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Entry version 204 (12 Aug 2020)
Sequence version 3 (23 Jan 2007)
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Protein

V-type proton ATPase subunit a, vacuolar isoform

Gene

VPH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in vacuolar V-ATPase complexes. Enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.3 Publications

Miscellaneous

Present with 55714 molecules/cell in log phase SD medium.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processHydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-33760-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1222556, ROS and RNS production in phagocytes
R-SCE-6798695, Neutrophil degranulation
R-SCE-77387, Insulin receptor recycling
R-SCE-917977, Transferrin endocytosis and recycling
R-SCE-9639288, Amino acids regulate mTORC1

Protein family/group databases

Transport Classification Database

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
V-type proton ATPase subunit a, vacuolar isoform
Short name:
V-ATPase a 1 subunit
Alternative name(s):
V-ATPase 95 kDa subunit
Vacuolar pH protein 1
Vacuolar proton pump a subunit
Vacuolar proton translocating ATPase subunit a 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VPH1
Ordered Locus Names:YOR270C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOR270C

Saccharomyces Genome Database

More...
SGDi
S000005796, VPH1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 404CytoplasmicSequence analysisAdd BLAST403
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei405 – 423HelicalSequence analysisAdd BLAST19
Topological domaini424 – 425VacuolarSequence analysis2
Transmembranei426 – 442HelicalSequence analysisAdd BLAST17
Topological domaini443 – 456CytoplasmicSequence analysisAdd BLAST14
Transmembranei457 – 486HelicalSequence analysisAdd BLAST30
Topological domaini487 – 534VacuolarSequence analysisAdd BLAST48
Transmembranei535 – 554HelicalSequence analysisAdd BLAST20
Topological domaini555 – 572CytoplasmicSequence analysisAdd BLAST18
Transmembranei573 – 593HelicalSequence analysisAdd BLAST21
Topological domaini594 – 636VacuolarSequence analysisAdd BLAST43
Transmembranei637 – 656HelicalSequence analysisAdd BLAST20
Topological domaini657 – 719CytoplasmicSequence analysisAdd BLAST63
Transmembranei720 – 744HelicalSequence analysisAdd BLAST25
Topological domaini745 – 765VacuolarSequence analysisAdd BLAST21
Transmembranei766 – 804HelicalSequence analysisAdd BLAST39
Topological domaini805 – 840CytoplasmicSequence analysisAdd BLAST36

Keywords - Cellular componenti

Membrane, Vacuole

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi425D → N: Reduces assembly of V-ATPase complexes and reduces ATPase activity of the assembled complexes. 1 Publication1
Mutagenesisi538K → A: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi593K → A: Reduces ATPase activity. 1 Publication1
Mutagenesisi634Q → L: Reduces subunit stability. 1 Publication1
Mutagenesisi729H → R: Reduces ATPase activity. 1 Publication1
Mutagenesisi735R → L: Reduces subunit stability. 1 Publication1
Mutagenesisi739L → S: Reduces ATPase activity. 1 Publication1
Mutagenesisi743H → A, E or Y: Reduces ATPase activity. 2 Publications1
Mutagenesisi746L → S: Reduces ATPase activity. 1 Publication1
Mutagenesisi780L → S: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi789E → A, D, H or Q: Abolishes ATPase activity and proton transport, but does not affect complex assembly. 2 Publications1
Mutagenesisi800L → S: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi802W → R: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi803V → D: Reduces ATPase activity. 1 Publication1
Mutagenesisi803V → F: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi809F → L: Reduces assembly of V-ATPase complexes. 1 Publication1
Mutagenesisi814G → D: Reduces assembly of V-ATPase complexes. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001192242 – 840V-type proton ATPase subunit a, vacuolar isoformAdd BLAST839

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Glycosylated.

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32563

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P32563

PRoteomics IDEntifications database

More...
PRIDEi
P32563

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32563

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
34659, 366 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1193, Vacuolar proton translocating ATPase complex, vacuole variant

Database of interacting proteins

More...
DIPi
DIP-2960N

Protein interaction database and analysis system

More...
IntActi
P32563, 35 interactors

Molecular INTeraction database

More...
MINTi
P32563

STRING: functional protein association networks

More...
STRINGi
4932.YOR270C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32563, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1840
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P32563

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32563

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili117 – 145Sequence analysisAdd BLAST29

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the V-ATPase 116 kDa subunit family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2189, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182881

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_005230_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32563

KEGG Orthology (KO)

More...
KOi
K02154

Identification of Orthologs from Complete Genome Data

More...
OMAi
LIYMFLQ

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002490, V-ATPase_116kDa_su
IPR026028, V-type_ATPase_116kDa_su_euka

The PANTHER Classification System

More...
PANTHERi
PTHR11629, PTHR11629, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01496, V_ATPase_I, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001293, ATP6V0A1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P32563-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEKEEAIFR SAEMALVQFY IPQEISRDSA YTLGQLGLVQ FRDLNSKVRA
60 70 80 90 100
FQRTFVNEIR RLDNVERQYR YFYSLLKKHD IKLYEGDTDK YLDGSGELYV
110 120 130 140 150
PPSGSVIDDY VRNASYLEER LIQMEDATDQ IEVQKNDLEQ YRFILQSGDE
160 170 180 190 200
FFLKGDNTDS TSYMDEDMID ANGENIAAAI GASVNYVTGV IARDKVATLE
210 220 230 240 250
QILWRVLRGN LFFKTVEIEQ PVYDVKTREY KHKNAFIVFS HGDLIIKRIR
260 270 280 290 300
KIAESLDANL YDVDSSNEGR SQQLAKVNKN LSDLYTVLKT TSTTLESELY
310 320 330 340 350
AIAKELDSWF QDVTREKAIF EILNKSNYDT NRKILIAEGW IPRDELATLQ
360 370 380 390 400
ARLGEMIARL GIDVPSIIQV LDTNHTPPTF HRTNKFTAGF QSICDCYGIA
410 420 430 440 450
QYREINAGLP TIVTFPFMFA IMFGDMGHGF LMTLAALSLV LNEKKINKMK
460 470 480 490 500
RGEIFDMAFT GRYIILLMGV FSMYTGFLYN DIFSKTMTIF KSGWKWPDHW
510 520 530 540 550
KKGESITATS VGTYPIGLDW AWHGTENALL FSNSYKMKLS ILMGFIHMTY
560 570 580 590 600
SYFFSLANHL YFNSMIDIIG NFIPGLLFMQ GIFGYLSVCI VYKWAVDWVK
610 620 630 640 650
DGKPAPGLLN MLINMFLSPG TIDDELYPHQ AKVQVFLLLM ALVCIPWLLL
660 670 680 690 700
VKPLHFKFTH KKKSHEPLPS TEADASSEDL EAQQLISAMD ADDAEEEEVG
710 720 730 740 750
SGSHGEDFGD IMIHQVIHTI EFCLNCVSHT ASYLRLWALS LAHAQLSSVL
760 770 780 790 800
WTMTIQIAFG FRGFVGVFMT VALFAMWFAL TCAVLVLMEG TSAMLHSLRL
810 820 830 840
HWVESMSKFF VGEGLPYEPF AFEYKDMEVA VASASSSASS
Length:840
Mass (Da):95,529
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i77709A914410CD4D
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M89778 Genomic DNA Translation: AAA35211.1
X89633 Genomic DNA Translation: CAA61776.1
Z75178 Genomic DNA Translation: CAA99494.1
Z75179 Genomic DNA Translation: CAA99496.1
BK006948 Genomic DNA Translation: DAA11036.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A42970

NCBI Reference Sequences

More...
RefSeqi
NP_014913.3, NM_001183689.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOR270C_mRNA; YOR270C; YOR270C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854444

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOR270C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89778 Genomic DNA Translation: AAA35211.1
X89633 Genomic DNA Translation: CAA61776.1
Z75178 Genomic DNA Translation: CAA99494.1
Z75179 Genomic DNA Translation: CAA99496.1
BK006948 Genomic DNA Translation: DAA11036.1
PIRiA42970
RefSeqiNP_014913.3, NM_001183689.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JTWNMR-A728-748[»]
2NVJNMR-A721-745[»]
2RPWNMR-X728-748[»]
3J9Telectron microscopy6.90b1-840[»]
3J9Uelectron microscopy7.60b1-840[»]
3J9Velectron microscopy8.30b1-840[»]
5I1Melectron microscopy7.00V383-840[»]
5TJ5electron microscopy3.90A400-829[»]
5VOXelectron microscopy6.80b1-840[»]
5VOYelectron microscopy7.90b1-840[»]
5VOZelectron microscopy7.60b1-840[»]
6C6Lelectron microscopy3.50A1-840[»]
6HH0NMR-A728-748[»]
6O7Telectron microscopy3.20a1-840[»]
6PE4electron microscopy3.10A1-840[»]
6PE5electron microscopy3.20A1-840[»]
SMRiP32563
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34659, 366 interactors
ComplexPortaliCPX-1193, Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-2960N
IntActiP32563, 35 interactors
MINTiP32563
STRINGi4932.YOR270C

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

PTM databases

iPTMnetiP32563

Proteomic databases

MaxQBiP32563
PaxDbiP32563
PRIDEiP32563

Genome annotation databases

EnsemblFungiiYOR270C_mRNA; YOR270C; YOR270C
GeneIDi854444
KEGGisce:YOR270C

Organism-specific databases

EuPathDBiFungiDB:YOR270C
SGDiS000005796, VPH1

Phylogenomic databases

eggNOGiKOG2189, Eukaryota
GeneTreeiENSGT00950000182881
HOGENOMiCLU_005230_0_2_1
InParanoidiP32563
KOiK02154
OMAiLIYMFLQ

Enzyme and pathway databases

BioCyciYEAST:G3O-33760-MONOMER
ReactomeiR-SCE-1222556, ROS and RNS production in phagocytes
R-SCE-6798695, Neutrophil degranulation
R-SCE-77387, Insulin receptor recycling
R-SCE-917977, Transferrin endocytosis and recycling
R-SCE-9639288, Amino acids regulate mTORC1

Miscellaneous databases

EvolutionaryTraceiP32563

Protein Ontology

More...
PROi
PR:P32563
RNActiP32563, protein

Family and domain databases

InterProiView protein in InterPro
IPR002490, V-ATPase_116kDa_su
IPR026028, V-type_ATPase_116kDa_su_euka
PANTHERiPTHR11629, PTHR11629, 2 hits
PfamiView protein in Pfam
PF01496, V_ATPase_I, 1 hit
PIRSFiPIRSF001293, ATP6V0A1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVPH1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32563
Secondary accession number(s): D6W2X0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 204 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

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