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P30657

- PSB7_YEAST

UniProt

P30657 - PSB7_YEAST

Protein

Proteasome subunit beta type-7

Gene

PRE4

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 Apr 1993)
      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. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.1 Publication

    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 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-30496-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

    MEROPSiT01.987.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-7 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PRE4
    Multicatalytic endopeptidase complex subunit PRE4
    Proteasome component PRE4
    Proteinase YSCE subunit PRE4
    Gene namesi
    Name:PRE4
    Ordered Locus Names:YFR050C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VI

    Organism-specific databases

    CYGDiYFR050c.
    SGDiS000001946. PRE4.

    Subcellular locationi

    Cytoplasm 1 PublicationPROSITE-ProRule annotation. Nucleus 1 Publication

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 3333PRO_0000331490Add
    BLAST
    Chaini34 – 266233Proteasome subunit beta type-7PRO_0000148073Add
    BLAST

    Proteomic databases

    MaxQBiP30657.
    PaxDbiP30657.
    PeptideAtlasiP30657.

    Expressioni

    Gene expression databases

    GenevestigatoriP30657.

    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 CIC1.3 Publications

    Protein-protein interaction databases

    BioGridi31208. 74 interactions.
    DIPiDIP-2807N.
    IntActiP30657. 20 interactions.
    MINTiMINT-592513.
    STRINGi4932.YFR050C.

    Structurei

    Secondary structure

    1
    266
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 413
    Beta strandi44 – 496
    Beta strandi52 – 587
    Beta strandi61 – 633
    Beta strandi66 – 705
    Beta strandi75 – 784
    Turni79 – 813
    Beta strandi82 – 898
    Helixi90 – 10819
    Turni112 – 1187
    Helixi122 – 13817
    Beta strandi145 – 1528
    Beta strandi158 – 1647
    Beta strandi169 – 1713
    Beta strandi173 – 1764
    Helixi179 – 18810
    Turni189 – 1913
    Beta strandi192 – 1943
    Helixi195 – 2006
    Helixi203 – 22018
    Beta strandi226 – 2349
    Turni235 – 2373
    Beta strandi238 – 2469
    Helixi253 – 2575
    Beta strandi260 – 2634

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20N/b34-265[»]
    1G0UX-ray2.401/M1-266[»]
    1G65X-ray2.251/M34-266[»]
    1JD2X-ray3.00M/T34-266[»]
    1RYPX-ray1.902/N34-266[»]
    1VSYX-ray3.002/N34-266[»]
    1Z7QX-ray3.22N/b34-266[»]
    2F16X-ray2.801/M34-266[»]
    2FAKX-ray2.801/M34-266[»]
    2GPLX-ray2.811/M34-266[»]
    2ZCYX-ray2.900/M1-266[»]
    3BDMX-ray2.700/M1-266[»]
    3D29X-ray2.601/M34-266[»]
    3DY3X-ray2.811/M34-266[»]
    3DY4X-ray2.801/M34-266[»]
    3E47X-ray3.001/M34-266[»]
    3GPJX-ray2.701/M34-266[»]
    3GPTX-ray2.411/M34-266[»]
    3GPWX-ray2.501/M34-266[»]
    3HYEX-ray2.501/M34-266[»]
    3L5QX-ray3.004/R34-266[»]
    3MG0X-ray2.681/M34-266[»]
    3MG4X-ray3.111/M34-266[»]
    3MG6X-ray2.601/M1-266[»]
    3MG7X-ray2.781/M1-266[»]
    3MG8X-ray2.591/M1-266[»]
    3NZJX-ray2.401/M1-266[»]
    3NZWX-ray2.501/M1-266[»]
    3NZXX-ray2.701/M1-266[»]
    3OEUX-ray2.601/M34-266[»]
    3OEVX-ray2.851/M34-266[»]
    3OKJX-ray2.701/M34-266[»]
    3SDIX-ray2.651/M34-253[»]
    3SDKX-ray2.701/M34-266[»]
    3SHJX-ray2.801/M34-266[»]
    3TDDX-ray2.701/M34-266[»]
    3UN4X-ray3.40M/a34-266[»]
    3UN8X-ray2.70M/a34-266[»]
    4CR2electron microscopy7.7071-266[»]
    4CR3electron microscopy9.3071-266[»]
    4CR4electron microscopy8.8071-266[»]
    4EU2X-ray2.512/N34-266[»]
    4FZCX-ray2.80M/a34-266[»]
    4FZGX-ray3.00M/a34-266[»]
    4G4SX-ray2.49N34-266[»]
    4GK7X-ray2.80M/a34-266[»]
    4HNPX-ray2.80M/a34-266[»]
    4HRCX-ray2.80M/a34-266[»]
    4HRDX-ray2.80M/a34-266[»]
    4INRX-ray2.70M/a34-266[»]
    4INTX-ray2.90M/a34-266[»]
    4INUX-ray3.10M/a34-266[»]
    4J70X-ray2.80M/a34-266[»]
    4JSQX-ray2.80M/a34-266[»]
    4JSUX-ray2.90M/a34-266[»]
    4JT0X-ray3.10M/a34-266[»]
    4LQIX-ray2.70M/a34-266[»]
    4NNNX-ray2.50M/a21-266[»]
    4NNWX-ray2.60M/a21-266[»]
    4NO1X-ray2.50M/a21-266[»]
    4NO6X-ray3.00M/a21-266[»]
    4NO8X-ray2.70M/a21-266[»]
    4NO9X-ray2.90M/a21-266[»]
    4QBYX-ray3.00M/a21-266[»]
    ProteinModelPortaliP30657.
    SMRiP30657. Positions 34-266.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30657.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00390000000698.
    HOGENOMiHOG000181719.
    KOiK02736.
    OMAiYHASTIA.
    OrthoDBiEOG73BVQ8.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
    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.

    P30657-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNHDPFSWGR PADSTYGAYN TQIANAGASP MVNTQQPIVT GTSVISMKYD    50
    NGVIIAADNL GSYGSLLRFN GVERLIPVGD NTVVGISGDI SDMQHIERLL 100
    KDLVTENAYD NPLADAEEAL EPSYIFEYLA TVMYQRRSKM NPLWNAIIVA 150
    GVQSNGDQFL RYVNLLGVTY SSPTLATGFG AHMANPLLRK VVDRESDIPK 200
    TTVQVAEEAI VNAMRVLYYR DARSSRNFSL AIIDKNTGLT FKKNLQVENM 250
    KWDFAKDIKG YGTQKI 266
    Length:266
    Mass (Da):29,443
    Last modified:April 1, 1993 - v1
    Checksum:iE585BB3B5D0C8E2C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881L → V in AAT92966. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68663 Genomic DNA. Translation: CAA48629.1.
    D50617 Genomic DNA. Translation: BAA09289.1.
    AY692947 Genomic DNA. Translation: AAT92966.1.
    BK006940 Genomic DNA. Translation: DAA12493.1.
    PIRiA46610.
    RefSeqiNP_116708.1. NM_001180015.1.

    Genome annotation databases

    EnsemblFungiiYFR050C; YFR050C; YFR050C.
    GeneIDi850611.
    KEGGisce:YFR050C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68663 Genomic DNA. Translation: CAA48629.1 .
    D50617 Genomic DNA. Translation: BAA09289.1 .
    AY692947 Genomic DNA. Translation: AAT92966.1 .
    BK006940 Genomic DNA. Translation: DAA12493.1 .
    PIRi A46610.
    RefSeqi NP_116708.1. NM_001180015.1.

    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 N/b 34-265 [» ]
    1G0U X-ray 2.40 1/M 1-266 [» ]
    1G65 X-ray 2.25 1/M 34-266 [» ]
    1JD2 X-ray 3.00 M/T 34-266 [» ]
    1RYP X-ray 1.90 2/N 34-266 [» ]
    1VSY X-ray 3.00 2/N 34-266 [» ]
    1Z7Q X-ray 3.22 N/b 34-266 [» ]
    2F16 X-ray 2.80 1/M 34-266 [» ]
    2FAK X-ray 2.80 1/M 34-266 [» ]
    2GPL X-ray 2.81 1/M 34-266 [» ]
    2ZCY X-ray 2.90 0/M 1-266 [» ]
    3BDM X-ray 2.70 0/M 1-266 [» ]
    3D29 X-ray 2.60 1/M 34-266 [» ]
    3DY3 X-ray 2.81 1/M 34-266 [» ]
    3DY4 X-ray 2.80 1/M 34-266 [» ]
    3E47 X-ray 3.00 1/M 34-266 [» ]
    3GPJ X-ray 2.70 1/M 34-266 [» ]
    3GPT X-ray 2.41 1/M 34-266 [» ]
    3GPW X-ray 2.50 1/M 34-266 [» ]
    3HYE X-ray 2.50 1/M 34-266 [» ]
    3L5Q X-ray 3.00 4/R 34-266 [» ]
    3MG0 X-ray 2.68 1/M 34-266 [» ]
    3MG4 X-ray 3.11 1/M 34-266 [» ]
    3MG6 X-ray 2.60 1/M 1-266 [» ]
    3MG7 X-ray 2.78 1/M 1-266 [» ]
    3MG8 X-ray 2.59 1/M 1-266 [» ]
    3NZJ X-ray 2.40 1/M 1-266 [» ]
    3NZW X-ray 2.50 1/M 1-266 [» ]
    3NZX X-ray 2.70 1/M 1-266 [» ]
    3OEU X-ray 2.60 1/M 34-266 [» ]
    3OEV X-ray 2.85 1/M 34-266 [» ]
    3OKJ X-ray 2.70 1/M 34-266 [» ]
    3SDI X-ray 2.65 1/M 34-253 [» ]
    3SDK X-ray 2.70 1/M 34-266 [» ]
    3SHJ X-ray 2.80 1/M 34-266 [» ]
    3TDD X-ray 2.70 1/M 34-266 [» ]
    3UN4 X-ray 3.40 M/a 34-266 [» ]
    3UN8 X-ray 2.70 M/a 34-266 [» ]
    4CR2 electron microscopy 7.70 7 1-266 [» ]
    4CR3 electron microscopy 9.30 7 1-266 [» ]
    4CR4 electron microscopy 8.80 7 1-266 [» ]
    4EU2 X-ray 2.51 2/N 34-266 [» ]
    4FZC X-ray 2.80 M/a 34-266 [» ]
    4FZG X-ray 3.00 M/a 34-266 [» ]
    4G4S X-ray 2.49 N 34-266 [» ]
    4GK7 X-ray 2.80 M/a 34-266 [» ]
    4HNP X-ray 2.80 M/a 34-266 [» ]
    4HRC X-ray 2.80 M/a 34-266 [» ]
    4HRD X-ray 2.80 M/a 34-266 [» ]
    4INR X-ray 2.70 M/a 34-266 [» ]
    4INT X-ray 2.90 M/a 34-266 [» ]
    4INU X-ray 3.10 M/a 34-266 [» ]
    4J70 X-ray 2.80 M/a 34-266 [» ]
    4JSQ X-ray 2.80 M/a 34-266 [» ]
    4JSU X-ray 2.90 M/a 34-266 [» ]
    4JT0 X-ray 3.10 M/a 34-266 [» ]
    4LQI X-ray 2.70 M/a 34-266 [» ]
    4NNN X-ray 2.50 M/a 21-266 [» ]
    4NNW X-ray 2.60 M/a 21-266 [» ]
    4NO1 X-ray 2.50 M/a 21-266 [» ]
    4NO6 X-ray 3.00 M/a 21-266 [» ]
    4NO8 X-ray 2.70 M/a 21-266 [» ]
    4NO9 X-ray 2.90 M/a 21-266 [» ]
    4QBY X-ray 3.00 M/a 21-266 [» ]
    ProteinModelPortali P30657.
    SMRi P30657. Positions 34-266.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31208. 74 interactions.
    DIPi DIP-2807N.
    IntActi P30657. 20 interactions.
    MINTi MINT-592513.
    STRINGi 4932.YFR050C.

    Protein family/group databases

    MEROPSi T01.987.

    Proteomic databases

    MaxQBi P30657.
    PaxDbi P30657.
    PeptideAtlasi P30657.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YFR050C ; YFR050C ; YFR050C .
    GeneIDi 850611.
    KEGGi sce:YFR050C.

    Organism-specific databases

    CYGDi YFR050c.
    SGDi S000001946. PRE4.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00390000000698.
    HOGENOMi HOG000181719.
    KOi K02736.
    OMAi YHASTIA.
    OrthoDBi EOG73BVQ8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30496-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 P30657.
    NextBioi 966499.
    PROi P30657.

    Gene expression databases

    Genevestigatori P30657.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR016295. Proteasome_endopept_cplx_B.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The PRE4 gene codes for a subunit of the yeast proteasome necessary for peptidylglutamyl-peptide-hydrolyzing activity. Mutations link the proteasome to stress- and ubiquitin-dependent proteolysis."
      Hilt W., Enenkel C., Gruhler A., Singer T., Wolf D.H.
      J. Biol. Chem. 268:3479-3486(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    2. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
      Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
      Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "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.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [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 34-266 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING.
    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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
    12. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
    13. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
    14. "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 34-266 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
    15. "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 34-266 IN COMPLEX WITH THE PROTEASOME.
    16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSB7_YEAST
    AccessioniPrimary (citable) accession number: P30657
    Secondary accession number(s): D6VTT3, E9P8Z8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    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 16900 molecules/cell in log phase SD medium.1 Publication

    Caution

    It is uncertain whether Met-1 or Met-31 is the initiator.Curated

    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 VI
      Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

    External Data

    Dasty 3