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Entry version 147 (02 Jun 2021)
Sequence version 1 (01 Nov 1997)
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Protein

1,3-beta-glucanosyltransferase GAS2

Gene

GAS2

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

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.

3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei1071,3-beta-glucan 1; donor substrate; via carbonyl oxygen1 Publication1
Binding sitei1751,3-beta-glucan 1; donor substrate1 Publication1
<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 sitei176Proton donor1
Binding sitei1761,3-beta-glucan 2; acceptor substrate1 Publication1
Binding sitei2171,3-beta-glucan 2; acceptor substrate; via carbonyl oxygen1 Publication1
Binding sitei2221,3-beta-glucan 2; acceptor substrate1 Publication1
Active sitei275Nucleophile1
Binding sitei3071,3-beta-glucan 1; donor substrate1 Publication1

<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 functionTransferase
Biological processCell wall biogenesis/degradation

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM43, Carbohydrate-Binding Module Family 43
GH72, Glycoside Hydrolase Family 72

<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:
1,3-beta-glucanosyltransferase GAS2 (EC:2.4.1.-1 Publication)
Alternative name(s):
Glycolipid-anchored surface protein 2
<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:GAS2
Ordered Locus Names:YLR343W
ORF Names:L8300.5
<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
S000004335, GAS2

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YLR343W

<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

Cell membrane, Membrane

<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>Mutagenesisi62Q → A: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi107Y → F or Q: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi132D → N: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi175N → A: Abolishes catalytic activity. 1 Publication1
Mutagenesisi176E → Q: Abolishes catalytic activity. 1 Publication1
Mutagenesisi244Y → F or Q: Moderately reduces hydrolysis, and causes a 10-fold reduction in transglycosylation activity. 1 Publication1
Mutagenesisi275E → Q: Abolishes catalytic activity. 1 Publication1
Mutagenesisi307Y → Q: Moderately reduces catalytic activity. 1 Publication1
Mutagenesisi404F → A: Slightly reduces catalytic activity. 1 Publication1
Mutagenesisi474Y → 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<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_000001047525 – 5311,3-beta-glucanosyltransferase GAS2Add BLAST507
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_0000010476532 – 555Removed in mature formSequence analysisAdd BLAST24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi89 ↔ 1182 Publications
Disulfide bondi231 ↔ 3672 Publications
Disulfide bondi247 ↔ 2782 Publications
Disulfide bondi390 ↔ 4422 Publications
Disulfide bondi392 ↔ 4892 Publications
Disulfide bondi399 ↔ 4662 Publications
Disulfide bondi419 ↔ 4242 Publications
<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>Glycosylationi498N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi531GPI-anchor amidated aspartateSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

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

More...
PaxDbi
Q06135

PRoteomics IDEntifications database

More...
PRIDEi
Q06135

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q06135

<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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed exclusively during sporulation (at protein level).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
31605, 72 interactors

Database of interacting proteins

More...
DIPi
DIP-4669N

Protein interaction database and analysis system

More...
IntActi
Q06135, 3 interactors

Molecular INTeraction database

More...
MINTi
Q06135

STRING: functional protein association networks

More...
STRINGi
4932.YLR343W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q06135, 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

1555
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
Q06135

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
Q06135

<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>Regioni134 – 1421,3-beta-glucan 1 binding; donor substrate1 Publication9

<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 glycosyl hydrolase 72 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QRZZ, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176308

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_021855_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q06135

Identification of Orthologs from Complete Genome Data

More...
OMAi
EWCGYST

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004886, Glucanosyltransferase
IPR017853, Glycoside_hydrolase_SF
IPR012946, X8

The PANTHER Classification System

More...
PANTHERi
PTHR31468, PTHR31468, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03198, Glyco_hydro_72, 1 hit
PF07983, X8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00768, X8, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445, SSF51445, 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.

Q06135-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNKKQNFYAA IIVAIFLCLQ LSHGSSGVSF EKTPAIKIVG NKFFDSESGE
60 70 80 90 100
QFFIKGIAYQ LQRSEEELSN ANGAFETSYI DALADPKICL RDIPFLKMLG
110 120 130 140 150
VNTLRVYAID PTKSHDICME ALSAEGMYVL LDLSEPDISI NRENPSWDVH
160 170 180 190 200
IFERYKSVID AMSSFPNLLG YFAGNEVTND HTNTFASPFV KAAIRDAKEY
210 220 230 240 250
ISHSNHRKIP VGYSTNDDAM TRDNLARYFV CGDVKADFYG INMYEWCGYS
260 270 280 290 300
TYGTSGYRER TKEFEGYPIP VFFSEFGCNL VRPRPFTEVS ALYGNKMSSV
310 320 330 340 350
WSGGLAYMYF EEENEYGVVK INDNDGVDIL PDFKNLKKEF AKADPKGITE
360 370 380 390 400
EEYLTAKEPT EVESVECPHI AVGVWEANEK LPETPDRSKC ACLDEILPCE
410 420 430 440 450
IVPFGAESGK YEEYFSYLCS KVDCSDILAN GKTGEYGEFS DCSVEQKLSL
460 470 480 490 500
QLSKLYCKIG ANDRHCPLND KNVYFNLESL QPLTSESICK NVFDSIRNIT
510 520 530 540 550
YNHGDYSKSN PSRSKESLNV KYPSSEEREN DGTIAFKTSG FVILLISMIA

AGILL
Length:555
Mass (Da):62,362
Last modified:November 1, 1997 - 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:i15395E4F137DAC7F
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
U19028 Genomic DNA Translation: AAB67255.1
BK006945 Genomic DNA Translation: DAA09648.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S51346

NCBI Reference Sequences

More...
RefSeqi
NP_013447.1, NM_001182232.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR343W_mRNA; YLR343W; YLR343W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851056

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR343W

<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
U19028 Genomic DNA Translation: AAB67255.1
BK006945 Genomic DNA Translation: DAA09648.1
PIRiS51346
RefSeqiNP_013447.1, NM_001182232.1

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
2W61X-ray1.62A1-555[»]
2W62X-ray1.85A1-555[»]
2W63X-ray1.90A1-555[»]
5FIHX-ray1.80A1-555[»]
5O9OX-ray1.90A1-555[»]
5O9PX-ray1.75A1-555[»]
5O9QX-ray1.40A1-555[»]
5O9RX-ray1.70A1-555[»]
5O9YX-ray1.57A1-555[»]
5OA2X-ray2.15A/B/C1-555[»]
5OA6X-ray1.94A1-555[»]
SMRiQ06135
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi31605, 72 interactors
DIPiDIP-4669N
IntActiQ06135, 3 interactors
MINTiQ06135
STRINGi4932.YLR343W

Protein family/group databases

CAZyiCBM43, Carbohydrate-Binding Module Family 43
GH72, Glycoside Hydrolase Family 72

PTM databases

iPTMnetiQ06135

Proteomic databases

PaxDbiQ06135
PRIDEiQ06135

Genome annotation databases

EnsemblFungiiYLR343W_mRNA; YLR343W; YLR343W
GeneIDi851056
KEGGisce:YLR343W

Organism-specific databases

SGDiS000004335, GAS2
VEuPathDBiFungiDB:YLR343W

Phylogenomic databases

eggNOGiENOG502QRZZ, Eukaryota
GeneTreeiENSGT00940000176308
HOGENOMiCLU_021855_2_0_1
InParanoidiQ06135
OMAiEWCGYST

Miscellaneous databases

EvolutionaryTraceiQ06135

Protein Ontology

More...
PROi
PR:Q06135
RNActiQ06135, protein

Family and domain databases

InterProiView protein in InterPro
IPR004886, Glucanosyltransferase
IPR017853, Glycoside_hydrolase_SF
IPR012946, X8
PANTHERiPTHR31468, PTHR31468, 1 hit
PfamiView protein in Pfam
PF03198, Glyco_hydro_72, 1 hit
PF07983, X8, 1 hit
SMARTiView protein in SMART
SM00768, X8, 1 hit
SUPFAMiSSF51445, SSF51445, 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 nameiGAS2_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: Q06135
Secondary accession number(s): D6VYY2
<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: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 2, 2021
This is version 147 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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