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1,3-beta-glucan synthase component FKS1 (EC 2.4.1.34) (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)

 FKS1_YEAST              Reviewed;        1876 AA.
P38631; D6VYY0; Q53YZ4; Q6TKS9; Q6TKT0;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
18-JUL-2018, entry version 165.
RecName: Full=1,3-beta-glucan synthase component FKS1;
EC=2.4.1.34;
AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
AltName: Full=Calcineurin dependent protein 1;
AltName: Full=Calcofluor white hypersensitivity protein 53;
AltName: Full=Echinocandin target gene protein 1;
AltName: Full=FK506 sensitivity protein 1;
AltName: Full=Glucan synthase of cerevisiae protein 1;
AltName: Full=Papulacandin B resistance protein 1;
Name=FKS1; Synonyms=CND1, CWH53, ETG1, GLS1, GSC1, PBR1;
OrderedLocusNames=YLR342W; ORFNames=L8300.6;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, AND DISRUPTION PHENOTYPE.
STRAIN=RC118D;
PubMed=7530227; DOI=10.1016/0378-1119(94)90633-5;
Eng W.-K., Faucette L., McLaughlin M.M., Cafferkey R., Koltin Y.,
Morris R.A., Young P.R., Johnson R.K., Livi G.P.;
"The yeast FKS1 gene encodes a novel membrane protein, mutations in
which confer FK506 and cyclosporin A hypersensitivity and calcineurin-
dependent growth.";
Gene 151:61-71(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY,
TOPOLOGY, AND DISRUPTION PHENOTYPE.
STRAIN=S288c / GRF88;
PubMed=7528927; DOI=10.1073/pnas.91.26.12907;
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.;
"The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral
membrane protein which is a subunit of 1,3-beta-D-glucan synthase.";
Proc. Natl. Acad. Sci. U.S.A. 91:12907-12911(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
STRAIN=ATCC 200589 / A451;
PubMed=7649185; DOI=10.1111/j.1432-1033.1995.0845d.x;
Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y.,
Miyamoto C., Arisawa M., Furuichi Y., Watanabe T.;
"Characterization and gene cloning of 1,3-beta-D-glucan synthase from
Saccharomyces cerevisiae.";
Eur. J. Biochem. 231:845-854(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
STRAIN=S288c / GRF88;
PubMed=7828729; DOI=10.1016/0014-5793(94)01418-Z;
Ram A.F.J., Brekelmans S.S.C., Oehlen L.J.W.M., Klis F.M.;
"Identification of two cell cycle regulated genes affecting the beta
1,3-glucan content of cell walls in Saccharomyces cerevisiae.";
FEBS Lett. 358:165-170(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, AND
DISRUPTION PHENOTYPE.
STRAIN=S288c / GRF88;
PubMed=7592316; DOI=10.1128/jb.177.20.5732-5739.1995;
Castro C., Ribas J.C., Valdivieso M.H., Varona R., del Rey F.,
Duran A.;
"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.";
J. Bacteriol. 177:5732-5739(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 204508 / S288c;
PubMed=7542741; DOI=10.1128/MCB.15.8.4103;
Garrett-Engele P., Moilanen B., Cyert M.S.;
"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.";
Mol. Cell. Biol. 15:4103-4114(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, MUTAGENESIS OF ASN-470
AND LEU-642, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 96519 / YPH250;
PubMed=14693557; DOI=10.1128/AAC.48.1.319-322.2004;
Ohyama T., Miyakoshi S., Isono F.;
"FKS1 mutations responsible for selective resistance of Saccharomyces
cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin
C.";
Antimicrob. Agents Chemother. 48:319-322(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[9]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[10]
DISRUPTION PHENOTYPE.
PubMed=7510323; DOI=10.1099/00221287-139-12-2973;
Parent S.A., Nielsen J.B., Morin N., Chrebet G., Ramadan N.,
Dahl A.M., Hsu M.J., Bostian K.A., Foor F.;
"Calcineurin-dependent growth of an FK506- and CsA-hypersensitive
mutant of Saccharomyces cerevisiae.";
J. Gen. Microbiol. 139:2973-2984(1993).
[11]
INDUCTION.
PubMed=7565718; DOI=10.1128/MCB.15.10.5671;
Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A.,
Nielsen J.B., Foor F.;
"Differential expression and function of two homologous subunits of
yeast 1,3-beta-D-glucan synthase.";
Mol. Cell. Biol. 15:5671-5681(1995).
[12]
ENZYME ACTIVITY, AND INTERACTION WITH RHO1.
PubMed=8662910; DOI=10.1074/jbc.271.24.14604;
Mazur P., Baginsky W.;
"In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-
binding protein Rho1.";
J. Biol. Chem. 271:14604-14609(1996).
[13]
INTERACTION WITH RHO1, AND SUBCELLULAR LOCATION.
PubMed=8602515; DOI=10.1126/science.272.5259.279;
Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y.,
Watanabe T., Levin D.E., Ohya Y.;
"Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-
beta-glucan synthase.";
Science 272:279-281(1996).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11856368; DOI=10.1046/j.1356-9597.2001.00495.x;
Utsugi T., Minemura M., Hirata A., Abe M., Watanabe D., Ohya Y.;
"Movement of yeast 1,3-beta-glucan synthase is essential for uniform
cell wall synthesis.";
Genes Cells 7:1-9(2002).
[15]
ENZYME ACTIVITY, AND MUTAGENESIS OF LYS-877; ALA-899 AND GLN-977.
PubMed=12399379;
Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K.,
Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y.;
"Dissection of upstream regulatory components of the Rho1p effector,
1,3-beta-glucan synthase, in Saccharomyces cerevisiae.";
Genetics 162:663-676(2002).
[16]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND 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.
PubMed=12185837; DOI=10.1002/yea.866;
Dijkgraaf G.J.P., Abe M., Ohya Y., Bussey H.;
"Mutations in Fks1p affect the cell wall content of beta-1,3- and
beta-1,6-glucan in Saccharomyces cerevisiae.";
Yeast 19:671-690(2002).
[17]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-910, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=14557538; DOI=10.1073/pnas.2135500100;
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response
to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[18]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[19]
CASPOFUNGIN HYPERSENSITIVITY.
PubMed=15166135; DOI=10.1534/genetics.167.1.35;
Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H.;
"Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae
using a synthetic interaction network and altered sensitivity to
caspofungin.";
Genetics 167:35-49(2004).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND THR-272, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[22]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-259; LYS-275; LYS-386;
LYS-910; LYS-915; LYS-1539 AND LYS-1547, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11856368}.
-!- CATALYTIC ACTIVITY: UDP-glucose + ((1->3)-beta-D-glucosyl)(n) =
UDP + ((1->3)-beta-D-glucosyl)(n+1). {ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379, ECO:0000269|PubMed:7528927,
ECO:0000269|PubMed:7592316, ECO:0000269|PubMed:8662910}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:8602515, ECO:0000269|PubMed:8662910}.
-!- INTERACTION:
P39704:ERP2; NbExp=2; IntAct=EBI-7708, EBI-6587;
P06780:RHO1; NbExp=3; IntAct=EBI-7708, EBI-15121;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11856368,
ECO:0000269|PubMed:12185837, ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:8602515}. Cell membrane {ECO:0000305}; Multi-
pass membrane protein {ECO:0000305}. Note=Localizes to the sites
of polarized growth. Colocalizes with cortical actin patches and
moves on the cell surface at the sites of cell wall remodeling.
Actin patch motility is required for the movement. Early at the
cell cycle, localizes at the presumed bud site of the mother cell
and at the tip of the small bud. As the bud enlarges, appears as
discernible spots in the medium-sized bud and these spots
colocalize with actin patches. Late in the cell cycle, disappears
in large budded cells, while the actin patches disperse over the
cell. During cytokinesis, is concentrated in the neck, overlapping
with the location of cortical actin patches.
-!- INDUCTION: During vegetative growth. Expressed periodically during
the cell cycle. {ECO:0000269|PubMed:7565718}.
-!- DISRUPTION PHENOTYPE: 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 Ca(2+) 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.
{ECO:0000269|PubMed:14693557, ECO:0000269|PubMed:7510323,
ECO:0000269|PubMed:7528927, ECO:0000269|PubMed:7530227,
ECO:0000269|PubMed:7542741, ECO:0000269|PubMed:7592316}.
-!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
{ECO:0000305}.
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EMBL; U08459; AAC13763.1; -; Genomic_DNA.
EMBL; U12893; AAC48981.1; -; Genomic_DNA.
EMBL; D42126; BAA07706.1; -; Genomic_DNA.
EMBL; X80817; CAA56783.1; -; Genomic_DNA.
EMBL; Z46262; CAA86404.1; -; Genomic_DNA.
EMBL; L35923; AAA79760.1; -; Genomic_DNA.
EMBL; AY395693; AAR86935.1; -; Genomic_DNA.
EMBL; AY395694; AAR86936.1; -; Genomic_DNA.
EMBL; AY395695; AAR86937.1; -; Genomic_DNA.
EMBL; U19028; AAB67256.1; -; Genomic_DNA.
EMBL; BK006945; DAA09646.1; -; Genomic_DNA.
PIR; S50235; S50235.
RefSeq; NP_013446.1; NM_001182231.1.
ProteinModelPortal; P38631; -.
BioGrid; 31604; 503.
ComplexPortal; CPX-1812; 1,3-beta-D-glucan synthase complex.
DIP; DIP-5749N; -.
IntAct; P38631; 77.
MINT; P38631; -.
STRING; 4932.YLR342W; -.
CAZy; GT48; Glycosyltransferase Family 48.
TCDB; 9.B.119.1.1; the glycan synthase, fks1 (fks1) family.
iPTMnet; P38631; -.
MaxQB; P38631; -.
PaxDb; P38631; -.
PRIDE; P38631; -.
EnsemblFungi; YLR342W; YLR342W; YLR342W.
GeneID; 851055; -.
KEGG; sce:YLR342W; -.
EuPathDB; FungiDB:YLR342W; -.
SGD; S000004334; FKS1.
GeneTree; ENSGT00390000004828; -.
HOGENOM; HOG000216604; -.
InParanoid; P38631; -.
KO; K00706; -.
OMA; ASSWYGY; -.
OrthoDB; EOG092C025F; -.
BioCyc; YEAST:YLR342W-MONOMER; -.
PRO; PR:P38631; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IDA:SGD.
GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IDA:SGD.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0008361; P:regulation of cell size; IMP:SGD.
InterPro; IPR026899; FKS1-like_dom1.
InterPro; IPR003440; Glyco_trans_48.
Pfam; PF14288; FKS1_dom1; 1.
Pfam; PF02364; Glucan_synthase; 1.
SMART; SM01205; FKS1_dom1; 1.
1: Evidence at protein level;
Cell membrane; Cell shape; Cell wall biogenesis/degradation;
Complete proteome; Glycosyltransferase; Isopeptide bond; Membrane;
Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 1876 1,3-beta-glucan synthase component FKS1.
/FTId=PRO_0000121725.
TOPO_DOM 1 454 Cytoplasmic. {ECO:0000255}.
TRANSMEM 455 475 Helical. {ECO:0000255}.
TOPO_DOM 476 492 Extracellular. {ECO:0000255}.
TRANSMEM 493 513 Helical. {ECO:0000255}.
TOPO_DOM 514 531 Cytoplasmic. {ECO:0000255}.
TRANSMEM 532 552 Helical. {ECO:0000255}.
TOPO_DOM 553 563 Extracellular. {ECO:0000255}.
TRANSMEM 564 584 Helical. {ECO:0000255}.
TOPO_DOM 585 621 Cytoplasmic. {ECO:0000255}.
TRANSMEM 622 642 Helical. {ECO:0000255}.
TOPO_DOM 643 678 Extracellular. {ECO:0000255}.
TRANSMEM 679 699 Helical. {ECO:0000255}.
TOPO_DOM 700 1358 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1359 1379 Helical. {ECO:0000255}.
TOPO_DOM 1380 1444 Extracellular. {ECO:0000255}.
TRANSMEM 1445 1465 Helical. {ECO:0000255}.
TOPO_DOM 1466 1469 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1470 1490 Helical. {ECO:0000255}.
TOPO_DOM 1491 1560 Extracellular. {ECO:0000255}.
TRANSMEM 1561 1581 Helical. {ECO:0000255}.
TOPO_DOM 1582 1601 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1602 1622 Helical. {ECO:0000255}.
TOPO_DOM 1623 1643 Extracellular. {ECO:0000255}.
TRANSMEM 1644 1664 Helical. {ECO:0000255}.
TOPO_DOM 1665 1672 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1673 1695 Helical. {ECO:0000255}.
TOPO_DOM 1696 1802 Extracellular. {ECO:0000255}.
TRANSMEM 1803 1823 Helical. {ECO:0000255}.
TOPO_DOM 1824 1876 Cytoplasmic. {ECO:0000255}.
MOD_RES 269 269 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 272 272 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 275 275 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 910 910 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 915 915 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 1539 1539 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 1547 1547 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 146 146 E->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 302 302 V->N: In 1082; temperature-sensitive
mutant; no gross alteration in beta-
glucan content of cells; when associated
with DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 329 329 Y->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 335 335 Y->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 470 470 N->K: In ACR79-5; selectively resistant
to antibiotic arborcandin C.
{ECO:0000269|PubMed:14693557}.
MUTAGEN 605 605 T->I: In 1093; temperature-sensitive
mutant; higher beta-glucan content of
cells; when associated with T-761 and
DEL-GSC2. {ECO:0000269|PubMed:12185837}.
MUTAGEN 642 642 L->S: In ACR1A3; selectively resistant to
antibiotic arborcandin C.
{ECO:0000269|PubMed:14693557}.
MUTAGEN 713 713 I->L: In 1163; temperature-sensitive
mutant; no gross alteration in beta-
glucan content of cells; when associated
with V-722 and DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 722 722 I->V: In 1163; temperature-sensitive
mutant; no gross alteration in beta-
glucan content of cells; when associated
with L-713 and DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 761 761 M->T: In 1093; temperature-sensitive
mutant; higher beta-glucan content of
cells; when associated with I-605 and
DEL-GSC2. {ECO:0000269|PubMed:12185837}.
MUTAGEN 823 823 A->V: In 1104; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with E-920 and
DEL-GSC2. {ECO:0000269|PubMed:12185837}.
MUTAGEN 828 828 T->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 853 853 I->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 855 855 L->R: In A6; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 872 872 L->F: In 1144; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with K-907; S-982
and DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 877 877 K->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. {ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379}.
MUTAGEN 899 899 A->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. {ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379}.
MUTAGEN 907 907 E->K: In 1144; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with F-872; S-982
and DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 920 920 D->E: In 1104; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with V-823 and
DEL-GSC2. {ECO:0000269|PubMed:12185837}.
MUTAGEN 932 932 A->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 934 934 E->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 977 977 Q->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. {ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379}.
MUTAGEN 982 982 N->S: In 1144; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with F-872; K-907
and DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 1020 1020 F->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 1047 1047 I->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 1111 1111 E->G: In F4; temperature-sensitive
mutant; lower beta-glucan content of
cells; when associated with DEL-GSC2.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 1258 1258 F->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.
{ECO:0000269|PubMed:12185837}.
MUTAGEN 1520 1520 N->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.
{ECO:0000269|PubMed:12185837}.
CONFLICT 19 19 G -> D (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 113 113 A -> P (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 236 236 I -> V (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 373 373 V -> I (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 437 437 K -> T (in Ref. 1; AAC13763).
{ECO:0000305}.
CONFLICT 470 470 N -> K (in Ref. 7; AAR86936).
{ECO:0000305}.
CONFLICT 492 492 K -> R (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 642 642 L -> S (in Ref. 7; AAR86937).
{ECO:0000305}.
CONFLICT 1341 1341 V -> F (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 1457 1457 M -> I (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 1790 1790 T -> S (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 1827 1828 KH -> DQ (in Ref. 1; AAC13763, 6;
AAA79760 and 7; AAR86935/AAR86936/
AAR86937). {ECO:0000305}.
CONFLICT 1834 1834 D -> T (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 1844 1844 I -> V (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
CONFLICT 1853 1853 S -> F (in Ref. 1; AAC13763, 6; AAA79760
and 7; AAR86935/AAR86936/AAR86937).
{ECO:0000305}.
SEQUENCE 1876 AA; 214851 MW; AD4B4CB8CB28B5D8 CRC64;
MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ
PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG TPGYDSYGGQ YTASQMSYGE
PNSSGTSTPI YGNYDPNAIA MALPNEPYPA WTADSQSPVS IEQIEDIFID LTNRLGFQRD
SMRNMFDHFM VLLDSRSSRM SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN
MSLGKLSRKA RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE
RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE GDFLNRVITP
IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP EGIAKIVLED GTKLIELPLE
ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ
QLVDNQPLAA YKWASCALGG TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG
INLGPIIFVF AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY
VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI LSTTAMRCTG
EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN TIFSVGKSFY LGISILTPWR
NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIIIS MYREHLLAID HVQKLLYHQV
PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP
TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA
YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL YRTISGFMNY
SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF LVSMQRLAKF KPHELENAEF
LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA LIDGHCEILD NGRRRPKFRV QLSGNPILGD
GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE
EQTTNHPVAI VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN
ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL GFGTILNFTT
KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN NLFIQLSLQM FMLTLVNLSS
LAHESIMCIY DRNKPKTDVL VPIGCYNFQP AVDWVRRYTL SIFIVFWIAF VPIVVQELIE
RGLWKATQRF FCHLLSLSPM FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI
LYSRFAGSAI YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF
LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG DASRAHRTNL
IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL RIIICTLAPI AVNLGVLFFC
MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI
QCQRLIFHCM TALMLTREFK NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF
AADFVLGHVI LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY
CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND TGSQMSTYQS
HYYTHTPSLK TWSTIK


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