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Entry version 173 (07 Oct 2020)
Sequence version 1 (01 Feb 1995)
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Protein

NADPH-dependent 1-acyldihydroxyacetone phosphate reductase

Gene

AYR1

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

Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA) (PubMed:1512203, PubMed:10617610). Also has triacylglycerol (TAG) lipase activity. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs (PubMed:24187129). Required for spore germination (PubMed:10617610). Plays a role in cell wall biogenesis, but this effect may be indirect by affecting the activities of cell wall synthesis enzymes (PubMed:23956635). Lipolysis of TAG by AYR1 is essential for starvation-induced autophagy (PubMed:26162625). Forms an NADPH-regulated cation-selective channel in the mitochondrial outer membrane (PubMed:28916712).6 Publications

Miscellaneous

Present with 3671 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by divalent cations and N-ethylmaleimide. Activity is reduced under anaerobic growth conditions.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=20 µM for NADPH1 Publication
  2. KM=15 µM for hexadecyl dihydroxyacetone-phosphate1 Publication
  3. KM=3.5 mM for p-nitrophenylacetate1 Publication
  4. KM=1.52 mM for p-nitrophenylbutyrate1 Publication
  5. KM=61.21 µM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol1 Publication
  1. Vmax=3.8 nmol/min/mg enzyme for hexadecyl dihydroxyacetone-phosphate1 Publication
  2. Vmax=18.5 µmol/min/mg enzyme for p-nitrophenylacetate1 Publication
  3. Vmax=14.06 µmol/min/mg enzyme for p-nitrophenylbutyrate1 Publication
  4. Vmax=10.93 pmol/h/mg enzyme for 1,2,3-tri-(9Z-octadecenoyl)-glycerol1 Publication

pH dependencei

Optimum pH is 6.7-7.2.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Thermostable for 10 min up to 45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei18Nucleophile; for lipase activity1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei144SubstrateBy similarity1
Active sitei157Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi13 – 21NADBy similarity9
Nucleotide bindingi63 – 65NADBy similarity3
Nucleotide bindingi157 – 161NADBy similarity5
Nucleotide bindingi190 – 192NADBy similarity3

<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

Molecular functionHydrolase, Oxidoreductase
Biological processLipid degradation, Lipid metabolism
LigandNAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YIL124W-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P40471

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.115.1.1, the pore-forming nadph-dependent 1-acyldihydroxyacetone phosphate reductase (ayr1) family

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000056

<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:
NADPH-dependent 1-acyldihydroxyacetone phosphate reductase1 Publication (EC:1.1.1.1011 Publication)
Short name:
ADR
Alternative name(s):
1-acyl DHAP reductase
Acyl/alkyl DHAP reductase
Acylglycerone-phosphate reductase
Triacylglycerol lipase AYR11 Publication (EC:3.1.1.31 Publication)
Short name:
TAG lipase
<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:AYR11 Publication
Synonyms:GBG11 Publication
Ordered Locus Names:YIL124W
<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 IX

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YIL124W

Saccharomyces Genome Database

More...
SGDi
S000001386, AYR1

<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

Endoplasmic reticulum, Lipid droplet, Membrane, Mitochondrion, Mitochondrion outer membrane

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Reduces the activities of beta-1,3-glucan synthase and chitin synthase III, while increasing chitin synthase I and II activities. Shows altered cell wall composition as well as susceptibility towards cell wall inhibitors such as zymolyase, calcofluor white, and nikkomycin Z.1 Publication

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>Mutagenesisi18S → A: Completely abolishes lipase activity. 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 '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_00000545201 – 297NADPH-dependent 1-acyldihydroxyacetone phosphate reductaseAdd BLAST297

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P40471

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

More...
PaxDbi
P40471

PRoteomics IDEntifications database

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PRIDEi
P40471

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P40471

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed during vegetative growth with a maximum level of transcription at G1 phase, after which it is decreased during the remainder of the cell cycle.1 Publication

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
34867, 139 interactors

Database of interacting proteins

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DIPi
DIP-4614N

Protein interaction database and analysis system

More...
IntActi
P40471, 11 interactors

Molecular INTeraction database

More...
MINTi
P40471

STRING: functional protein association networks

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STRINGi
4932.YIL124W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P40471, protein

<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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi16 – 20GXSXG1 Publication5

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1209, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154593

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010194_2_9_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P40471

KEGG Orthology (KO)

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KOi
K06123

Identification of Orthologs from Complete Genome Data

More...
OMAi
WDVDILL

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036291, NAD(P)-bd_dom_sf
IPR020904, Sc_DH/Rdtase_CS
IPR002347, SDR_fam

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00106, adh_short, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00081, GDHRDH
PR00080, SDRFAMILY

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735, SSF51735, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00061, ADH_SHORT, 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.

P40471-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSELQSQPKK IAVVTGASGG IGYEVTKELA RNGYLVYACA RRLEPMAQLA
60 70 80 90 100
IQFGNDSIKP YKLDISKPEE IVTFSGFLRA NLPDGKLDLL YNNAGQSCTF
110 120 130 140 150
PALDATDAAV EQCFKVNVFG HINMCRELSE FLIKAKGTIV FTGSLAGVVS
160 170 180 190 200
FPFGSIYSAS KAAIHQYARG LHLEMKPFNV RVINAITGGV ATDIADKRPL
210 220 230 240 250
PETSIYNFPE GREAFNSRKT MAKDNKPMPA DAYAKQLVKD ILSTSDPVDV
260 270 280 290
YRGTFANIMR FVMIFVPYWL LEKGLSKKFK LDKVNNALKS KQKNKDD
Length:297
Mass (Da):32,814
Last modified:February 1, 1995 - v1
<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:iB614C0E0B1FB0CE0
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
Z46833 Genomic DNA Translation: CAA86868.1
BK006942 Genomic DNA Translation: DAA08429.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S49885

NCBI Reference Sequences

More...
RefSeqi
NP_012142.3, NM_001179472.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YIL124W_mRNA; YIL124W; YIL124W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854682

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YIL124W

<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
Z46833 Genomic DNA Translation: CAA86868.1
BK006942 Genomic DNA Translation: DAA08429.1
PIRiS49885
RefSeqiNP_012142.3, NM_001179472.3

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi34867, 139 interactors
DIPiDIP-4614N
IntActiP40471, 11 interactors
MINTiP40471
STRINGi4932.YIL124W

Chemistry databases

SwissLipidsiSLP:000000056

Protein family/group databases

TCDBi1.A.115.1.1, the pore-forming nadph-dependent 1-acyldihydroxyacetone phosphate reductase (ayr1) family

PTM databases

iPTMnetiP40471

Proteomic databases

MaxQBiP40471
PaxDbiP40471
PRIDEiP40471

Genome annotation databases

EnsemblFungiiYIL124W_mRNA; YIL124W; YIL124W
GeneIDi854682
KEGGisce:YIL124W

Organism-specific databases

EuPathDBiFungiDB:YIL124W
SGDiS000001386, AYR1

Phylogenomic databases

eggNOGiKOG1209, Eukaryota
GeneTreeiENSGT00940000154593
HOGENOMiCLU_010194_2_9_1
InParanoidiP40471
KOiK06123
OMAiWDVDILL

Enzyme and pathway databases

BioCyciMetaCyc:YIL124W-MONOMER
SABIO-RKiP40471

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P40471
RNActiP40471, protein

Family and domain databases

InterProiView protein in InterPro
IPR036291, NAD(P)-bd_dom_sf
IPR020904, Sc_DH/Rdtase_CS
IPR002347, SDR_fam
PfamiView protein in Pfam
PF00106, adh_short, 1 hit
PRINTSiPR00081, GDHRDH
PR00080, SDRFAMILY
SUPFAMiSSF51735, SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061, ADH_SHORT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiAYR1_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: P40471
Secondary accession number(s): D6VVG3
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 7, 2020
This is version 173 of the entry and version 1 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

Direct protein sequencing, Reference proteome

Documents

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