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P00445

- SODC_YEAST

UniProt

P00445 - SODC_YEAST

Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

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 174 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.

    Cofactori

    Binds 1 copper ion per subunit.
    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi43 – 431Zinc 2; shared with CCS1; in apo form2 Publications
    Metal bindingi47 – 471Copper; catalytic2 Publications
    Metal bindingi49 – 491Copper; catalytic2 Publications
    Metal bindingi64 – 641Copper; catalytic2 Publications
    Metal bindingi64 – 641Zinc 1; structural2 Publications
    Metal bindingi72 – 721Zinc 1; structural2 Publications
    Metal bindingi81 – 811Zinc 1; structural2 Publications
    Metal bindingi84 – 841Zinc 1; structural2 Publications
    Metal bindingi121 – 1211Copper; catalytic2 Publications
    Binding sitei144 – 1441SubstrateCurated

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. superoxide dismutase activity Source: SGD

    GO - Biological processi

    1. age-dependent response to reactive oxygen species involved in chronological cell aging Source: SGD
    2. cellular copper ion homeostasis Source: SGD
    3. cellular zinc ion homeostasis Source: SGD
    4. fungal-type cell wall organization Source: SGD
    5. negative regulation of cellular respiration Source: SGD
    6. positive regulation of sequence-specific DNA binding transcription factor activity Source: SGD
    7. positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: SGD
    8. protein stabilization Source: SGD
    9. removal of superoxide radicals Source: GOC
    10. superoxide metabolic process Source: SGD

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:MONOMER3O-1629.
    ReactomeiREACT_191152. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
    Gene namesi
    Name:SOD1
    Ordered Locus Names:YJR104C
    ORF Names:J1968
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    SGDiS000003865. SOD1.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion intermembrane space 1 Publication
    Note: A small percentage (around 1-5 percent) localizes to the mitochondrial intermembrane space.

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. mitochondrial intermembrane space Source: SGD
    3. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi123 – 1231G → K: Does not enable copper chaperone-independent activation. 1 Publication
    Mutagenesisi131 – 1322DT → GN: Does not enable copper chaperone-independent activation.
    Mutagenesisi143 – 1431P → A or S: Enables copper chaperone-independent activation; when associated with A-145 or with L-145. 2 Publications
    Mutagenesisi145 – 1451P → A or L: Enables copper chaperone-independent activation; when associated with A-143 or with S-143. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 154153Superoxide dismutase [Cu-Zn]PRO_0000164129Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki19 – 19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei26 – 261Phosphoserine1 Publication
    Modified residuei39 – 391Phosphoserine3 Publications
    Disulfide bondi58 ↔ 147
    Disulfide bondi58 – 58Interchain (with C-229 in CCS1); in linked form
    Cross-linki70 – 70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei99 – 991Phosphoserine3 Publications
    Modified residuei117 – 1171Phosphoserine1 Publication
    Modified residuei132 – 1321Phosphothreonine1 Publication
    Modified residuei138 – 1381Phosphothreonine1 Publication

    Keywords - PTMi

    Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP00445.
    PaxDbiP00445.
    PeptideAtlasiP00445.
    PRIDEiP00445.

    2D gel databases

    SWISS-2DPAGEP00445.

    Expressioni

    Gene expression databases

    GenevestigatoriP00445.

    Interactioni

    Subunit structurei

    Homodimer in holo form. In apo form, heterodimer with CCS1. Zinc-binding at 'His-16' of CCS1 and Glu-43 of apo-SOD1 is required for this heterodimerization.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCS1P402022EBI-17635,EBI-10287

    Protein-protein interaction databases

    BioGridi33860. 209 interactions.
    DIPiDIP-5859N.
    IntActiP00445. 4 interactions.
    MINTiMINT-429649.
    STRINGi4932.YJR104C.

    Structurei

    Secondary structure

    1
    154
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Beta strandi11 – 133
    Beta strandi15 – 217
    Beta strandi23 – 275
    Beta strandi29 – 379
    Beta strandi43 – 508
    Turni55 – 584
    Helixi59 – 613
    Beta strandi77 – 804
    Beta strandi84 – 896
    Beta strandi96 – 1049
    Beta strandi107 – 1093
    Beta strandi116 – 1205
    Beta strandi130 – 1323
    Helixi135 – 1384
    Beta strandi146 – 1494
    Beta strandi151 – 1533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B4LX-ray1.80A2-154[»]
    1B4TX-ray1.80A2-154[»]
    1F18X-ray1.70A1-154[»]
    1F1AX-ray1.80A1-154[»]
    1F1DX-ray2.10A1-154[»]
    1F1GX-ray1.35A/B/C/D/E/F1-154[»]
    1JCVX-ray1.55A2-154[»]
    1JK9X-ray2.90A/C2-154[»]
    1SDYX-ray2.50A/B/C/D2-154[»]
    1YAZX-ray1.70A2-154[»]
    1YSOX-ray1.73A2-154[»]
    2JCWX-ray1.70A2-154[»]
    ProteinModelPortaliP00445.
    SMRiP00445. Positions 2-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00445.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Phylogenomic databases

    eggNOGiCOG2032.
    GeneTreeiENSGT00530000063226.
    HOGENOMiHOG000263447.
    KOiK04565.
    OMAiTVNARIT.
    OrthoDBiEOG7HQNMC.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    PfamiPF00080. Sod_Cu. 1 hit.
    [Graphical view]
    PRINTSiPR00068. CUZNDISMTASE.
    SUPFAMiSSF49329. SSF49329. 1 hit.
    PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00445-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQAVAVLKG DAGVSGVVKF EQASESEPTT VSYEIAGNSP NAERGFHIHE    50
    FGDATNGCVS AGPHFNPFKK THGAPTDEVR HVGDMGNVKT DENGVAKGSF 100
    KDSLIKLIGP TSVVGRSVVI HAGQDDLGKG DTEESLKTGN AGPRPACGVI 150
    GLTN 154
    Length:154
    Mass (Da):15,855
    Last modified:January 23, 2007 - v2
    Checksum:iE263A74679AF11F7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561N → D AA sequence (PubMed:6993479)Curated
    Sequence conflicti93 – 931N → D AA sequence (PubMed:6993479)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03279 Genomic DNA. Translation: AAA34543.1.
    AY690619 Genomic DNA. Translation: AAT99430.1.
    Z49604 Genomic DNA. Translation: CAA89634.1.
    AY558073 Genomic DNA. Translation: AAS56399.1.
    BK006943 Genomic DNA. Translation: DAA08889.1.
    PIRiA36171. DSBYC.
    RefSeqiNP_012638.1. NM_001181762.1.

    Genome annotation databases

    EnsemblFungiiYJR104C; YJR104C; YJR104C.
    GeneIDi853568.
    KEGGisce:YJR104C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03279 Genomic DNA. Translation: AAA34543.1 .
    AY690619 Genomic DNA. Translation: AAT99430.1 .
    Z49604 Genomic DNA. Translation: CAA89634.1 .
    AY558073 Genomic DNA. Translation: AAS56399.1 .
    BK006943 Genomic DNA. Translation: DAA08889.1 .
    PIRi A36171. DSBYC.
    RefSeqi NP_012638.1. NM_001181762.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B4L X-ray 1.80 A 2-154 [» ]
    1B4T X-ray 1.80 A 2-154 [» ]
    1F18 X-ray 1.70 A 1-154 [» ]
    1F1A X-ray 1.80 A 1-154 [» ]
    1F1D X-ray 2.10 A 1-154 [» ]
    1F1G X-ray 1.35 A/B/C/D/E/F 1-154 [» ]
    1JCV X-ray 1.55 A 2-154 [» ]
    1JK9 X-ray 2.90 A/C 2-154 [» ]
    1SDY X-ray 2.50 A/B/C/D 2-154 [» ]
    1YAZ X-ray 1.70 A 2-154 [» ]
    1YSO X-ray 1.73 A 2-154 [» ]
    2JCW X-ray 1.70 A 2-154 [» ]
    ProteinModelPortali P00445.
    SMRi P00445. Positions 2-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33860. 209 interactions.
    DIPi DIP-5859N.
    IntActi P00445. 4 interactions.
    MINTi MINT-429649.
    STRINGi 4932.YJR104C.

    2D gel databases

    SWISS-2DPAGE P00445.

    Proteomic databases

    MaxQBi P00445.
    PaxDbi P00445.
    PeptideAtlasi P00445.
    PRIDEi P00445.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR104C ; YJR104C ; YJR104C .
    GeneIDi 853568.
    KEGGi sce:YJR104C.

    Organism-specific databases

    SGDi S000003865. SOD1.

    Phylogenomic databases

    eggNOGi COG2032.
    GeneTreei ENSGT00530000063226.
    HOGENOMi HOG000263447.
    KOi K04565.
    OMAi TVNARIT.
    OrthoDBi EOG7HQNMC.

    Enzyme and pathway databases

    BioCyci YEAST:MONOMER3O-1629.
    Reactomei REACT_191152. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    EvolutionaryTracei P00445.
    NextBioi 974334.
    PROi P00445.

    Gene expression databases

    Genevestigatori P00445.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    PRINTSi PR00068. CUZNDISMTASE.
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity."
      Bermingham-Mcdonogh O., Gralla E., Valentine J.
      Proc. Natl. Acad. Sci. U.S.A. 85:4789-4793(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and sequence analysis of copper, zinc-superoxide dismutase gene."
      Ping Y.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae."
      Johansen J.T., Overballe-Petersen C., Martin B., Hasemann V., Svendsen I.
      Carlsberg Res. Commun. 44:201-217(1979)
      Cited for: PROTEIN SEQUENCE OF 2-154.
    7. "The amino acid sequence of copper-zinc superoxide dismutase from bakers' yeast."
      Steinman H.M.
      J. Biol. Chem. 255:6758-6765(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-154.
    8. Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Strain: ATCC 26786 / X2180-1A.
    9. "A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage."
      Sturtz L.A., Diekert K., Jensen L.T., Lill R., Culotta V.C.
      J. Biol. Chem. 276:38084-38089(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses."
      Zhou W., Ryan J.J., Zhou H.
      J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-70.
    12. "Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone."
      Carroll M.C., Girouard J.B., Ulloa J.L., Subramaniam J.R., Wong P.C., Valentine J.S., Culotta V.C.
      Proc. Natl. Acad. Sci. U.S.A. 101:5964-5969(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-123; 131-ASP-THR-132; PRO-143 AND PRO-145.
    13. "Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS."
      Jensen L.T., Culotta V.C.
      J. Biol. Chem. 280:41373-41379(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-143 AND PRO-145.
    14. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    15. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-117 AND THR-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-26; SER-39 AND SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-99 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structure solution and molecular dynamics refinement of the yeast Cu,Zn enzyme superoxide dismutase."
      Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M., Marmocchi F., Rotilio G., Bolognesi M.
      Acta Crystallogr. B 47:918-927(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    19. "Crystal structure of yeast Cu,Zn superoxide dismutase. Crystallographic refinement at 2.5-A resolution."
      Djinovic K., Gatti G., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M., Marmocchi F., Rotilio G., Bolognesi M.
      J. Mol. Biol. 225:791-809(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    20. "Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase."
      Ogihara N.L., Parge H.E., Hart P.J., Weiss M.S., Goto J.J., Crane B.R., Tsang J., Slater K., Roe J.A., Valentine J.S., Eisenberg D., Tainer J.A.
      Biochemistry 35:2316-2321(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG; COPPER AND ZINC, DISULFIDE BONDS.
    22. "Heterodimeric structure of superoxide dismutase in complex with its metallochaperone."
      Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C.
      Nat. Struct. Biol. 8:751-755(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ZINC AND CCS1, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiSODC_YEAST
    AccessioniPrimary (citable) accession number: P00445
    Secondary accession number(s): D6VWS3, Q68HB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 174 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 519000 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. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3