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Entry version 185 (08 May 2019)
Sequence version 4 (23 Jan 2007)
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Protein

V-type proton ATPase subunit E

Gene

VMA4

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 peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Miscellaneous

Present with 16134 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

  • proton-transporting ATPase activity, rotational mechanism Source: SGD

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-33808-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1222556 ROS and RNS production in phagocytes
R-SCE-77387 Insulin receptor recycling

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_and_taxonomy_section">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 E
Short name:
V-ATPase subunit E
Alternative name(s):
V-ATPase 27 kDa subunit
Vacuolar proton pump subunit E
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:VMA4
Synonyms:VAT5
Ordered Locus Names:YOR332W
ORF Names:O6241
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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:YOR332W

Saccharomyces Genome Database

More...
SGDi
S000005859 VMA4

<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

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_and_biotech_section">'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>Mutagenesisi2S → A: Reduces ATPase activity by 11%. 1 Publication1
Mutagenesisi6T → A: Reduces ATPase activity by 73%. 1 Publication1
Mutagenesisi9T → A: Increases ATPase activity 1.4-fold. 1 Publication1
Mutagenesisi78S → A: Reduces ATPase activity by 88%. Prevents assembly of V1 subunits at the membrane. 1 Publication1
Mutagenesisi145D → G in VMA4-1; is rapidly degraded at 37 degrees Celsius. 1 Publication1
Mutagenesisi160Y → A: Reduces ATPase activity by 22%. 1 Publication1
Mutagenesisi202T → A: Increases ATPase activity 2.1-fold by increasing Vmax for ATP hydrolysis 2-fold. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-233. 1 Publication1
Mutagenesisi230K → A: Increases ATPase activity 1.3-fold. 1 Publication1
Mutagenesisi233D → A: Reduces ATPase activity by 74%. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-202. 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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001173102 – 233V-type proton ATPase subunit EAdd BLAST232

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-acetylserineCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22203

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

More...
PaxDbi
P22203

PRoteomics IDEntifications database

More...
PRIDEi
P22203

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P22203

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P22203

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22203

<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_section">'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_section">'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). VMA4 forms a homodimer within this complex and interacts directly with VMA5 and VMA10. Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34716, 88 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant

Database of interacting proteins

More...
DIPi
DIP-4595N

Protein interaction database and analysis system

More...
IntActi
P22203, 26 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YOR332W

<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

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2KZ9NMR-A1-69[»]
3J9Telectron microscopy6.90G/I/K1-233[»]
3J9Uelectron microscopy7.60G/I/K1-233[»]
3J9Velectron microscopy8.30G/I/K1-233[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
5BW9X-ray7.00I/K/M/i/k/m1-233[»]
5D80X-ray6.20I/K/M/i/k/m1-233[»]
5VOXelectron microscopy6.80G/I/K1-233[»]
5VOYelectron microscopy7.90G/I/K1-233[»]
5VOZelectron microscopy7.60G/I/K1-233[»]

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

More...
SMRi
P22203

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni8 – 20Interaction with VMA51 PublicationAdd BLAST13
Regioni19 – 38Interaction with VMA101 PublicationAdd BLAST20

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 coili15 – 45Sequence analysisAdd BLAST31

<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 E subunit family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000002730

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000202506

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22203

KEGG Orthology (KO)

More...
KOi
K02150

Identification of Orthologs from Complete Genome Data

More...
OMAi
TIRCRKQ

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.2320.30, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00311 ATP_synth_E_arch, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038495 ATPase_E_C
IPR002842 ATPase_V1_Esu

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01991 vATP-synt_E, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P22203-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSAITALTP NQVNDELNKM QAFIRKEAEE KAKEIQLKAD QEYEIEKTNI
60 70 80 90 100
VRNETNNIDG NFKSKLKKAM LSQQITKSTI ANKMRLKVLS AREQSLDGIF
110 120 130 140 150
EETKEKLSGI ANNRDEYKPI LQSLIVEALL KLLEPKAIVK ALERDVDLIE
160 170 180 190 200
SMKDDIMREY GEKAQRAPLE EIVISNDYLN KDLVSGGVVV SNASDKIEIN
210 220 230
NTLEERLKLL SEEALPAIRL ELYGPSKTRK FFD
Length:233
Mass (Da):26,471
Last modified:January 23, 2007 - v4
<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:i7AC5169FF7E5A39C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti97 – 98DG → ER in AAA35209 (PubMed:2145285).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M60663 Genomic DNA Translation: AAA35209.1
Z49821 Genomic DNA Translation: CAA89978.1
Z75239 Genomic DNA Translation: CAA99654.1
BK006948 Genomic DNA Translation: DAA11094.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S62063

NCBI Reference Sequences

More...
RefSeqi
NP_014977.3, NM_001183752.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOR332W_mRNA; YOR332W_mRNA; YOR332W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854509

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOR332W

<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
M60663 Genomic DNA Translation: AAA35209.1
Z49821 Genomic DNA Translation: CAA89978.1
Z75239 Genomic DNA Translation: CAA99654.1
BK006948 Genomic DNA Translation: DAA11094.1
PIRiS62063
RefSeqiNP_014977.3, NM_001183752.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KZ9NMR-A1-69[»]
3J9Telectron microscopy6.90G/I/K1-233[»]
3J9Uelectron microscopy7.60G/I/K1-233[»]
3J9Velectron microscopy8.30G/I/K1-233[»]
4DL0X-ray2.90E/J1-233[»]
4EFAX-ray2.82E1-233[»]
5BW9X-ray7.00I/K/M/i/k/m1-233[»]
5D80X-ray6.20I/K/M/i/k/m1-233[»]
5VOXelectron microscopy6.80G/I/K1-233[»]
5VOYelectron microscopy7.90G/I/K1-233[»]
5VOZelectron microscopy7.60G/I/K1-233[»]
SMRiP22203
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34716, 88 interactors
ComplexPortaliCPX-1192 Vacuolar proton translocating ATPase complex, Golgi variant
CPX-1193 Vacuolar proton translocating ATPase complex, vacuole variant
DIPiDIP-4595N
IntActiP22203, 26 interactors
STRINGi4932.YOR332W

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

iPTMnetiP22203

2D gel databases

SWISS-2DPAGEiP22203

Proteomic databases

MaxQBiP22203
PaxDbiP22203
PRIDEiP22203
TopDownProteomicsiP22203

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR332W_mRNA; YOR332W_mRNA; YOR332W
GeneIDi854509
KEGGisce:YOR332W

Organism-specific databases

EuPathDBiFungiDB:YOR332W
SGDiS000005859 VMA4

Phylogenomic databases

GeneTreeiENSGT00390000002730
HOGENOMiHOG000202506
InParanoidiP22203
KOiK02150
OMAiTIRCRKQ

Enzyme and pathway databases

BioCyciYEAST:G3O-33808-MONOMER
ReactomeiR-SCE-1222556 ROS and RNS production in phagocytes
R-SCE-77387 Insulin receptor recycling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22203

Family and domain databases

Gene3Di3.30.2320.30, 1 hit
HAMAPiMF_00311 ATP_synth_E_arch, 1 hit
InterProiView protein in InterPro
IPR038495 ATPase_E_C
IPR002842 ATPase_V1_Esu
PfamiView protein in Pfam
PF01991 vATP-synt_E, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiVATE_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: P22203
Secondary accession number(s): D6W328
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 185 of the entry and version 4 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, Complete proteome, 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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