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Entry version 168 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Endopolyphosphatase

Gene

PPN1

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 hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths both by cleaving phosphate from the chain end and by fragmenting long-chain polymers into shorter ones. The limited digestion products are 1 and 3 P(i) residues (PubMed:11102525, PubMed:11447286, PubMed:15170373, PubMed:15342119, PubMed:15792812, PubMed:8900207, Ref. 16).

Also releases phosphate from dATP. dATP phosphohydrolase activity is about 7-fold lower than the exopolyphosphatase activity (Ref. 16).

7 Publications

Miscellaneous

Inactivation of PPN1 leads to the inhibition of expression of both exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1.
Present with 319 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Mn2+1 Publication, Mg2+1 Publication, Co2+1 PublicationNote: Divalent metal cations. Exopolyphosphatase activity is predominant in the presence of Co2+, while endopolyphosphatase activity is predominant in the presence of Mg2+ (PubMed:8900207, PubMed:25742176). Co2+ is more effective than Mn2+ for dATP phosphohydrolase activity (Ref.16).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 heparin and EDTA.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=185 nM for polyP(750)1 Publication
  2. KM=3.5 µM for polyP(208)1 Publication
  3. KM=75 µM for polyP(15)1 Publication
  4. KM=1100 µM for polyP31 Publication
  5. KM=0.88 mM for dATP1 Publication

pH dependencei

Optimum pH is about 7.5.1 Publication

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

GO - Biological processi

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

Molecular functionHydrolase
LigandMetal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.1.10, 984
3.6.1.11, 984

<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:
Endopolyphosphatase1 Publication (EC:3.6.1.101 Publication)
Alternative name(s):
Deoxyadenosine triphosphate phosphohydrolase1 Publication (EC:3.6.1.-1 Publication)
Short name:
dATP phosphohydrolase1 Publication
Exopolyphosphatase (EC:3.6.1.111 Publication)
Phosphate metabolism protein 51 Publication
<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:PPN11 Publication
Synonyms:PHM51 Publication
Ordered Locus Names:YDR452WImported
ORF Names:D9461.37
<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 IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002860, PPN1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDR452W

<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_location_section">'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 – 21CytoplasmicSequence analysisAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini43 – 674VacuolarSequence analysisAdd BLAST632

Keywords - Cellular componenti

Cytoplasm, 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>Mutagenesisi6K → R or G: Causes accumulation in vacuoles and abolishes sorting into internal vesicles in late endosomes. 1 Publication1
Mutagenesisi11N → A: Abolishes enzyme activity; when associated with A-505 and A-511. 1 Publication1
Mutagenesisi505N → A: Abolishes enzyme activity; when associated with A-11 and A-511. 1 Publication1
Mutagenesisi511N → A: Abolishes enzyme activity; when associated with A-11 and A-505. 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 describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000220891 – 83Removed in mature form1 PublicationAdd BLAST83
<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_000002209084 – 384EndopolyphosphataseAdd BLAST301
PropeptideiPRO_0000022091385 – 674Removed in mature form1 PublicationAdd BLAST290

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi58N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi505N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi511N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Processing by proteases in the vacuole is required for activation.1 Publication
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 and RSP5 are required for ubiquitination. Other cytoplasmic Lys residues than Lys-6 may also be ubiquitinated.1 Publication
N-glycosylated (Probable). N-glycosylation is essential for the protease-mediated maturation.Curated1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Ubl conjugation, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q04119

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

More...
PaxDbi
Q04119

PRoteomics IDEntifications database

More...
PRIDEi
Q04119

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q04119

<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

Homotetramer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
32507, 67 interactors

Database of interacting proteins

More...
DIPi
DIP-2584N

Protein interaction database and analysis system

More...
IntActi
Q04119, 13 interactors

Molecular INTeraction database

More...
MINTi
Q04119

STRING: functional protein association networks

More...
STRINGi
4932.YDR452W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q04119, 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
Q04119

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>Regioni384 – 403DisorderedSequence analysisAdd BLAST20

<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 transmembrane domain contains polar residues that mediate the recognition by TUL1.1 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 endopolyphosphatase PPN1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3770, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183182

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013424_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q04119

Identification of Orthologs from Complete Genome Data

More...
OMAi
TFGNNDI

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00842, MPP_ASMase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041805, ASMase/PPN1_MPP
IPR004843, Calcineurin-like_PHP_ApaH
IPR012358, EndopolyPtase_N1
IPR029052, Metallo-depent_PP-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00149, Metallophos, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF027093, EndopolyPtase_N1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56300, SSF56300, 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>. 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_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.

Q04119-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVVVGKSEVR NVSMSRPKKK SLIAILSTCV LFFLVFIIGA KFQYVSVFSK
60 70 80 90 100
FLDDRGDNES LQLLNDIEFT RLGLTPREPV IIKDVKTGKE RKLHGRFLHI
110 120 130 140 150
TDIHPDPYYV EGSSIDAVCH TGKPSKKKDV APKFGKAMSG CDSPVILMEE
160 170 180 190 200
TLRWIKENLR DKIDFVIWTG DNIRHDNDRK HPRTEAQIFD MNNIVADKMT
210 220 230 240 250
ELFSAGNEED PRDFDVSVIP SLGNNDVFPH NMFALGPTLQ TREYYRIWKN
260 270 280 290 300
FVPQQQQRTF DRSASFLTEV IPGKLAVLSI NTLYLFKANP LVDNCNSKKE
310 320 330 340 350
PGYQLLLWFG YVLEELRSRG MKVWLSGHVP PIAKNFDQSC YDKFTLWTHE
360 370 380 390 400
YRDIIIGGLY GHMNIDHFIP TDGKKARKSL LKAMEQSTRV QQGEDSNEED
410 420 430 440 450
EETELNRILD HAMAAKEVFL MGAKPSNKEA YMNTVRDTYY RKVWNKLERV
460 470 480 490 500
DEKNVENEKK KKEKKDKKKK KPITRKELIE RYSIVNIGGS VIPTFNPSFR
510 520 530 540 550
IWEYNITDIV NDSNFAVSEY KPWDEFFESL NKIMEDSLLE DEMDSSNIEV
560 570 580 590 600
GINREKMGEK KNKKKKKNDK TMPIEMPDKY ELGPAYVPQL FTPTRFVQFY
610 620 630 640 650
ADLEKINQEL HNSFVESKDI FRYEIEYTSD EKPYSMDSLT VGSYLDLAGR
660 670
LYENKPAWEK YVEWSFASSG YKDD
Length:674
Mass (Da):78,344
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:iEEC78BC7568098B3
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
AF322107 Genomic DNA Translation: AAG37278.1
U33007 Genomic DNA Translation: AAB64872.1
BK006938 Genomic DNA Translation: DAA12287.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S69731

NCBI Reference Sequences

More...
RefSeqi
NP_010740.3, NM_001180760.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR452W_mRNA; YDR452W; YDR452W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852063

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR452W

<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
AF322107 Genomic DNA Translation: AAG37278.1
U33007 Genomic DNA Translation: AAB64872.1
BK006938 Genomic DNA Translation: DAA12287.1
PIRiS69731
RefSeqiNP_010740.3, NM_001180760.3

3D structure databases

SMRiQ04119
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi32507, 67 interactors
DIPiDIP-2584N
IntActiQ04119, 13 interactors
MINTiQ04119
STRINGi4932.YDR452W

PTM databases

iPTMnetiQ04119

Proteomic databases

MaxQBiQ04119
PaxDbiQ04119
PRIDEiQ04119

Genome annotation databases

EnsemblFungiiYDR452W_mRNA; YDR452W; YDR452W
GeneIDi852063
KEGGisce:YDR452W

Organism-specific databases

SGDiS000002860, PPN1
VEuPathDBiFungiDB:YDR452W

Phylogenomic databases

eggNOGiKOG3770, Eukaryota
GeneTreeiENSGT00950000183182
HOGENOMiCLU_013424_1_0_1
InParanoidiQ04119
OMAiTFGNNDI

Enzyme and pathway databases

BRENDAi3.6.1.10, 984
3.6.1.11, 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q04119
RNActiQ04119, protein

Family and domain databases

CDDicd00842, MPP_ASMase, 1 hit
InterProiView protein in InterPro
IPR041805, ASMase/PPN1_MPP
IPR004843, Calcineurin-like_PHP_ApaH
IPR012358, EndopolyPtase_N1
IPR029052, Metallo-depent_PP-like
PfamiView protein in Pfam
PF00149, Metallophos, 1 hit
PIRSFiPIRSF027093, EndopolyPtase_N1, 1 hit
SUPFAMiSSF56300, SSF56300, 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 nameiPPN1_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: Q04119
Secondary accession number(s): D6VT77
<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: May 10, 2005
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 168 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
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