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P22803

- TRX2_YEAST

UniProt

P22803 - TRX2_YEAST

Protein

Thioredoxin-2

Gene

TRX2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.9 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei25 – 251Deprotonates C-terminal active site Cys
    Active sitei31 – 311Nucleophile
    Sitei32 – 321Contributes to redox potential value
    Sitei33 – 331Contributes to redox potential value
    Active sitei34 – 341Nucleophile

    GO - Molecular functioni

    1. disulfide oxidoreductase activity Source: SGD
    2. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: SGD
    2. cellular response to oxidative stress Source: SGD
    3. deoxyribonucleotide biosynthetic process Source: UniProtKB-KW
    4. ER to Golgi vesicle-mediated transport Source: SGD
    5. glycerol ether metabolic process Source: InterPro
    6. protein deglutathionylation Source: SGD
    7. protein transport Source: UniProtKB-KW
    8. retrograde vesicle-mediated transport, Golgi to ER Source: SGD
    9. sulfate assimilation Source: SGD
    10. vacuole fusion, non-autophagic Source: SGD
    11. vacuole inheritance Source: SGD

    Keywords - Biological processi

    Deoxyribonucleotide synthesis, Electron transport, Protein transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30891-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin-2
    Alternative name(s):
    Thioredoxin II
    Short name:
    TR-II
    Thioredoxin-1
    Gene namesi
    Name:TRX2
    Synonyms:TRX1
    Ordered Locus Names:YGR209C
    ORF Names:G7746
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    SGDiS000003441. TRX2.

    Subcellular locationi

    Cytoplasm 1 Publication. Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. fungal-type vacuole Source: SGD
    3. Golgi membrane Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 104103Thioredoxin-2PRO_0000120045Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 34Redox-active1 PublicationPROSITE-ProRule annotation
    Modified residuei62 – 621Phosphoserine2 Publications

    Post-translational modificationi

    Reversible disulfide bond formation between Cys-31 and Cys-34, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP22803.
    PaxDbiP22803.
    PeptideAtlasiP22803.

    Expressioni

    Inductioni

    Strongly induced by hydrogen peroxide and diamide stress in a YAP1- and SKN7-dependent manner. Also induced by reducing stress by DTT.

    Gene expression databases

    GenevestigatoriP22803.

    Interactioni

    Subunit structurei

    Monomer. Part of the heterodimeric LMA1 complex together with the proteinase inhibitor PBI2. LMA1 binds to the ATPase SEC18.3 Publications

    Protein-protein interaction databases

    BioGridi33462. 43 interactions.
    DIPiDIP-5552N.
    IntActiP22803. 9 interactions.
    MINTiMINT-474704.
    STRINGi4932.YGR209C.

    Structurei

    Secondary structure

    1
    104
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi8 – 158
    Beta strandi19 – 279
    Helixi32 – 4716
    Beta strandi51 – 577
    Turni58 – 603
    Helixi62 – 676
    Beta strandi72 – 809
    Beta strandi83 – 919
    Helixi93 – 1019

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FA4X-ray2.38A/B1-104[»]
    2HSYNMR-A1-104[»]
    3PINX-ray2.70A1-104[»]
    4DSSX-ray2.10B1-104[»]
    ProteinModelPortaliP22803.
    SMRiP22803. Positions 1-104.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22803.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 104103ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thioredoxin family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0526.
    GeneTreeiENSGT00530000063008.
    HOGENOMiHOG000292977.
    KOiK03671.
    OMAiCKAMEPR.
    OrthoDBiEOG71CFZN.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PANTHERiPTHR10438. PTHR10438. 1 hit.
    PfamiPF00085. Thioredoxin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000077. Thioredoxin. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P22803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTQLKSASE YDSALASGDK LVVVDFFATW CGPCKMIAPM IEKFAEQYSD    50
    AAFYKLDVDE VSDVAQKAEV SSMPTLIFYK GGKEVTRVVG ANPAAIKQAI 100
    ASNV 104
    Length:104
    Mass (Da):11,204
    Last modified:January 23, 2007 - v3
    Checksum:i071503762C90D451
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59168 Genomic DNA. Translation: AAA35170.1.
    M62648 Genomic DNA. Translation: AAA35178.1.
    U40843 Genomic DNA. Translation: AAA85584.1.
    Z49133 Genomic DNA. Translation: CAA89002.1.
    Z72994 Genomic DNA. Translation: CAA97236.1.
    AY557817 Genomic DNA. Translation: AAS56143.1.
    BK006941 Genomic DNA. Translation: DAA08303.1.
    PIRiS15049. TXBY1.
    RefSeqiNP_011725.3. NM_001181338.3.

    Genome annotation databases

    EnsemblFungiiYGR209C; YGR209C; YGR209C.
    GeneIDi853123.
    KEGGisce:YGR209C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59168 Genomic DNA. Translation: AAA35170.1 .
    M62648 Genomic DNA. Translation: AAA35178.1 .
    U40843 Genomic DNA. Translation: AAA85584.1 .
    Z49133 Genomic DNA. Translation: CAA89002.1 .
    Z72994 Genomic DNA. Translation: CAA97236.1 .
    AY557817 Genomic DNA. Translation: AAS56143.1 .
    BK006941 Genomic DNA. Translation: DAA08303.1 .
    PIRi S15049. TXBY1.
    RefSeqi NP_011725.3. NM_001181338.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FA4 X-ray 2.38 A/B 1-104 [» ]
    2HSY NMR - A 1-104 [» ]
    3PIN X-ray 2.70 A 1-104 [» ]
    4DSS X-ray 2.10 B 1-104 [» ]
    ProteinModelPortali P22803.
    SMRi P22803. Positions 1-104.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33462. 43 interactions.
    DIPi DIP-5552N.
    IntActi P22803. 9 interactions.
    MINTi MINT-474704.
    STRINGi 4932.YGR209C.

    Proteomic databases

    MaxQBi P22803.
    PaxDbi P22803.
    PeptideAtlasi P22803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR209C ; YGR209C ; YGR209C .
    GeneIDi 853123.
    KEGGi sce:YGR209C.

    Organism-specific databases

    SGDi S000003441. TRX2.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00530000063008.
    HOGENOMi HOG000292977.
    KOi K03671.
    OMAi CKAMEPR.
    OrthoDBi EOG71CFZN.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30891-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P22803.
    NextBioi 973163.

    Gene expression databases

    Genevestigatori P22803.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    PANTHERi PTHR10438. PTHR10438. 1 hit.
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000077. Thioredoxin. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR01068. thioredoxin. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Yeast thioredoxin genes."
      Gan Z.-R.
      J. Biol. Chem. 266:1692-1696(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle."
      Muller E.G.D.
      J. Biol. Chem. 266:9194-9202(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Analysis of the 15.6-kb fragment encompassing the ADE3 gene."
      Song J.M., Cheung E., Rabinowitz J.C.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / GRF88.
    4. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
      Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
      Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    8. "Thioredoxin-dependent peroxide reductase from yeast."
      Chae H.Z., Chung S.J., Rhee S.G.
      J. Biol. Chem. 269:27670-27678(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13, TSA1 DEPENDENCE ON THIOREDOXIN.
      Strain: ATCC 200358 / YNN 295.
    9. "Yeast thioredoxin. Amino-acid sequence around the active-center disulfide of thioredoxin I and II."
      Hall D.E., Baldesten A., Holmgren A., Reichard P.
      Eur. J. Biochem. 23:328-335(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-43, REDOX-ACTIVE DISULFIDE BOND.
    10. "Yeast PAPS reductase: properties and requirements of the purified enzyme."
      Schwenn J.D., Krone F.A., Husmann K.
      Arch. Microbiol. 150:313-319(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SULFATE ASSIMILATION AND METHIONINE METABOLISM.
    11. "A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance."
      Xu Z., Mayer A., Muller E.G.D., Wickner W.
      J. Cell Biol. 136:299-306(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE LMA1 COMPLEX.
    12. "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion."
      Xu Z., Sato K., Wickner W.
      Cell 93:1125-1134(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION OF THE LMA1 COMPLEX WITH SEC18.
    13. "Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae."
      Park S.G., Cha M.-K., Jeong W., Kim I.-H.
      J. Biol. Chem. 275:5723-5732(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOT5 AND TSA2 DEPENDENCE ON THIOREDOXIN.
    14. "A new antioxidant with alkyl hydroperoxide defense properties in yeast."
      Lee J., Spector D., Godon C., Labarre J., Toledano M.B.
      J. Biol. Chem. 274:4537-4544(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REDUCTION OF AHP1.
    15. "H2O2 sensing through oxidation of the Yap1 transcription factor."
      Delaunay A., Isnard A.D., Toledano M.B.
      EMBO J. 19:5157-5166(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REGULATION OF YAP1.
    16. "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation."
      Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.
      Cell 111:471-481(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REGULATION OF HYR1/GPX3.
    17. "Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae."
      Trotter E.W., Grant C.M.
      Mol. Microbiol. 46:869-878(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTECTION AGAINST REDUCING STRESS.
    18. "Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress."
      Carmel-Harel O., Storz G.
      Annu. Rev. Microbiol. 54:439-461(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, OXIDATIVE STRESS.
    19. "Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions."
      Grant C.M.
      Mol. Microbiol. 39:533-541(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    20. "Involvement of LMA1 and GATE-16 family members in intracellular membrane dynamics."
      Elazar Z., Scherz-Shouval R., Shorer H.
      Biochim. Biophys. Acta 1641:145-156(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, FUNCTION OF THE LMA1 COMPLEX IN VESICLE FUSION.
    21. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    22. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    23. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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].
    26. "Crystal structure of the yeast cytoplasmic thioredoxin Trx2."
      Bao R., Chen Y., Tang Y.-J., Janin J., Zhou C.-Z.
      Proteins 66:246-249(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS), DISULFIDE BOND, SUBUNIT.

    Entry informationi

    Entry nameiTRX2_YEAST
    AccessioniPrimary (citable) accession number: P22803
    Secondary accession number(s): D6VUZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 17237 molecules/cell in log phase SD medium.1 Publication
    Yeast has two cytoplasmic thioredoxins, TRX1 and TRX2, and one mitochondrial, TRX3.

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

    External Data

    Dasty 3