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Entry version 187 (23 Feb 2022)
Sequence version 2 (01 Feb 1996)
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Protein

1,3-beta-glucanosyltransferase GAS1

Gene

GAS1

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 cell wall biosynthesis and morphogenesis.

2 Publications

Miscellaneous

Present with 11000 wall-bound molecules/cell in log phase YPD medium.1 Publication

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 sitei921,3-beta-glucan 1; donor substrate; via carbonyl oxygenBy similarity1
Binding sitei1601,3-beta-glucan 1; donor substrateBy similarity1
<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 sitei161Proton donor1
Binding sitei1611,3-beta-glucan 2; acceptor substrateBy similarity1
Binding sitei2021,3-beta-glucan 2; acceptor substrate; via carbonyl oxygenBy similarity1
Binding sitei2071,3-beta-glucan 2; acceptor substrateBy similarity1
Active sitei262Nucleophile1
Binding sitei2941,3-beta-glucan 1; donor substrateBy 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

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 GAS1 (EC:2.4.1.-)
Alternative name(s):
Glycolipid-anchored surface protein 1
Glycoprotein GP115
<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:GAS1
Synonyms:GGP1
Ordered Locus Names:YMR307W
ORF Names:YM9952.09
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004924, GAS1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YMR307W

<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, Cell wall, Membrane, Secreted

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Increases cellular chitin level (PubMed:17142567). Increases chitin chain length (PubMed:17142567).1 Publication

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>Mutagenesisi74C → S: Impairs the folding and stability of the protein. 1 Publication1
Mutagenesisi103C → S: Partially impairs the folding and stability of the protein. 1 Publication1
Mutagenesisi161E → Q: Loss of function. 1 Publication1
Mutagenesisi262E → Q: Loss of function. 1 Publication1
Mutagenesisi265C → S: Partially impairs the folding and stability of the protein. 1 Publication1
Mutagenesisi348C → S: Impairs the folding and stability of the protein. 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 – 221 PublicationAdd BLAST22
<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_000001047323 – 5281,3-beta-glucanosyltransferase GAS1Add BLAST506
<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_0000010474529 – 559Removed in mature formAdd BLAST31

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>Glycosylationi40N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi57N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi74 ↔ 103By similarity
Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi149N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi165N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi216 ↔ 348By similarity
Disulfide bondi234 ↔ 265By similarity
Glycosylationi253N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi283N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi321N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi370 ↔ 421By similarity
Disulfide bondi372 ↔ 462By similarity
Disulfide bondi379 ↔ 445By similarity
Disulfide bondi398 ↔ 403By similarity
Glycosylationi409N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi495N-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>Lipidationi528GPI-anchor amidated asparagine1 Publication1

<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

Extensively N- and O-glycosylated.1 Publication
The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22146

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

More...
PaxDbi
P22146

PRoteomics IDEntifications database

More...
PRIDEi
P22146

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...
COMPLUYEAST-2DPAGEi
P22146

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22146

<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 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
35487, 806 interactors

Database of interacting proteins

More...
DIPi
DIP-4390N

Protein interaction database and analysis system

More...
IntActi
P22146, 11 interactors

Molecular INTeraction database

More...
MINTi
P22146

STRING: functional protein association networks

More...
STRINGi
4932.YMR307W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P22146, 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
P22146

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni119 – 1271,3-beta-glucan 1 binding; donor substrateBy similarity9
Regioni474 – 526DisorderedSequence analysisAdd BLAST53

<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
ENOG502QPST, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176308

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_021855_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22146

Identification of Orthologs from Complete Genome Data

More...
OMAi
AEYGCIE

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.

P22146-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA
60 70 80 90 100
YQADTANETS GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH
110 120 130 140 150
SECMKALNDA DIYVIADLAA PATSINRDDP TWTVDLFNSY KTVVDTFANY
160 170 180 190 200
TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR DVRQYISDKN YRKIPVGYSS
210 220 230 240 250
NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK TSGYADRTAE
260 270 280 290 300
FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET
310 320 330 340 350
NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA
360 370 380 390 400
TGKYWSAATE LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE
410 420 430 440 450
VDCSGISANG TAGKYGAYSF CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS
460 470 480 490 500
ATLQTATTQA SCSSALKEIG SMGTNSASGS VDLGSGTESS TASSNASGSS
510 520 530 540 550
SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV VFTSIISLSI

AAGVGFALV
Length:559
Mass (Da):59,582
Last modified:February 1, 1996 - v2
<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:iD6E39568DCB4C5AE
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 conflicti211T → A in CAA37512 (PubMed:1824714).Curated1

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
X53424 Genomic DNA Translation: CAA37512.1
X56399 Genomic DNA Translation: CAA39809.1
Z49212 Genomic DNA Translation: CAA89140.1
BK006946 Genomic DNA Translation: DAA10208.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S53977, RWBYS1

NCBI Reference Sequences

More...
RefSeqi
NP_014038.1, NM_001182818.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YMR307W_mRNA; YMR307W; YMR307W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855355

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YMR307W

<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
X53424 Genomic DNA Translation: CAA37512.1
X56399 Genomic DNA Translation: CAA39809.1
Z49212 Genomic DNA Translation: CAA89140.1
BK006946 Genomic DNA Translation: DAA10208.1
PIRiS53977, RWBYS1
RefSeqiNP_014038.1, NM_001182818.1

3D structure databases

SMRiP22146
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35487, 806 interactors
DIPiDIP-4390N
IntActiP22146, 11 interactors
MINTiP22146
STRINGi4932.YMR307W

Protein family/group databases

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

PTM databases

iPTMnetiP22146

2D gel databases

COMPLUYEAST-2DPAGEiP22146

Proteomic databases

MaxQBiP22146
PaxDbiP22146
PRIDEiP22146

Genome annotation databases

EnsemblFungiiYMR307W_mRNA; YMR307W; YMR307W
GeneIDi855355
KEGGisce:YMR307W

Organism-specific databases

SGDiS000004924, GAS1
VEuPathDBiFungiDB:YMR307W

Phylogenomic databases

eggNOGiENOG502QPST, Eukaryota
GeneTreeiENSGT00940000176308
HOGENOMiCLU_021855_2_1_1
InParanoidiP22146
OMAiAEYGCIE

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22146
RNActiP22146, 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 nameiGAS1_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: P22146
Secondary accession number(s): D6W0D4, P23151
<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: August 1, 1991
Last sequence update: February 1, 1996
Last modified: February 23, 2022
This is version 187 of the entry and version 2 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
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