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P05030

- PMA1_YEAST

UniProt

P05030 - PMA1_YEAST

Protein

Plasma membrane ATPase 1

Gene

PMA1

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 161 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.

    Catalytic activityi

    ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei378 – 37814-aspartylphosphate intermediateBy similarity
    Metal bindingi634 – 6341MagnesiumBy similarity
    Metal bindingi638 – 6381MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. ATP biosynthetic process Source: InterPro
    2. hydrogen ion transmembrane transport Source: GOC
    3. proteasome storage granule assembly Source: SGD
    4. proton transport Source: SGD
    5. regulation of pH Source: SGD
    6. transmembrane transport Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Prion

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30531-MONOMER.

    Protein family/group databases

    TCDBi3.A.3.3.6. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plasma membrane ATPase 1 (EC:3.6.3.6)
    Alternative name(s):
    Proton pump 1
    Gene namesi
    Name:PMA1
    Ordered Locus Names:YGL008C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL008c.
    SGDiS000002976. PMA1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane raft Source: SGD
    3. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Amyloid, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291E → L or Q: Normal activity. 1 Publication
    Mutagenesisi200 – 2001D → N: Activity reduced to 23%. 1 Publication
    Mutagenesisi233 – 2331E → Q: Activity reduced to 33%. 1 Publication
    Mutagenesisi271 – 2711R → T: Normal activity. 1 Publication
    Mutagenesisi335 – 3351P → A: Activity reduced to 53%. 1 Publication
    Mutagenesisi378 – 3781D → E: Activity reduced to 67%. 1 Publication
    Mutagenesisi378 – 3781D → N: Activity reduced to 73%. 1 Publication
    Mutagenesisi378 – 3781D → T: Activity reduced to 49%. 1 Publication
    Mutagenesisi474 – 4741K → Q: Activity reduced to 19%. 1 Publication
    Mutagenesisi534 – 5341D → N: Activity reduced to 37%. 1 Publication
    Mutagenesisi560 – 5601D → N: Activity reduced to 24%. 1 Publication
    Mutagenesisi638 – 6381D → N: Activity reduced to 24%. 1 Publication
    Mutagenesisi848 – 8481N → D: Normal activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 918918Plasma membrane ATPase 1PRO_0000046271Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611Phosphoserine1 Publication
    Modified residuei175 – 1751Phosphothreonine1 Publication
    Cross-linki555 – 555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki566 – 566Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki644 – 644Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei911 – 9111Phosphoserine2 Publications
    Modified residuei912 – 9121Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated on multiple Ser and Thr residues.3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP05030.
    PeptideAtlasiP05030.
    PRIDEiP05030.

    Expressioni

    Gene expression databases

    GenevestigatoriP05030.

    Interactioni

    Protein-protein interaction databases

    BioGridi33238. 256 interactions.
    DIPiDIP-2537N.
    IntActiP05030. 6 interactions.
    MINTiMINT-685556.
    STRINGi4932.YGL008C.

    Structurei

    3D structure databases

    ProteinModelPortaliP05030.
    SMRiP05030. Positions 2-916.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 115115CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini137 – 1404ExtracellularSequence Analysis
    Topological domaini161 – 291131CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini314 – 32512ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini348 – 719372CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini739 – 75416ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini775 – 82450CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini846 – 85712ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini875 – 91844CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei116 – 13621Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei141 – 16020Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei292 – 31322Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei326 – 34722Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei720 – 73819Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei755 – 77420Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei825 – 84521Helical; Name=7Sequence AnalysisAdd
    BLAST
    Transmembranei858 – 87417Helical; Name=8Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 1713Poly-SerAdd
    BLAST
    Compositional biasi31 – 7848Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi39 – 446Poly-Asp
    Compositional biasi585 – 5906Poly-Gly

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00730000113900.
    HOGENOMiHOG000160005.
    KOiK01535.
    OMAiFMVITAT.
    OrthoDBiEOG789CKN.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 2 hits.
    InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR006534. H+_ATPase_P-typ_IIIA.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 2 hits.
    TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05030-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL    50
    QSNHGVDDED SDNDGPVAAG EARPVPEEYL QTDPSYGLTS DEVLKRRKKY 100
    GLNQMADEKE SLVVKFVMFF VGPIQFVMEA AAILAAGLSD WVDFGVICGL 150
    LMLNAGVGFV QEFQAGSIVD ELKKTLANTA VVIRDGQLVE IPANEVVPGD 200
    ILQLEDGTVI PTDGRIVTED CFLQIDQSAI TGESLAVDKH YGDQTFSSST 250
    VKRGEGFMVV TATGDNTFVG RAAALVNKAA GGQGHFTEVL NGIGIILLVL 300
    VIATLLLVWT ACFYRTNGIV RILRYTLGIT IIGVPVGLPA VVTTTMAVGA 350
    AYLAKKQAIV QKLSAIESLA GVEILCSDKT GTLTKNKLSL HEPYTVEGVS 400
    PDDLMLTACL AASRKKKGLD AIDKAFLKSL KQYPKAKDAL TKYKVLEFHP 450
    FDPVSKKVTA VVESPEGERI VCVKGAPLFV LKTVEEDHPI PEDVHENYEN 500
    KVAELASRGF RALGVARKRG EGHWEILGVM PCMDPPRDDT AQTVSEARHL 550
    GLRVKMLTGD AVGIAKETCR QLGLGTNIYN AERLGLGGGG DMPGSELADF 600
    VENADGFAEV FPQHKYRVVE ILQNRGYLVA MTGDGVNDAP SLKKADTGIA 650
    VEGATDAARS AADIVFLAPG LSAIIDALKT SRQIFHRMYS YVVYRIALSL 700
    HLEIFLGLWI AILDNSLDID LIVFIAIFAD VATLAIAYDN APYSPKPVKW 750
    NLPRLWGMSI ILGIVLAIGS WITLTTMFLP KGGIIQNFGA MNGIMFLQIS 800
    LTENWLIFIT RAAGPFWSSI PSWQLAGAVF AVDIIATMFT LFGWWSENWT 850
    DIVTVVRVWI WSIGIFCVLG GFYYEMSTSE AFDRLMNGKP MKEKKSTRSV 900
    EDFMAAMQRV STQHEKET 918
    Length:918
    Mass (Da):99,619
    Last modified:November 1, 1995 - v2
    Checksum:iAA1E93966B37E8E1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03534 Genomic DNA. Translation: CAA27237.1.
    Z72530 Genomic DNA. Translation: CAA96708.1.
    BK006941 Genomic DNA. Translation: DAA08090.1.
    PIRiS64010. PXBY1P.
    RefSeqiNP_011507.1. NM_001180873.1.

    Genome annotation databases

    EnsemblFungiiYGL008C; YGL008C; YGL008C.
    GeneIDi852876.
    KEGGisce:YGL008C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03534 Genomic DNA. Translation: CAA27237.1 .
    Z72530 Genomic DNA. Translation: CAA96708.1 .
    BK006941 Genomic DNA. Translation: DAA08090.1 .
    PIRi S64010. PXBY1P.
    RefSeqi NP_011507.1. NM_001180873.1.

    3D structure databases

    ProteinModelPortali P05030.
    SMRi P05030. Positions 2-916.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33238. 256 interactions.
    DIPi DIP-2537N.
    IntActi P05030. 6 interactions.
    MINTi MINT-685556.
    STRINGi 4932.YGL008C.

    Protein family/group databases

    TCDBi 3.A.3.3.6. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    MaxQBi P05030.
    PeptideAtlasi P05030.
    PRIDEi P05030.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL008C ; YGL008C ; YGL008C .
    GeneIDi 852876.
    KEGGi sce:YGL008C.

    Organism-specific databases

    CYGDi YGL008c.
    SGDi S000002976. PMA1.

    Phylogenomic databases

    GeneTreei ENSGT00730000113900.
    HOGENOMi HOG000160005.
    KOi K01535.
    OMAi FMVITAT.
    OrthoDBi EOG789CKN.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30531-MONOMER.

    Miscellaneous databases

    NextBioi 972514.

    Gene expression databases

    Genevestigatori P05030.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 2 hits.
    InterProi IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR006534. H+_ATPase_P-typ_IIIA.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    PR00120. HATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 2 hits.
    TIGRFAMsi TIGR01647. ATPase-IIIA_H. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases."
      Serrano R., Kielland-Brandt M.C., Fink G.R.
      Nature 319:689-693(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The ATP binding site of the yeast plasma membrane proton-translocating ATPase."
      Davis C.B., Smith K.E., Campbell B.N. Jr., Hammes G.G.
      J. Biol. Chem. 265:1300-1305(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 556-566.
    5. "Dissection of functional domains of the yeast proton-pumping ATPase by directed mutagenesis."
      Portillo F., Serrano R.
      EMBO J. 7:1793-1798(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-129; ASP-200; GLU-233; ARG-271; PRO-335; ASP-378; LYS-474; ASP-534; ASP-560; ASP-638 AND ASN-848.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
      Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-555; LYS-566 AND LYS-644.
    8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
      Kim H., Melen K., Oesterberg M., von Heijne G.
      Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: ATCC 208353 / W303-1A.
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "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-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "A heritable switch in carbon source utilization driven by an unusual yeast prion."
      Brown J.C., Lindquist S.
      Genes Dev. 23:2320-2332(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION IDENTIFICATION, INTERACTION WITH STD1.
    12. "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 THR-175; SER-911 AND THR-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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].

    Entry informationi

    Entry nameiPMA1_YEAST
    AccessioniPrimary (citable) accession number: P05030
    Secondary accession number(s): D6VUC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The prion state [GAR+] is provoked by the interaction of the two proteins STD1 and PMA1. It involves a complex between a small fraction of the cellular complement of PMA1, and STD1, a much lower-abundance protein, and it is transmissible by non-Mendelian, cytoplasmic inheritance. [GAR+] makes cells resistant to the glucose-associated repression of alternative carbon sources. In contrast to other prion forms, [GAR+] cannot be cured by GdnHCl or by inactivation of the molecular chaperone HSP104 (PubMed:19797769).1 Publication
    There are two plasma membrane ATPases in yeast. This is the major isoform.
    Present with 1260000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3