Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P40303

- PSA4_YEAST

UniProt

P40303 - PSA4_YEAST

Protein

Proteasome subunit alpha type-4

Gene

PRE6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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-mediated ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33452-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-4 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PRE6
    Multicatalytic endopeptidase complex subunit PRE6
    Proteasome component PRE6
    Proteinase YSCE subunit PRE6
    Gene namesi
    Name:PRE6
    Ordered Locus Names:YOL038W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL038w.
    SGDiS000005398. PRE6.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. mitochondrion 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 – 254254Proteasome subunit alpha type-4PRO_0000124165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP40303.
    PaxDbiP40303.
    PeptideAtlasiP40303.
    PRIDEiP40303.

    Expressioni

    Gene expression databases

    GenevestigatoriP40303.

    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. Interacts with CIC1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CIC1P387795EBI-13980,EBI-24538
    cut8P389372EBI-13980,EBI-1152591From a different organism.
    PRE1P221413EBI-13980,EBI-13988

    Protein-protein interaction databases

    BioGridi34364. 103 interactions.
    DIPiDIP-4844N.
    IntActiP40303. 42 interactions.
    MINTiMINT-478854.
    STRINGi4932.YOL038W.

    Structurei

    Secondary structure

    1
    254
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Turni13 – 153
    Helixi18 – 2710
    Beta strandi33 – 375
    Beta strandi42 – 476
    Beta strandi53 – 553
    Turni57 – 593
    Beta strandi63 – 686
    Beta strandi71 – 777
    Helixi79 – 10022
    Helixi106 – 11914
    Turni120 – 1223
    Beta strandi123 – 1264
    Beta strandi130 – 1378
    Beta strandi146 – 1505
    Turni152 – 1543
    Beta strandi156 – 16510
    Helixi168 – 1769
    Beta strandi181 – 1833
    Helixi188 – 20316
    Beta strandi204 – 2063
    Helixi207 – 2093
    Beta strandi210 – 2167
    Turni217 – 2193
    Beta strandi220 – 2234
    Helixi226 – 23611
    Helixi238 – 2414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20D/R1-254[»]
    1G0UX-ray2.40C/Q1-243[»]
    1G65X-ray2.25C/Q3-243[»]
    1JD2X-ray3.00C/X3-243[»]
    1RYPX-ray1.90D/R3-243[»]
    1VSYX-ray3.00D/R17-243[»]
    1Z7QX-ray3.22D/R1-254[»]
    2F16X-ray2.80C/Q3-243[»]
    2FAKX-ray2.80C/Q3-243[»]
    2GPLX-ray2.81C/Q3-243[»]
    2ZCYX-ray2.90C/Q1-254[»]
    3BDMX-ray2.70C/Q1-254[»]
    3D29X-ray2.60C/Q3-236[»]
    3DY3X-ray2.81C/Q3-243[»]
    3DY4X-ray2.80C/Q3-243[»]
    3E47X-ray3.00C/Q3-243[»]
    3GPJX-ray2.70C/Q3-243[»]
    3GPTX-ray2.41C/Q3-243[»]
    3GPWX-ray2.50C/Q3-243[»]
    3HYEX-ray2.50C/Q3-243[»]
    3L5QX-ray3.00I/U17-243[»]
    3MG0X-ray2.68C/Q3-243[»]
    3MG4X-ray3.11C/Q3-243[»]
    3MG6X-ray2.60C/Q1-243[»]
    3MG7X-ray2.78C/Q1-243[»]
    3MG8X-ray2.59C/Q1-243[»]
    3NZJX-ray2.40C/Q1-254[»]
    3NZWX-ray2.50C/Q1-254[»]
    3NZXX-ray2.70C/Q1-254[»]
    3OEUX-ray2.60C/Q3-243[»]
    3OEVX-ray2.85C/Q3-243[»]
    3OKJX-ray2.70C/Q3-243[»]
    3SDIX-ray2.65C/Q3-243[»]
    3SDKX-ray2.70C/Q3-243[»]
    3SHJX-ray2.80C/Q3-243[»]
    3TDDX-ray2.70C/Q3-243[»]
    3UN4X-ray3.40C/Q1-254[»]
    3UN8X-ray2.70C/Q1-254[»]
    4CR2electron microscopy7.70D1-254[»]
    4CR3electron microscopy9.30D1-254[»]
    4CR4electron microscopy8.80D1-254[»]
    4EU2X-ray2.51D/R3-243[»]
    4FZCX-ray2.80C/Q3-243[»]
    4FZGX-ray3.00C/Q3-243[»]
    4G4SX-ray2.49D1-254[»]
    4GK7X-ray2.80C/Q3-243[»]
    4HNPX-ray2.80C/Q3-243[»]
    4HRCX-ray2.80C/Q3-243[»]
    4HRDX-ray2.80C/Q3-243[»]
    4INRX-ray2.70C/Q1-254[»]
    4INTX-ray2.90C/Q1-254[»]
    4INUX-ray3.10C/Q1-254[»]
    4J70X-ray2.80C/Q1-254[»]
    4JSQX-ray2.80C/Q1-254[»]
    4JSUX-ray2.90C/Q1-254[»]
    4JT0X-ray3.10C/Q1-254[»]
    4LQIX-ray2.70C/Q3-243[»]
    4NNNX-ray2.50C/Q1-254[»]
    4NNWX-ray2.60C/Q1-254[»]
    4NO1X-ray2.50C/Q1-254[»]
    4NO6X-ray3.00C/Q1-254[»]
    4NO8X-ray2.70C/Q1-254[»]
    4NO9X-ray2.90C/Q1-254[»]
    4QBYX-ray3.00C/Q1-254[»]
    ProteinModelPortaliP40303.
    SMRiP40303. Positions 3-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40303.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074753.
    HOGENOMiHOG000091085.
    KOiK02731.
    OMAiITRHIAG.
    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.

    P40303-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGYDRALSI FSPDGHIFQV EYALEAVKRG TCAVGVKGKN CVVLGCERRS    50
    TLKLQDTRIT PSKVSKIDSH VVLSFSGLNA DSRILIEKAR VEAQSHRLTL 100
    EDPVTVEYLT RYVAGVQQRY TQSGGVRPFG VSTLIAGFDP RDDEPKLYQT 150
    EPSGIYSSWS AQTIGRNSKT VREFLEKNYD RKEPPATVEE CVKLTVRSLL 200
    EVVQTGAKNI EITVVKPDSD IVALSSEEIN QYVTQIEQEK QEQQEQDKKK 250
    KSNH 254
    Length:254
    Mass (Da):28,439
    Last modified:February 1, 1995 - v1
    Checksum:i73AEE63B836E618A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34348 Genomic DNA. Translation: AAA34903.1.
    Z74780 Genomic DNA. Translation: CAA99040.1.
    BK006948 Genomic DNA. Translation: DAA10745.1.
    PIRiB55904.
    RefSeqiNP_014604.1. NM_001183292.1.

    Genome annotation databases

    EnsemblFungiiYOL038W; YOL038W; YOL038W.
    GeneIDi854119.
    KEGGisce:YOL038W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34348 Genomic DNA. Translation: AAA34903.1 .
    Z74780 Genomic DNA. Translation: CAA99040.1 .
    BK006948 Genomic DNA. Translation: DAA10745.1 .
    PIRi B55904.
    RefSeqi NP_014604.1. NM_001183292.1.

    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 D/R 1-254 [» ]
    1G0U X-ray 2.40 C/Q 1-243 [» ]
    1G65 X-ray 2.25 C/Q 3-243 [» ]
    1JD2 X-ray 3.00 C/X 3-243 [» ]
    1RYP X-ray 1.90 D/R 3-243 [» ]
    1VSY X-ray 3.00 D/R 17-243 [» ]
    1Z7Q X-ray 3.22 D/R 1-254 [» ]
    2F16 X-ray 2.80 C/Q 3-243 [» ]
    2FAK X-ray 2.80 C/Q 3-243 [» ]
    2GPL X-ray 2.81 C/Q 3-243 [» ]
    2ZCY X-ray 2.90 C/Q 1-254 [» ]
    3BDM X-ray 2.70 C/Q 1-254 [» ]
    3D29 X-ray 2.60 C/Q 3-236 [» ]
    3DY3 X-ray 2.81 C/Q 3-243 [» ]
    3DY4 X-ray 2.80 C/Q 3-243 [» ]
    3E47 X-ray 3.00 C/Q 3-243 [» ]
    3GPJ X-ray 2.70 C/Q 3-243 [» ]
    3GPT X-ray 2.41 C/Q 3-243 [» ]
    3GPW X-ray 2.50 C/Q 3-243 [» ]
    3HYE X-ray 2.50 C/Q 3-243 [» ]
    3L5Q X-ray 3.00 I/U 17-243 [» ]
    3MG0 X-ray 2.68 C/Q 3-243 [» ]
    3MG4 X-ray 3.11 C/Q 3-243 [» ]
    3MG6 X-ray 2.60 C/Q 1-243 [» ]
    3MG7 X-ray 2.78 C/Q 1-243 [» ]
    3MG8 X-ray 2.59 C/Q 1-243 [» ]
    3NZJ X-ray 2.40 C/Q 1-254 [» ]
    3NZW X-ray 2.50 C/Q 1-254 [» ]
    3NZX X-ray 2.70 C/Q 1-254 [» ]
    3OEU X-ray 2.60 C/Q 3-243 [» ]
    3OEV X-ray 2.85 C/Q 3-243 [» ]
    3OKJ X-ray 2.70 C/Q 3-243 [» ]
    3SDI X-ray 2.65 C/Q 3-243 [» ]
    3SDK X-ray 2.70 C/Q 3-243 [» ]
    3SHJ X-ray 2.80 C/Q 3-243 [» ]
    3TDD X-ray 2.70 C/Q 3-243 [» ]
    3UN4 X-ray 3.40 C/Q 1-254 [» ]
    3UN8 X-ray 2.70 C/Q 1-254 [» ]
    4CR2 electron microscopy 7.70 D 1-254 [» ]
    4CR3 electron microscopy 9.30 D 1-254 [» ]
    4CR4 electron microscopy 8.80 D 1-254 [» ]
    4EU2 X-ray 2.51 D/R 3-243 [» ]
    4FZC X-ray 2.80 C/Q 3-243 [» ]
    4FZG X-ray 3.00 C/Q 3-243 [» ]
    4G4S X-ray 2.49 D 1-254 [» ]
    4GK7 X-ray 2.80 C/Q 3-243 [» ]
    4HNP X-ray 2.80 C/Q 3-243 [» ]
    4HRC X-ray 2.80 C/Q 3-243 [» ]
    4HRD X-ray 2.80 C/Q 3-243 [» ]
    4INR X-ray 2.70 C/Q 1-254 [» ]
    4INT X-ray 2.90 C/Q 1-254 [» ]
    4INU X-ray 3.10 C/Q 1-254 [» ]
    4J70 X-ray 2.80 C/Q 1-254 [» ]
    4JSQ X-ray 2.80 C/Q 1-254 [» ]
    4JSU X-ray 2.90 C/Q 1-254 [» ]
    4JT0 X-ray 3.10 C/Q 1-254 [» ]
    4LQI X-ray 2.70 C/Q 3-243 [» ]
    4NNN X-ray 2.50 C/Q 1-254 [» ]
    4NNW X-ray 2.60 C/Q 1-254 [» ]
    4NO1 X-ray 2.50 C/Q 1-254 [» ]
    4NO6 X-ray 3.00 C/Q 1-254 [» ]
    4NO8 X-ray 2.70 C/Q 1-254 [» ]
    4NO9 X-ray 2.90 C/Q 1-254 [» ]
    4QBY X-ray 3.00 C/Q 1-254 [» ]
    ProteinModelPortali P40303.
    SMRi P40303. Positions 3-243.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34364. 103 interactions.
    DIPi DIP-4844N.
    IntActi P40303. 42 interactions.
    MINTi MINT-478854.
    STRINGi 4932.YOL038W.

    Proteomic databases

    MaxQBi P40303.
    PaxDbi P40303.
    PeptideAtlasi P40303.
    PRIDEi P40303.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL038W ; YOL038W ; YOL038W .
    GeneIDi 854119.
    KEGGi sce:YOL038W.

    Organism-specific databases

    CYGDi YOL038w.
    SGDi S000005398. PRE6.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074753.
    HOGENOMi HOG000091085.
    KOi K02731.
    OMAi ITRHIAG.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33452-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 P40303.
    NextBioi 975822.

    Gene expression databases

    Genevestigatori P40303.

    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. "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].
      Strain: ATCC 204508 / S288c.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(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. Troendle N.
      Thesis (1991), University of Stuttgart, Germany
      Cited for: PROTEIN SEQUENCE OF 112-133.
    5. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
      Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
      EMBO J. 20:4423-4431(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIC1.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 3-343 OF COMPLEX WITH THE 20S PROTEASOME.
    10. "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.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-243 OF COMPLEX WITH THE 20S PROTEASOME.
    12. "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 3-243 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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
    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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
    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 3-243 OF COMPLEX WITH THE 20S PROTEASOME.
    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) OF 17-243 IN COMPLEX WITH THE PROTEASOME.
    17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA4_YEAST
    AccessioniPrimary (citable) accession number: P40303
    Secondary accession number(s): D6W229
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    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 16800 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3