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Entry version 154 (08 May 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Glutathione hydrolase proenzyme

Gene

ECM38

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 transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation.1 Publication

Miscellaneous

Present with 672 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 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

Activity is decreased by glutathione and ammonium ion.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei177GlutamateBy similarity1
<p>This subsection of the ‘Function’ 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 sitei470NucleophileBy similarity1
Binding sitei488GlutamateBy similarity1
Binding sitei490GlutamateBy similarity1
Binding sitei509GlutamateBy similarity1
Binding sitei512GlutamateBy similarity1

<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

  • glutathione hydrolase activity Source: SGD
  • hypoglycin A gamma-glutamyl transpeptidase activity Source: UniProtKB-EC
  • leukotriene C4 gamma-glutamyl transferase activity Source: UniProtKB-EC
  • peptidyltransferase activity Source: GO_Central

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 functionAcyltransferase, Hydrolase, Protease, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YLR299W-MONOMER
YEAST:YLR299W-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-SCE-5423646 Aflatoxin activation and detoxification

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00204

Protein family/group databases

MEROPS protease database

More...
MEROPSi
T03.012

<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:
Glutathione hydrolase proenzyme (EC:3.4.19.132 Publications)
Alternative name(s):
CIK1 suppressor protein 2
Extracellular mutant protein 38
Gamma-glutamyltransferase (EC:2.3.2.22 Publications)
Gamma-glutamyltranspeptidase
Short name:
Gamma-GT
Cleaved into the following 2 chains:
<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:ECM38
Synonyms:CIS2
Ordered Locus Names:YLR299W
<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 XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR299W

Saccharomyces Genome Database

More...
SGDi
S000004290 ECM38

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 – 13CytoplasmicSequence analysisAdd BLAST13
<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>Transmembranei14 – 34Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini35 – 660LumenalSequence analysisAdd BLAST626

Keywords - Cellular componenti

Membrane, Vacuole

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000110781 – 469Glutathione hydrolase heavy chainBy similarityAdd BLAST469
ChainiPRO_0000011079470 – 660Glutathione hydrolase light chainBy similarityAdd BLAST191

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 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>Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi191N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi270N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi298N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi454N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi517N-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

Cleaved by autocatalysis into a large and a small subunit.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q05902

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

More...
PaxDbi
Q05902

PRoteomics IDEntifications database

More...
PRIDEi
Q05902

<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 upon nitrogen starvation. Repressed by ammonium ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible inhibitors whereas serine-borate is a reversible inhibitor.4 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_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

Heterodimer composed of a light and a heavy chain. The active site is located in the light chain.By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31563, 58 interactors

Database of interacting proteins

More...
DIPi
DIP-4682N

Molecular INTeraction database

More...
MINTi
Q05902

STRING: functional protein association networks

More...
STRINGi
4932.YLR299W

<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
Q05902

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni540 – 541Glutamate bindingBy similarity2
Regioni562 – 563Glutamate bindingBy similarity2

<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 gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156917

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000175620

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q05902

KEGG Orthology (KO)

More...
KOi
K00681

Identification of Orthologs from Complete Genome Data

More...
OMAi
KATKNMF

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000101 GGT_peptidase
IPR029055 Ntn_hydrolases_N

The PANTHER Classification System

More...
PANTHERi
PTHR11686 PTHR11686, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56235 SSF56235, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00066 g_glut_trans, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00462 G_GLU_TRANSPEPTIDASE, 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>.<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.

Q05902-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLCNRKVPK TLNTCFILHI FTLLTLGVLV SGMPSKMVSF ASQETLQRIN
60 70 80 90 100
NLLRGSANRD VDIIAEYLKK DDDDDGGDKD HHNIDIDPLP RRPSLTPDRQ
110 120 130 140 150
LLKVGLHGAI SSDLEVCSNL TINEVLLKFP GSNAADAAVT QALCKGMVNF
160 170 180 190 200
FNSGIGGGGY VVFSGKDDED HLSIDFREKA PMDSHKFMFE NCSLCSKIGG
210 220 230 240 250
LAVGVPGELM GLYRLFKERG SGQVDWRDLI EPVAKLGSVG WQIGEALGAT
260 270 280 290 300
LELYEDVFLT LKEDWSFVLN STHDGVLKEG DWIKRPALSN MLMELAKNGS
310 320 330 340 350
VAPFYDPDHW IAKSMIDTVA KYNGIMNLQD VSSYDVHVTK PLSMKIRKGA
360 370 380 390 400
NFIPDNDMTV LTSSGSSSGA ALLAALRIMD NFQNQEGGDY EKETTYHLLE
410 420 430 440 450
SMKWMASARS RLGDFEGEAL PKHIEEVLDP EWALKAVKSI KRNSQDGNFK
460 470 480 490 500
TLENWTLYDP AYDINNPHGT AHFSIVDSHG NAVSLTTTIN LLFGSLVHDP
510 520 530 540 550
KTGVIFNNEM DDFAQFNKSN SFELAPSIYN FPEPGKRPLS STAPTIVLSE
560 570 580 590 600
LGIPDLVVGA SGGSRITTSV LQTIVRTYWY NMPILETIAY PRIHHQLLPD
610 620 630 640 650
RIELESFPMI GKAVLSTLKE MGYTMKEVFP KSVVNAIRNV RGEWHAVSDY
660
WRKRGISSVY
Length:660
Mass (Da):73,180
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:i9896E9EBFF822F55
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti171H → R in strain: YPH499. 1 Publication1
Natural varianti494G → D in strain: YPH499; lack of gamma-glutamyl transferase activity. 1 Publication1

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
U17243 Genomic DNA Translation: AAB67344.1
BK006945 Genomic DNA Translation: DAA09609.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S50383

NCBI Reference Sequences

More...
RefSeqi
NP_013402.1, NM_001182187.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR299W_mRNA; YLR299W_mRNA; YLR299W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851006

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR299W

<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
U17243 Genomic DNA Translation: AAB67344.1
BK006945 Genomic DNA Translation: DAA09609.1
PIRiS50383
RefSeqiNP_013402.1, NM_001182187.1

3D structure databases

SMRiQ05902
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31563, 58 interactors
DIPiDIP-4682N
MINTiQ05902
STRINGi4932.YLR299W

Protein family/group databases

MEROPSiT03.012

Proteomic databases

MaxQBiQ05902
PaxDbiQ05902
PRIDEiQ05902

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR299W_mRNA; YLR299W_mRNA; YLR299W
GeneIDi851006
KEGGisce:YLR299W

Organism-specific databases

EuPathDBiFungiDB:YLR299W
SGDiS000004290 ECM38

Phylogenomic databases

GeneTreeiENSGT00940000156917
HOGENOMiHOG000175620
InParanoidiQ05902
KOiK00681
OMAiKATKNMF

Enzyme and pathway databases

UniPathwayi
UPA00204

BioCyciMetaCyc:YLR299W-MONOMER
YEAST:YLR299W-MONOMER
ReactomeiR-SCE-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-SCE-5423646 Aflatoxin activation and detoxification

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q05902

Family and domain databases

InterProiView protein in InterPro
IPR000101 GGT_peptidase
IPR029055 Ntn_hydrolases_N
PANTHERiPTHR11686 PTHR11686, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR00066 g_glut_trans, 1 hit
PROSITEiView protein in PROSITE
PS00462 G_GLU_TRANSPEPTIDASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiECM38_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: Q05902
Secondary accession number(s): D6VYU3
<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: March 1, 2005
Last sequence update: November 1, 1996
Last modified: May 8, 2019
This is version 154 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

Complete proteome, Reference proteome

Documents

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