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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-Experimental evidence at protein leveli

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

Catalytic activityi

UDP-glucose + ((1->3)-beta-D-glucosyl)(n) = UDP + ((1->3)-beta-D-glucosyl)(n+1).5 Publications

GO - Molecular functioni

  • 1,3-beta-D-glucan synthase activity Source: SGD

GO - Biological processi

  • (1->3)-beta-D-glucan biosynthetic process Source: SGD
  • cell wall organization Source: UniProtKB-KW
  • positive regulation of endocytosis Source: SGD
  • regulation of cell shape Source: UniProtKB-KW
  • regulation of cell size Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:YLR342W-MONOMER.

Protein family/group databases

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

Names & Taxonomyi

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
Gene namesi
Name:FKS1
Synonyms:CND1, CWH53, ETG1, GLS1, GSC1, PBR1
Ordered Locus Names:YLR342W
ORF Names:L8300.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR342W.
SGDiS000004334. FKS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 454454CytoplasmicSequence analysisAdd
BLAST
Transmembranei455 – 47521HelicalSequence analysisAdd
BLAST
Topological domaini476 – 49217ExtracellularSequence analysisAdd
BLAST
Transmembranei493 – 51321HelicalSequence analysisAdd
BLAST
Topological domaini514 – 53118CytoplasmicSequence analysisAdd
BLAST
Transmembranei532 – 55221HelicalSequence analysisAdd
BLAST
Topological domaini553 – 56311ExtracellularSequence analysisAdd
BLAST
Transmembranei564 – 58421HelicalSequence analysisAdd
BLAST
Topological domaini585 – 62137CytoplasmicSequence analysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence analysisAdd
BLAST
Topological domaini643 – 67836ExtracellularSequence analysisAdd
BLAST
Transmembranei679 – 69921HelicalSequence analysisAdd
BLAST
Topological domaini700 – 1358659CytoplasmicSequence analysisAdd
BLAST
Transmembranei1359 – 137921HelicalSequence analysisAdd
BLAST
Topological domaini1380 – 144465ExtracellularSequence analysisAdd
BLAST
Transmembranei1445 – 146521HelicalSequence analysisAdd
BLAST
Topological domaini1466 – 14694CytoplasmicSequence analysis
Transmembranei1470 – 149021HelicalSequence analysisAdd
BLAST
Topological domaini1491 – 156070ExtracellularSequence analysisAdd
BLAST
Transmembranei1561 – 158121HelicalSequence analysisAdd
BLAST
Topological domaini1582 – 160120CytoplasmicSequence analysisAdd
BLAST
Transmembranei1602 – 162221HelicalSequence analysisAdd
BLAST
Topological domaini1623 – 164321ExtracellularSequence analysisAdd
BLAST
Transmembranei1644 – 166421HelicalSequence analysisAdd
BLAST
Topological domaini1665 – 16728CytoplasmicSequence analysis
Transmembranei1673 – 169523HelicalSequence analysisAdd
BLAST
Topological domaini1696 – 1802107ExtracellularSequence analysisAdd
BLAST
Transmembranei1803 – 182321HelicalSequence analysisAdd
BLAST
Topological domaini1824 – 187653CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • 1,3-beta-D-glucan synthase complex Source: SGD
  • actin cortical patch Source: SGD
  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrion Source: UniProtKB-SubCell
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

Pathology & Biotechi

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi146 – 1461E → 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 Publication
Mutagenesisi302 – 3021V → N in 1082; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with DEL-GSC2. 1 Publication
Mutagenesisi329 – 3291Y → 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 Publication
Mutagenesisi335 – 3351Y → 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 Publication
Mutagenesisi470 – 4701N → K in ACR79-5; selectively resistant to antibiotic arborcandin C. 1 Publication
Mutagenesisi605 – 6051T → I in 1093; temperature-sensitive mutant; higher beta-glucan content of cells; when associated with T-761 and DEL-GSC2. 1 Publication
Mutagenesisi642 – 6421L → S in ACR1A3; selectively resistant to antibiotic arborcandin C. 1 Publication
Mutagenesisi713 – 7131I → L in 1163; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with V-722 and DEL-GSC2. 1 Publication
Mutagenesisi722 – 7221I → V in 1163; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with L-713 and DEL-GSC2. 1 Publication
Mutagenesisi761 – 7611M → T in 1093; temperature-sensitive mutant; higher beta-glucan content of cells; when associated with I-605 and DEL-GSC2. 1 Publication
Mutagenesisi823 – 8231A → V in 1104; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with E-920 and DEL-GSC2. 1 Publication
Mutagenesisi828 – 8281T → 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 Publication
Mutagenesisi853 – 8531I → 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 Publication
Mutagenesisi855 – 8551L → R in A6; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with DEL-GSC2. 1 Publication
Mutagenesisi872 – 8721L → F in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with K-907; S-982 and DEL-GSC2. 1 Publication
Mutagenesisi877 – 8771K → 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 Publications
Mutagenesisi899 – 8991A → 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 Publications
Mutagenesisi907 – 9071E → K in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with F-872; S-982 and DEL-GSC2. 1 Publication
Mutagenesisi920 – 9201D → E in 1104; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with V-823 and DEL-GSC2. 1 Publication
Mutagenesisi932 – 9321A → 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 Publication
Mutagenesisi934 – 9341E → 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 Publication
Mutagenesisi977 – 9771Q → 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 Publications
Mutagenesisi982 – 9821N → S in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with F-872; K-907 and DEL-GSC2. 1 Publication
Mutagenesisi1020 – 10201F → 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 Publication
Mutagenesisi1047 – 10471I → 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 Publication
Mutagenesisi1111 – 11111E → G in F4; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with DEL-GSC2. 1 Publication
Mutagenesisi1258 – 12581F → 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 Publication
Mutagenesisi1520 – 15201N → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 187618761,3-beta-glucan synthase component FKS1PRO_0000121725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691PhosphothreonineCombined sources
Modified residuei272 – 2721PhosphothreonineCombined sources
Cross-linki910 – 910Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP38631.
PeptideAtlasiP38631.

PTM databases

iPTMnetiP38631.

Expressioni

Inductioni

During vegetative growth. Expressed periodically during the cell cycle.1 Publication

Interactioni

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi31604. 265 interactions.
DIPiDIP-5749N.
IntActiP38631. 67 interactions.
MINTiMINT-619820.

Structurei

3D structure databases

ProteinModelPortaliP38631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 48 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000004828.
HOGENOMiHOG000216604.
InParanoidiP38631.
KOiK00706.
OMAiFLIYFWF.
OrthoDBiEOG7JT74G.

Family and domain databases

InterProiIPR026899. FKS1-like_dom1.
IPR003440. Glyco_trans_48.
[Graphical view]
PfamiPF14288. FKS1_dom1. 1 hit.
PF02364. Glucan_synthase. 1 hit.
[Graphical view]
SMARTiSM01205. FKS1_dom1. 1 hit.
[Graphical view]

Sequencei

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
Checksum:iAD4B4CB8CB28B5D8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191G → D in AAC13763 (PubMed:7530227).Curated
Sequence conflicti19 – 191G → D in AAA79760 (PubMed:7542741).Curated
Sequence conflicti19 – 191G → D in AAR86935 (PubMed:14693557).Curated
Sequence conflicti19 – 191G → D in AAR86936 (PubMed:14693557).Curated
Sequence conflicti19 – 191G → D in AAR86937 (PubMed:14693557).Curated
Sequence conflicti113 – 1131A → P in AAC13763 (PubMed:7530227).Curated
Sequence conflicti113 – 1131A → P in AAA79760 (PubMed:7542741).Curated
Sequence conflicti113 – 1131A → P in AAR86935 (PubMed:14693557).Curated
Sequence conflicti113 – 1131A → P in AAR86936 (PubMed:14693557).Curated
Sequence conflicti113 – 1131A → P in AAR86937 (PubMed:14693557).Curated
Sequence conflicti236 – 2361I → V in AAC13763 (PubMed:7530227).Curated
Sequence conflicti236 – 2361I → V in AAA79760 (PubMed:7542741).Curated
Sequence conflicti236 – 2361I → V in AAR86935 (PubMed:14693557).Curated
Sequence conflicti236 – 2361I → V in AAR86936 (PubMed:14693557).Curated
Sequence conflicti236 – 2361I → V in AAR86937 (PubMed:14693557).Curated
Sequence conflicti373 – 3731V → I in AAC13763 (PubMed:7530227).Curated
Sequence conflicti373 – 3731V → I in AAA79760 (PubMed:7542741).Curated
Sequence conflicti373 – 3731V → I in AAR86935 (PubMed:14693557).Curated
Sequence conflicti373 – 3731V → I in AAR86936 (PubMed:14693557).Curated
Sequence conflicti373 – 3731V → I in AAR86937 (PubMed:14693557).Curated
Sequence conflicti437 – 4371K → T in AAC13763 (PubMed:7530227).Curated
Sequence conflicti470 – 4701N → K in AAR86936 (PubMed:14693557).Curated
Sequence conflicti492 – 4921K → R in AAC13763 (PubMed:7530227).Curated
Sequence conflicti492 – 4921K → R in AAA79760 (PubMed:7542741).Curated
Sequence conflicti492 – 4921K → R in AAR86935 (PubMed:14693557).Curated
Sequence conflicti492 – 4921K → R in AAR86936 (PubMed:14693557).Curated
Sequence conflicti492 – 4921K → R in AAR86937 (PubMed:14693557).Curated
Sequence conflicti642 – 6421L → S in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1341 – 13411V → F in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1341 – 13411V → F in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1341 – 13411V → F in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1341 – 13411V → F in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1341 – 13411V → F in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1457 – 14571M → I in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1457 – 14571M → I in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1457 – 14571M → I in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1457 – 14571M → I in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1457 – 14571M → I in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1790 – 17901T → S in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1790 – 17901T → S in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1790 – 17901T → S in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1790 – 17901T → S in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1790 – 17901T → S in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1827 – 18282KH → DQ in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1827 – 18282KH → DQ in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1827 – 18282KH → DQ in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1827 – 18282KH → DQ in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1827 – 18282KH → DQ in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1834 – 18341D → T in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1834 – 18341D → T in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1834 – 18341D → T in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1834 – 18341D → T in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1834 – 18341D → T in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1844 – 18441I → V in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1844 – 18441I → V in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1844 – 18441I → V in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1844 – 18441I → V in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1844 – 18441I → V in AAR86937 (PubMed:14693557).Curated
Sequence conflicti1853 – 18531S → F in AAC13763 (PubMed:7530227).Curated
Sequence conflicti1853 – 18531S → F in AAA79760 (PubMed:7542741).Curated
Sequence conflicti1853 – 18531S → F in AAR86935 (PubMed:14693557).Curated
Sequence conflicti1853 – 18531S → F in AAR86936 (PubMed:14693557).Curated
Sequence conflicti1853 – 18531S → F in AAR86937 (PubMed:14693557).Curated

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.

Genome annotation databases

EnsemblFungiiYLR342W; YLR342W; YLR342W.
GeneIDi851055.
KEGGisce:YLR342W.

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

ProteinModelPortaliP38631.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31604. 265 interactions.
DIPiDIP-5749N.
IntActiP38631. 67 interactions.
MINTiMINT-619820.

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.
PeptideAtlasiP38631.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR342W; YLR342W; YLR342W.
GeneIDi851055.
KEGGisce:YLR342W.

Organism-specific databases

EuPathDBiFungiDB:YLR342W.
SGDiS000004334. FKS1.

Phylogenomic databases

GeneTreeiENSGT00390000004828.
HOGENOMiHOG000216604.
InParanoidiP38631.
KOiK00706.
OMAiFLIYFWF.
OrthoDBiEOG7JT74G.

Enzyme and pathway databases

BioCyciYEAST:YLR342W-MONOMER.

Miscellaneous databases

NextBioi967673.
PROiP38631.

Family and domain databases

InterProiIPR026899. FKS1-like_dom1.
IPR003440. Glyco_trans_48.
[Graphical view]
PfamiPF14288. FKS1_dom1. 1 hit.
PF02364. Glucan_synthase. 1 hit.
[Graphical view]
SMARTiSM01205. FKS1_dom1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast FKS1 gene encodes a novel membrane protein, mutations in which confer FK506 and cyclosporin A hypersensitivity and calcineurin-dependent growth."
    Eng W.-K., Faucette L., McLaughlin M.M., Cafferkey R., Koltin Y., Morris R.A., Young P.R., Johnson R.K., Livi G.P.
    Gene 151:61-71(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, DISRUPTION PHENOTYPE.
    Strain: RC118D.
  2. "The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral membrane protein which is a subunit of 1,3-beta-D-glucan synthase."
    Douglas C.M., Foor F., Marrinan J.A., Morin N., Nielsen J.B., Dahl A.M., Mazur P., Baginsky W., Li W., El-Sherbeini M., Clemas J.A., Mandala S.M., Frommer B.R., Kurtz M.B.
    Proc. Natl. Acad. Sci. U.S.A. 91:12907-12911(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, TOPOLOGY, DISRUPTION PHENOTYPE.
    Strain: S288c / GRF88.
  3. "Characterization and gene cloning of 1,3-beta-D-glucan synthase from Saccharomyces cerevisiae."
    Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y., Miyamoto C., Arisawa M., Furuichi Y., Watanabe T.
    Eur. J. Biochem. 231:845-854(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME.
    Strain: ATCC 200589 / A451.
  4. "Identification of two cell cycle regulated genes affecting the beta 1,3-glucan content of cell walls in Saccharomyces cerevisiae."
    Ram A.F.J., Brekelmans S.S.C., Oehlen L.J.W.M., Klis F.M.
    FEBS Lett. 358:165-170(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME.
    Strain: S288c / GRF88.
  5. "Papulacandin B resistance in budding and fission yeasts: isolation and characterization of a gene involved in (1,3)beta-D-glucan synthesis in Saccharomyces cerevisiae."
    Castro C., Ribas J.C., Valdivieso M.H., Varona R., del Rey F., Duran A.
    J. Bacteriol. 177:5732-5739(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, DISRUPTION PHENOTYPE.
    Strain: S288c / GRF88.
  6. "Calcineurin, the Ca2+/calmodulin-dependent protein phosphatase, is essential in yeast mutants with cell integrity defects and in mutants that lack a functional vacuolar H(+)-ATPase."
    Garrett-Engele P., Moilanen B., Cyert M.S.
    Mol. Cell. Biol. 15:4103-4114(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, DISRUPTION PHENOTYPE.
    Strain: ATCC 204508 / S288c.
  7. "FKS1 mutations responsible for selective resistance of Saccharomyces cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin C."
    Ohyama T., Miyakoshi S., Isono F.
    Antimicrob. Agents Chemother. 48:319-322(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, MUTAGENESIS OF ASN-470 AND LEU-642, DISRUPTION PHENOTYPE.
    Strain: ATCC 96519 / YPH250.
  8. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  9. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  10. "Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of Saccharomyces cerevisiae."
    Parent S.A., Nielsen J.B., Morin N., Chrebet G., Ramadan N., Dahl A.M., Hsu M.J., Bostian K.A., Foor F.
    J. Gen. Microbiol. 139:2973-2984(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. "Differential expression and function of two homologous subunits of yeast 1,3-beta-D-glucan synthase."
    Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A., Nielsen J.B., Foor F.
    Mol. Cell. Biol. 15:5671-5681(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding protein Rho1."
    Mazur P., Baginsky W.
    J. Biol. Chem. 271:14604-14609(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, INTERACTION WITH RHO1.
  13. "Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-glucan synthase."
    Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y., Watanabe T., Levin D.E., Ohya Y.
    Science 272:279-281(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHO1, SUBCELLULAR LOCATION.
  14. "Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell wall synthesis."
    Utsugi T., Minemura M., Hirata A., Abe M., Watanabe D., Ohya Y.
    Genes Cells 7:1-9(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "Dissection of upstream regulatory components of the Rho1p effector, 1,3-beta-glucan synthase, in Saccharomyces cerevisiae."
    Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K., Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y.
    Genetics 162:663-676(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF LYS-877; ALA-899 AND GLN-977.
  16. "Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae."
    Dijkgraaf G.J.P., Abe M., Ohya Y., Bussey H.
    Yeast 19:671-690(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-146; VAL-302; TYR-329; TYR-335; THR-605; ILE-713; ILE-722; MET-761; ALA-823; THR-828; ILE-853; LEU-855; LEU-872; LYS-877; ALA-899; GLU-907; ASP-920; ALA-932; GLU-934; GLN-977; ASN-982; PHE-1020; ILE-1047; GLU-1111; PHE-1258 AND ASN-1520.
  17. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-910.
  18. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  19. "Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin."
    Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H.
    Genetics 167:35-49(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CASPOFUNGIN HYPERSENSITIVITY.
  20. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
    Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
    J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  21. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND THR-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFKS1_YEAST
AccessioniPrimary (citable) accession number: P38631
Secondary accession number(s): D6VYY0
, Q53YZ4, Q6TKS9, Q6TKT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.