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)

P21242

- PSA7_YEAST

UniProt

P21242 - PSA7_YEAST

Protein

Probable proteasome subunit alpha type-7

Gene

PRE10

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 165 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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. mRNA binding 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-mediated ubiquitin-dependent protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33832-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:
    Probable proteasome subunit alpha type-7 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C1
    Multicatalytic endopeptidase complex subunit C1
    Proteasome component C1
    Proteinase YSCE subunit 1
    Gene namesi
    Name:PRE10
    Synonyms:PRC1, PRS1
    Ordered Locus Names:YOR362C
    ORF Names:O6650
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    SGDiS000005889. PRE10.

    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
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 288287Probable proteasome subunit alpha type-7PRO_0000124102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication

    Post-translational modificationi

    The alpha and beta forms are probably products of the same gene with different post-translational modifications.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP21242.
    PaxDbiP21242.
    PeptideAtlasiP21242.

    Expressioni

    Gene expression databases

    GenevestigatoriP21242.

    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
    PRE1P221413EBI-13963,EBI-13988
    SCL1P212436EBI-13963,EBI-13975

    Protein-protein interaction databases

    BioGridi34747. 92 interactions.
    DIPiDIP-1526N.
    IntActiP21242. 29 interactions.
    MINTiMINT-411846.
    STRINGi4932.YOR362C.

    Structurei

    Secondary structure

    1
    288
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 114
    Beta strandi17 – 193
    Helixi22 – 3211
    Beta strandi37 – 426
    Beta strandi45 – 539
    Turni61 – 633
    Beta strandi68 – 703
    Turni71 – 733
    Beta strandi74 – 807
    Helixi82 – 10322
    Helixi109 – 12214
    Turni123 – 1253
    Beta strandi127 – 1293
    Beta strandi134 – 1429
    Beta strandi145 – 1517
    Turni153 – 1553
    Beta strandi157 – 16610
    Helixi169 – 18214
    Helixi189 – 20315
    Helixi204 – 2074
    Beta strandi212 – 2209
    Turni221 – 2233
    Beta strandi227 – 2304
    Helixi234 – 24512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20G/U2-288[»]
    1G0UX-ray2.40F/T1-248[»]
    1G65X-ray2.25F/T5-248[»]
    1JD2X-ray3.001/F5-248[»]
    1RYPX-ray1.90G/U5-248[»]
    1VSYX-ray3.00G/U5-248[»]
    1Z7QX-ray3.22G/U1-288[»]
    2F16X-ray2.80F/T5-248[»]
    2FAKX-ray2.80F/T5-248[»]
    2GPLX-ray2.81F/T5-248[»]
    2ZCYX-ray2.90F/T2-288[»]
    3BDMX-ray2.70F/T2-288[»]
    3D29X-ray2.60F/T5-248[»]
    3DY3X-ray2.81F/T5-248[»]
    3DY4X-ray2.80F/T5-248[»]
    3E47X-ray3.00F/T5-248[»]
    3GPJX-ray2.70F/T5-248[»]
    3GPTX-ray2.41F/T5-248[»]
    3GPWX-ray2.50F/T5-248[»]
    3HYEX-ray2.50F/T5-248[»]
    3L5QX-ray3.00L/X5-248[»]
    3MG0X-ray2.68F/T5-248[»]
    3MG4X-ray3.11F/T5-248[»]
    3MG6X-ray2.60F/T1-248[»]
    3MG7X-ray2.78F/T1-248[»]
    3MG8X-ray2.59F/T1-248[»]
    3NZJX-ray2.40F/T1-288[»]
    3NZWX-ray2.50F/T1-288[»]
    3NZXX-ray2.70F/T1-288[»]
    3OEUX-ray2.60F/T7-248[»]
    3OEVX-ray2.85F/T7-248[»]
    3OKJX-ray2.70F/T5-248[»]
    3SDIX-ray2.65F/T7-248[»]
    3SDKX-ray2.70F/T7-248[»]
    3SHJX-ray2.80F/T5-248[»]
    3TDDX-ray2.70F/T5-248[»]
    3UN4X-ray3.40F/T1-288[»]
    3UN8X-ray2.70F/T1-288[»]
    4CR2electron microscopy7.70G1-288[»]
    4CR3electron microscopy9.30G1-288[»]
    4CR4electron microscopy8.80G1-288[»]
    4EU2X-ray2.51G/U5-248[»]
    4FZCX-ray2.80F/T5-248[»]
    4FZGX-ray3.00F/T5-248[»]
    4G4SX-ray2.49G1-288[»]
    4GK7X-ray2.80F/T5-248[»]
    4HNPX-ray2.80F/T5-248[»]
    4HRCX-ray2.80F/T5-248[»]
    4HRDX-ray2.80F/T5-248[»]
    4INRX-ray2.70F/T1-288[»]
    4INTX-ray2.90F/T1-288[»]
    4INUX-ray3.10F/T1-288[»]
    4J70X-ray2.80F/T1-288[»]
    4JSQX-ray2.80F/T1-288[»]
    4JSUX-ray2.90F/T1-288[»]
    4JT0X-ray3.10F/T1-288[»]
    4LQIX-ray2.70F/T5-248[»]
    4NNNX-ray2.50F/T1-288[»]
    4NNWX-ray2.60F/T1-288[»]
    4NO1X-ray2.50F/T1-288[»]
    4NO6X-ray3.00F/T1-288[»]
    4NO8X-ray2.70F/T1-288[»]
    4NO9X-ray2.90F/T1-288[»]
    4QBYX-ray3.00F/T1-288[»]
    ProteinModelPortaliP21242.
    SMRiP21242. Positions 5-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21242.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074912.
    HOGENOMiHOG000091086.
    KOiK02727.
    OMAiVPDGRHF.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P21242-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV    50
    EKLITSKLLV PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK 100
    KLYKTPIPIP AFADRLGQYV QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM 150
    LEPSGSYWGY KGAATGKGRQ SAKAELEKLV DHHPEGLSAR EAVKQAAKII 200
    YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI DFAQKEINGD 250
    DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE 288
    Length:288
    Mass (Da):31,536
    Last modified:January 23, 2007 - v2
    Checksum:i1E51D904CF336747
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55436 mRNA. Translation: AAA35227.1.
    Z75270 Genomic DNA. Translation: CAA99691.1.
    BK006948 Genomic DNA. Translation: DAA11123.1.
    PIRiS11182. SNBYC1.
    RefSeqiNP_015007.1. NM_001183782.1.

    Genome annotation databases

    EnsemblFungiiYOR362C; YOR362C; YOR362C.
    GeneIDi854544.
    KEGGisce:YOR362C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55436 mRNA. Translation: AAA35227.1 .
    Z75270 Genomic DNA. Translation: CAA99691.1 .
    BK006948 Genomic DNA. Translation: DAA11123.1 .
    PIRi S11182. SNBYC1.
    RefSeqi NP_015007.1. NM_001183782.1.

    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 G/U 2-288 [» ]
    1G0U X-ray 2.40 F/T 1-248 [» ]
    1G65 X-ray 2.25 F/T 5-248 [» ]
    1JD2 X-ray 3.00 1/F 5-248 [» ]
    1RYP X-ray 1.90 G/U 5-248 [» ]
    1VSY X-ray 3.00 G/U 5-248 [» ]
    1Z7Q X-ray 3.22 G/U 1-288 [» ]
    2F16 X-ray 2.80 F/T 5-248 [» ]
    2FAK X-ray 2.80 F/T 5-248 [» ]
    2GPL X-ray 2.81 F/T 5-248 [» ]
    2ZCY X-ray 2.90 F/T 2-288 [» ]
    3BDM X-ray 2.70 F/T 2-288 [» ]
    3D29 X-ray 2.60 F/T 5-248 [» ]
    3DY3 X-ray 2.81 F/T 5-248 [» ]
    3DY4 X-ray 2.80 F/T 5-248 [» ]
    3E47 X-ray 3.00 F/T 5-248 [» ]
    3GPJ X-ray 2.70 F/T 5-248 [» ]
    3GPT X-ray 2.41 F/T 5-248 [» ]
    3GPW X-ray 2.50 F/T 5-248 [» ]
    3HYE X-ray 2.50 F/T 5-248 [» ]
    3L5Q X-ray 3.00 L/X 5-248 [» ]
    3MG0 X-ray 2.68 F/T 5-248 [» ]
    3MG4 X-ray 3.11 F/T 5-248 [» ]
    3MG6 X-ray 2.60 F/T 1-248 [» ]
    3MG7 X-ray 2.78 F/T 1-248 [» ]
    3MG8 X-ray 2.59 F/T 1-248 [» ]
    3NZJ X-ray 2.40 F/T 1-288 [» ]
    3NZW X-ray 2.50 F/T 1-288 [» ]
    3NZX X-ray 2.70 F/T 1-288 [» ]
    3OEU X-ray 2.60 F/T 7-248 [» ]
    3OEV X-ray 2.85 F/T 7-248 [» ]
    3OKJ X-ray 2.70 F/T 5-248 [» ]
    3SDI X-ray 2.65 F/T 7-248 [» ]
    3SDK X-ray 2.70 F/T 7-248 [» ]
    3SHJ X-ray 2.80 F/T 5-248 [» ]
    3TDD X-ray 2.70 F/T 5-248 [» ]
    3UN4 X-ray 3.40 F/T 1-288 [» ]
    3UN8 X-ray 2.70 F/T 1-288 [» ]
    4CR2 electron microscopy 7.70 G 1-288 [» ]
    4CR3 electron microscopy 9.30 G 1-288 [» ]
    4CR4 electron microscopy 8.80 G 1-288 [» ]
    4EU2 X-ray 2.51 G/U 5-248 [» ]
    4FZC X-ray 2.80 F/T 5-248 [» ]
    4FZG X-ray 3.00 F/T 5-248 [» ]
    4G4S X-ray 2.49 G 1-288 [» ]
    4GK7 X-ray 2.80 F/T 5-248 [» ]
    4HNP X-ray 2.80 F/T 5-248 [» ]
    4HRC X-ray 2.80 F/T 5-248 [» ]
    4HRD X-ray 2.80 F/T 5-248 [» ]
    4INR X-ray 2.70 F/T 1-288 [» ]
    4INT X-ray 2.90 F/T 1-288 [» ]
    4INU X-ray 3.10 F/T 1-288 [» ]
    4J70 X-ray 2.80 F/T 1-288 [» ]
    4JSQ X-ray 2.80 F/T 1-288 [» ]
    4JSU X-ray 2.90 F/T 1-288 [» ]
    4JT0 X-ray 3.10 F/T 1-288 [» ]
    4LQI X-ray 2.70 F/T 5-248 [» ]
    4NNN X-ray 2.50 F/T 1-288 [» ]
    4NNW X-ray 2.60 F/T 1-288 [» ]
    4NO1 X-ray 2.50 F/T 1-288 [» ]
    4NO6 X-ray 3.00 F/T 1-288 [» ]
    4NO8 X-ray 2.70 F/T 1-288 [» ]
    4NO9 X-ray 2.90 F/T 1-288 [» ]
    4QBY X-ray 3.00 F/T 1-288 [» ]
    ProteinModelPortali P21242.
    SMRi P21242. Positions 5-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34747. 92 interactions.
    DIPi DIP-1526N.
    IntActi P21242. 29 interactions.
    MINTi MINT-411846.
    STRINGi 4932.YOR362C.

    Proteomic databases

    MaxQBi P21242.
    PaxDbi P21242.
    PeptideAtlasi P21242.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR362C ; YOR362C ; YOR362C .
    GeneIDi 854544.
    KEGGi sce:YOR362C.

    Organism-specific databases

    SGDi S000005889. PRE10.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074912.
    HOGENOMi HOG000091086.
    KOi K02727.
    OMAi VPDGRHF.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33832-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 P21242.
    NextBioi 976955.
    PROi P21242.

    Gene expression databases

    Genevestigatori P21242.

    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. "Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits."
      Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A.
      J. Biol. Chem. 265:16604-16613(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 106-135; 180-195 AND 200-209, CLEAVAGE OF INITIATOR METHIONINE.
    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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "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].
    6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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 5-248 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 1-288 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-248 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 5-248 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 5-248 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 5-248 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 5-248 IN COMPLEX WITH THE PROTEASOME.
    14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA7_YEAST
    AccessioniPrimary (citable) accession number: P21242
    Secondary accession number(s): D6W357
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 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 12000 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