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P16140 (VATB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:VMA2
Synonyms:VAT2
Ordered Locus Names:YBR127C
ORF Names:YBR1002
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.9

Miscellaneous

Present with 131000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Caution

Ref.7 sequence was incorrectly thought to originate from bovine.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAV1P471044EBI-20254,EBI-25471

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517V-type proton ATPase subunit B HAMAP-Rule MF_00310
PRO_0000144648

Amino acid modifications

Modified residue41Phosphoserine Ref.11 Ref.14
Modified residue1371Phosphoserine Ref.14 Ref.15
Modified residue5031Phosphoserine Ref.14
Modified residue5041Phosphoserine Ref.14
Modified residue5111Phosphoserine; by ATM or ATR Ref.12 Ref.15
Modified residue5151Phosphoserine Ref.12 Ref.15

Experimental info

Sequence conflict141K → V AA sequence Ref.8
Sequence conflict791V → L in AAA66890. Ref.1
Sequence conflict2271Q → R in AAA30389. Ref.7
Sequence conflict500 – 51718DTRSS…EESLI → TQEAPVRRRTPAKKNL in AAA66890. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16140 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 02A7DEC571EFF7C2

FASTA51757,749
        10         20         30         40         50         60 
MVLSDKELFA INKKAVEQGF NVKPRLNYNT VSGVNGPLVI LEKVKFPRYN EIVNLTLPDG 

        70         80         90        100        110        120 
TVRQGQVLEI RGDRAIVQVF EGTSGIDVKK TTVEFTGESL RIPVSEDMLG RIFDGSGRPI 

       130        140        150        160        170        180 
DNGPKVFAED YLDINGSPIN PYARIYPEEM ISTGVSAIDT MNSIARGQKI PIFSASGLPH 

       190        200        210        220        230        240 
NEIAAQICRQ AGLVRPTKDV HDGHEENFSI VFAAMGVNLE TARFFKQDFE ENGSLERTSL 

       250        260        270        280        290        300 
FLNLANDPTI ERIITPRLAL TTAEYLAYQT ERHVLTILTD MSSYADALRE VSAAREEVPG 

       310        320        330        340        350        360 
RRGYPGYMYT DLSTIYERAG RVEGRNGSIT QIPILTMPND DITHPIPDLT GYITEGQIFV 

       370        380        390        400        410        420 
DRQLHNKGIY PPINVLPSLS RLMKSAIGEG MTRKDHGDVS NQLYAKYAIG KDAAAMKAVV 

       430        440        450        460        470        480 
GEEALSIEDK LSLEFLEKFE KTFITQGAYE DRTVFESLDQ AWSLLRIYPK EMLNRISPKI 

       490        500        510 
LDEFYDRARD DADEDEEDPD TRSSGKKKDA SQEESLI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB42254.
S45996.
RefSeqNP_009685.3. NM_001178475.3.

3D structure databases

ProteinModelPortalP16140.
SMRP16140. Positions 27-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32828. 140 interactions.
DIPDIP-2292N.
IntActP16140. 516 interactions.
MINTMINT-563511.
STRING4932.YBR127C.

Chemistry

ChEMBLCHEMBL6106.

Protein family/group databases

TCDB3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

MaxQBP16140.
PaxDbP16140.
PeptideAtlasP16140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR127C; YBR127C; YBR127C.
GeneID852424.
KEGGsce:YBR127C.

Organism-specific databases

CYGDYBR127c.
SGDS000000331. VMA2.

Phylogenomic databases

eggNOGCOG1156.
GeneTreeENSGT00550000074724.
HOGENOMHOG000165320.
KOK02147.
OMAGFKIKPR.
OrthoDBEOG7H79BK.

Enzyme and pathway databases

BioCycYEAST:G3O-29082-MONOMER.

Gene expression databases

GenevestigatorP16140.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00310. ATP_synth_B_arch.
InterProIPR020003. 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]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971294.
PROP16140.

Entry information

Entry nameVATB_YEAST
AccessionPrimary (citable) accession number: P16140
Secondary accession number(s): D6VQC4, P32123
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families