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Entry version 51 (17 Jun 2020)
Sequence version 1 (28 Jun 2011)
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Protein

L-asparaginase 2-2

Gene

ASP3-2

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

Miscellaneous

Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
There are 4 copies for L-asparaginase 2 in yeast. The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in tandem repeats located near a ribosomal DNA cluster.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section 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

Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine.
  1. KM=0.27 mM for L-asparagine2 Publications
  2. KM=0.27 mM for D-asparagine2 Publications
  3. KM=0.27 mM for N-acetyl-L-asparagine2 Publications
  4. KM=0.07 mM for N-carbamyl-L-asparagine2 Publications
  5. KM=0.06 mM for N-isoleucyl-L-asparagine2 Publications
  6. KM=0.06 mM for N-glycyl-L-asparagine2 Publications
  7. KM=0.06 mM for N-valyl-L-asparagine2 Publications
  8. KM=0.2 mM for N-methionyl-L-asparagine2 Publications
  9. KM=0.4 mM for N-glycyl-D-asparagine2 Publications
  1. Vmax=42 µmol/min/mg enzyme for L-asparagine2 Publications
  2. Vmax=60 µmol/min/mg enzyme for D-asparagine2 Publications
  3. Vmax=167 µmol/min/mg enzyme for N-acetyl-L-asparagine2 Publications
  4. Vmax=79 µmol/min/mg enzyme for N-carbamyl-L-asparagine2 Publications
  5. Vmax=67 µmol/min/mg enzyme for N-isoleucyl-L-asparagine2 Publications
  6. Vmax=135 µmol/min/mg enzyme for N-glycyl-L-asparagine2 Publications
  7. Vmax=56 µmol/min/mg enzyme for N-valyl-L-asparagine2 Publications
  8. Vmax=92 µmol/min/mg enzyme for N-methionyl-L-asparagine2 Publications
  9. Vmax=8 µmol/min/mg enzyme for N-glycyl-D-asparagine2 Publications

pH dependencei

Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei43O-isoaspartyl threonine intermediatePROSITE-ProRule annotation1
<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 sitei89SubstrateBy 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

  • asparaginase activity Source: SGD

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YLR157C-MONOMER

<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:
L-asparaginase 2-2 (EC:3.5.1.1)
Alternative name(s):
L-asparaginase II
L-asparagine amidohydrolase II
Short name:
ASP II
<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:ASP3-2
Ordered Locus Names:YLR157C
ORF Names:L9632.7
<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 XII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004147, ASP3-2

<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

Keywords - Cellular componenti

Periplasm, Secreted

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 251 PublicationAdd BLAST25
<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_000041044126 – 362L-asparaginase 2-2Add BLAST337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi29N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P0CX77

<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

Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
31428, 39 interactors
31431, 61 interactors
31433, 31 interactors

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P0CX77, 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
P0CX77

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini33 – 359Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST327

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>Regioni122 – 123Substrate 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 asparaginase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_019134_1_1_1

KEGG Orthology (KO)

More...
KOi
K01424

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08964, L-asparaginase_II, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1170, 1 hit
3.40.50.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004550, AsnASE_II
IPR036152, Asp/glu_Ase-like_sf
IPR006034, Asparaginase/glutaminase-like
IPR020827, Asparaginase/glutaminase_AS1
IPR027475, Asparaginase/glutaminase_AS2
IPR040919, Asparaginase_C
IPR027473, L-asparaginase_C
IPR027474, L-asparaginase_N
IPR037152, L-asparaginase_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00710, Asparaginase, 1 hit
PF17763, Asparaginase_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001220, L-ASNase_gatD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00139, ASNGLNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00870, Asparaginase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53774, SSF53774, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00520, asnASE_II, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00144, ASN_GLN_ASE_1, 1 hit
PS00917, ASN_GLN_ASE_2, 1 hit
PS51732, ASN_GLN_ASE_3, 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.

<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 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.

P0CX77-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST
60 70 80 90 100
SATTAGYSVG LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL
110 120 130 140 150
YHGISEALAS DDYAGAVVTH GTDTMEETAF FLDLTINSEK PVCIAGAMRP
160 170 180 190 200
ATATSADGPM NLYQAVSIAA SEKSLGRGTM ITLNDRIASG FWTTKMNANS
210 220 230 240 250
LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL TDPSEIPEVI
260 270 280 290 300
ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY
310 320 330 340 350
GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD
360
QIRSVFSGVY GG
Length:362
Mass (Da):38,687
Last modified:June 28, 2011 - 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:i1DE5DC8692BF0461
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti243P → L in AAS56284 (PubMed:17322287).Curated1

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 varianti26 – 55Missing 1 PublicationAdd BLAST30

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
U51921 Genomic DNA Translation: AAB67481.1
AY557958 Genomic DNA Translation: AAS56284.1
BK006945 Genomic DNA Translation: DAA09472.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S68471

NCBI Reference Sequences

More...
RefSeqi
NP_013256.1, NM_001182042.1
NP_013258.1, NM_001182044.1
NP_013259.1, NM_001182045.1
NP_013261.1, NM_001182047.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR155C_mRNA; YLR155C; YLR155C
YLR157C_mRNA; YLR157C; YLR157C
YLR158C_mRNA; YLR158C; YLR158C
YLR160C_mRNA; YLR160C; YLR160C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850850
850852
850855
850857

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR155C
sce:YLR157C
sce:YLR158C
sce:YLR160C

<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
U51921 Genomic DNA Translation: AAB67481.1
AY557958 Genomic DNA Translation: AAS56284.1
BK006945 Genomic DNA Translation: DAA09472.1
PIRiS68471
RefSeqiNP_013256.1, NM_001182042.1
NP_013258.1, NM_001182044.1
NP_013259.1, NM_001182045.1
NP_013261.1, NM_001182047.1

3D structure databases

SMRiP0CX77
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi31428, 39 interactors
31431, 61 interactors
31433, 31 interactors

Proteomic databases

PRIDEiP0CX77

Genome annotation databases

EnsemblFungiiYLR155C_mRNA; YLR155C; YLR155C
YLR157C_mRNA; YLR157C; YLR157C
YLR158C_mRNA; YLR158C; YLR158C
YLR160C_mRNA; YLR160C; YLR160C
GeneIDi850850
850852
850855
850857
KEGGisce:YLR155C
sce:YLR157C
sce:YLR158C
sce:YLR160C

Organism-specific databases

SGDiS000004147, ASP3-2

Phylogenomic databases

HOGENOMiCLU_019134_1_1_1
KOiK01424

Enzyme and pathway databases

BioCyciYEAST:YLR157C-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0CX77
RNActiP0CX77, protein

Family and domain databases

CDDicd08964, L-asparaginase_II, 1 hit
Gene3Di3.40.50.1170, 1 hit
3.40.50.40, 1 hit
InterProiView protein in InterPro
IPR004550, AsnASE_II
IPR036152, Asp/glu_Ase-like_sf
IPR006034, Asparaginase/glutaminase-like
IPR020827, Asparaginase/glutaminase_AS1
IPR027475, Asparaginase/glutaminase_AS2
IPR040919, Asparaginase_C
IPR027473, L-asparaginase_C
IPR027474, L-asparaginase_N
IPR037152, L-asparaginase_N_sf
PfamiView protein in Pfam
PF00710, Asparaginase, 1 hit
PF17763, Asparaginase_C, 1 hit
PIRSFiPIRSF001220, L-ASNase_gatD, 1 hit
PRINTSiPR00139, ASNGLNASE
SMARTiView protein in SMART
SM00870, Asparaginase, 1 hit
SUPFAMiSSF53774, SSF53774, 1 hit
TIGRFAMsiTIGR00520, asnASE_II, 1 hit
PROSITEiView protein in PROSITE
PS00144, ASN_GLN_ASE_1, 1 hit
PS00917, ASN_GLN_ASE_2, 1 hit
PS51732, ASN_GLN_ASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiASP22_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: P0CX77
Secondary accession number(s): D6VYF3
, P11163, Q12268, Q6Q5K8, Q6Q5K9
<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: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 17, 2020
This is version 51 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
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