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Entry version 151 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase

Gene

PNG1

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

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. Involved in the formation of free oligosaccharide in cytosol.

6 Publications

Miscellaneous

Present with 4850 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

  • Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. EC:3.5.1.52

<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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.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

Inhibited by Z-VAD-fmk, a well-known caspase inhibitor. Also inhibited by Man9GlcNAc2-iodoacetoamide. Both molecules inhibit enzyme activity through covalent binding of the carbohydrate to the single Cys-191 residue.3 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. KM=210 µM for asialofetuin1 Publication
  1. Vmax=140 nmol/min/mg enzyme with asialofetuin as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi129Zinc1
Metal bindingi132Zinc1
Metal bindingi165Zinc1
Metal bindingi168Zinc1
<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 sitei191Nucleophile1
Active sitei2181
Active sitei2351
<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 sitei238Substrate1

<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, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YPL096W-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.52, 984

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q02890

<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:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Short name:
PNGase
Alternative name(s):
Peptide:N-glycanase 1
Short name:
yPNG1
<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:PNG1
Ordered Locus Names:YPL096W
<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 XVI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000006017, PNG1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YPL096W

<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, 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>Mutagenesisi123W → A: No effect. 1 Publication1
Mutagenesisi129C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi132C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi165C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi168C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi174F → A: No effect. 1 Publication1
Mutagenesisi177Y → A: No effect. 1 Publication1
Mutagenesisi187R → A: No effect. 1 Publication1
Mutagenesisi189G → A: No effect. 1 Publication1
Mutagenesisi191C → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi194W → A: No effect. 1 Publication1
Mutagenesisi198F → A: No effect. 1 Publication1
Mutagenesisi199T → A: No effect. 1 Publication1
Mutagenesisi203K → A: No effect. 1 Publication1
Mutagenesisi206G → A: No effect. 1 Publication1
Mutagenesisi210R → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi212V → A: No effect. 1 Publication1
Mutagenesisi218H → A: Abolishes enzyme activity. 2 Publications1
Mutagenesisi218H → Y in png1-1; abolishes enzyme activity. 2 Publications1
Mutagenesisi220W → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi220W → F: No effect. 1 Publication1
Mutagenesisi222E → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi224F → A: No effect. 1 Publication1
Mutagenesisi230R → A: No effect. 1 Publication1
Mutagenesisi231W → A: Abolishes enzyme activity. 1
Mutagenesisi231W → F: No effect. 1
Mutagenesisi234V → A: No effect. 1 Publication1
Mutagenesisi235D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi242D → A: No effect. 1 Publication1
Mutagenesisi251W → A: No effect. 1 Publication1
Mutagenesisi253K → A: No effect. 1 Publication1
Mutagenesisi257Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi261F → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi264D → A: No effect. 1 Publication1
Mutagenesisi266V → A: No effect. 1 Publication1
Mutagenesisi268D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi273Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi281R → A: No effect. 1 Publication1
Mutagenesisi347R → A: No effect. 1 Publication1
Mutagenesisi354W → A: No effect. 1 Publication1
Mutagenesisi358R → A: No effect. 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_00002489961 – 363Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidaseAdd BLAST363

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q02890

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

More...
PaxDbi
Q02890

PRoteomics IDEntifications database

More...
PRIDEi
Q02890

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q02890

<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 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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with RAD23 subunit of 26S proteasome.

3 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
36085, 66 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1320, Peptide:N-glycanase-Rad23 complex

Database of interacting proteins

More...
DIPi
DIP-4008N

Protein interaction database and analysis system

More...
IntActi
Q02890, 3 interactors

Molecular INTeraction database

More...
MINTi
Q02890

STRING: functional protein association networks

More...
STRINGi
4932.YPL096W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q02890, 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

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q02890

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q02890

<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>Regioni325 – 363DisorderedSequence analysisAdd BLAST39

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi330 – 350Polar residuesSequence analysisAdd BLAST21

<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
KOG0909, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000006540

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_031058_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q02890

Identification of Orthologs from Complete Genome Data

More...
OMAi
WIHVDAC

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038765, Papain-like_cys_pep_sf
IPR018325, Rad4/PNGase_transGLS-fold
IPR002931, Transglutaminase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03835, Rad4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00460, TGc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54001, SSF54001, 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.

Q02890-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGEVYEKNNI DFDSIAKMLL IKYKDFILSK FKKAAPVENI RFQNLVHTNQ
60 70 80 90 100
FAQGVLGQSQ HLCTVYDNPS WHSIVLETLD LDLIYKNVDK EFAKDGHAEG
110 120 130 140 150
ENIYTDYLVK ELLRYFKQDF FKWCNKPDCN HCGQNTSENM TPLGSQGPNG
160 170 180 190 200
EESKFNCGTV EIYKCNRCGN ITRFPRYNDP IKLLETRKGR CGEWCNLFTL
210 220 230 240 250
ILKSFGLDVR YVWNREDHVW CEYFSNFLNR WVHVDSCEQS FDQPYIYSIN
260 270 280 290 300
WNKKMSYCIA FGKDGVVDVS KRYILQNELP RDQIKEEDLK FLCQFITKRL
310 320 330 340 350
RYSLNDDEIY QLACRDEQEQ IELIRGKTQE TKSESVSAAS KSSNRGRESG
360
SADWKAQRGE DGK
Length:363
Mass (Da):42,485
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:i004F3E3E07C3B954
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 43208 Da. Determined by MALDI. 1 Publication

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
U43281 Genomic DNA Translation: AAB68203.1
BK006949 Genomic DNA Translation: DAA11337.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S61970

NCBI Reference Sequences

More...
RefSeqi
NP_015229.1, NM_001183910.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPL096W_mRNA; YPL096W; YPL096W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856009

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL096W

<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
U43281 Genomic DNA Translation: AAB68203.1
BK006949 Genomic DNA Translation: DAA11337.1
PIRiS61970
RefSeqiNP_015229.1, NM_001183910.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3WX-ray3.00A8-342[»]
1X3ZX-ray2.80A8-342[»]
3ESWX-ray3.40A8-341[»]
SMRiQ02890
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36085, 66 interactors
ComplexPortaliCPX-1320, Peptide:N-glycanase-Rad23 complex
DIPiDIP-4008N
IntActiQ02890, 3 interactors
MINTiQ02890
STRINGi4932.YPL096W

PTM databases

iPTMnetiQ02890

Proteomic databases

MaxQBiQ02890
PaxDbiQ02890
PRIDEiQ02890

Genome annotation databases

EnsemblFungiiYPL096W_mRNA; YPL096W; YPL096W
GeneIDi856009
KEGGisce:YPL096W

Organism-specific databases

SGDiS000006017, PNG1
VEuPathDBiFungiDB:YPL096W

Phylogenomic databases

eggNOGiKOG0909, Eukaryota
GeneTreeiENSGT00390000006540
HOGENOMiCLU_031058_0_1_1
InParanoidiQ02890
OMAiWIHVDAC

Enzyme and pathway databases

BioCyciMetaCyc:YPL096W-MONOMER
BRENDAi3.5.1.52, 984
SABIO-RKiQ02890

Miscellaneous databases

EvolutionaryTraceiQ02890

Protein Ontology

More...
PROi
PR:Q02890
RNActiQ02890, protein

Family and domain databases

InterProiView protein in InterPro
IPR038765, Papain-like_cys_pep_sf
IPR018325, Rad4/PNGase_transGLS-fold
IPR002931, Transglutaminase-like
PfamiView protein in Pfam
PF03835, Rad4, 1 hit
SMARTiView protein in SMART
SM00460, TGc, 1 hit
SUPFAMiSSF54001, SSF54001, 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 nameiPNG1_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: Q02890
Secondary accession number(s): D6W3S1
<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: September 5, 2006
Last sequence update: November 1, 1996
Last modified: June 2, 2021
This is version 151 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

3D-structure, Reference proteome

Documents

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