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P22141

- PSB4_YEAST

UniProt

P22141 - PSB4_YEAST

Protein

Proteasome subunit beta type-4

Gene

PRE1

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 157 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      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. This subunit has a chymotrypsin-like activity.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    GO - Molecular functioni

    1. endopeptidase activator activity Source: SGD
    2. protein binding Source: IntAct
    3. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. positive regulation of endopeptidase activity Source: GOC
    2. proteasomal ubiquitin-independent protein catabolic process 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-30199-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

    MEROPSiT01.984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-4 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C11
    Multicatalytic endopeptidase complex subunit C11
    Proteasome component C11
    Proteinase YSCE subunit 11
    Gene namesi
    Name:PRE1
    Ordered Locus Names:YER012W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER012w.
    SGDiS000000814. PRE1.

    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
    Chaini1 – 198198Proteasome subunit beta type-4PRO_0000148055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei76 – 761Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22141.
    PaxDbiP22141.
    PeptideAtlasiP22141.

    Expressioni

    Gene expression databases

    GenevestigatoriP22141.

    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
    PRE10P212423EBI-13988,EBI-13963
    PRE6P403033EBI-13988,EBI-13980
    RPT1P332992EBI-13988,EBI-13910

    Protein-protein interaction databases

    BioGridi36744. 134 interactions.
    DIPiDIP-2808N.
    IntActiP22141. 26 interactions.
    MINTiMINT-592869.
    STRINGi4932.YER012W.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi13 – 186
    Beta strandi21 – 233
    Beta strandi26 – 305
    Beta strandi35 – 395
    Beta strandi42 – 498
    Helixi50 – 7122
    Helixi77 – 9115
    Beta strandi94 – 963
    Beta strandi100 – 1089
    Turni109 – 1124
    Beta strandi113 – 1197
    Turni121 – 1233
    Beta strandi125 – 1273
    Beta strandi129 – 1324
    Helixi136 – 14712
    Helixi154 – 17118
    Beta strandi179 – 1857
    Beta strandi188 – 1925
    Turni194 – 1974

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FNTX-ray3.20K/Y1-198[»]
    1G0UX-ray2.40J/X1-198[»]
    1G65X-ray2.25J/X1-198[»]
    1JD2X-ray3.00J/Q1-198[»]
    1RYPX-ray1.90K/Y1-198[»]
    1VSYX-ray3.00K/Y1-198[»]
    1Z7QX-ray3.22K/Y1-198[»]
    2F16X-ray2.80J/X1-198[»]
    2FAKX-ray2.80J/X1-198[»]
    2GPLX-ray2.81J/X1-198[»]
    2ZCYX-ray2.90J/X1-198[»]
    3BDMX-ray2.70J/X1-198[»]
    3D29X-ray2.60J/X1-198[»]
    3DY3X-ray2.81J/X1-198[»]
    3DY4X-ray2.80J/X1-198[»]
    3E47X-ray3.00J/X1-198[»]
    3GPJX-ray2.70J/X1-198[»]
    3GPTX-ray2.41J/X1-198[»]
    3GPWX-ray2.50J/X1-198[»]
    3HYEX-ray2.50J/X1-198[»]
    3L5QX-ray3.001/O1-198[»]
    3MG0X-ray2.68J/X1-198[»]
    3MG4X-ray3.11J/X1-198[»]
    3MG6X-ray2.60J/X1-198[»]
    3MG7X-ray2.78J/X1-198[»]
    3MG8X-ray2.59J/X1-198[»]
    3NZJX-ray2.40J/X1-198[»]
    3NZWX-ray2.50J/X1-198[»]
    3NZXX-ray2.70J/X1-198[»]
    3OEUX-ray2.60J/X1-198[»]
    3OEVX-ray2.85J/X1-198[»]
    3OKJX-ray2.70J/X1-198[»]
    3SDIX-ray2.65J/X1-198[»]
    3SDKX-ray2.70J/X1-198[»]
    3SHJX-ray2.80J/X1-198[»]
    3TDDX-ray2.70J/X1-198[»]
    3UN4X-ray3.40J/X1-198[»]
    3UN8X-ray2.70J/X1-198[»]
    4CR2electron microscopy7.7041-198[»]
    4CR3electron microscopy9.3041-198[»]
    4CR4electron microscopy8.8041-198[»]
    4EU2X-ray2.51K/Y1-198[»]
    4FZCX-ray2.80J/X1-198[»]
    4FZGX-ray3.00J/X1-198[»]
    4G4SX-ray2.49K1-198[»]
    4GK7X-ray2.80J/X1-198[»]
    4HNPX-ray2.80J/X1-198[»]
    4HRCX-ray2.80J/X1-198[»]
    4HRDX-ray2.80J/X1-198[»]
    4INRX-ray2.70J/X1-198[»]
    4INTX-ray2.90J/X1-198[»]
    4INUX-ray3.10J/X1-198[»]
    4J70X-ray2.80J/X1-198[»]
    4JSQX-ray2.80J/X1-198[»]
    4JSUX-ray2.90J/X1-198[»]
    4JT0X-ray3.10J/X1-198[»]
    4LQIX-ray2.70J/X1-198[»]
    4NNNX-ray2.50J/X1-198[»]
    4NNWX-ray2.60J/X1-198[»]
    4NO1X-ray2.50J/X1-198[»]
    4NO6X-ray3.00J/X1-198[»]
    4NO8X-ray2.70J/X1-198[»]
    4NO9X-ray2.90J/X1-198[»]
    4QBYX-ray3.00J/X1-198[»]
    ProteinModelPortaliP22141.
    SMRiP22141. Positions 1-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22141.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00640000091536.
    HOGENOMiHOG000188743.
    KOiK02734.
    OMAiHFVRGEL.
    OrthoDBiEOG7SJDGT.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22141-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDIILGIRVQ DSVILASSKA VTRGISVLKD SDDKTRQLSP HTLMSFAGEA    50
    GDTVQFAEYI QANIQLYSIR EDYELSPQAV SSFVRQELAK SIRSRRPYQV 100
    NVLIGGYDKK KNKPELYQID YLGTKVELPY GAHGYSGFYT FSLLDHHYRP 150
    DMTTEEGLDL LKLCVQELEK RMPMDFKGVI VKIVDKDGIR QVDDFQAQ 198
    Length:198
    Mass (Da):22,517
    Last modified:February 1, 1995 - v2
    Checksum:iED43D319A5895B40
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti183 – 1831I → T(PubMed:2001673)Curated
    Sequence conflicti188 – 1881G → R(PubMed:2001673)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56812 Genomic DNA. Translation: CAA40149.1.
    U18778 Genomic DNA. Translation: AAB64545.1.
    AY557807 Genomic DNA. Translation: AAS56133.1.
    BK006939 Genomic DNA. Translation: DAA07663.1.
    PIRiS50470.
    RefSeqiNP_010928.1. NM_001178903.1.

    Genome annotation databases

    EnsemblFungiiYER012W; YER012W; YER012W.
    GeneIDi856731.
    KEGGisce:YER012W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56812 Genomic DNA. Translation: CAA40149.1 .
    U18778 Genomic DNA. Translation: AAB64545.1 .
    AY557807 Genomic DNA. Translation: AAS56133.1 .
    BK006939 Genomic DNA. Translation: DAA07663.1 .
    PIRi S50470.
    RefSeqi NP_010928.1. NM_001178903.1.

    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 K/Y 1-198 [» ]
    1G0U X-ray 2.40 J/X 1-198 [» ]
    1G65 X-ray 2.25 J/X 1-198 [» ]
    1JD2 X-ray 3.00 J/Q 1-198 [» ]
    1RYP X-ray 1.90 K/Y 1-198 [» ]
    1VSY X-ray 3.00 K/Y 1-198 [» ]
    1Z7Q X-ray 3.22 K/Y 1-198 [» ]
    2F16 X-ray 2.80 J/X 1-198 [» ]
    2FAK X-ray 2.80 J/X 1-198 [» ]
    2GPL X-ray 2.81 J/X 1-198 [» ]
    2ZCY X-ray 2.90 J/X 1-198 [» ]
    3BDM X-ray 2.70 J/X 1-198 [» ]
    3D29 X-ray 2.60 J/X 1-198 [» ]
    3DY3 X-ray 2.81 J/X 1-198 [» ]
    3DY4 X-ray 2.80 J/X 1-198 [» ]
    3E47 X-ray 3.00 J/X 1-198 [» ]
    3GPJ X-ray 2.70 J/X 1-198 [» ]
    3GPT X-ray 2.41 J/X 1-198 [» ]
    3GPW X-ray 2.50 J/X 1-198 [» ]
    3HYE X-ray 2.50 J/X 1-198 [» ]
    3L5Q X-ray 3.00 1/O 1-198 [» ]
    3MG0 X-ray 2.68 J/X 1-198 [» ]
    3MG4 X-ray 3.11 J/X 1-198 [» ]
    3MG6 X-ray 2.60 J/X 1-198 [» ]
    3MG7 X-ray 2.78 J/X 1-198 [» ]
    3MG8 X-ray 2.59 J/X 1-198 [» ]
    3NZJ X-ray 2.40 J/X 1-198 [» ]
    3NZW X-ray 2.50 J/X 1-198 [» ]
    3NZX X-ray 2.70 J/X 1-198 [» ]
    3OEU X-ray 2.60 J/X 1-198 [» ]
    3OEV X-ray 2.85 J/X 1-198 [» ]
    3OKJ X-ray 2.70 J/X 1-198 [» ]
    3SDI X-ray 2.65 J/X 1-198 [» ]
    3SDK X-ray 2.70 J/X 1-198 [» ]
    3SHJ X-ray 2.80 J/X 1-198 [» ]
    3TDD X-ray 2.70 J/X 1-198 [» ]
    3UN4 X-ray 3.40 J/X 1-198 [» ]
    3UN8 X-ray 2.70 J/X 1-198 [» ]
    4CR2 electron microscopy 7.70 4 1-198 [» ]
    4CR3 electron microscopy 9.30 4 1-198 [» ]
    4CR4 electron microscopy 8.80 4 1-198 [» ]
    4EU2 X-ray 2.51 K/Y 1-198 [» ]
    4FZC X-ray 2.80 J/X 1-198 [» ]
    4FZG X-ray 3.00 J/X 1-198 [» ]
    4G4S X-ray 2.49 K 1-198 [» ]
    4GK7 X-ray 2.80 J/X 1-198 [» ]
    4HNP X-ray 2.80 J/X 1-198 [» ]
    4HRC X-ray 2.80 J/X 1-198 [» ]
    4HRD X-ray 2.80 J/X 1-198 [» ]
    4INR X-ray 2.70 J/X 1-198 [» ]
    4INT X-ray 2.90 J/X 1-198 [» ]
    4INU X-ray 3.10 J/X 1-198 [» ]
    4J70 X-ray 2.80 J/X 1-198 [» ]
    4JSQ X-ray 2.80 J/X 1-198 [» ]
    4JSU X-ray 2.90 J/X 1-198 [» ]
    4JT0 X-ray 3.10 J/X 1-198 [» ]
    4LQI X-ray 2.70 J/X 1-198 [» ]
    4NNN X-ray 2.50 J/X 1-198 [» ]
    4NNW X-ray 2.60 J/X 1-198 [» ]
    4NO1 X-ray 2.50 J/X 1-198 [» ]
    4NO6 X-ray 3.00 J/X 1-198 [» ]
    4NO8 X-ray 2.70 J/X 1-198 [» ]
    4NO9 X-ray 2.90 J/X 1-198 [» ]
    4QBY X-ray 3.00 J/X 1-198 [» ]
    ProteinModelPortali P22141.
    SMRi P22141. Positions 1-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36744. 134 interactions.
    DIPi DIP-2808N.
    IntActi P22141. 26 interactions.
    MINTi MINT-592869.
    STRINGi 4932.YER012W.

    Chemistry

    BindingDBi P22141.
    ChEMBLi CHEMBL4206.

    Protein family/group databases

    MEROPSi T01.984.

    Proteomic databases

    MaxQBi P22141.
    PaxDbi P22141.
    PeptideAtlasi P22141.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER012W ; YER012W ; YER012W .
    GeneIDi 856731.
    KEGGi sce:YER012W.

    Organism-specific databases

    CYGDi YER012w.
    SGDi S000000814. PRE1.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00640000091536.
    HOGENOMi HOG000188743.
    KOi K02734.
    OMAi HFVRGEL.
    OrthoDBi EOG7SJDGT.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30199-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 P22141.
    NextBioi 982843.
    PROi P22141.

    Gene expression databases

    Genevestigatori P22141.

    Family and domain databases

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

    Publicationsi

    1. "Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival."
      Heinemeyer W., Kleinschmidt J.A., Saidowsky J., Escher C., Wolf D.H.
      EMBO J. 10:555-562(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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) IN COMPLEX WITH THE PROTEASOME.
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

    Entry informationi

    Entry nameiPSB4_YEAST
    AccessioniPrimary (citable) accession number: P22141
    Secondary accession number(s): D3DLQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 157 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 21800 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3