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P00830

- ATPB_YEAST

UniProt

P00830 - ATPB_YEAST

Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP2

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 159 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    Catalytic activityi

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1978ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. proton-transporting ATPase activity, rotational mechanism Source: SGD
    3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. ATP hydrolysis coupled proton transport Source: InterPro
    3. ATP synthesis coupled proton transport Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31742-MONOMER.
    ReactomeiREACT_189012. Mitochondrial protein import.

    Protein family/group databases

    TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
    Gene namesi
    Name:ATP2
    Ordered Locus Names:YJR121W
    ORF Names:J2041
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJR121w.
    SGDiS000003882. ATP2.

    Subcellular locationi

    Mitochondrion. Mitochondrion inner membrane
    Note: Peripheral membrane protein.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial inner membrane Source: Reactome
    3. mitochondrial intermembrane space Source: Reactome
    4. mitochondrial proton-transporting ATP synthase, catalytic core Source: SGD
    5. mitochondrion Source: SGD
    6. proton-transporting ATP synthase complex, catalytic core F(1) Source: SGD

    Keywords - Cellular componenti

    CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionAdd
    BLAST
    Chaini34 – 511478ATP synthase subunit beta, mitochondrialPRO_0000002454Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei112 – 1121Phosphothreonine1 Publication
    Modified residuei237 – 2371Phosphothreonine1 Publication
    Modified residuei373 – 3731Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP00830.
    PaxDbiP00830.
    PeptideAtlasiP00830.
    PRIDEiP00830.

    2D gel databases

    SWISS-2DPAGEP00830.

    Expressioni

    Gene expression databases

    GenevestigatoriP00830.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

    Protein-protein interaction databases

    BioGridi33877. 73 interactions.
    DIPiDIP-3028N.
    IntActiP00830. 66 interactions.
    MINTiMINT-534087.
    STRINGi4932.YJR121W.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 508
    Beta strandi53 – 586
    Beta strandi59 – 613
    Beta strandi69 – 724
    Beta strandi75 – 773
    Beta strandi79 – 8810
    Beta strandi91 – 988
    Beta strandi108 – 1114
    Beta strandi113 – 1153
    Beta strandi117 – 1193
    Helixi122 – 1243
    Beta strandi128 – 1303
    Beta strandi131 – 1333
    Beta strandi137 – 1393
    Beta strandi147 – 1504
    Helixi157 – 1593
    Helixi172 – 1776
    Beta strandi180 – 1834
    Beta strandi184 – 1907
    Beta strandi192 – 1954
    Helixi196 – 20712
    Turni208 – 2103
    Beta strandi211 – 2133
    Beta strandi215 – 2228
    Helixi224 – 23512
    Turni236 – 2383
    Beta strandi242 – 2443
    Beta strandi247 – 2537
    Helixi259 – 27820
    Beta strandi283 – 2897
    Helixi292 – 30211
    Helixi303 – 3053
    Helixi311 – 3133
    Helixi318 – 3269
    Beta strandi332 – 3343
    Beta strandi335 – 34410
    Helixi346 – 3483
    Helixi353 – 3586
    Helixi359 – 3613
    Beta strandi363 – 3686
    Helixi370 – 3745
    Turni383 – 3853
    Helixi393 – 3964
    Helixi398 – 42326
    Helixi426 – 4283
    Helixi431 – 44616
    Helixi455 – 4584
    Helixi467 – 47913
    Turni480 – 4845
    Helixi487 – 4893
    Turni490 – 4923
    Helixi496 – 50712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HLDX-ray2.80D/E/F/M/N/O/V/W/X34-511[»]
    2WPDX-ray3.43D/E/F34-511[»]
    2XOKX-ray3.01D/E/F1-507[»]
    3FKSX-ray3.59D/E/F/M/N/O/V/W/X36-511[»]
    3OE7X-ray3.19D/E/F/M/N/O/V/W/X36-511[»]
    3OEEX-ray2.74D/E/F/M/N/O/V/W/X36-511[»]
    3OEHX-ray3.00D/E/F/M/N/O/V/W/X36-511[»]
    3OFNX-ray3.20D/E/F/M/N/O/V/W/X36-511[»]
    3ZIAX-ray2.50D/E/F/N/O/P34-511[»]
    3ZRYX-ray6.50D/E/F34-511[»]
    4B2Qelectron microscopy37.00D/d39-508[»]
    E/F/e/f39-511[»]
    ProteinModelPortaliP00830.
    SMRiP00830. Positions 39-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00830.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0055.
    GeneTreeiENSGT00550000074800.
    HOGENOMiHOG000009605.
    KOiK02133.
    OMAiVVRGIHQ.
    OrthoDBiEOG7F7WJV.

    Family and domain databases

    Gene3Di1.10.1140.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01347. ATP_synth_beta_bact.
    InterProiIPR003593. AAA+_ATPase.
    IPR020003. ATPase_a/bsu_AS.
    IPR005722. ATPase_F1-cplx_bsu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01039. atpD. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00830-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLPRLYTAT SRAAFKAAKQ SAPLLSTSWK RCMASAAQST PITGKVTAVI    50
    GAIVDVHFEQ SELPAILNAL EIKTPQGKLV LEVAQHLGEN TVRTIAMDGT 100
    EGLVRGEKVL DTGGPISVPV GRETLGRIIN VIGEPIDERG PIKSKLRKPI 150
    HADPPSFAEQ STSAEILETG IKVVDLLAPY ARGGKIGLFG GAGVGKTVFI 200
    QELINNIAKA HGGFSVFTGV GERTREGNDL YREMKETGVI NLEGESKVAL 250
    VFGQMNEPPG ARARVALTGL TIAEYFRDEE GQDVLLFIDN IFRFTQAGSE 300
    VSALLGRIPS AVGYQPTLAT DMGLLQERIT TTKKGSVTSV QAVYVPADDL 350
    TDPAPATTFA HLDATTVLSR GISELGIYPA VDPLDSKSRL LDAAVVGQEH 400
    YDVASKVQET LQTYKSLQDI IAILGMDELS EQDKLTVERA RKIQRFLSQP 450
    FAVAEVFTGI PGKLVRLKDT VASFKAVLEG KYDNIPEHAF YMVGGIEDVV 500
    AKAEKLAAEA N 511
    Length:511
    Mass (Da):54,794
    Last modified:December 20, 2005 - v2
    Checksum:iEDFF256826F68F0C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011Q → M in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti218 – 2181T → A in AAA34444. (PubMed:2866186)Curated
    Sequence conflicti218 – 2181T → A in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti232 – 2376REMKET → HEMEDS in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti260 – 2601G → E in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti287 – 2882FI → Y in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti354 – 3585APATT → SPSTS in AAA34444. (PubMed:2866186)Curated
    Sequence conflicti365 – 3662TT → SS in AAA34444. (PubMed:2866186)Curated
    Sequence conflicti365 – 3662TT → SS in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti469 – 4735DTVAS → RTRCL in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti489 – 4891A → R in AAA34443. (PubMed:6225776)Curated
    Sequence conflicti501 – 5011A → R in AAA34444. (PubMed:2866186)Curated
    Sequence conflicti508 – 5081A → R in AAA34444. (PubMed:2866186)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12082 Genomic DNA. Translation: AAA34444.1.
    U46215 Genomic DNA. Translation: AAC49475.1.
    Z49621 Genomic DNA. Translation: CAA89652.1.
    X52004 Genomic DNA. Translation: CAA36255.1.
    K00560 Genomic DNA. Translation: AAA34443.1.
    BK006943 Genomic DNA. Translation: DAA08906.1.
    PIRiS57144. PWBYB.
    RefSeqiNP_012655.3. NM_001181779.3.

    Genome annotation databases

    EnsemblFungiiYJR121W; YJR121W; YJR121W.
    GeneIDi853585.
    KEGGisce:YJR121W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12082 Genomic DNA. Translation: AAA34444.1 .
    U46215 Genomic DNA. Translation: AAC49475.1 .
    Z49621 Genomic DNA. Translation: CAA89652.1 .
    X52004 Genomic DNA. Translation: CAA36255.1 .
    K00560 Genomic DNA. Translation: AAA34443.1 .
    BK006943 Genomic DNA. Translation: DAA08906.1 .
    PIRi S57144. PWBYB.
    RefSeqi NP_012655.3. NM_001181779.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HLD X-ray 2.80 D/E/F/M/N/O/V/W/X 34-511 [» ]
    2WPD X-ray 3.43 D/E/F 34-511 [» ]
    2XOK X-ray 3.01 D/E/F 1-507 [» ]
    3FKS X-ray 3.59 D/E/F/M/N/O/V/W/X 36-511 [» ]
    3OE7 X-ray 3.19 D/E/F/M/N/O/V/W/X 36-511 [» ]
    3OEE X-ray 2.74 D/E/F/M/N/O/V/W/X 36-511 [» ]
    3OEH X-ray 3.00 D/E/F/M/N/O/V/W/X 36-511 [» ]
    3OFN X-ray 3.20 D/E/F/M/N/O/V/W/X 36-511 [» ]
    3ZIA X-ray 2.50 D/E/F/N/O/P 34-511 [» ]
    3ZRY X-ray 6.50 D/E/F 34-511 [» ]
    4B2Q electron microscopy 37.00 D/d 39-508 [» ]
    E/F/e/f 39-511 [» ]
    ProteinModelPortali P00830.
    SMRi P00830. Positions 39-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33877. 73 interactions.
    DIPi DIP-3028N.
    IntActi P00830. 66 interactions.
    MINTi MINT-534087.
    STRINGi 4932.YJR121W.

    Chemistry

    BindingDBi P00830.
    ChEMBLi CHEMBL1075103.

    Protein family/group databases

    TCDBi 3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    2D gel databases

    SWISS-2DPAGE P00830.

    Proteomic databases

    MaxQBi P00830.
    PaxDbi P00830.
    PeptideAtlasi P00830.
    PRIDEi P00830.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR121W ; YJR121W ; YJR121W .
    GeneIDi 853585.
    KEGGi sce:YJR121W.

    Organism-specific databases

    CYGDi YJR121w.
    SGDi S000003882. ATP2.

    Phylogenomic databases

    eggNOGi COG0055.
    GeneTreei ENSGT00550000074800.
    HOGENOMi HOG000009605.
    KOi K02133.
    OMAi VVRGIHQ.
    OrthoDBi EOG7F7WJV.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31742-MONOMER.
    Reactomei REACT_189012. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei P00830.
    NextBioi 974382.
    PROi P00830.

    Gene expression databases

    Genevestigatori P00830.

    Family and domain databases

    Gene3Di 1.10.1140.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_01347. ATP_synth_beta_bact.
    InterProi IPR003593. AAA+_ATPase.
    IPR020003. ATPase_a/bsu_AS.
    IPR005722. ATPase_F1-cplx_bsu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01039. atpD. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Primary sequence analysis of ATP2 encoding the F1-ATPase beta-subunit precursor."
      Takeda M., Vassarotti A., Douglas M.G.
      J. Biol. Chem. 260:15458-15465(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Erratum
      Takeda M., Vassarotti A., Douglas M.G.
      J. Biol. Chem. 261:10466-10466(1986)
    3. Takeda M.
      Submitted (JUL-1986) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Characterization of mutations in the beta subunit of the mitochondrial F1-ATPase that produce defects in enzyme catalysis and assembly."
      Liang Y., Ackerman S.H.
      J. Biol. Chem. 271:26522-26528(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 24657 / D273-10B.
    5. "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.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Transport of the yeast ATP synthase beta-subunit into mitochondria. Effects of amino acid substitutions on targeting."
      Walker M.E., Valentin E., Reid G.A.
      Biochem. J. 266:227-234(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
    8. "Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the F1-ATPase beta subunit."
      Saltzgaber-Muller J., Kunapuli S.P., Douglas M.G.
      J. Biol. Chem. 258:11465-11470(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-507.
    9. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
      Norbeck J., Blomberg A.
      FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 371-379 AND 390-398.
      Strain: ATCC 38531 / Y41.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112; THR-237 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    12. "Molecular architecture of the rotary motor in ATP synthase."
      Stock D., Leslie A.G., Walker J.E.
      Science 286:1700-1705(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiATPB_YEAST
    AccessioniPrimary (citable) accession number: P00830
    Secondary accession number(s): D6VWU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 159 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 164000 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