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UniProtKB - Q05521 (DPP1_YEAST)

Entry version 170 (25 May 2022)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

Diacylglycerol pyrophosphate phosphatase 1

Gene

DPP1

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

Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with LPP1, regulates intracellular DGPP and PA levels, which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. Substrate preference is DGPP > LPA > PA. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.

5 Publications

Miscellaneous

Present with 3038 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 sodium fluoride (NaF) and pyrophosphate. Strongly inhibited by manganese ion and, to a lower extent, by magnesium and calcium ions. Also inhibited by Cu2+ ion. In an indirect manner, it is also inhibited by the zinc ion which is able to form a complex with DGPP and prevent the enzyme from removing the phosphate from the substrate. Not inhibited by N-ethylmaleimide.2 Publications

<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. Vmax=167 µmol/min/mg enzyme with lysophosphatidic acid as substrate1 Publication

pH dependencei

Optimum pH is 6.0-8.5 (PubMed:8940025). Optimum pH for geranylgeranyl-P-P phosphatase reaction is 5.0-5.5 (PubMed:10329682).2 Publications

<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

  • phospholipid metabolic process Source: SGD
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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.3.81, 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-1660661, Sphingolipid de novo biosynthesis
R-SCE-2029485, Role of phospholipids in phagocytosis
R-SCE-419408, Lysosphingolipid and LPA receptors

Protein family/group databases

Transport Classification Database

More...TCDBi		9.B.105.3.2, the lead resistance fusion protein (pbrbc) family

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000057

<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:
Diacylglycerol pyrophosphate phosphatase 12 Publications (EC:3.1.3.81)
Short name:
DGPP phosphatase
Alternative name(s):
Lysophosphatidate phosphatase (EC:3.1.3.106)
Phosphatidate phosphatase (EC:3.1.3.4)
<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:DPP1
Synonyms:ZRG1
Ordered Locus Names:YDR284C
<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 IV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000002692, DPP1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YDR284C

<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

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 domaini1 – 21VacuolarSequence analysisAdd BLAST21
<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>Transmembranei22 – 42Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini43 – 65CytoplasmicSequence analysisAdd BLAST23
Transmembranei66 – 86Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini87 – 92VacuolarSequence analysis6
Transmembranei93 – 113Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini114 – 172CytoplasmicSequence analysisAdd BLAST59
Transmembranei173 – 193Helical; Name=4Sequence analysisAdd BLAST21
Transmembranei194 – 214Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini215 – 222CytoplasmicSequence analysis8
Transmembranei223 – 243Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini244 – 289VacuolarSequence analysisAdd BLAST46

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>Mutagenesisi125R → A: Complete loss of DGPP phosphatase activity. 1 Publication1
Mutagenesisi169H → A: 91% decrease of DGPP phosphatase activity. 1 Publication1
Mutagenesisi223H → A: Complete loss of DGPP phosphatase 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_00002209181 – 289Diacylglycerol pyrophosphate phosphatase 1Add BLAST289

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 residuei285PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q05521

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

More...PaxDbi		Q05521

PRoteomics IDEntifications database

More...PRIDEi		Q05521

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q05521

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q05521

<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

Induced by the transcription factor ZAP1 during zinc depletion and negatively regulated by the transcription factor GIS1 predominantly during nutrient limitation. Induced by inositol supplementation.3 Publications

<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 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

Q05521
With#Exp.IntAct
itself3EBI-2054360,EBI-2054360

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		32337, 65 interactors

Database of interacting proteins

More...DIPi		DIP-8807N

Protein interaction database and analysis system

More...IntActi		Q05521, 11 interactors

Molecular INTeraction database

More...MINTi		Q05521

STRING: functional protein association networks

More...STRINGi		4932.YDR284C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q05521, 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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q05521

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

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

<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>Regioni118 – 126Phosphatase sequence motif I9
Regioni166 – 169Phosphatase sequence motif II4
Regioni216 – 227Phosphatase sequence motif IIIAdd BLAST12

<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 phosphatase sequence motif I (including Arg-125) and II (including His-169) are part of the cytoplasmic loop 2 and phosphatase sequence motif III (including His-223) is part of the cytoplasmic loop 3.

<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 PA-phosphatase related phosphoesterase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3030, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000174574

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021458_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q05521

Identification of Orthologs from Complete Genome Data

More...OMAi		CTPLIVI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036938, P_Acid_Pase_2/haloperoxi_sf
IPR000326, P_Acid_Pase_2/haloperoxidase
IPR043216, PA_PP_rel

The PANTHER Classification System

More...PANTHERi		PTHR10165, PTHR10165, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01569, PAP2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00014, acidPPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48317, SSF48317, 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.

Q05521-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL 
        60         70         80         90        100
TISHPYATTE RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL 
       110        120        130        140        150
LGLSLAWFST SFFTNFIKNW IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC 
       160        170        180        190        200
TTKNHERLLD GFRTTPSGHS SESFAGLGYL YFWLCGQLLT ESPLMPLWRK 
       210        220        230        240        250
MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH FFYRRIFPPI 
       260        270        280 
DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM
Length:289
Mass (Da):33,514
Last modified:November 1, 1996 - 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:i9CBEA0D7A0F0E13A
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
U51031 Genomic DNA Translation: AAB64475.1
AY557744 Genomic DNA Translation: AAS56070.1
BK006938 Genomic DNA Translation: DAA12124.1

Protein sequence database of the Protein Information Resource

More...PIRi		S70114

NCBI Reference Sequences

More...RefSeqi		NP_010570.1, NM_001180592.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YDR284C_mRNA; YDR284C; YDR284C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		851878

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YDR284C

<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
U51031 Genomic DNA Translation: AAB64475.1
AY557744 Genomic DNA Translation: AAS56070.1
BK006938 Genomic DNA Translation: DAA12124.1
PIRiS70114
RefSeqiNP_010570.1, NM_001180592.1

3D structure databases

AlphaFoldDBiQ05521
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...

Protein-protein interaction databases

BioGRIDi32337, 65 interactors
DIPiDIP-8807N
IntActiQ05521, 11 interactors
MINTiQ05521
STRINGi4932.YDR284C

Chemistry databases

SwissLipidsiSLP:000000057

Protein family/group databases

TCDBi9.B.105.3.2, the lead resistance fusion protein (pbrbc) family

PTM databases

iPTMnetiQ05521

Proteomic databases

MaxQBiQ05521
PaxDbiQ05521
PRIDEiQ05521
TopDownProteomicsiQ05521

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		851878

Genome annotation databases

EnsemblFungiiYDR284C_mRNA; YDR284C; YDR284C
GeneIDi851878
KEGGisce:YDR284C

Organism-specific databases

SGDiS000002692, DPP1
VEuPathDBiFungiDB:YDR284C

Phylogenomic databases

eggNOGiKOG3030, Eukaryota
GeneTreeiENSGT00940000174574
HOGENOMiCLU_021458_6_1_1
InParanoidiQ05521
OMAiCTPLIVI

Enzyme and pathway databases

BRENDAi3.1.3.81, 984
ReactomeiR-SCE-1660661, Sphingolipid de novo biosynthesis
R-SCE-2029485, Role of phospholipids in phagocytosis
R-SCE-419408, Lysosphingolipid and LPA receptors

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q05521
RNActiQ05521, protein

Family and domain databases

InterProiView protein in InterPro
IPR036938, P_Acid_Pase_2/haloperoxi_sf
IPR000326, P_Acid_Pase_2/haloperoxidase
IPR043216, PA_PP_rel
PANTHERiPTHR10165, PTHR10165, 1 hit
PfamiView protein in Pfam
PF01569, PAP2, 1 hit
SMARTiView protein in SMART
SM00014, acidPPc, 1 hit
SUPFAMiSSF48317, SSF48317, 1 hit

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 nameiDPP1_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: Q05521
Secondary accession number(s): D6VSR4
<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 11, 2004
Last sequence update: November 1, 1996
Last modified: May 25, 2022
This is version 170 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
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