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P23639

- PSA2_YEAST

UniProt

P23639 - PSA2_YEAST

Protein

Proteasome subunit alpha type-2

Gene

PRE8

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 1 (01 Nov 1991)
      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. 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-32677-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-2 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit Y7
    Multicatalytic endopeptidase complex subunit Y7
    Proteasome component Y7
    Proteinase YSCE subunit 7
    Gene namesi
    Name:PRE8
    Synonyms:PRS4
    Ordered Locus Names:YML092C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML092c.
    SGDiS000004557. PRE8.

    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
    Chaini1 – 250250Proteasome subunit alpha type-2PRO_0000124090Add
    BLAST

    Proteomic databases

    MaxQBiP23639.
    PaxDbiP23639.
    PeptideAtlasiP23639.

    Expressioni

    Gene expression databases

    GenevestigatoriP23639.

    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
    PRE9P236384EBI-13959,EBI-13967
    SCL1P212436EBI-13959,EBI-13975

    Protein-protein interaction databases

    BioGridi35051. 54 interactions.
    DIPiDIP-2822N.
    IntActiP23639. 21 interactions.
    MINTiMINT-475016.
    STRINGi4932.YML092C.

    Structurei

    Secondary structure

    1
    250
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Turni14 – 163
    Helixi19 – 2911
    Beta strandi34 – 396
    Beta strandi42 – 487
    Beta strandi54 – 563
    Helixi58 – 603
    Beta strandi63 – 686
    Beta strandi71 – 777
    Helixi79 – 9517
    Helixi98 – 1014
    Helixi107 – 12014
    Turni121 – 1233
    Beta strandi132 – 1409
    Turni141 – 1433
    Beta strandi144 – 1507
    Beta strandi156 – 16510
    Helixi168 – 17811
    Helixi185 – 19915
    Turni206 – 2083
    Beta strandi209 – 2146
    Helixi219 – 2213
    Beta strandi223 – 2264
    Beta strandi234 – 2374
    Helixi240 – 2478

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20B/P1-250[»]
    1G0UX-ray2.40A/O1-250[»]
    1G65X-ray2.25A/O1-250[»]
    1JD2X-ray3.00A/V1-250[»]
    1RYPX-ray1.90B/P1-250[»]
    1VSYX-ray3.00B/P20-250[»]
    1Z7QX-ray3.22B/P1-250[»]
    2F16X-ray2.80A/O1-250[»]
    2FAKX-ray2.80A/O1-250[»]
    2GPLX-ray2.81A/O1-250[»]
    2ZCYX-ray2.90A/O1-250[»]
    3BDMX-ray2.70A/O1-250[»]
    3D29X-ray2.60A/O1-250[»]
    3DY3X-ray2.81A/O1-250[»]
    3DY4X-ray2.80A/O1-250[»]
    3E47X-ray3.00A/O1-250[»]
    3GPJX-ray2.70A/O1-250[»]
    3GPTX-ray2.41A/O1-250[»]
    3GPWX-ray2.50A/O1-250[»]
    3HYEX-ray2.50A/O1-250[»]
    3L5QX-ray3.00G/S20-250[»]
    3MG0X-ray2.68A/O1-250[»]
    3MG4X-ray3.11A/O1-250[»]
    3MG6X-ray2.60A/O1-250[»]
    3MG7X-ray2.78A/O1-250[»]
    3MG8X-ray2.59A/O1-250[»]
    3NZJX-ray2.40A/O1-250[»]
    3NZWX-ray2.50A/O1-250[»]
    3NZXX-ray2.70A/O1-250[»]
    3OEUX-ray2.60A/O1-250[»]
    3OEVX-ray2.85A/O1-250[»]
    3OKJX-ray2.70A/O1-250[»]
    3SDIX-ray2.65A/O1-250[»]
    3SDKX-ray2.70A/O1-250[»]
    3SHJX-ray2.80A/O1-250[»]
    3TDDX-ray2.70A/O1-250[»]
    3UN4X-ray3.40A/O1-250[»]
    3UN8X-ray2.70A/O1-250[»]
    4CR2electron microscopy7.70B1-250[»]
    4CR3electron microscopy9.30B1-250[»]
    4CR4electron microscopy8.80B1-250[»]
    4EU2X-ray2.51B/P1-250[»]
    4FZCX-ray2.80A/O1-250[»]
    4FZGX-ray3.00A/O1-250[»]
    4G4SX-ray2.49B1-250[»]
    4GK7X-ray2.80A/O1-250[»]
    4HNPX-ray2.80A/O1-250[»]
    4HRCX-ray2.80A/O2-250[»]
    4HRDX-ray2.80A/O1-250[»]
    4INRX-ray2.70A/O1-250[»]
    4INTX-ray2.90A/O1-250[»]
    4INUX-ray3.10A/O1-250[»]
    4J70X-ray2.80A/O1-250[»]
    4JSQX-ray2.80A/O1-250[»]
    4JSUX-ray2.90A/O1-250[»]
    4JT0X-ray3.10A/O1-250[»]
    4LQIX-ray2.70A/O1-250[»]
    4NNNX-ray2.50A/O1-250[»]
    4NNWX-ray2.60A/O1-250[»]
    4NO1X-ray2.50A/O1-250[»]
    4NO6X-ray3.00A/O1-250[»]
    4NO8X-ray2.70A/O1-250[»]
    4NO9X-ray2.90A/O1-250[»]
    4QBYX-ray3.00A/O1-250[»]
    ProteinModelPortaliP23639.
    SMRiP23639. Positions 1-250.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23639.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074870.
    HOGENOMiHOG000091085.
    KOiK02726.
    OMAiWKATALG.
    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.

    P23639-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDRYSFSLT TFSPSGKLGQ IDYALTAVKQ GVTSLGIKAT NGVVIATEKK    50
    SSSPLAMSET LSKVSLLTPD IGAVYSGMGP DYRVLVDKSR KVAHTSYKRI 100
    YGEYPPTKLL VSEVAKIMQE ATQSGGVRPF GVSLLIAGHD EFNGFSLYQV 150
    DPSGSYFPWK ATAIGKGSVA AKTFLEKRWN DELELEDAIH IALLTLKESV 200
    EGEFNGDTIE LAIIGDENPD LLGYTGIPTD KGPRFRKLTS QEINDRLEAL 250
    Length:250
    Mass (Da):27,162
    Last modified:November 1, 1991 - v1
    Checksum:i12D7DFB1AA10E9FE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56731 Genomic DNA. Translation: CAA40055.1.
    Z46660 Genomic DNA. Translation: CAA86646.1.
    AY557762 Genomic DNA. Translation: AAS56088.1.
    BK006946 Genomic DNA. Translation: DAA09807.1.
    PIRiS12938. SNBYY7.
    RefSeqiNP_013618.1. NM_001182451.1.

    Genome annotation databases

    EnsemblFungiiYML092C; YML092C; YML092C.
    GeneIDi854882.
    KEGGisce:YML092C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56731 Genomic DNA. Translation: CAA40055.1 .
    Z46660 Genomic DNA. Translation: CAA86646.1 .
    AY557762 Genomic DNA. Translation: AAS56088.1 .
    BK006946 Genomic DNA. Translation: DAA09807.1 .
    PIRi S12938. SNBYY7.
    RefSeqi NP_013618.1. NM_001182451.1.

    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 B/P 1-250 [» ]
    1G0U X-ray 2.40 A/O 1-250 [» ]
    1G65 X-ray 2.25 A/O 1-250 [» ]
    1JD2 X-ray 3.00 A/V 1-250 [» ]
    1RYP X-ray 1.90 B/P 1-250 [» ]
    1VSY X-ray 3.00 B/P 20-250 [» ]
    1Z7Q X-ray 3.22 B/P 1-250 [» ]
    2F16 X-ray 2.80 A/O 1-250 [» ]
    2FAK X-ray 2.80 A/O 1-250 [» ]
    2GPL X-ray 2.81 A/O 1-250 [» ]
    2ZCY X-ray 2.90 A/O 1-250 [» ]
    3BDM X-ray 2.70 A/O 1-250 [» ]
    3D29 X-ray 2.60 A/O 1-250 [» ]
    3DY3 X-ray 2.81 A/O 1-250 [» ]
    3DY4 X-ray 2.80 A/O 1-250 [» ]
    3E47 X-ray 3.00 A/O 1-250 [» ]
    3GPJ X-ray 2.70 A/O 1-250 [» ]
    3GPT X-ray 2.41 A/O 1-250 [» ]
    3GPW X-ray 2.50 A/O 1-250 [» ]
    3HYE X-ray 2.50 A/O 1-250 [» ]
    3L5Q X-ray 3.00 G/S 20-250 [» ]
    3MG0 X-ray 2.68 A/O 1-250 [» ]
    3MG4 X-ray 3.11 A/O 1-250 [» ]
    3MG6 X-ray 2.60 A/O 1-250 [» ]
    3MG7 X-ray 2.78 A/O 1-250 [» ]
    3MG8 X-ray 2.59 A/O 1-250 [» ]
    3NZJ X-ray 2.40 A/O 1-250 [» ]
    3NZW X-ray 2.50 A/O 1-250 [» ]
    3NZX X-ray 2.70 A/O 1-250 [» ]
    3OEU X-ray 2.60 A/O 1-250 [» ]
    3OEV X-ray 2.85 A/O 1-250 [» ]
    3OKJ X-ray 2.70 A/O 1-250 [» ]
    3SDI X-ray 2.65 A/O 1-250 [» ]
    3SDK X-ray 2.70 A/O 1-250 [» ]
    3SHJ X-ray 2.80 A/O 1-250 [» ]
    3TDD X-ray 2.70 A/O 1-250 [» ]
    3UN4 X-ray 3.40 A/O 1-250 [» ]
    3UN8 X-ray 2.70 A/O 1-250 [» ]
    4CR2 electron microscopy 7.70 B 1-250 [» ]
    4CR3 electron microscopy 9.30 B 1-250 [» ]
    4CR4 electron microscopy 8.80 B 1-250 [» ]
    4EU2 X-ray 2.51 B/P 1-250 [» ]
    4FZC X-ray 2.80 A/O 1-250 [» ]
    4FZG X-ray 3.00 A/O 1-250 [» ]
    4G4S X-ray 2.49 B 1-250 [» ]
    4GK7 X-ray 2.80 A/O 1-250 [» ]
    4HNP X-ray 2.80 A/O 1-250 [» ]
    4HRC X-ray 2.80 A/O 2-250 [» ]
    4HRD X-ray 2.80 A/O 1-250 [» ]
    4INR X-ray 2.70 A/O 1-250 [» ]
    4INT X-ray 2.90 A/O 1-250 [» ]
    4INU X-ray 3.10 A/O 1-250 [» ]
    4J70 X-ray 2.80 A/O 1-250 [» ]
    4JSQ X-ray 2.80 A/O 1-250 [» ]
    4JSU X-ray 2.90 A/O 1-250 [» ]
    4JT0 X-ray 3.10 A/O 1-250 [» ]
    4LQI X-ray 2.70 A/O 1-250 [» ]
    4NNN X-ray 2.50 A/O 1-250 [» ]
    4NNW X-ray 2.60 A/O 1-250 [» ]
    4NO1 X-ray 2.50 A/O 1-250 [» ]
    4NO6 X-ray 3.00 A/O 1-250 [» ]
    4NO8 X-ray 2.70 A/O 1-250 [» ]
    4NO9 X-ray 2.90 A/O 1-250 [» ]
    4QBY X-ray 3.00 A/O 1-250 [» ]
    ProteinModelPortali P23639.
    SMRi P23639. Positions 1-250.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35051. 54 interactions.
    DIPi DIP-2822N.
    IntActi P23639. 21 interactions.
    MINTi MINT-475016.
    STRINGi 4932.YML092C.

    Proteomic databases

    MaxQBi P23639.
    PaxDbi P23639.
    PeptideAtlasi P23639.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML092C ; YML092C ; YML092C .
    GeneIDi 854882.
    KEGGi sce:YML092C.

    Organism-specific databases

    CYGDi YML092c.
    SGDi S000004557. PRE8.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074870.
    HOGENOMi HOG000091085.
    KOi K02726.
    OMAi WKATALG.
    OrthoDBi EOG7SBP0C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32677-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 P23639.
    NextBioi 977831.
    PROi P23639.

    Gene expression databases

    Genevestigatori P23639.

    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 and functional analysis of three subunits of yeast proteasome."
      Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
      Mol. Cell. Biol. 11:344-353(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 26786 / X2180-1A.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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].
    7. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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 COMPLEX WITH THE 20S PROTEASOME.
    9. "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 AND A 11S REGULATORY COMPLEX.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
    11. "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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
    12. "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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
    13. "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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
    14. "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 20-250 IN COMPLEX WITH THE PROTEASOME.
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSA2_YEAST
    AccessioniPrimary (citable) accession number: P23639
    Secondary accession number(s): D6W0J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 158 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 7060 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3