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P30656

- PSB5_YEAST

UniProt

P30656 - PSB5_YEAST

Protein

Proteasome subunit beta type-5

Gene

PRE2

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 153 (01 Oct 2014)
      Sequence version 3 (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. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.
    This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei76 – 761Nucleophile1 Publication
    Binding sitei124 – 1241Bortezomib; via amide nitrogen

    GO - Molecular functioni

    1. endopeptidase activity Source: SGD
    2. protein binding Source: IntAct
    3. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
    2. proteasome core complex assembly Source: SGD
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34243-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

    MEROPSiT01.012.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-5 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PRE2
    Multicatalytic endopeptidase complex subunit PRE2
    Proteasome component PRE2
    Proteinase YSCE subunit PRE2
    Gene namesi
    Name:PRE2
    Synonyms:DOA3, PRG1
    Ordered Locus Names:YPR103W
    ORF Names:P8283.10
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPR103w.
    SGDiS000006307. PRE2.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi126 – 1261D → N in DOA3-1; decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 7575Removed in mature form1 PublicationPRO_0000026611Add
    BLAST
    Chaini76 – 287212Proteasome subunit beta type-5PRO_0000026612Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiP30656.
    PaxDbiP30656.
    PeptideAtlasiP30656.

    Expressioni

    Gene expression databases

    GenevestigatoriP30656.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLM10P435833EBI-14001,EBI-22761

    Protein-protein interaction databases

    BioGridi36269. 119 interactions.
    DIPiDIP-2806N.
    IntActiP30656. 20 interactions.
    MINTiMINT-489734.
    STRINGi4932.YPR103W.

    Structurei

    Secondary structure

    1
    287
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi78 – 836
    Beta strandi86 – 916
    Beta strandi95 – 973
    Beta strandi100 – 1045
    Beta strandi109 – 1135
    Beta strandi116 – 1194
    Beta strandi121 – 1233
    Helixi124 – 14522
    Helixi151 – 16414
    Turni165 – 1673
    Beta strandi172 – 1809
    Turni181 – 1833
    Beta strandi184 – 1918
    Turni192 – 1943
    Beta strandi196 – 1983
    Beta strandi200 – 2056
    Helixi208 – 21811
    Helixi225 – 24218
    Beta strandi243 – 2464
    Beta strandi248 – 2569
    Beta strandi259 – 2679
    Helixi268 – 27912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20L/Z76-287[»]
    1G0UX-ray2.40K/Y76-287[»]
    1G65X-ray2.25K/Y76-287[»]
    1JD2X-ray3.00K/R76-287[»]
    1RYPX-ray1.90L/Z76-287[»]
    1VSYX-ray3.00L/Z76-287[»]
    1Z7QX-ray3.22L/Z76-287[»]
    2F16X-ray2.80K/Y76-287[»]
    2FAKX-ray2.80K/Y76-287[»]
    2GPLX-ray2.81K/Y76-287[»]
    2ZCYX-ray2.90K/Y76-287[»]
    3BDMX-ray2.70K/Y76-287[»]
    3D29X-ray2.60K/Y76-287[»]
    3DY3X-ray2.81K/Y76-287[»]
    3DY4X-ray2.80K/Y76-287[»]
    3E47X-ray3.00K/Y76-287[»]
    3GPJX-ray2.70K/Y76-287[»]
    3GPTX-ray2.41K/Y76-287[»]
    3GPWX-ray2.50K/Y76-287[»]
    3HYEX-ray2.50K/Y76-287[»]
    3L5QX-ray3.002/P76-287[»]
    3MG0X-ray2.68K/Y76-287[»]
    3MG4X-ray3.11K/Y76-287[»]
    3MG6X-ray2.60K/Y76-287[»]
    3MG7X-ray2.78K/Y76-287[»]
    3MG8X-ray2.59K/Y76-287[»]
    3NZJX-ray2.40K/Y1-287[»]
    3NZWX-ray2.50K/Y1-287[»]
    3NZXX-ray2.70K/Y1-287[»]
    3OEUX-ray2.60K/Y76-287[»]
    3OEVX-ray2.85K/Y76-287[»]
    3OKJX-ray2.70K/Y76-287[»]
    3SDIX-ray2.65K/Y76-287[»]
    3SDKX-ray2.70K/Y76-287[»]
    3SHJX-ray2.80K/Y76-287[»]
    3TDDX-ray2.70K/Y76-287[»]
    3UN4X-ray3.40K/Y76-287[»]
    3UN8X-ray2.70K/Y76-287[»]
    4CR2electron microscopy7.7051-287[»]
    4CR3electron microscopy9.3051-287[»]
    4CR4electron microscopy8.8051-287[»]
    4EU2X-ray2.51L/Z76-287[»]
    4FZCX-ray2.80K/Y76-287[»]
    4FZGX-ray3.00K/Y76-287[»]
    4G4SX-ray2.49L76-287[»]
    4GK7X-ray2.80K/Y76-287[»]
    4HNPX-ray2.80K/Y76-287[»]
    4HRCX-ray2.80K/Y76-287[»]
    4HRDX-ray2.80K/Y76-287[»]
    4INRX-ray2.70K/Y76-287[»]
    4INTX-ray2.90K/Y76-287[»]
    4INUX-ray3.10K/Y76-287[»]
    4J70X-ray2.80K/Y76-287[»]
    4JSQX-ray2.80K/Y76-287[»]
    4JSUX-ray2.90K/Y76-287[»]
    4JT0X-ray3.10K/Y76-287[»]
    4LQIX-ray2.70K/Y76-287[»]
    4NNNX-ray2.50K/Y76-287[»]
    4NNWX-ray2.60K/Y76-287[»]
    4NO1X-ray2.50K/Y76-287[»]
    4NO6X-ray3.00K/Y76-287[»]
    4NO8X-ray2.70K/Y76-287[»]
    4NO9X-ray2.90K/Y76-287[»]
    4QBYX-ray3.00K/Y76-287[»]
    ProteinModelPortaliP30656.
    SMRiP30656. Positions 49-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30656.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046395.
    HOGENOMiHOG000091082.
    KOiK02737.
    OMAiTMCAGVT.
    OrthoDBiEOG70W3R5.

    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.

    P30656-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQAIADSFSV PNRLVKELQY DNEQNLESDF VTGASQFQRL APSLTVPPIA    50
    SPQQFLRAHT DDSRNPDCKI KIAHGTTTLA FRFQGGIIVA VDSRATAGNW 100
    VASQTVKKVI EINPFLLGTM AGGAADCQFW ETWLGSQCRL HELREKERIS 150
    VAAASKILSN LVYQYKGAGL SMGTMICGYT RKEGPTIYYV DSDGTRLKGD 200
    IFCVGSGQTF AYGVLDSNYK WDLSVEDALY LGKRSILAAA HRDAYSGGSV 250
    NLYHVTEDGW IYHGNHDVGE LFWKVKEEEG SFNNVIG 287
    Length:287
    Mass (Da):31,637
    Last modified:February 1, 1995 - v3
    Checksum:iD0EBAC611F7A4F37
    GO

    Sequence cautioni

    The sequence CAA82203.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti282 – 2876FNNVIG → STTLLAK in AAA34906. (PubMed:1452031)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96667 Genomic DNA. Translation: AAA34906.1.
    X68662 Genomic DNA. Translation: CAA48628.1.
    U32445 Genomic DNA. Translation: AAB68073.1.
    Z28348 Genomic DNA. Translation: CAA82203.1. Different initiation.
    BK006949 Genomic DNA. Translation: DAA11517.1.
    PIRiA45411.
    RefSeqiNP_015428.1. NM_001184200.1.

    Genome annotation databases

    EnsemblFungiiYPR103W; YPR103W; YPR103W.
    GeneIDi856218.
    KEGGisce:YPR103W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96667 Genomic DNA. Translation: AAA34906.1 .
    X68662 Genomic DNA. Translation: CAA48628.1 .
    U32445 Genomic DNA. Translation: AAB68073.1 .
    Z28348 Genomic DNA. Translation: CAA82203.1 . Different initiation.
    BK006949 Genomic DNA. Translation: DAA11517.1 .
    PIRi A45411.
    RefSeqi NP_015428.1. NM_001184200.1.

    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 L/Z 76-287 [» ]
    1G0U X-ray 2.40 K/Y 76-287 [» ]
    1G65 X-ray 2.25 K/Y 76-287 [» ]
    1JD2 X-ray 3.00 K/R 76-287 [» ]
    1RYP X-ray 1.90 L/Z 76-287 [» ]
    1VSY X-ray 3.00 L/Z 76-287 [» ]
    1Z7Q X-ray 3.22 L/Z 76-287 [» ]
    2F16 X-ray 2.80 K/Y 76-287 [» ]
    2FAK X-ray 2.80 K/Y 76-287 [» ]
    2GPL X-ray 2.81 K/Y 76-287 [» ]
    2ZCY X-ray 2.90 K/Y 76-287 [» ]
    3BDM X-ray 2.70 K/Y 76-287 [» ]
    3D29 X-ray 2.60 K/Y 76-287 [» ]
    3DY3 X-ray 2.81 K/Y 76-287 [» ]
    3DY4 X-ray 2.80 K/Y 76-287 [» ]
    3E47 X-ray 3.00 K/Y 76-287 [» ]
    3GPJ X-ray 2.70 K/Y 76-287 [» ]
    3GPT X-ray 2.41 K/Y 76-287 [» ]
    3GPW X-ray 2.50 K/Y 76-287 [» ]
    3HYE X-ray 2.50 K/Y 76-287 [» ]
    3L5Q X-ray 3.00 2/P 76-287 [» ]
    3MG0 X-ray 2.68 K/Y 76-287 [» ]
    3MG4 X-ray 3.11 K/Y 76-287 [» ]
    3MG6 X-ray 2.60 K/Y 76-287 [» ]
    3MG7 X-ray 2.78 K/Y 76-287 [» ]
    3MG8 X-ray 2.59 K/Y 76-287 [» ]
    3NZJ X-ray 2.40 K/Y 1-287 [» ]
    3NZW X-ray 2.50 K/Y 1-287 [» ]
    3NZX X-ray 2.70 K/Y 1-287 [» ]
    3OEU X-ray 2.60 K/Y 76-287 [» ]
    3OEV X-ray 2.85 K/Y 76-287 [» ]
    3OKJ X-ray 2.70 K/Y 76-287 [» ]
    3SDI X-ray 2.65 K/Y 76-287 [» ]
    3SDK X-ray 2.70 K/Y 76-287 [» ]
    3SHJ X-ray 2.80 K/Y 76-287 [» ]
    3TDD X-ray 2.70 K/Y 76-287 [» ]
    3UN4 X-ray 3.40 K/Y 76-287 [» ]
    3UN8 X-ray 2.70 K/Y 76-287 [» ]
    4CR2 electron microscopy 7.70 5 1-287 [» ]
    4CR3 electron microscopy 9.30 5 1-287 [» ]
    4CR4 electron microscopy 8.80 5 1-287 [» ]
    4EU2 X-ray 2.51 L/Z 76-287 [» ]
    4FZC X-ray 2.80 K/Y 76-287 [» ]
    4FZG X-ray 3.00 K/Y 76-287 [» ]
    4G4S X-ray 2.49 L 76-287 [» ]
    4GK7 X-ray 2.80 K/Y 76-287 [» ]
    4HNP X-ray 2.80 K/Y 76-287 [» ]
    4HRC X-ray 2.80 K/Y 76-287 [» ]
    4HRD X-ray 2.80 K/Y 76-287 [» ]
    4INR X-ray 2.70 K/Y 76-287 [» ]
    4INT X-ray 2.90 K/Y 76-287 [» ]
    4INU X-ray 3.10 K/Y 76-287 [» ]
    4J70 X-ray 2.80 K/Y 76-287 [» ]
    4JSQ X-ray 2.80 K/Y 76-287 [» ]
    4JSU X-ray 2.90 K/Y 76-287 [» ]
    4JT0 X-ray 3.10 K/Y 76-287 [» ]
    4LQI X-ray 2.70 K/Y 76-287 [» ]
    4NNN X-ray 2.50 K/Y 76-287 [» ]
    4NNW X-ray 2.60 K/Y 76-287 [» ]
    4NO1 X-ray 2.50 K/Y 76-287 [» ]
    4NO6 X-ray 3.00 K/Y 76-287 [» ]
    4NO8 X-ray 2.70 K/Y 76-287 [» ]
    4NO9 X-ray 2.90 K/Y 76-287 [» ]
    4QBY X-ray 3.00 K/Y 76-287 [» ]
    ProteinModelPortali P30656.
    SMRi P30656. Positions 49-287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36269. 119 interactions.
    DIPi DIP-2806N.
    IntActi P30656. 20 interactions.
    MINTi MINT-489734.
    STRINGi 4932.YPR103W.

    Chemistry

    BindingDBi P30656.
    ChEMBLi CHEMBL4659.

    Protein family/group databases

    MEROPSi T01.012.

    Proteomic databases

    MaxQBi P30656.
    PaxDbi P30656.
    PeptideAtlasi P30656.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPR103W ; YPR103W ; YPR103W .
    GeneIDi 856218.
    KEGGi sce:YPR103W.

    Organism-specific databases

    CYGDi YPR103w.
    SGDi S000006307. PRE2.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046395.
    HOGENOMi HOG000091082.
    KOi K02737.
    OMAi TMCAGVT.
    OrthoDBi EOG70W3R5.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-34243-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 P30656.
    NextBioi 981441.
    PROi P30656.

    Gene expression databases

    Genevestigatori P30656.

    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. "A homolog of the proteasome-related RING10 gene is essential for yeast cell growth."
      Friedman H., Goebel M., Snyder M.
      Gene 122:203-206(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins."
      Heinemeyer W., Gruhler A., Moehrle V., Mahe Y., Wolf D.H.
      J. Biol. Chem. 268:5115-5120(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 5288C.
    3. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 76-90, MUTAGENESIS OF ASP-126.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding for a fork head protein involved in rRNA processing."
      Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P.
      Mol. Cell. Biol. 14:2905-2913(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 176-287.
      Strain: ATCC 28383 / FL100 / VTT C-80102.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [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 76-287 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 76-287 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 76-287 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 76-287 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 76-287 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 76-287 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 76-287 IN COMPLEX WITH THE PROTEASOME.
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSB5_YEAST
    AccessioniPrimary (citable) accession number: P30656
    Secondary accession number(s): D6W4A1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The side chain of Thr-76 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
    Present with 8530 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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3