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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)DescriptionActionsGraphical viewLength
Topological domaini1 – 454CytoplasmicSequence analysisAdd BLAST454
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

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)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001217251 – 18761,3-beta-glucan synthase component FKS1Add BLAST1876

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
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 sources1 Publication
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

MaxQBiP38631.
PRIDEiP38631.

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 interactors.
DIPiDIP-5749N.
IntActiP38631. 67 interactors.
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.
OMAiRRWIVVK.
OrthoDBiEOG092C025F.

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)DescriptionActionsGraphical viewLength
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:
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 interactors.
DIPiDIP-5749N.
IntActiP38631. 67 interactors.
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.
PRIDEiP38631.

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.
OMAiRRWIVVK.
OrthoDBiEOG092C025F.

Enzyme and pathway databases

BioCyciYEAST:YLR342W-MONOMER.

Miscellaneous databases

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...

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: November 2, 2016
This is version 149 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.