS 200
    LRDESLTVDN LSIAIVGKDT PFTIYDGEAV AKYI 234
    Length:234
    Mass (Da):25,604
    Last modified:February 1, 1995 - v1
    Checksum:iC43CBCC1C6B9E39E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34347 Genomic DNA. Translation: AAA53544.1.
    Z54141 Genomic DNA. Translation: CAA90832.1.
    AY557978 Genomic DNA. Translation: AAS56304.1.
    BK006946 Genomic DNA. Translation: DAA10215.1.
    PIRiA55904.
    RefSeqiNP_014045.1. NM_001182825.1.

    Genome annotation databases

    EnsemblFungiiYMR314W; YMR314W; YMR314W.
    GeneIDi855362.
    KEGGisce:YMR314W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34347 Genomic DNA. Translation: AAA53544.1 .
    Z54141 Genomic DNA. Translation: CAA90832.1 .
    AY557978 Genomic DNA. Translation: AAS56304.1 .
    BK006946 Genomic DNA. Translation: DAA10215.1 .
    PIRi A55904.
    RefSeqi NP_014045.1. NM_001182825.1.

    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 F/T 1-234 [» ]
    1G0U X-ray 2.40 E/S 1-234 [» ]
    1G65 X-ray 2.25 E/S 2-234 [» ]
    1JD2 X-ray 3.00 E/Z 2-234 [» ]
    1RYP X-ray 1.90 F/T 2-234 [» ]
    1VSY X-ray 3.00 F/T 1-234 [» ]
    1Z7Q X-ray 3.22 F/T 1-234 [» ]
    2F16 X-ray 2.80 E/S 2-234 [» ]
    2FAK X-ray 2.80 E/S 2-234 [» ]
    2GPL X-ray 2.81 E/S 2-234 [» ]
    2ZCY X-ray 2.90 E/S 1-234 [» ]
    3BDM X-ray 2.70 E/S 1-234 [» ]
    3D29 X-ray 2.60 E/S 2-234 [» ]
    3DY3 X-ray 2.81 E/S 2-234 [» ]
    3DY4 X-ray 2.80 E/S 2-234 [» ]
    3E47 X-ray 3.00 E/S 2-234 [» ]
    3GPJ X-ray 2.70 E/S 2-234 [» ]
    3GPT X-ray 2.41 E/S 2-234 [» ]
    3GPW X-ray 2.50 E/S 2-234 [» ]
    3HYE X-ray 2.50 E/S 2-234 [» ]
    3L5Q X-ray 3.00 K/W 1-234 [» ]
    3MG0 X-ray 2.68 E/S 2-234 [» ]
    3MG4 X-ray 3.11 E/S 2-234 [» ]
    3MG6 X-ray 2.60 E/S 1-234 [» ]
    3MG7 X-ray 2.78 E/S 1-234 [» ]
    3MG8 X-ray 2.59 E/S 1-234 [» ]
    3NZJ X-ray 2.40 E/S 1-234 [» ]
    3NZW X-ray 2.50 E/S 1-234 [» ]
    3NZX X-ray 2.70 E/S 1-234 [» ]
    3OEU X-ray 2.60 E/S 2-234 [» ]
    3OEV X-ray 2.85 E/S 2-234 [» ]
    3OKJ X-ray 2.70 E/S 2-234 [» ]
    3SDI X-ray 2.65 E/S 2-234 [» ]
    3SDK X-ray 2.70 E/S 2-234 [» ]
    3SHJ X-ray 2.80 E/S 2-234 [» ]
    3TDD X-ray 2.70 E/S 2-234 [» ]
    3UN4 X-ray 3.40 E/S 1-234 [» ]
    3UN8 X-ray 2.70 E/S 1-234 [» ]
    4CR2 electron microscopy 7.70 F 1-234 [» ]
    4CR3 electron microscopy 9.30 F 1-234 [» ]
    4CR4 electron microscopy 8.80 F 1-234 [» ]
    4EU2 X-ray 2.51 F/T 2-234 [» ]
    4FZC X-ray 2.80 E/S 2-234 [» ]
    4FZG X-ray 3.00 E/S 2-234 [» ]
    4G4S X-ray 2.49 F 1-234 [» ]
    4GK7 X-ray 2.80 E/S 2-234 [» ]
    4HNP X-ray 2.80 E/S 2-234 [» ]
    4HRC X-ray 2.80 E/S 2-234 [» ]
    4HRD X-ray 2.80 E/S 2-234 [» ]
    4INR X-ray 2.70 E/S 1-234 [» ]
    4INT X-ray 2.90 E/S 1-234 [» ]
    4INU X-ray 3.10 E/S 1-234 [» ]
    4J70 X-ray 2.80 E/S 1-234 [» ]
    4JSQ X-ray 2.80 E/S 1-234 [» ]
    4JSU X-ray 2.90 E/S 1-234 [» ]
    4JT0 X-ray 3.10 E/S 1-234 [» ]
    4LQI X-ray 2.70 E/S 2-234 [» ]
    4NNN X-ray 2.50 E/S 1-234 [» ]
    4NNW X-ray 2.60 E/S 1-234 [» ]
    4NO1 X-ray 2.50 E/S 1-234 [» ]
    4NO6 X-ray 3.00 E/S 1-234 [» ]
    4NO8 X-ray 2.70 E/S 1-234 [» ]
    4NO9 X-ray 2.90 E/S 1-234 [» ]
    4QBY X-ray 3.00 E/S 1-234 [» ]
    ProteinModelPortali P40302.
    SMRi P40302. Positions 2-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35494. 85 interactions.
    DIPi DIP-1528N.
    IntActi P40302. 33 interactions.
    MINTi MINT-400436.
    STRINGi 4932.YMR314W.

    Protein family/group databases

    MEROPSi T01.976.

    2D gel databases

    UCD-2DPAGE P40302.

    Proteomic databases

    MaxQBi P40302.
    PaxDbi P40302.
    PeptideAtlasi P40302.
    PRIDEi P40302.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR314W ; YMR314W ; YMR314W .
    GeneIDi 855362.
    KEGGi sce:YMR314W.

    Organism-specific databases

    CYGDi YMR314w.
    SGDi S000004931. PRE5.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074855.
    HOGENOMi HOG000091080.
    KOi K02725.
    OMAi FMKQQCL.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32978-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 P40302.
    NextBioi 979136.
    PROi P40302.

    Gene expression databases

    Genevestigatori P40302.

    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. "PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core."
      Heinemeyer W., Troendle N., Albrecht G., Wolf D.H.
      Biochemistry 33:12229-12237(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 141-149 AND 220-228.
      Strain: ATCC 204508 / S288c.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "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].
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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 COMPLEX WITH THE 20S PROTEASOME.
    11. "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 COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
    13. "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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
    14. "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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
    15. "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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
    16. "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) IN COMPLEX WITH THE PROTEASOME.
    17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA6_YEAST
    AccessioniPrimary (citable) accession number: P40302
    Secondary accession number(s): D6W0E1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7210 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3