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Entry version 172 (08 May 2019)
Sequence version 2 (01 Feb 1996)
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Protein

1,3-beta-glucan synthase component FKS1

Gene

FKS1

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

Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and cell wall remodeling.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>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 functionGlycosyltransferase, Transferase
Biological processCell shape, Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:YLR342W-MONOMER

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT48 Glycosyltransferase Family 48

Transport Classification Database

More...
TCDBi
9.B.119.1.1 the glycan synthase, fks1 (fks1) family

<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:
1,3-beta-glucan synthase component FKS1 (EC:2.4.1.34)
Alternative name(s):
1,3-beta-D-glucan-UDP glucosyltransferase
Calcineurin dependent protein 1
Calcofluor white hypersensitivity protein 53
Echinocandin target gene protein 1
FK506 sensitivity protein 1
Glucan synthase of cerevisiae protein 1
Papulacandin B resistance protein 1
<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:FKS1
Synonyms:CND1, CWH53, ETG1, GLS1, GSC1, PBR1
Ordered Locus Names:YLR342W
ORF Names:L8300.6
<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:YLR342W

Saccharomyces Genome Database

More...
SGDi
S000004334 FKS1

<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 – 454CytoplasmicSequence analysisAdd BLAST454
<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>Transmembranei455 – 475HelicalSequence analysisAdd BLAST21
Topological domaini476 – 492ExtracellularSequence analysisAdd BLAST17
Transmembranei493 – 513HelicalSequence analysisAdd BLAST21
Topological domaini514 – 531CytoplasmicSequence analysisAdd BLAST18
Transmembranei532 – 552HelicalSequence analysisAdd BLAST21
Topological domaini553 – 563ExtracellularSequence analysisAdd BLAST11
Transmembranei564 – 584HelicalSequence analysisAdd BLAST21
Topological domaini585 – 621CytoplasmicSequence analysisAdd BLAST37
Transmembranei622 – 642HelicalSequence analysisAdd BLAST21
Topological domaini643 – 678ExtracellularSequence analysisAdd BLAST36
Transmembranei679 – 699HelicalSequence analysisAdd BLAST21
Topological domaini700 – 1358CytoplasmicSequence analysisAdd BLAST659
Transmembranei1359 – 1379HelicalSequence analysisAdd BLAST21
Topological domaini1380 – 1444ExtracellularSequence analysisAdd BLAST65
Transmembranei1445 – 1465HelicalSequence analysisAdd BLAST21
Topological domaini1466 – 1469CytoplasmicSequence analysis4
Transmembranei1470 – 1490HelicalSequence analysisAdd BLAST21
Topological domaini1491 – 1560ExtracellularSequence analysisAdd BLAST70
Transmembranei1561 – 1581HelicalSequence analysisAdd BLAST21
Topological domaini1582 – 1601CytoplasmicSequence analysisAdd BLAST20
Transmembranei1602 – 1622HelicalSequence analysisAdd BLAST21
Topological domaini1623 – 1643ExtracellularSequence analysisAdd BLAST21
Transmembranei1644 – 1664HelicalSequence analysisAdd BLAST21
Topological domaini1665 – 1672CytoplasmicSequence analysis8
Transmembranei1673 – 1695HelicalSequence analysisAdd BLAST23
Topological domaini1696 – 1802ExtracellularSequence analysisAdd BLAST107
Transmembranei1803 – 1823HelicalSequence analysisAdd BLAST21
Topological domaini1824 – 1876CytoplasmicSequence analysisAdd BLAST53

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

<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

Cells are hypersensitive to immunosuppressant drugs FK506 and cyclosporin A (CsA) due to the inhibition of calcineurin phosphatase activity by the receptor-drug complexes and is dependent on calcineurin for vegetative growth. It confers a slow growth phenotype which is partially suppressed by exogenously added Ca2+ and exacerbated by EGTA. Simultaneous disruption of CNA1 and CNA2 or CNB1 is lethal in FKS1-1. Disruption of FPR1 or CPR1 results in the loss of hypersensitivity. Overexpression of CNA1 or CNA2, in conjunction with CNB1, results in a significant decrease in hypersensitivity to FK506 and CsA. FKS1-8 mutant is sensitive to FK506 and cyclosporin A, has increased tendency to lyse and exhibits slow growth that is improved by the addition of osmotic stabilizing agents. It is more sensitive to the drugs when grown on galactose compared to dextrose. ETG1-1 mutant is resistant to the cell wall active echinocandins, which are inhibitors of 1,3-beta-D-glucan synthase. ETG1-4 mutant is hypersensitive to the chitin synthase inhibitor nikkomycin Z. Deletion of FKS1 leads to hypersensitivity to echinocandin-like antifungal lipopeptide caspofungin, a 1,3-beta-glucan synthase inhibitor. Deletion mutant also displays a 30% reduction in 1,3-beta-glucan and 15% reduction in alkali-insoluble 1,6-beta-glucan compared to wild-type.6 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi146E → V in 1132; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with N-329; N-335 and DEL-GSC2. 1 Publication1
Mutagenesisi302V → N in 1082; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with DEL-GSC2. 1 Publication1
Mutagenesisi329Y → N in 1132; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with V-146; N-335 and DEL-GSC2. 1 Publication1
Mutagenesisi335Y → N in 1132; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with V-146; N-329 and DEL-GSC2. 1 Publication1
Mutagenesisi470N → K in ACR79-5; selectively resistant to antibiotic arborcandin C. 1 Publication1
Mutagenesisi605T → I in 1093; temperature-sensitive mutant; higher beta-glucan content of cells; when associated with T-761 and DEL-GSC2. 1 Publication1
Mutagenesisi642L → S in ACR1A3; selectively resistant to antibiotic arborcandin C. 1 Publication1
Mutagenesisi713I → L in 1163; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with V-722 and DEL-GSC2. 1 Publication1
Mutagenesisi722I → V in 1163; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with L-713 and DEL-GSC2. 1 Publication1
Mutagenesisi761M → T in 1093; temperature-sensitive mutant; higher beta-glucan content of cells; when associated with I-605 and DEL-GSC2. 1 Publication1
Mutagenesisi823A → V in 1104; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with E-920 and DEL-GSC2. 1 Publication1
Mutagenesisi828T → A in 1014; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; partially K1 killer toxin-sensitive; when associated with DEL-GSC2. 1 Publication1
Mutagenesisi853I → T in 1114; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with G-932; D-934; Y-1020; N-1047 and DEL-GSC2. 1 Publication1
Mutagenesisi855L → R in A6; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with DEL-GSC2. 1 Publication1
Mutagenesisi872L → F in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with K-907; S-982 and DEL-GSC2. 1 Publication1
Mutagenesisi877K → N in 1154; temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius; defective in 1,3-beta-glucan synthesis and thus has lower beta-glucan content; hypersensitive to echinocandin B and to a chitin-binding reagent, Calcofluor white; fails to grow in a low glucose medium; when associated with S-899; P-977 and DEL-GSC2. 2 Publications1
Mutagenesisi899A → S in 1154; temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius; defective in 1,3-beta-glucan synthesis and thus has lower beta-glucan content; hypersensitive to echinocandin B and to a chitin-binding reagent, Calcofluor white; fails to grow in a low glucose medium; when associated with N-877; P-977 and DEL-GSC2. 2 Publications1
Mutagenesisi907E → K in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with F-872; S-982 and DEL-GSC2. 1 Publication1
Mutagenesisi920D → E in 1104; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with V-823 and DEL-GSC2. 1 Publication1
Mutagenesisi932A → G in 1114; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with T-853; D-934; Y-1020; N-1047 and DEL-GSC2. 1 Publication1
Mutagenesisi934E → D in 1114; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with T-853; G-932; Y-1020; N-1047 and DEL-GSC2. 1 Publication1
Mutagenesisi977Q → P in 1154; temperature-sensitive mutant which is able to grow at 25 degrees Celsius but fails to grow at temperatures above 35 degrees Celsius; defective in 1,3-beta-glucan synthesis and thus has lower beta-glucan content; hypersensitive to echinocandin B and to a chitin-binding reagent, Calcofluor white; fails to grow in a low glucose medium; when associated with N-877; S-899 and DEL-GSC2. 2 Publications1
Mutagenesisi982N → S in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with F-872; K-907 and DEL-GSC2. 1 Publication1
Mutagenesisi1020F → Y in 1114; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with T-853; G-932; D-934; N-1047 and DEL-GSC2. 1 Publication1
Mutagenesisi1047I → N in 1114; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with T-853; G-932; D-934; Y-1020 and DEL-GSC2. 1 Publication1
Mutagenesisi1111E → G in F4; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with DEL-GSC2. 1 Publication1
Mutagenesisi1258F → Y in 1125; temperature-sensitive mutant; lower beta-glucan content of cells and partially K1 killer toxin-resistant; when associated with D-1520 and DEL-GSC2. 1 Publication1
Mutagenesisi1520N → D in 1125; temperature-sensitive mutant; lower beta-glucan content of cells and partial K1 killer toxin-resistant phenotype; when associated with Y-1258 and DEL-GSC2. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001217251 – 18761,3-beta-glucan synthase component FKS1Add BLAST1876

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 describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei269PhosphothreonineCombined sources1
Modified residuei272PhosphothreonineCombined sources1
Cross-linki275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki910Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki915Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki1539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki1547Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38631

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

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PaxDbi
P38631

PRoteomics IDEntifications database

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PRIDEi
P38631

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P38631

<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

During vegetative growth. Expressed periodically during the cell cycle.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

<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

Component of the 1,3-beta-glucan synthase (GS), composed of two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit RHO1. Interacts with RHO1, which is a GTP-binding protein.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
RHO1P067803EBI-7708,EBI-15121

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31604, 513 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1812 1,3-beta-D-glucan synthase complex

Database of interacting proteins

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DIPi
DIP-5749N

Protein interaction database and analysis system

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IntActi
P38631, 68 interactors

Molecular INTeraction database

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MINTi
P38631

STRING: functional protein association networks

More...
STRINGi
4932.YLR342W

<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

<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 glycosyltransferase 48 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000176776

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000216604

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P38631

KEGG Orthology (KO)

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KOi
K00706

Identification of Orthologs from Complete Genome Data

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OMAi
FMRDQGY

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026899 FKS1-like_dom1
IPR003440 Glyco_trans_48

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14288 FKS1_dom1, 1 hit
PF02364 Glucan_synthase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01205 FKS1_dom1, 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.

P38631-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA
60 70 80 90 100
GTEADMYGQQ PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG
110 120 130 140 150
TPGYDSYGGQ YTASQMSYGE PNSSGTSTPI YGNYDPNAIA MALPNEPYPA
160 170 180 190 200
WTADSQSPVS IEQIEDIFID LTNRLGFQRD SMRNMFDHFM VLLDSRSSRM
210 220 230 240 250
SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN MSLGKLSRKA
260 270 280 290 300
RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE
310 320 330 340 350
RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE
360 370 380 390 400
GDFLNRVITP IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP
410 420 430 440 450
EGIAKIVLED GTKLIELPLE ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT
460 470 480 490 500
NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ QLVDNQPLAA YKWASCALGG
510 520 530 540 550
TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG INLGPIIFVF
560 570 580 590 600
AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY
610 620 630 640 650
VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI
660 670 680 690 700
LSTTAMRCTG EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN
710 720 730 740 750
TIFSVGKSFY LGISILTPWR NIFTRLPKRI YSKILATTDM EIKYKPKVLI
760 770 780 790 800
SQVWNAIIIS MYREHLLAID HVQKLLYHQV PSEIEGKRTL RAPTFFVSQD
810 820 830 840 850
DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP TFTVLTPHYA
860 870 880 890 900
ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA
910 920 930 940 950
YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL
960 970 980 990 1000
YRTISGFMNY SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF
1010 1020 1030 1040 1050
LVSMQRLAKF KPHELENAEF LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA
1060 1070 1080 1090 1100
LIDGHCEILD NGRRRPKFRV QLSGNPILGD GKSDNQNHAL IFYRGEYIQL
1110 1120 1130 1140 1150
IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE EQTTNHPVAI
1160 1170 1180 1190 1200
VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN
1210 1220 1230 1240 1250
ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL
1260 1270 1280 1290 1300
GFGTILNFTT KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN
1310 1320 1330 1340 1350
NLFIQLSLQM FMLTLVNLSS LAHESIMCIY DRNKPKTDVL VPIGCYNFQP
1360 1370 1380 1390 1400
AVDWVRRYTL SIFIVFWIAF VPIVVQELIE RGLWKATQRF FCHLLSLSPM
1410 1420 1430 1440 1450
FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI LYSRFAGSAI
1460 1470 1480 1490 1500
YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF
1510 1520 1530 1540 1550
LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG
1560 1570 1580 1590 1600
DASRAHRTNL IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL
1610 1620 1630 1640 1650
RIIICTLAPI AVNLGVLFFC MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA
1660 1670 1680 1690 1700
VIVHIAFFIV MWVLESFNFV RMLIGVVTCI QCQRLIFHCM TALMLTREFK
1710 1720 1730 1740 1750
NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF AADFVLGHVI
1760 1770 1780 1790 1800
LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY
1810 1820 1830 1840 1850
CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND
1860 1870
TGSQMSTYQS HYYTHTPSLK TWSTIK
Length:1,876
Mass (Da):214,851
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:iAD4B4CB8CB28B5D8
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 conflicti19G → D in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti19G → D in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti19G → D in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti19G → D in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti19G → D in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti113A → P in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti113A → P in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti113A → P in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti113A → P in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti113A → P in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti236I → V in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti236I → V in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti236I → V in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti236I → V in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti236I → V in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti373V → I in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti373V → I in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti373V → I in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti373V → I in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti373V → I in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti437K → T in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti470N → K in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti492K → R in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti492K → R in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti492K → R in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti492K → R in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti492K → R in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti642L → S in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti1341V → F in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti1341V → F in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti1341V → F in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti1341V → F in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti1341V → F in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti1457M → I in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti1457M → I in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti1457M → I in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti1457M → I in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti1457M → I in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti1790T → S in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti1790T → S in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti1790T → S in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti1790T → S in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti1790T → S in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti1827 – 1828KH → DQ in AAC13763 (PubMed:7530227).Curated2
Sequence conflicti1827 – 1828KH → DQ in AAA79760 (PubMed:7542741).Curated2
Sequence conflicti1827 – 1828KH → DQ in AAR86935 (PubMed:14693557).Curated2
Sequence conflicti1827 – 1828KH → DQ in AAR86936 (PubMed:14693557).Curated2
Sequence conflicti1827 – 1828KH → DQ in AAR86937 (PubMed:14693557).Curated2
Sequence conflicti1834D → T in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti1834D → T in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti1834D → T in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti1834D → T in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti1834D → T in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti1844I → V in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti1844I → V in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti1844I → V in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti1844I → V in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti1844I → V in AAR86937 (PubMed:14693557).Curated1
Sequence conflicti1853S → F in AAC13763 (PubMed:7530227).Curated1
Sequence conflicti1853S → F in AAA79760 (PubMed:7542741).Curated1
Sequence conflicti1853S → F in AAR86935 (PubMed:14693557).Curated1
Sequence conflicti1853S → F in AAR86936 (PubMed:14693557).Curated1
Sequence conflicti1853S → F in AAR86937 (PubMed:14693557).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
U08459 Genomic DNA Translation: AAC13763.1
U12893 Genomic DNA Translation: AAC48981.1
D42126 Genomic DNA Translation: BAA07706.1
X80817 Genomic DNA Translation: CAA56783.1
Z46262 Genomic DNA Translation: CAA86404.1
L35923 Genomic DNA Translation: AAA79760.1
AY395693 Genomic DNA Translation: AAR86935.1
AY395694 Genomic DNA Translation: AAR86936.1
AY395695 Genomic DNA Translation: AAR86937.1
U19028 Genomic DNA Translation: AAB67256.1
BK006945 Genomic DNA Translation: DAA09646.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S50235

NCBI Reference Sequences

More...
RefSeqi
NP_013446.1, NM_001182231.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR342W_mRNA; YLR342W_mRNA; YLR342W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851055

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR342W

<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
U08459 Genomic DNA Translation: AAC13763.1
U12893 Genomic DNA Translation: AAC48981.1
D42126 Genomic DNA Translation: BAA07706.1
X80817 Genomic DNA Translation: CAA56783.1
Z46262 Genomic DNA Translation: CAA86404.1
L35923 Genomic DNA Translation: AAA79760.1
AY395693 Genomic DNA Translation: AAR86935.1
AY395694 Genomic DNA Translation: AAR86936.1
AY395695 Genomic DNA Translation: AAR86937.1
U19028 Genomic DNA Translation: AAB67256.1
BK006945 Genomic DNA Translation: DAA09646.1
PIRiS50235
RefSeqiNP_013446.1, NM_001182231.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi31604, 513 interactors
ComplexPortaliCPX-1812 1,3-beta-D-glucan synthase complex
DIPiDIP-5749N
IntActiP38631, 68 interactors
MINTiP38631
STRINGi4932.YLR342W

Protein family/group databases

CAZyiGT48 Glycosyltransferase Family 48
TCDBi9.B.119.1.1 the glycan synthase, fks1 (fks1) family

PTM databases

iPTMnetiP38631

Proteomic databases

MaxQBiP38631
PaxDbiP38631
PRIDEiP38631

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR342W_mRNA; YLR342W_mRNA; YLR342W
GeneIDi851055
KEGGisce:YLR342W

Organism-specific databases

EuPathDBiFungiDB:YLR342W
SGDiS000004334 FKS1

Phylogenomic databases

GeneTreeiENSGT00940000176776
HOGENOMiHOG000216604
InParanoidiP38631
KOiK00706
OMAiFMRDQGY

Enzyme and pathway databases

BioCyciYEAST:YLR342W-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P38631

Family and domain databases

InterProiView protein in InterPro
IPR026899 FKS1-like_dom1
IPR003440 Glyco_trans_48
PfamiView protein in Pfam
PF14288 FKS1_dom1, 1 hit
PF02364 Glucan_synthase, 1 hit
SMARTiView protein in SMART
SM01205 FKS1_dom1, 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 nameiFKS1_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: P38631
Secondary accession number(s): D6VYY0
, Q53YZ4, Q6TKS9, Q6TKT0
<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: October 1, 1994
Last sequence update: February 1, 1996
Last modified: May 8, 2019
This is version 172 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

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
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