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P23638

- PSA3_YEAST

UniProt

P23638 - PSA3_YEAST

Protein

Proteasome subunit alpha type-3

Gene

PRE9

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 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.PROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. 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-30841-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

    MEROPSiT01.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-3 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit Y13
    Multicatalytic endopeptidase complex subunit Y13
    Proteasome component Y13
    Proteinase YSCE subunit 13
    Gene namesi
    Name:PRE9
    Synonyms:PRS5
    Ordered Locus Names:YGR135W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR135w.
    SGDiS000003367. PRE9.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
    2. nucleus Source: SGD
    3. proteasome core complex, alpha-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
    Chaini1 – 258258Proteasome subunit alpha type-3PRO_0000124116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki199 – 199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP23638.
    PaxDbiP23638.
    PeptideAtlasiP23638.

    Expressioni

    Gene expression databases

    GenevestigatoriP23638.

    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
    PRE8P236394EBI-13967,EBI-13959

    Protein-protein interaction databases

    BioGridi33383. 327 interactions.
    DIPiDIP-2823N.
    IntActiP23638. 17 interactions.
    MINTiMINT-484272.
    STRINGi4932.YGR135W.

    Structurei

    Secondary structure

    1
    258
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Turni15 – 173
    Helixi20 – 2910
    Beta strandi35 – 406
    Beta strandi43 – 497
    Beta strandi55 – 573
    Beta strandi59 – 613
    Beta strandi64 – 7916
    Helixi81 – 10222
    Helixi108 – 12417
    Beta strandi125 – 1273
    Beta strandi133 – 1419
    Turni142 – 1443
    Beta strandi145 – 1517
    Beta strandi157 – 16610
    Helixi169 – 17911
    Helixi186 – 20015
    Beta strandi202 – 2054
    Helixi208 – 2103
    Beta strandi211 – 2177
    Beta strandi220 – 2245
    Beta strandi226 – 2294
    Helixi232 – 24110
    Turni242 – 2443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20C/Q1-245[»]
    1G0UX-ray2.40B/P1-245[»]
    1G65X-ray2.25B/P2-245[»]
    1JD2X-ray3.00B/W2-245[»]
    1RYPX-ray1.90C/Q2-245[»]
    1VSYX-ray3.00C/Q14-245[»]
    1Z7QX-ray3.22C/Q1-258[»]
    2F16X-ray2.80B/P2-245[»]
    2FAKX-ray2.80B/P2-245[»]
    2GPLX-ray2.81B/P2-245[»]
    2ZCYX-ray2.90B/P1-258[»]
    3BDMX-ray2.70B/P1-258[»]
    3D29X-ray2.60B/P2-245[»]
    3DY3X-ray2.81B/P2-245[»]
    3DY4X-ray2.80B/P2-245[»]
    3E47X-ray3.00B/P2-245[»]
    3GPJX-ray2.70B/P2-245[»]
    3GPTX-ray2.41B/P2-245[»]
    3GPWX-ray2.50B/P2-245[»]
    3HYEX-ray2.50B/P2-245[»]
    3L5QX-ray3.00H/T14-245[»]
    3MG0X-ray2.68B/P2-245[»]
    3MG4X-ray3.11B/P2-245[»]
    3MG6X-ray2.60B/P1-245[»]
    3MG7X-ray2.78B/P1-245[»]
    3MG8X-ray2.59B/P1-245[»]
    3NZJX-ray2.40B/P1-258[»]
    3NZWX-ray2.50B/P1-258[»]
    3NZXX-ray2.70B/P1-258[»]
    3OEUX-ray2.60B/P11-245[»]
    3OEVX-ray2.85B/P11-245[»]
    3OKJX-ray2.70B/P2-245[»]
    3SDIX-ray2.65B/P11-245[»]
    3SDKX-ray2.70B/P11-245[»]
    3SHJX-ray2.80B/P2-245[»]
    3TDDX-ray2.70B/P2-245[»]
    3UN4X-ray3.40B/P1-258[»]
    3UN8X-ray2.70B/P1-258[»]
    4CR2electron microscopy7.70C1-258[»]
    4CR3electron microscopy9.30C1-258[»]
    4CR4electron microscopy8.80C1-258[»]
    4EU2X-ray2.51C/Q2-245[»]
    4FZCX-ray2.80B/P2-245[»]
    4FZGX-ray3.00B/P2-245[»]
    4G4SX-ray2.49C1-258[»]
    4GK7X-ray2.80B/P2-245[»]
    4HNPX-ray2.80B/P2-245[»]
    4HRCX-ray2.80B/P2-245[»]
    4HRDX-ray2.80B/P2-245[»]
    4INRX-ray2.70B/P1-258[»]
    4INTX-ray2.90B/P1-258[»]
    4INUX-ray3.10B/P1-258[»]
    4J70X-ray2.80B/P1-258[»]
    4JSQX-ray2.80B/P1-258[»]
    4JSUX-ray2.90B/P1-258[»]
    4JT0X-ray3.10B/P1-258[»]
    4LQIX-ray2.70B/P2-245[»]
    4NNNX-ray2.50B/P1-258[»]
    4NNWX-ray2.60B/P1-258[»]
    4NO1X-ray2.50B/P1-258[»]
    4NO6X-ray3.00B/P1-258[»]
    4NO8X-ray2.70B/P1-258[»]
    4NO9X-ray2.90B/P1-258[»]
    4QBYX-ray3.00B/P1-258[»]
    ProteinModelPortaliP23638.
    SMRiP23638. Positions 2-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23638.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074827.
    HOGENOMiHOG000091085.
    KOiK02728.
    OMAiKQEYKDD.
    OrthoDBiEOG7SBP0C.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR016050. Proteasome_bsu_CS.
    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.

    P23638-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTAIGIMA SDGIVLAAER    50
    KVTSTLLEQD TSTEKLYKLN DKIAVAVAGL TADAEILINT ARIHAQNYLK 100
    TYNEDIPVEI LVRRLSDIKQ GYTQHGGLRP FGVSFIYAGY DDRYGYQLYT 150
    SNPSGNYTGW KAISVGANTS AAQTLLQMDY KDDMKVDDAI ELALKTLSKT 200
    TDSSALTYDR LEFATIRKGA NDGEVYQKIF KPQEIKDILV KTGITKKDED 250
    EEADEDMK 258
    Length:258
    Mass (Da):28,714
    Last modified:November 1, 1991 - v1
    Checksum:iB43BB05233A01A9E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63851 Genomic DNA. Translation: AAA34907.1.
    X56730 Genomic DNA. Translation: CAA40054.1.
    Z72920 Genomic DNA. Translation: CAA97148.1.
    BK006941 Genomic DNA. Translation: DAA08228.1.
    PIRiS12940. SNBYY3.
    RefSeqiNP_011651.3. NM_001181264.3.

    Genome annotation databases

    EnsemblFungiiYGR135W; YGR135W; YGR135W.
    GeneIDi853036.
    KEGGisce:YGR135W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63851 Genomic DNA. Translation: AAA34907.1 .
    X56730 Genomic DNA. Translation: CAA40054.1 .
    Z72920 Genomic DNA. Translation: CAA97148.1 .
    BK006941 Genomic DNA. Translation: DAA08228.1 .
    PIRi S12940. SNBYY3.
    RefSeqi NP_011651.3. NM_001181264.3.

    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 C/Q 1-245 [» ]
    1G0U X-ray 2.40 B/P 1-245 [» ]
    1G65 X-ray 2.25 B/P 2-245 [» ]
    1JD2 X-ray 3.00 B/W 2-245 [» ]
    1RYP X-ray 1.90 C/Q 2-245 [» ]
    1VSY X-ray 3.00 C/Q 14-245 [» ]
    1Z7Q X-ray 3.22 C/Q 1-258 [» ]
    2F16 X-ray 2.80 B/P 2-245 [» ]
    2FAK X-ray 2.80 B/P 2-245 [» ]
    2GPL X-ray 2.81 B/P 2-245 [» ]
    2ZCY X-ray 2.90 B/P 1-258 [» ]
    3BDM X-ray 2.70 B/P 1-258 [» ]
    3D29 X-ray 2.60 B/P 2-245 [» ]
    3DY3 X-ray 2.81 B/P 2-245 [» ]
    3DY4 X-ray 2.80 B/P 2-245 [» ]
    3E47 X-ray 3.00 B/P 2-245 [» ]
    3GPJ X-ray 2.70 B/P 2-245 [» ]
    3GPT X-ray 2.41 B/P 2-245 [» ]
    3GPW X-ray 2.50 B/P 2-245 [» ]
    3HYE X-ray 2.50 B/P 2-245 [» ]
    3L5Q X-ray 3.00 H/T 14-245 [» ]
    3MG0 X-ray 2.68 B/P 2-245 [» ]
    3MG4 X-ray 3.11 B/P 2-245 [» ]
    3MG6 X-ray 2.60 B/P 1-245 [» ]
    3MG7 X-ray 2.78 B/P 1-245 [» ]
    3MG8 X-ray 2.59 B/P 1-245 [» ]
    3NZJ X-ray 2.40 B/P 1-258 [» ]
    3NZW X-ray 2.50 B/P 1-258 [» ]
    3NZX X-ray 2.70 B/P 1-258 [» ]
    3OEU X-ray 2.60 B/P 11-245 [» ]
    3OEV X-ray 2.85 B/P 11-245 [» ]
    3OKJ X-ray 2.70 B/P 2-245 [» ]
    3SDI X-ray 2.65 B/P 11-245 [» ]
    3SDK X-ray 2.70 B/P 11-245 [» ]
    3SHJ X-ray 2.80 B/P 2-245 [» ]
    3TDD X-ray 2.70 B/P 2-245 [» ]
    3UN4 X-ray 3.40 B/P 1-258 [» ]
    3UN8 X-ray 2.70 B/P 1-258 [» ]
    4CR2 electron microscopy 7.70 C 1-258 [» ]
    4CR3 electron microscopy 9.30 C 1-258 [» ]
    4CR4 electron microscopy 8.80 C 1-258 [» ]
    4EU2 X-ray 2.51 C/Q 2-245 [» ]
    4FZC X-ray 2.80 B/P 2-245 [» ]
    4FZG X-ray 3.00 B/P 2-245 [» ]
    4G4S X-ray 2.49 C 1-258 [» ]
    4GK7 X-ray 2.80 B/P 2-245 [» ]
    4HNP X-ray 2.80 B/P 2-245 [» ]
    4HRC X-ray 2.80 B/P 2-245 [» ]
    4HRD X-ray 2.80 B/P 2-245 [» ]
    4INR X-ray 2.70 B/P 1-258 [» ]
    4INT X-ray 2.90 B/P 1-258 [» ]
    4INU X-ray 3.10 B/P 1-258 [» ]
    4J70 X-ray 2.80 B/P 1-258 [» ]
    4JSQ X-ray 2.80 B/P 1-258 [» ]
    4JSU X-ray 2.90 B/P 1-258 [» ]
    4JT0 X-ray 3.10 B/P 1-258 [» ]
    4LQI X-ray 2.70 B/P 2-245 [» ]
    4NNN X-ray 2.50 B/P 1-258 [» ]
    4NNW X-ray 2.60 B/P 1-258 [» ]
    4NO1 X-ray 2.50 B/P 1-258 [» ]
    4NO6 X-ray 3.00 B/P 1-258 [» ]
    4NO8 X-ray 2.70 B/P 1-258 [» ]
    4NO9 X-ray 2.90 B/P 1-258 [» ]
    4QBY X-ray 3.00 B/P 1-258 [» ]
    ProteinModelPortali P23638.
    SMRi P23638. Positions 2-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33383. 327 interactions.
    DIPi DIP-2823N.
    IntActi P23638. 17 interactions.
    MINTi MINT-484272.
    STRINGi 4932.YGR135W.

    Protein family/group databases

    MEROPSi T01.973.

    Proteomic databases

    MaxQBi P23638.
    PaxDbi P23638.
    PeptideAtlasi P23638.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR135W ; YGR135W ; YGR135W .
    GeneIDi 853036.
    KEGGi sce:YGR135W.

    Organism-specific databases

    CYGDi YGR135w.
    SGDi S000003367. PRE9.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074827.
    HOGENOMi HOG000091085.
    KOi K02728.
    OMAi KQEYKDD.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30841-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 P23638.
    NextBioi 972935.
    PROi P23638.

    Gene expression databases

    Genevestigatori P23638.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR016050. Proteasome_bsu_CS.
    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. "Molecular cloning and functional analysis of three subunits of yeast proteasome."
      Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
      Mol. Cell. Biol. 11:344-353(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 73-92; 120-139 AND 200-236.
      Strain: ATCC 26786 / X2180-1A.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-199.
    6. "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].
    7. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME.
    8. "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 1-245 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S PROTEASOME.
    10. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
    11. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
    12. "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 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
    13. "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 14-245 IN COMPLEX WITH THE PROTEASOME.
    14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA3_YEAST
    AccessioniPrimary (citable) accession number: P23638
    Secondary accession number(s): D6VUR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 153 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 17100 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3