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P25043

- PSB2_YEAST

UniProt

P25043 - PSB2_YEAST

Protein

Proteasome subunit beta type-2

Gene

PUP1

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 149 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei30 – 301Nucleophile1 Publication

    GO - Molecular functioni

    1. endopeptidase activity 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-33674-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

    MEROPSiT01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-2 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit PUP1
    Multicatalytic endopeptidase complex subunit PUP1
    Proteasome component PUP1
    Proteinase YSCE subunit PUP1
    Gene namesi
    Name:PUP1
    Ordered Locus Names:YOR157C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR157c.
    SGDiS000005683. PUP1.

    Subcellular locationi

    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 – 2929Removed in mature formPRO_0000026657Add
    BLAST
    Chaini30 – 261232Proteasome subunit beta type-2PRO_0000026658Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiP25043.
    PaxDbiP25043.
    PeptideAtlasiP25043.

    Expressioni

    Gene expression databases

    GenevestigatoriP25043.

    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
    PUP3P254513EBI-14009,EBI-13993

    Protein-protein interaction databases

    BioGridi34553. 56 interactions.
    DIPiDIP-2818N.
    IntActiP25043. 9 interactions.
    MINTiMINT-498378.
    STRINGi4932.YOR157C.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 376
    Beta strandi40 – 456
    Beta strandi49 – 513
    Beta strandi54 – 596
    Beta strandi63 – 675
    Beta strandi70 – 767
    Helixi78 – 9922
    Helixi105 – 11814
    Turni119 – 1213
    Beta strandi125 – 1339
    Beta strandi136 – 1427
    Turni144 – 1463
    Beta strandi148 – 1503
    Beta strandi152 – 1576
    Helixi160 – 17011
    Helixi177 – 19418
    Beta strandi202 – 2087
    Beta strandi213 – 2208
    Beta strandi241 – 2466

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20I/W30-261[»]
    1G0UX-ray2.40H/V30-251[»]
    1G65X-ray2.25H/V30-251[»]
    1JD2X-ray3.00H/O30-251[»]
    1RYPX-ray1.90I/W30-251[»]
    1VSYX-ray3.00I/W30-251[»]
    1Z7QX-ray3.22I/W30-251[»]
    2F16X-ray2.80H/V30-251[»]
    2FAKX-ray2.80H/V30-251[»]
    2GPLX-ray2.81H/V30-251[»]
    2ZCYX-ray2.90H/V30-261[»]
    3BDMX-ray2.70H/V30-261[»]
    3D29X-ray2.60H/V30-251[»]
    3DY3X-ray2.81H/V30-251[»]
    3DY4X-ray2.80H/V30-251[»]
    3E47X-ray3.00H/V30-251[»]
    3GPJX-ray2.70H/V30-251[»]
    3GPTX-ray2.41H/V30-251[»]
    3GPWX-ray2.50H/V30-251[»]
    3HYEX-ray2.50H/V30-251[»]
    3L5QX-ray3.00M/Y30-251[»]
    3MG0X-ray2.68H/V30-251[»]
    3MG4X-ray3.11H/V30-251[»]
    3MG6X-ray2.60H/V30-251[»]
    3MG7X-ray2.78H/V30-251[»]
    3MG8X-ray2.59H/V30-251[»]
    3NZJX-ray2.40H/V1-261[»]
    3NZWX-ray2.50H/V1-261[»]
    3NZXX-ray2.70H/V1-261[»]
    3OEUX-ray2.60H/V30-251[»]
    3OEVX-ray2.85H/V30-251[»]
    3OKJX-ray2.70H/V30-251[»]
    3SDIX-ray2.65H/V30-251[»]
    3SDKX-ray2.70H/V30-251[»]
    3SHJX-ray2.80H/V30-251[»]
    3TDDX-ray2.70H/V30-251[»]
    3UN4X-ray3.40H/V30-261[»]
    3UN8X-ray2.70H/V30-261[»]
    4CR2electron microscopy7.7021-261[»]
    4CR3electron microscopy9.3021-261[»]
    4CR4electron microscopy8.8021-261[»]
    4EU2X-ray2.51I/W30-251[»]
    4FZCX-ray2.80H/V30-251[»]
    4FZGX-ray3.00H/V30-251[»]
    4G4SX-ray2.49I30-261[»]
    4GK7X-ray2.80H/V30-251[»]
    4HNPX-ray2.80H/V30-251[»]
    4HRCX-ray2.80H/V30-251[»]
    4HRDX-ray2.80H/V30-251[»]
    4INRX-ray2.70H/V30-261[»]
    4INTX-ray2.90H/V30-261[»]
    4INUX-ray3.10H/V30-261[»]
    4J70X-ray2.80H/V30-261[»]
    4JSQX-ray2.80H/V30-261[»]
    4JSUX-ray2.90H/V30-261[»]
    4JT0X-ray3.10H/V30-261[»]
    4LQIX-ray2.70H/V30-251[»]
    4NNNX-ray2.50H/V30-261[»]
    4NNWX-ray2.60H/V30-261[»]
    4NO1X-ray2.50H/V30-261[»]
    4NO6X-ray3.00H/V30-261[»]
    4NO8X-ray2.70H/V30-261[»]
    4NO9X-ray2.90H/V30-261[»]
    4QBYX-ray3.00H/V30-261[»]
    ProteinModelPortaliP25043.
    SMRiP25043. Positions 30-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25043.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046533.
    HOGENOMiHOG000182856.
    KOiK02739.
    OMAiQIWCAGA.
    OrthoDBiEOG7TJ3V6.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF12465. Pr_beta_C. 1 hit.
    PF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    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.

    P25043-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGLSFDNYQ RNNFLAENSH TQPKATSTGT TIVGVKFNNG VVIAADTRST    50
    QGPIVADKNC AKLHRISPKI WCAGAGTAAD TEAVTQLIGS NIELHSLYTS 100
    REPRVVSALQ MLKQHLFKYQ GHIGAYLIVA GVDPTGSHLF SIHAHGSTDV 150
    GYYLSLGSGS LAAMAVLESH WKQDLTKEEA IKLASDAIQA GIWNDLGSGS 200
    NVDVCVMEIG KDAEYLRNYL TPNVREEKQK SYKFPRGTTA VLKESIVNIC 250
    DIQEEQVDIT A 261
    Length:261
    Mass (Da):28,268
    Last modified:May 1, 1992 - v1
    Checksum:i13A8F2B75584539A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61189 Genomic DNA. Translation: CAA43492.1.
    U55020 Genomic DNA. Translation: AAC49643.1.
    Z75065 Genomic DNA. Translation: CAA99363.1.
    BK006948 Genomic DNA. Translation: DAA10930.1.
    PIRiS26996.
    RefSeqiNP_014800.3. NM_001183576.3.

    Genome annotation databases

    EnsemblFungiiYOR157C; YOR157C; YOR157C.
    GeneIDi854328.
    KEGGisce:YOR157C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61189 Genomic DNA. Translation: CAA43492.1 .
    U55020 Genomic DNA. Translation: AAC49643.1 .
    Z75065 Genomic DNA. Translation: CAA99363.1 .
    BK006948 Genomic DNA. Translation: DAA10930.1 .
    PIRi S26996.
    RefSeqi NP_014800.3. NM_001183576.3.

    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 I/W 30-261 [» ]
    1G0U X-ray 2.40 H/V 30-251 [» ]
    1G65 X-ray 2.25 H/V 30-251 [» ]
    1JD2 X-ray 3.00 H/O 30-251 [» ]
    1RYP X-ray 1.90 I/W 30-251 [» ]
    1VSY X-ray 3.00 I/W 30-251 [» ]
    1Z7Q X-ray 3.22 I/W 30-251 [» ]
    2F16 X-ray 2.80 H/V 30-251 [» ]
    2FAK X-ray 2.80 H/V 30-251 [» ]
    2GPL X-ray 2.81 H/V 30-251 [» ]
    2ZCY X-ray 2.90 H/V 30-261 [» ]
    3BDM X-ray 2.70 H/V 30-261 [» ]
    3D29 X-ray 2.60 H/V 30-251 [» ]
    3DY3 X-ray 2.81 H/V 30-251 [» ]
    3DY4 X-ray 2.80 H/V 30-251 [» ]
    3E47 X-ray 3.00 H/V 30-251 [» ]
    3GPJ X-ray 2.70 H/V 30-251 [» ]
    3GPT X-ray 2.41 H/V 30-251 [» ]
    3GPW X-ray 2.50 H/V 30-251 [» ]
    3HYE X-ray 2.50 H/V 30-251 [» ]
    3L5Q X-ray 3.00 M/Y 30-251 [» ]
    3MG0 X-ray 2.68 H/V 30-251 [» ]
    3MG4 X-ray 3.11 H/V 30-251 [» ]
    3MG6 X-ray 2.60 H/V 30-251 [» ]
    3MG7 X-ray 2.78 H/V 30-251 [» ]
    3MG8 X-ray 2.59 H/V 30-251 [» ]
    3NZJ X-ray 2.40 H/V 1-261 [» ]
    3NZW X-ray 2.50 H/V 1-261 [» ]
    3NZX X-ray 2.70 H/V 1-261 [» ]
    3OEU X-ray 2.60 H/V 30-251 [» ]
    3OEV X-ray 2.85 H/V 30-251 [» ]
    3OKJ X-ray 2.70 H/V 30-251 [» ]
    3SDI X-ray 2.65 H/V 30-251 [» ]
    3SDK X-ray 2.70 H/V 30-251 [» ]
    3SHJ X-ray 2.80 H/V 30-251 [» ]
    3TDD X-ray 2.70 H/V 30-251 [» ]
    3UN4 X-ray 3.40 H/V 30-261 [» ]
    3UN8 X-ray 2.70 H/V 30-261 [» ]
    4CR2 electron microscopy 7.70 2 1-261 [» ]
    4CR3 electron microscopy 9.30 2 1-261 [» ]
    4CR4 electron microscopy 8.80 2 1-261 [» ]
    4EU2 X-ray 2.51 I/W 30-251 [» ]
    4FZC X-ray 2.80 H/V 30-251 [» ]
    4FZG X-ray 3.00 H/V 30-251 [» ]
    4G4S X-ray 2.49 I 30-261 [» ]
    4GK7 X-ray 2.80 H/V 30-251 [» ]
    4HNP X-ray 2.80 H/V 30-251 [» ]
    4HRC X-ray 2.80 H/V 30-251 [» ]
    4HRD X-ray 2.80 H/V 30-251 [» ]
    4INR X-ray 2.70 H/V 30-261 [» ]
    4INT X-ray 2.90 H/V 30-261 [» ]
    4INU X-ray 3.10 H/V 30-261 [» ]
    4J70 X-ray 2.80 H/V 30-261 [» ]
    4JSQ X-ray 2.80 H/V 30-261 [» ]
    4JSU X-ray 2.90 H/V 30-261 [» ]
    4JT0 X-ray 3.10 H/V 30-261 [» ]
    4LQI X-ray 2.70 H/V 30-251 [» ]
    4NNN X-ray 2.50 H/V 30-261 [» ]
    4NNW X-ray 2.60 H/V 30-261 [» ]
    4NO1 X-ray 2.50 H/V 30-261 [» ]
    4NO6 X-ray 3.00 H/V 30-261 [» ]
    4NO8 X-ray 2.70 H/V 30-261 [» ]
    4NO9 X-ray 2.90 H/V 30-261 [» ]
    4QBY X-ray 3.00 H/V 30-261 [» ]
    ProteinModelPortali P25043.
    SMRi P25043. Positions 30-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34553. 56 interactions.
    DIPi DIP-2818N.
    IntActi P25043. 9 interactions.
    MINTi MINT-498378.
    STRINGi 4932.YOR157C.

    Protein family/group databases

    MEROPSi T01.011.

    Proteomic databases

    MaxQBi P25043.
    PaxDbi P25043.
    PeptideAtlasi P25043.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR157C ; YOR157C ; YOR157C .
    GeneIDi 854328.
    KEGGi sce:YOR157C.

    Organism-specific databases

    CYGDi YOR157c.
    SGDi S000005683. PUP1.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046533.
    HOGENOMi HOG000182856.
    KOi K02739.
    OMAi QIWCAGA.
    OrthoDBi EOG7TJ3V6.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33674-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 P25043.
    NextBioi 976378.
    PROi P25043.

    Gene expression databases

    Genevestigatori P25043.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF12465. Pr_beta_C. 1 hit.
    PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of PUP1 encoding a putative proteasome subunit in Saccharomyces cerevisiae."
      Haffter P., Fox T.D.
      Nucleic Acids Res. 19:5075-5075(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae chromosome XV."
      Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.
      Yeast 13:73-83(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / FY1678.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. 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 30-251 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING, ACTIVE SITE.
    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 30-261 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) 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 30-251 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 30-251 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 30-251 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 30-251 IN COMPLEX WITH THE PROTEASOME.
    14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSB2_YEAST
    AccessioniPrimary (citable) accession number: P25043
    Secondary accession number(s): D6W2L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The side chain of Thr-30 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
    Present with 11400 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3