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P32379

- PSA5_YEAST

UniProt

P32379 - PSA5_YEAST

Protein

Proteasome subunit alpha type-5

Gene

PUP2

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 158 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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-30926-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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-5 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PUP2
    Multicatalytic endopeptidase complex subunit PUP2
    Proteasome component PUP2
    Proteinase YSCE subunit PUP2
    Gene namesi
    Name:PUP2
    Synonyms:DOA5
    Ordered Locus Names:YGR253C
    ORF Names:G9155
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR253c.
    SGDiS000003485. PUP2.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491G → D in DOA5-1; slight decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Proteasome subunit alpha type-5PRO_0000124129Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphothreonine1 Publication
    Modified residuei56 – 561Phosphoserine1 Publication
    Modified residuei251 – 2511Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32379.
    PaxDbiP32379.
    PeptideAtlasiP32379.
    PRIDEiP32379.

    Expressioni

    Gene expression databases

    GenevestigatoriP32379.

    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

    BioGridi33504. 58 interactions.
    DIPiDIP-1193N.
    IntActiP32379. 9 interactions.
    MINTiMINT-386734.
    STRINGi4932.YGR253C.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Beta strandi19 – 213
    Helixi22 – 3110
    Beta strandi37 – 415
    Beta strandi46 – 516
    Beta strandi55 – 595
    Helixi61 – 633
    Beta strandi67 – 715
    Beta strandi74 – 818
    Helixi82 – 843
    Helixi85 – 10319
    Helixi109 – 1179
    Turni118 – 1214
    Beta strandi124 – 1263
    Beta strandi128 – 1314
    Beta strandi134 – 1363
    Beta strandi139 – 14810
    Turni149 – 1513
    Beta strandi152 – 1587
    Turni160 – 1623
    Beta strandi164 – 17310
    Helixi176 – 18611
    Helixi193 – 20715
    Beta strandi208 – 2103
    Beta strandi216 – 2238
    Turni224 – 2263
    Beta strandi227 – 2304
    Helixi233 – 24715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20E/S1-260[»]
    1G0UX-ray2.40D/R1-250[»]
    1G65X-ray2.25D/R9-250[»]
    1JD2X-ray3.00D/Y9-120[»]
    D/Y131-250[»]
    1RYPX-ray1.90E/S9-250[»]
    1VSYX-ray3.00E/S1-250[»]
    1Z7QX-ray3.22E/S1-260[»]
    2F16X-ray2.80D/R9-250[»]
    2FAKX-ray2.80D/R9-250[»]
    2GPLX-ray2.81D/R9-250[»]
    2Z5CX-ray2.90C/F1-260[»]
    2ZCYX-ray2.90D/R1-260[»]
    3BDMX-ray2.70D/R1-260[»]
    3D29X-ray2.60D/R9-250[»]
    3DY3X-ray2.81D/R9-250[»]
    3DY4X-ray2.80D/R9-250[»]
    3E47X-ray3.00D/R9-250[»]
    3GPJX-ray2.70D/R9-250[»]
    3GPTX-ray2.41D/R9-250[»]
    3GPWX-ray2.50D/R9-250[»]
    3HYEX-ray2.50D/R9-250[»]
    3L5QX-ray3.00J/V1-250[»]
    3MG0X-ray2.68D/R9-250[»]
    3MG4X-ray3.11D/R9-250[»]
    3MG6X-ray2.60D/R1-250[»]
    3MG7X-ray2.78D/R1-250[»]
    3MG8X-ray2.59D/R1-250[»]
    3NZJX-ray2.40D/R1-260[»]
    3NZWX-ray2.50D/R1-260[»]
    3NZXX-ray2.70D/R1-260[»]
    3OEUX-ray2.60D/R1-260[»]
    3OEVX-ray2.85D/R1-260[»]
    3OKJX-ray2.70D/R9-250[»]
    3SDIX-ray2.65D/R1-260[»]
    3SDKX-ray2.70D/R1-260[»]
    3SHJX-ray2.80D/R9-250[»]
    3TDDX-ray2.70D/R9-250[»]
    3UN4X-ray3.40D/R1-260[»]
    3UN8X-ray2.70D/R1-260[»]
    4CR2electron microscopy7.70E1-260[»]
    4CR3electron microscopy9.30E1-260[»]
    4CR4electron microscopy8.80E1-260[»]
    4EU2X-ray2.51E/S9-250[»]
    4FZCX-ray2.80D/R9-250[»]
    4FZGX-ray3.00D/R9-250[»]
    4G4SX-ray2.49E1-260[»]
    4GK7X-ray2.80D/R9-250[»]
    4HNPX-ray2.80D/R9-250[»]
    4HRCX-ray2.80D/R9-250[»]
    4HRDX-ray2.80D/R9-250[»]
    4INRX-ray2.70D/R1-260[»]
    4INTX-ray2.90D/R1-260[»]
    4INUX-ray3.10D/R1-260[»]
    4J70X-ray2.80D/R1-260[»]
    4JSQX-ray2.80D/R1-260[»]
    4JSUX-ray2.90D/R1-260[»]
    4JT0X-ray3.10D/R1-260[»]
    4LQIX-ray2.70D/R9-250[»]
    4NNNX-ray2.50D/R1-260[»]
    4NNWX-ray2.60D/R1-260[»]
    4NO1X-ray2.50D/R1-260[»]
    4NO6X-ray3.00D/R1-260[»]
    4NO8X-ray2.70D/R1-260[»]
    4NO9X-ray2.90D/R1-260[»]
    4QBYX-ray3.00D/R1-260[»]
    ProteinModelPortaliP32379.
    SMRiP32379. Positions 9-250.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32379.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074958.
    HOGENOMiHOG000091085.
    KOiK02729.
    OMAiCAMSGLT.
    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.

    P32379-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLTRSEYDR GVSTFSPEGR LFQVEYSLEA IKLGSTAIGI ATKEGVVLGV    50
    EKRATSPLLE SDSIEKIVEI DRHIGCAMSG LTADARSMIE HARTAAVTHN 100
    LYYDEDINVE SLTQSVCDLA LRFGEGASGE ERLMSRPFGV ALLIAGHDAD 150
    DGYQLFHAEP SGTFYRYNAK AIGSGSEGAQ AELLNEWHSS LTLKEAELLV 200
    LKILKQVMEE KLDENNAQLS CITKQDGFKI YDNEKTAELI KELKEKEAAE 250
    SPEEADVEMS 260
    Length:260
    Mass (Da):28,617
    Last modified:October 1, 1996 - v2
    Checksum:iE8EDEB212BF4EC6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921T → S in CAA46111. (PubMed:1544471)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64918 Genomic DNA. Translation: CAA46111.1.
    X99228 Genomic DNA. Translation: CAA67615.1.
    Z73038 Genomic DNA. Translation: CAA97282.1.
    AY558511 Genomic DNA. Translation: AAS56837.1.
    BK006941 Genomic DNA. Translation: DAA08344.1.
    PIRiS64585.
    RefSeqiNP_011769.1. NM_001181382.1.

    Genome annotation databases

    EnsemblFungiiYGR253C; YGR253C; YGR253C.
    GeneIDi853168.
    KEGGisce:YGR253C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64918 Genomic DNA. Translation: CAA46111.1 .
    X99228 Genomic DNA. Translation: CAA67615.1 .
    Z73038 Genomic DNA. Translation: CAA97282.1 .
    AY558511 Genomic DNA. Translation: AAS56837.1 .
    BK006941 Genomic DNA. Translation: DAA08344.1 .
    PIRi S64585.
    RefSeqi NP_011769.1. NM_001181382.1.

    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 E/S 1-260 [» ]
    1G0U X-ray 2.40 D/R 1-250 [» ]
    1G65 X-ray 2.25 D/R 9-250 [» ]
    1JD2 X-ray 3.00 D/Y 9-120 [» ]
    D/Y 131-250 [» ]
    1RYP X-ray 1.90 E/S 9-250 [» ]
    1VSY X-ray 3.00 E/S 1-250 [» ]
    1Z7Q X-ray 3.22 E/S 1-260 [» ]
    2F16 X-ray 2.80 D/R 9-250 [» ]
    2FAK X-ray 2.80 D/R 9-250 [» ]
    2GPL X-ray 2.81 D/R 9-250 [» ]
    2Z5C X-ray 2.90 C/F 1-260 [» ]
    2ZCY X-ray 2.90 D/R 1-260 [» ]
    3BDM X-ray 2.70 D/R 1-260 [» ]
    3D29 X-ray 2.60 D/R 9-250 [» ]
    3DY3 X-ray 2.81 D/R 9-250 [» ]
    3DY4 X-ray 2.80 D/R 9-250 [» ]
    3E47 X-ray 3.00 D/R 9-250 [» ]
    3GPJ X-ray 2.70 D/R 9-250 [» ]
    3GPT X-ray 2.41 D/R 9-250 [» ]
    3GPW X-ray 2.50 D/R 9-250 [» ]
    3HYE X-ray 2.50 D/R 9-250 [» ]
    3L5Q X-ray 3.00 J/V 1-250 [» ]
    3MG0 X-ray 2.68 D/R 9-250 [» ]
    3MG4 X-ray 3.11 D/R 9-250 [» ]
    3MG6 X-ray 2.60 D/R 1-250 [» ]
    3MG7 X-ray 2.78 D/R 1-250 [» ]
    3MG8 X-ray 2.59 D/R 1-250 [» ]
    3NZJ X-ray 2.40 D/R 1-260 [» ]
    3NZW X-ray 2.50 D/R 1-260 [» ]
    3NZX X-ray 2.70 D/R 1-260 [» ]
    3OEU X-ray 2.60 D/R 1-260 [» ]
    3OEV X-ray 2.85 D/R 1-260 [» ]
    3OKJ X-ray 2.70 D/R 9-250 [» ]
    3SDI X-ray 2.65 D/R 1-260 [» ]
    3SDK X-ray 2.70 D/R 1-260 [» ]
    3SHJ X-ray 2.80 D/R 9-250 [» ]
    3TDD X-ray 2.70 D/R 9-250 [» ]
    3UN4 X-ray 3.40 D/R 1-260 [» ]
    3UN8 X-ray 2.70 D/R 1-260 [» ]
    4CR2 electron microscopy 7.70 E 1-260 [» ]
    4CR3 electron microscopy 9.30 E 1-260 [» ]
    4CR4 electron microscopy 8.80 E 1-260 [» ]
    4EU2 X-ray 2.51 E/S 9-250 [» ]
    4FZC X-ray 2.80 D/R 9-250 [» ]
    4FZG X-ray 3.00 D/R 9-250 [» ]
    4G4S X-ray 2.49 E 1-260 [» ]
    4GK7 X-ray 2.80 D/R 9-250 [» ]
    4HNP X-ray 2.80 D/R 9-250 [» ]
    4HRC X-ray 2.80 D/R 9-250 [» ]
    4HRD X-ray 2.80 D/R 9-250 [» ]
    4INR X-ray 2.70 D/R 1-260 [» ]
    4INT X-ray 2.90 D/R 1-260 [» ]
    4INU X-ray 3.10 D/R 1-260 [» ]
    4J70 X-ray 2.80 D/R 1-260 [» ]
    4JSQ X-ray 2.80 D/R 1-260 [» ]
    4JSU X-ray 2.90 D/R 1-260 [» ]
    4JT0 X-ray 3.10 D/R 1-260 [» ]
    4LQI X-ray 2.70 D/R 9-250 [» ]
    4NNN X-ray 2.50 D/R 1-260 [» ]
    4NNW X-ray 2.60 D/R 1-260 [» ]
    4NO1 X-ray 2.50 D/R 1-260 [» ]
    4NO6 X-ray 3.00 D/R 1-260 [» ]
    4NO8 X-ray 2.70 D/R 1-260 [» ]
    4NO9 X-ray 2.90 D/R 1-260 [» ]
    4QBY X-ray 3.00 D/R 1-260 [» ]
    ProteinModelPortali P32379.
    SMRi P32379. Positions 9-250.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33504. 58 interactions.
    DIPi DIP-1193N.
    IntActi P32379. 9 interactions.
    MINTi MINT-386734.
    STRINGi 4932.YGR253C.

    Proteomic databases

    MaxQBi P32379.
    PaxDbi P32379.
    PeptideAtlasi P32379.
    PRIDEi P32379.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR253C ; YGR253C ; YGR253C .
    GeneIDi 853168.
    KEGGi sce:YGR253C.

    Organism-specific databases

    CYGDi YGR253c.
    SGDi S000003485. PUP2.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074958.
    HOGENOMi HOG000091085.
    KOi K02729.
    OMAi CAMSGLT.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30926-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 P32379.
    NextBioi 973285.
    PROi P32379.

    Gene expression databases

    Genevestigatori P32379.

    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. "Molecular cloning of an essential yeast gene encoding a proteasomal subunit."
      Georgatsou E., Georgakopoulos T., Thireos G.
      FEBS Lett. 299:39-43(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-49.
    3. "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene."
      Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.
      Yeast 13:369-372(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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 THR-55; SER-56 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
    12. "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).
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-250 OF COMPLEX WITH THE 20S PROTEASOME.
    14. "Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
      Groll M., Koguchi Y., Huber R., Kohno J.
      J. Mol. Biol. 311:543-548(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
    15. "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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
    16. "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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
    17. "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 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
    18. "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 1-250 IN COMPLEX WITH THE PROTEASOME.
    19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA5_YEAST
    AccessioniPrimary (citable) accession number: P32379
    Secondary accession number(s): D6VV33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 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, 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