Skip Header

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

UniProtKB - P32567 (PAH1_YEAST)

Entry version 171 (07 Apr 2021)
Sequence version 1 (01 Oct 1993)
Previous versions | rss
Add a publicationFeedback
Protein

Phosphatidic acid phosphohydrolase 1

Gene

PAH1

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

Mg2+-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. Required for de novo lipid synthesis and formation of lipid droplets. Controles transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope. Involved in plasmid maintenance, in respiration and in cell proliferation.9 Publications

Miscellaneous

Present with 3910 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<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

Phenylglyoxal and propranolol inhibit activity in dose-dependent manners with IC50 values of 1.3 mM and 0.2 mM, respectively.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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
Biological processLipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:G3O-32855-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-1483191, Synthesis of PC
R-SCE-1483213, Synthesis of PE
R-SCE-4419969, Depolymerisation of the Nuclear Lamina
R-SCE-75109, Triglyceride biosynthesis

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000045

<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:
Phosphatidic acid phosphohydrolase 1 (EC:3.1.3.4)
Short name:
PAP1
Alternative name(s):
Protein SMP2
<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:PAH1
Synonyms:PAP1, SMP2
Ordered Locus Names:YMR165C
ORF Names:YM8520.14C
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000004775, PAH1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YMR165C

<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

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

<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>Mutagenesisi8L → A: Impairs membrane recruitiment; when associated with A-11 and A-15. 1 Publication1
Mutagenesisi11V → A: Impairs membrane recruitiment; when associated with A-8 and A-15. 1 Publication1
Mutagenesisi15W → A: Impairs membrane recruitiment; when associated with A-8 and A-11. 1 Publication1
Mutagenesisi80G → R: Impairs phosphatidate phosphatase activity. 2 Publications1
Mutagenesisi398D → E: Impairs phosphatidate phosphatase activity. 2 Publications1
Mutagenesisi400D → E: Impairs phosphatidate phosphatase activity. 2 Publications1

<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_00002098871 – 862Phosphatidic acid phosphohydrolase 1Add BLAST862

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 residuei110Phosphoserine1 Publication1
Modified residuei114Phosphoserine1 Publication1
Modified residuei168Phosphoserine1 Publication1
Modified residuei511PhosphoserineCombined sources1
Modified residuei602Phosphoserine; by CDC28Combined sources2 Publications1
Modified residuei723Phosphothreonine; by CDC282 Publications1
Modified residuei744Phosphoserine; by CDC28Combined sources2 Publications1
Modified residuei748PhosphoserineCombined sources1 Publication1
Modified residuei773PhosphoserineCombined sources1
Modified residuei774PhosphoserineCombined sources1
Modified residuei810PhosphoserineCombined sources1
Modified residuei814PhosphoserineCombined sources1
Modified residuei816PhosphothreonineCombined sources1
Modified residuei844PhosphoserineCombined sources1
Modified residuei847PhosphoserineCombined sources1

<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

Phosphorylated by CDC28 at the onset of mitosis, and dephosphorylated by the NEM1-SPO7 complex. Phosphorylation regulates recruitment on promoters of lipid biosynthetic enzymes.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P32567

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

More...PaxDbi		P32567

PRoteomics IDEntifications database

More...PRIDEi		P32567

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P32567

<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		35343, 221 interactors

Database of interacting proteins

More...DIPi		DIP-1454N

Protein interaction database and analysis system

More...IntActi		P32567, 10 interactors

Molecular INTeraction database

More...MINTi		P32567

STRING: functional protein association networks

More...STRINGi		4932.YMR165C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P32567, 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

3D structure databases

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

More...SMRi		P32567

Database of comparative protein structure models

More...ModBasei		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>Regioni19 – 104N-LIPAdd BLAST86

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>Motifi398 – 402DXDXT motif5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal amphipathic helix (residues 1 to 18) is involved in the membrane recruitment.1 Publication
Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity.1 Publication

<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 lipin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2116, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000168260

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002546_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P32567

Identification of Orthologs from Complete Genome Data

More...OMAi		MACLNDI

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036412, HAD-like_sf
IPR023214, HAD_sf
IPR026058, LIPIN
IPR007651, Lipin_N
IPR013209, LNS2
IPR031315, LNS2/PITP

The PANTHER Classification System

More...PANTHERi		PTHR12181, PTHR12181, 2 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04571, Lipin_N, 1 hit
PF08235, LNS2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00775, LNS2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56784, SSF56784, 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.

P32567-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQYVGRALGS VSKTWSSINP ATLSGAIDVI VVEHPDGRLS CSPFHVRFGK 
        60         70         80         90        100
FQILKPSQKK VQVFINEKLS NMPMKLSDSG EAYFVFEMGD QVTDVPDELL 
       110        120        130        140        150
VSPVMSATSS PPQSPETSIL EGGTEGEGEG ENENKKKEKK VLEEPDFLDI 
       160        170        180        190        200
NDTGDSGSKN SETTGSLSPT ESSTTTPPDS VEERKLVEQR TKNFQQKLNK 
       210        220        230        240        250
KLTEIHIPSK LDNNGDLLLD TEGYKPNKNM MHDTDIQLKQ LLKDEFGNDS 
       260        270        280        290        300
DISSFIKEDK NGNIKIVNPY EHLTDLSPPG TPPTMATSGS VLGLDAMESG 
       310        320        330        340        350
STLNSLSSSP SGSDTEDETS FSKEQSSKSE KTSKKGTAGS GETEKRYIRT 
       360        370        380        390        400
IRLTNDQLKC LNLTYGENDL KFSVDHGKAI VTSKLFVWRW DVPIVISDID 
       410        420        430        440        450
GTITKSDALG HVLAMIGKDW THLGVAKLFS EISRNGYNIL YLTARSAGQA 
       460        470        480        490        500
DSTRSYLRSI EQNGSKLPNG PVILSPDRTM AALRREVILK KPEVFKIACL 
       510        520        530        540        550
NDIRSLYFED SDNEVDTEEK STPFFAGFGN RITDALSYRT VGIPSSRIFT 
       560        570        580        590        600
INTEGEVHME LLELAGYRSS YIHINELVDH FFPPVSLDSV DLRTNTSMVP 
       610        620        630        640        650
GSPPNRTLDN FDSEITSGRK TLFRGNQEEK FTDVNFWRDP LVDIDNLSDI 
       660        670        680        690        700
SNDDSDNIDE DTDVSQQSNI SRNRANSVKT AKVTKAPQRN VSGSTNNNEV 
       710        720        730        740        750
LAASSDVENA SDLVSSHSSS GSTPNKSTMS KGDIGKQIYL ELGSPLASPK 
       760        770        780        790        800
LRYLDDMDDE DSNYNRTKSR RASSAAATSI DKEFKKLSVS KAGAPTRIVS 
       810        820        830        840        850
KINVSNDVHS LGNSDTESRR EQSVNETGRN QLPHNSMDDK DLDSRVSDEF 
       860 
DDDEFDEDEF ED
Length:862
Mass (Da):95,031
Last modified:October 1, 1993 - 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:i28132EED1906ACBD
GO

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
D01095 Genomic DNA Translation: BAA00880.1
Z49705 Genomic DNA Translation: CAA89801.1
BK006946 Genomic DNA Translation: DAA10061.1

Protein sequence database of the Protein Information Resource

More...PIRi		S30911

NCBI Reference Sequences

More...RefSeqi		NP_013888.1, NM_001182669.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YMR165C_mRNA; YMR165C; YMR165C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		855201

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YMR165C

<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
D01095 Genomic DNA Translation: BAA00880.1
Z49705 Genomic DNA Translation: CAA89801.1
BK006946 Genomic DNA Translation: DAA10061.1
PIRiS30911
RefSeqiNP_013888.1, NM_001182669.1

3D structure databases

SMRiP32567
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35343, 221 interactors
DIPiDIP-1454N
IntActiP32567, 10 interactors
MINTiP32567
STRINGi4932.YMR165C

Chemistry databases

SwissLipidsiSLP:000000045

PTM databases

iPTMnetiP32567

Proteomic databases

MaxQBiP32567
PaxDbiP32567
PRIDEiP32567

Genome annotation databases

EnsemblFungiiYMR165C_mRNA; YMR165C; YMR165C
GeneIDi855201
KEGGisce:YMR165C

Organism-specific databases

SGDiS000004775, PAH1
VEuPathDBiFungiDB:YMR165C

Phylogenomic databases

eggNOGiKOG2116, Eukaryota
GeneTreeiENSGT00940000168260
HOGENOMiCLU_002546_3_1_1
InParanoidiP32567
OMAiMACLNDI

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32855-MONOMER
ReactomeiR-SCE-1483191, Synthesis of PC
R-SCE-1483213, Synthesis of PE
R-SCE-4419969, Depolymerisation of the Nuclear Lamina
R-SCE-75109, Triglyceride biosynthesis

Miscellaneous databases

Protein Ontology

More...PROi		PR:P32567
RNActiP32567, protein

Family and domain databases

Gene3Di3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR036412, HAD-like_sf
IPR023214, HAD_sf
IPR026058, LIPIN
IPR007651, Lipin_N
IPR013209, LNS2
IPR031315, LNS2/PITP
PANTHERiPTHR12181, PTHR12181, 2 hits
PfamiView protein in Pfam
PF04571, Lipin_N, 1 hit
PF08235, LNS2, 1 hit
SMARTiView protein in SMART
SM00775, LNS2, 1 hit
SUPFAMiSSF56784, SSF56784, 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 nameiPAH1_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: P32567
Secondary accession number(s): D6VZY7
<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: October 1, 1993
Last modified: April 7, 2021
This is version 171 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

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again