SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16140

- VATB_YEAST

UniProt

P16140 - VATB_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

V-type proton ATPase subunit B

Gene
VMA2, VAT2, YBR127C, YBR1002
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517V-type proton ATPase subunit BUniRule annotationPRO_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.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141K → V AA sequence 1 Publication
Sequence conflicti79 – 791V → L in AAA66890. 1 Publication
Sequence conflicti227 – 2271Q → R in AAA30389. 1 Publication
Sequence conflicti500 – 51718DTRSS…EESLI → TQEAPVRRRTPAKKNL in AAA66890. 1 PublicationAdd
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 154 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.

Caution

1 Publication sequence was incorrectly thought to originate from bovine.

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

Similar proteinsi