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P16140

- VATB_YEAST

UniProt

P16140 - VATB_YEAST

Protein

V-type proton ATPase subunit B

Gene

VMA2

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 155 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mv, inside positive and acidic, in the vacuolar membrane vesicles.1 Publication

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. protein binding Source: IntAct
    3. proton-transporting ATPase activity, rotational mechanism Source: SGD

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. cellular calcium ion homeostasis Source: SGD
    3. proteasome storage granule assembly Source: SGD
    4. transmembrane transport Source: SGD
    5. vacuolar acidification Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29082-MONOMER.

    Protein family/group databases

    TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V-type proton ATPase subunit B
    Short name:
    V-ATPase subunit B
    Alternative name(s):
    V-ATPase 57 kDa subunit
    Vacuolar proton pump subunit B
    Gene namesi
    Name:VMA2
    Synonyms:VAT2
    Ordered Locus Names:YBR127C
    ORF Names:YBR1002
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR127c.
    SGDiS000000331. VMA2.

    Subcellular locationi

    GO - Cellular componenti

    1. fungal-type vacuole membrane Source: SGD
    2. vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 517517V-type proton ATPase subunit BPRO_0000144648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphoserine2 Publications
    Modified residuei137 – 1371Phosphoserine2 Publications
    Modified residuei503 – 5031Phosphoserine1 Publication
    Modified residuei504 – 5041Phosphoserine1 Publication
    Modified residuei511 – 5111Phosphoserine; by ATM or ATR2 Publications
    Modified residuei515 – 5151Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16140.
    PaxDbiP16140.
    PeptideAtlasiP16140.

    Expressioni

    Gene expression databases

    GenevestigatoriP16140.

    Interactioni

    Subunit structurei

    V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAV1P471044EBI-20254,EBI-25471

    Protein-protein interaction databases

    BioGridi32828. 140 interactions.
    DIPiDIP-2292N.
    IntActiP16140. 516 interactions.
    MINTiMINT-563511.
    STRINGi4932.YBR127C.

    Structurei

    3D structure databases

    ProteinModelPortaliP16140.
    SMRiP16140. Positions 27-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Phylogenomic databases

    eggNOGiCOG1156.
    GeneTreeiENSGT00550000074724.
    HOGENOMiHOG000165320.
    KOiK02147.
    OMAiGFKIKPR.
    OrthoDBiEOG7H79BK.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00310. ATP_synth_B_arch.
    InterProiIPR020003. ATPase_a/bsu_AS.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR005723. ATPase_V1-cplx_bsu.
    IPR027417. P-loop_NTPase.
    IPR022879. V-ATPase_su_B/beta.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16140-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLSDKELFA INKKAVEQGF NVKPRLNYNT VSGVNGPLVI LEKVKFPRYN    50
    EIVNLTLPDG TVRQGQVLEI RGDRAIVQVF EGTSGIDVKK TTVEFTGESL 100
    RIPVSEDMLG RIFDGSGRPI DNGPKVFAED YLDINGSPIN PYARIYPEEM 150
    ISTGVSAIDT MNSIARGQKI PIFSASGLPH NEIAAQICRQ AGLVRPTKDV 200
    HDGHEENFSI VFAAMGVNLE TARFFKQDFE ENGSLERTSL FLNLANDPTI 250
    ERIITPRLAL TTAEYLAYQT ERHVLTILTD MSSYADALRE VSAAREEVPG 300
    RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT 350
    GYITEGQIFV DRQLHNKGIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS 400
    NQLYAKYAIG KDAAAMKAVV GEEALSIEDK LSLEFLEKFE KTFITQGAYE 450
    DRTVFESLDQ AWSLLRIYPK EMLNRISPKI LDEFYDRARD DADEDEEDPD 500
    TRSSGKKKDA SQEESLI 517
    Length:517
    Mass (Da):57,749
    Last modified:October 1, 1994 - v2
    Checksum:i02A7DEC571EFF7C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141K → V AA sequence (PubMed:2141385)Curated
    Sequence conflicti79 – 791V → L in AAA66890. (PubMed:2521486)Curated
    Sequence conflicti227 – 2271Q → R in AAA30389. (PubMed:1371275)Curated
    Sequence conflicti500 – 51718DTRSS…EESLI → TQEAPVRRRTPAKKNL in AAA66890. (PubMed:2521486)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04450 Genomic DNA. Translation: AAA66890.1.
    X75891 Genomic DNA. Translation: CAA53486.1.
    Z35996 Genomic DNA. Translation: CAA85084.1.
    AY693158 Genomic DNA. Translation: AAT93177.1.
    M83130 mRNA. Translation: AAA30389.1.
    BK006936 Genomic DNA. Translation: DAA07244.1.
    PIRiB42254.
    S45996.
    RefSeqiNP_009685.3. NM_001178475.3.

    Genome annotation databases

    EnsemblFungiiYBR127C; YBR127C; YBR127C.
    GeneIDi852424.
    KEGGisce:YBR127C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04450 Genomic DNA. Translation: AAA66890.1 .
    X75891 Genomic DNA. Translation: CAA53486.1 .
    Z35996 Genomic DNA. Translation: CAA85084.1 .
    AY693158 Genomic DNA. Translation: AAT93177.1 .
    M83130 mRNA. Translation: AAA30389.1 .
    BK006936 Genomic DNA. Translation: DAA07244.1 .
    PIRi B42254.
    S45996.
    RefSeqi NP_009685.3. NM_001178475.3.

    3D structure databases

    ProteinModelPortali P16140.
    SMRi P16140. Positions 27-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32828. 140 interactions.
    DIPi DIP-2292N.
    IntActi P16140. 516 interactions.
    MINTi MINT-563511.
    STRINGi 4932.YBR127C.

    Chemistry

    ChEMBLi CHEMBL6106.

    Protein family/group databases

    TCDBi 3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Proteomic databases

    MaxQBi P16140.
    PaxDbi P16140.
    PeptideAtlasi P16140.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR127C ; YBR127C ; YBR127C .
    GeneIDi 852424.
    KEGGi sce:YBR127C.

    Organism-specific databases

    CYGDi YBR127c.
    SGDi S000000331. VMA2.

    Phylogenomic databases

    eggNOGi COG1156.
    GeneTreei ENSGT00550000074724.
    HOGENOMi HOG000165320.
    KOi K02147.
    OMAi GFKIKPR.
    OrthoDBi EOG7H79BK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29082-MONOMER.

    Miscellaneous databases

    NextBioi 971294.
    PROi P16140.

    Gene expression databases

    Genevestigatori P16140.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00310. ATP_synth_B_arch.
    InterProi IPR020003. ATPase_a/bsu_AS.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR005723. ATPase_V1-cplx_bsu.
    IPR027417. P-loop_NTPase.
    IPR022879. V-ATPase_su_B/beta.
    [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 ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01040. V-ATPase_V1_B. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A conserved gene encoding the 57-kDa subunit of the yeast vacuolar H+-ATPase."
      Nelson H., Mandiyan S., Nelson N.
      J. Biol. Chem. 264:1775-1778(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Erratum
      Nelson H., Mandiyan S., Nelson N.
      J. Biol. Chem. 264:5313-5313(1989)
      Cited for: SEQUENCE REVISION.
    3. "The sequence of 29.7 kb from the right arm of chromosome II reveals 13 complete open reading frames, of which ten correspond to new genes."
      Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J.
      Yeast 10:S1-S11(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "Differential expression of the 'B' subunit of the vacuolar H(+)-ATPase in bovine tissues."
      Puopolo K., Kumamoto C., Adachi I., Magner R., Forgac M.
      J. Biol. Chem. 267:3696-3706(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-517.
    8. "Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase."
      Yamashiro C.T., Kane P.M., Wolczyk D.F., Preston R.A., Stevens T.H.
      Mol. Cell. Biol. 10:3737-3749(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 13-28, FUNCTION.
    9. "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
      Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
      Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAV1 AND RAV2.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "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-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    12. "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-511 AND SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-4; SER-137; SER-503 AND SER-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-137; SER-511 AND SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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 nameiVATB_YEAST
    AccessioniPrimary (citable) accession number: P16140
    Secondary accession number(s): D6VQC4, P32123
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 155 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 131000 molecules/cell in log phase SD medium.1 Publication

    Caution

    PubMed:1371275 sequence was incorrectly thought to originate from bovine.Curated

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

    External Data

    Dasty 3