GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

High osmolarity signaling protein SHO1 (Osmosensor SHO1) (Suppressor of SUA8-1 mutation) (Synthetic high osmolarity-sensitive protein 1)

 SHO1_YEAST              Reviewed;         367 AA.
P40073; D3DM24;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-APR-2020, entry version 170.
RecName: Full=High osmolarity signaling protein SHO1;
AltName: Full=Osmosensor SHO1;
AltName: Full=Suppressor of SUA8-1 mutation;
AltName: Full=Synthetic high osmolarity-sensitive protein 1;
Name=SHO1; Synonyms=SSU81; OrderedLocusNames=YER118C;
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].
Berroteran R.W., Hampsey M.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=7624781; DOI=10.1126/science.7624781;
Maeda T., Takekawa M., Saito H.;
"Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-
containing osmosensor.";
Science 269:554-558(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
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).
[5]
FUNCTION, AND INTERACTION WITH PBS2.
PubMed=9180081; DOI=10.1126/science.276.5319.1702;
Posas F., Saito H.;
"Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold
role of Pbs2p MAPKK.";
Science 276:1702-1705(1997).
[6]
FUNCTION.
PubMed=9744864; DOI=10.1101/gad.12.18.2874;
O'Rourke S.M., Herskowitz I.;
"The Hog1 MAPK prevents cross talk between the HOG and pheromone response
MAPK pathways in Saccharomyces cerevisiae.";
Genes Dev. 12:2874-2886(1998).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PBS2.
PubMed=10970855; DOI=10.1093/emboj/19.17.4623;
Raitt D.C., Posas F., Saito H.;
"Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent
activation of the Hog1 MAPK pathway.";
EMBO J. 19:4623-4631(2000).
[8]
FUNCTION.
PubMed=11084293; DOI=10.1016/s0891-5849(00)00432-9;
Singh K.K.;
"The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates
response to oxidative stress and in an oxidant-specific fashion.";
Free Radic. Biol. Med. 29:1043-1050(2000).
[9]
FUNCTION.
PubMed=10762242; DOI=10.1128/jb.182.9.2428-2437.2000;
Garcia-Rodriguez L.J., Duran A., Roncero C.;
"Calcofluor antifungal action depends on chitin and a functional high-
osmolarity glycerol response (HOG) pathway: evidence for a physiological
role of the Saccharomyces cerevisiae HOG pathway under noninducing
conditions.";
J. Bacteriol. 182:2428-2437(2000).
[10]
FUNCTION.
PubMed=10931333; DOI=10.1046/j.1365-2958.2000.02002.x;
Van Wuytswinkel O., Reiser V., Siderius M., Kelders M.C., Ammerer G.,
Ruis H., Mager W.H.;
"Response of Saccharomyces cerevisiae to severe osmotic stress: evidence
for a novel activation mechanism of the HOG MAP kinase pathway.";
Mol. Microbiol. 37:382-397(2000).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10980703; DOI=10.1038/35023568;
Reiser V., Salah S.M., Ammerer G.;
"Polarized localization of yeast Pbs2 depends on osmostress, the membrane
protein Sho1 and Cdc42.";
Nat. Cell Biol. 2:620-627(2000).
[12]
FUNCTION.
PubMed=11922108; DOI=10.1266/ggs.76.393;
Toh-e A., Oguchi T.;
"Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate
Hog1 kinase and confer copper-resistance in Saccharomyces cerevisisae.";
Genes Genet. Syst. 76:393-410(2001).
[13]
FUNCTION.
PubMed=12455951; DOI=10.1128/ec.1.2.163-173.2002;
Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K., Ota I.M.;
"Heat stress activates the yeast high-osmolarity glycerol mitogen-activated
protein kinase pathway, and protein tyrosine phosphatases are essential
under heat stress.";
Eukaryot. Cell 1:163-173(2002).
[14]
SUBCELLULAR LOCATION.
PubMed=12374868; DOI=10.1073/pnas.172517799;
Bagnat M., Simons K.;
"Cell surface polarization during yeast mating.";
Proc. Natl. Acad. Sci. U.S.A. 99:14183-14188(2002).
[15]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[16]
DOMAIN, AND INTERACTION WITH PBS2.
PubMed=14668868; DOI=10.1038/nature02178;
Zarrinpar A., Park S.H., Lim W.A.;
"Optimization of specificity in a cellular protein interaction network by
negative selection.";
Nature 426:676-680(2003).
[17]
FUNCTION.
PubMed=12511654; DOI=10.1126/science.1076979;
Park S.H., Zarrinpar A., Lim W.A.;
"Rewiring MAP kinase pathways using alternative scaffold assembly
mechanisms.";
Science 299:1061-1064(2003).
[18]
FUNCTION, AND INTERACTION WITH MSB2.
PubMed=15256499; DOI=10.1101/gad.1178604;
Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K.,
Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.;
"A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous
growth pathway in yeast.";
Genes Dev. 18:1695-1708(2004).
[19]
FUNCTION, AND INTERACTION WITH FUS1.
PubMed=15020407; DOI=10.1534/genetics.166.1.67;
Nelson B., Parsons A.B., Evangelista M., Schaefer K., Kennedy K.,
Ritchie S., Petryshen T.L., Boone C.;
"Fus1p interacts with components of the Hog1p mitogen-activated protein
kinase and Cdc42p morphogenesis signaling pathways to control cell fusion
during yeast mating.";
Genetics 166:67-77(2004).
[20]
FUNCTION.
PubMed=14595107; DOI=10.1091/mbc.e03-07-0521;
O'Rourke S.M., Herskowitz I.;
"Unique and redundant roles for HOG MAPK pathway components as revealed by
whole-genome expression analysis.";
Mol. Biol. Cell 15:532-542(2004).
[21]
FUNCTION, INTERACTION WITH PBS2, DOMAIN, AND MUTAGENESIS OF TYR-309;
ASP-317 AND TYR-355.
PubMed=15200958; DOI=10.1016/j.molcel.2004.05.024;
Marles J.A., Dahesh S., Haynes J., Andrews B.J., Davidson A.R.;
"Protein-protein interaction affinity plays a crucial role in controlling
the Sho1p-mediated signal transduction pathway in yeast.";
Mol. Cell 14:813-823(2004).
[22]
FUNCTION, AND INTERACTION WITH STE11.
PubMed=15200959; DOI=10.1016/j.molcel.2004.06.011;
Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A.;
"Sho1 and Pbs2 act as coscaffolds linking components in the yeast high
osmolarity MAP kinase pathway.";
Mol. Cell 14:825-832(2004).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling
pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[24]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STE11 AND STE50.
PubMed=16778768; DOI=10.1038/sj.emboj.7601192;
Tatebayashi K., Yamamoto K., Tanaka K., Tomida T., Maruoka T., Kasukawa E.,
Saito H.;
"Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory
HOG MAPK pathway.";
EMBO J. 25:3033-3044(2006).
[25]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[26]
PHOSPHORYLATION AT SER-166, MUTAGENESIS OF SER-166, AND SUBUNIT.
PubMed=17363249; DOI=10.1016/j.cub.2007.02.044;
Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H., Elston T.C.,
Dohlman H.G.;
"A systems-biology analysis of feedback inhibition in the Sho1 osmotic-
stress-response pathway.";
Curr. Biol. 17:659-667(2007).
[27]
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).
[28]
FUNCTION.
PubMed=18480263; DOI=10.1073/pnas.0710770105;
Hersen P., McClean M.N., Mahadevan L., Ramanathan S.;
"Signal processing by the HOG MAP kinase pathway.";
Proc. Natl. Acad. Sci. U.S.A. 105:7165-7170(2008).
[29]
FUNCTION.
PubMed=19439450; DOI=10.1091/mbc.e08-07-0760;
Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.;
"The signaling mucins Msb2 and Hkr1 differentially regulate the
filamentation mitogen-activated protein kinase pathway and contribute to a
multimodal response.";
Mol. Biol. Cell 20:3101-3114(2009).
[30]
FUNCTION.
PubMed=19318625; DOI=10.1126/scisignal.2000056;
Macia J., Regot S., Peeters T., Conde N., Sole R., Posas F.;
"Dynamic signaling in the Hog1 MAPK pathway relies on high basal signal
transduction.";
Sci. Signal. 2:RA13-RA13(2009).
[31]
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).
[32]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 298-367.
Kursula P., Kursula I., Song Y.H., Paraskevopoulos M., Wilmanns M.;
"Structural genomics of yeast SH3 domains.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Detects changes in external osmolarity and activates PBS2 through the
stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2
activation leads to changes in glycerol production that helps to
balance the intracellular and external osmotic pressures. Activates
also HOG1 in response to heat stress and mediates resistance to
oxidative stress. Involved in the regulation of the mating pathway. May
be a receptor that feeds into the pseudohyphal growth pathway.
{ECO:0000269|PubMed:10762242, ECO:0000269|PubMed:10931333,
ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:10980703,
ECO:0000269|PubMed:11084293, ECO:0000269|PubMed:11922108,
ECO:0000269|PubMed:12455951, ECO:0000269|PubMed:12511654,
ECO:0000269|PubMed:14595107, ECO:0000269|PubMed:15020407,
ECO:0000269|PubMed:15200958, ECO:0000269|PubMed:15200959,
ECO:0000269|PubMed:15256499, ECO:0000269|PubMed:16778768,
ECO:0000269|PubMed:18480263, ECO:0000269|PubMed:19318625,
ECO:0000269|PubMed:19439450, ECO:0000269|PubMed:7624781,
ECO:0000269|PubMed:9180081, ECO:0000269|PubMed:9744864}.
-!- SUBUNIT: Forms homooligomers. Interacts (via the SH3 domain) with PBS2.
Interacts with FUS1, STE11, STE50 and RNA polymerase II.
{ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:14668868,
ECO:0000269|PubMed:15020407, ECO:0000269|PubMed:15200958,
ECO:0000269|PubMed:15200959, ECO:0000269|PubMed:15256499,
ECO:0000269|PubMed:16778768, ECO:0000269|PubMed:17363249,
ECO:0000269|PubMed:9180081}.
-!- INTERACTION:
P40073; P42884: AAD14; NbExp=2; IntAct=EBI-18140, EBI-1994;
P40073; P36122: BCH2; NbExp=2; IntAct=EBI-18140, EBI-26374;
P40073; Q07533: CYK3; NbExp=4; IntAct=EBI-18140, EBI-31510;
P40073; P11710: FUS1; NbExp=7; IntAct=EBI-18140, EBI-7179;
P40073; P40036: GIP2; NbExp=2; IntAct=EBI-18140, EBI-7612;
P40073; Q05080: HOF1; NbExp=5; IntAct=EBI-18140, EBI-5412;
P40073; P53901: INN1; NbExp=4; IntAct=EBI-18140, EBI-28955;
P40073; Q12446: LAS17; NbExp=5; IntAct=EBI-18140, EBI-10022;
P40073; P53153: LCL3; NbExp=2; IntAct=EBI-18140, EBI-23857;
P40073; P21339: MSB1; NbExp=2; IntAct=EBI-18140, EBI-11322;
P40073; P08018: PBS2; NbExp=8; IntAct=EBI-18140, EBI-12972;
P40073; P39081: PCF11; NbExp=2; IntAct=EBI-18140, EBI-12980;
P40073; P39083: RGA1; NbExp=2; IntAct=EBI-18140, EBI-15044;
P40073; P23561: STE11; NbExp=3; IntAct=EBI-18140, EBI-18259;
P40073; P25344: STE50; NbExp=3; IntAct=EBI-18140, EBI-18305;
P40073; Q06412: TUS1; NbExp=3; IntAct=EBI-18140, EBI-37117;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Bud.
Bud neck. Cell projection. Note=Localizes at the tip of the mating
projection during conjugation.
-!- MISCELLANEOUS: Present with 2330 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; U15653; AAA61904.1; -; Genomic_DNA.
EMBL; L41926; AAC41664.1; -; Genomic_DNA.
EMBL; U18916; AAC03216.1; -; Genomic_DNA.
EMBL; BK006939; DAA07778.1; -; Genomic_DNA.
PIR; S50621; S50621.
RefSeq; NP_011043.1; NM_001179008.1.
PDB; 2VKN; X-ray; 2.05 A; A=298-367.
PDBsum; 2VKN; -.
SMR; P40073; -.
BioGrid; 36863; 287.
ComplexPortal; CPX-1140; HICS complex.
DIP; DIP-2472N; -.
IntAct; P40073; 78.
MINT; P40073; -.
STRING; 4932.YER118C; -.
iPTMnet; P40073; -.
PaxDb; P40073; -.
PRIDE; P40073; -.
EnsemblFungi; YER118C_mRNA; YER118C; YER118C.
GeneID; 856854; -.
KEGG; sce:YER118C; -.
EuPathDB; FungiDB:YER118C; -.
SGD; S000000920; SHO1.
HOGENOM; CLU_043316_0_0_1; -.
InParanoid; P40073; -.
KO; K11246; -.
OMA; WWQAKKA; -.
BioCyc; YEAST:G3O-30282-MONOMER; -.
Reactome; R-SCE-194840; Rho GTPase cycle.
Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
EvolutionaryTrace; P40073; -.
PRO; PR:P40073; -.
Proteomes; UP000002311; Chromosome V.
RNAct; P40073; protein.
GO; GO:0071944; C:cell periphery; HDA:SGD.
GO; GO:0005933; C:cellular bud; IDA:SGD.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
GO; GO:0044697; C:HICS complex; IPI:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043332; C:mating projection tip; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:SGD.
GO; GO:0005034; F:osmosensor activity; IPI:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:SGD.
GO; GO:0030010; P:establishment of cell polarity; IGI:SGD.
GO; GO:0007231; P:osmosensory signaling pathway; IGI:SGD.
GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
CDD; cd11855; SH3_Sho1p; 1.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR039644; Sho1.
InterPro; IPR035522; Sho1_SH3.
PANTHER; PTHR15735:SF15; PTHR15735:SF15; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Glycoprotein; Membrane;
Phosphoprotein; Reference proteome; SH3 domain; Stress response;
Transmembrane; Transmembrane helix.
CHAIN 1..367
/note="High osmolarity signaling protein SHO1"
/id="PRO_0000072231"
TOPO_DOM 1..32
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 33..53
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 54..65
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 66..86
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 87..93
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 94..114
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 115..122
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 123..143
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 144..367
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 300..361
/note="SH3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
MOD_RES 166
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:17363249"
CARBOHYD 59
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
MUTAGEN 166
/note="S->E: Diminishes the formation of oligomers, dampens
activation of the HOG1 kinase, and impairs growth in high-
salt or sorbitol conditions."
/evidence="ECO:0000269|PubMed:17363249"
MUTAGEN 309
/note="Y->A: Decreases the interaction with PBS2 and leads
to decreased HOG pathway response and increased aberrant
mating pathway activation."
/evidence="ECO:0000269|PubMed:15200958"
MUTAGEN 317
/note="D->I,H: Decreases the interaction with PBS2 and
leads to decreased HOG pathway response and increased
aberrant mating pathway activation."
/evidence="ECO:0000269|PubMed:15200958"
MUTAGEN 355
/note="Y->A,F,I,M: Decreases the interaction with PBS2 and
leads to decreased HOG pathway response and increased
aberrant mating pathway activation."
/evidence="ECO:0000269|PubMed:15200958"
STRAND 302..309
/evidence="ECO:0000244|PDB:2VKN"
STRAND 315..317
/evidence="ECO:0000244|PDB:2VKN"
STRAND 328..332
/evidence="ECO:0000244|PDB:2VKN"
STRAND 336..342
/evidence="ECO:0000244|PDB:2VKN"
STRAND 348..352
/evidence="ECO:0000244|PDB:2VKN"
HELIX 353..355
/evidence="ECO:0000244|PDB:2VKN"
STRAND 356..363
/evidence="ECO:0000244|PDB:2VKN"
SEQUENCE 367 AA; 41126 MW; E467A4D50AA3EDB6 CRC64;
MSISSKIRPT PRKPSRMATD HSFKMKKFYA DPFAISSISL AIVSWVIAIG GSISSASTNE
SFPRFTWWGI VYQFLIICSL MLFYCFDLVD HYRIFITTSI AVAFVYNTNS ATNLVYADGP
KKAAASAGVI LLSIINLIWI LYYGGDNASP TNRWIDSFSI KGIRPSPLEN SLHRARRRGN
RNTTPYQNNV YNDAIRDSGY ATQFDGYPQQ QPSHTNYVSS TALAGFENTQ PNTSEAVNLH
LNTLQQRINS ASNAKETNDN SNNQTNTNIG NTFDTDFSNG NTETTMGDTL GLYSDIGDDN
FIYKAKALYP YDADDDDAYE ISFEQNEILQ VSDIEGRWWK ARRANGETGI IPSNYVQLID
GPEEMHR


Related products :

Catalog number Product name Quantity
25-743 RIOK3 was identified by the similarity to the Aspergillus nidulans SUDD protein, an extragenic suppressor of the heat-sensitive bimD6 mutation that fails to attach properly to the spindle microtubules 0.05 mg
AC-405L High Density Chelate Kit, Kit + 40 empty mini columns Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capaci 1 Kit
AC-405L High Density Chelate Kit, Kit + 40 empty mini columns Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capacity 1Kit
KT184 C_Reactive Protein (CRP) high sensitive 96 Tests
KT184 C_Reactive Protein (CRP) high sensitive 96 Tests
KT097 C_Reactive Protein (CRP) high sensitive 96 Tests
KT097 C_Reactive Protein (CRP) high sensitive 96 Tests
KT095 C_Reactive Protein (CRP) high sensitive 96 Tests
KT095 C_Reactive Protein (CRP) high sensitive 96 Tests
AC-405 High Density Chelate Kit, Kit Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capacity 1Kit
AC-405 High Density Chelate Kit, Kit Includes 2 ml High Density Metal Free, 2 ml High Density Nickel, 2 ml High Density Zinc and 2 ml High Density Cobalt Agarose High Binding Capacity 1 Kit
ELI-6449 CRP High Sensitive (C-reactive Protein) ELISA 96 Wells
ELI-6449 CRP High Sensitive (С-reactive Protein) ELISA 10 kits
KT099 C_Reactive Protein (CRP) ELISA (High Sensitive) 96 Tests
KT099 C_Reactive Protein (CRP) ELISA (High Sensitive) 96 Tests
KT100 C_Reactive Protein (CRP) high sensitive rat reference serum 1 ml
KT-184 Research Kits: C-Reactive Protein ELISA (High-Sensitive), Pig 96 tests
KT098 C_Reactive Protein (CRP) high sensitive reference serum 1 ml
KT098 C_Reactive Protein (CRP) high sensitive reference serum 1 ml
ELI-6449 CRP High Sensitive (C-reactive Protein) ELISA with CE mark 96 Wells
KT100 C_Reactive Protein (CRP) high sensitive rat reference serum 1 ml
KT096 C_Reactive Protein (CRP) high sensitive mouse reference serum 1 ml
HEX655Ge High Sensitive ELISA Kit for Escherichia coli Protein (ECP) General 96T
ELI-6449 CRP High Sensitive (С-reactive Protein) ELISA, Virology-Serology 10 kits
KT096 C_Reactive Protein (CRP) high sensitive mouse reference serum 1 ml
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP232: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP1371: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP211: BMP signaling pathway
WP1049: G Protein Signaling Pathways
WP35: G Protein Signaling Pathways
WP2032: TSH signaling pathway
WP2292: Chemokine signaling pathway
WP510: MAPK Signaling Pathway
WP1673: Naphthalene and anthracene degradation
WP731: Sterol regulatory element binding protein related
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1678: Nucleotide excision repair
WP1690: Propanoate metabolism
WP1625: Base excision repair
WP1654: gamma-Hexachlorocyclohexane degradation
WP1694: Pyrimidine metabolism
WP1502: Mitochondrial biogenesis
WP1713: Two-component system

Related Genes :
[SHO1 SSU81 YER118C] High osmolarity signaling protein SHO1 (Osmosensor SHO1) (Suppressor of SUA8-1 mutation) (Synthetic high osmolarity-sensitive protein 1)
[MOS1 SHO1 MAA_01571] High osmolarity signaling protein MOS1 (Osmosensor MOS1)
[HOG1 SSK3 YLR113W L2931 L9354.2] Mitogen-activated protein kinase HOG1 (MAP kinase HOG1) (EC 2.7.11.24) (High osmolarity glycerol response protein 1)
[sho1 NCU08067] High osmolarity signaling protein sho1 (Osmosensor sho1)
[DCL4 SHO1 Os04g0509300 LOC_Os04g43050 OSJNBb0065L13.5] Endoribonuclease Dicer homolog 4 (EC 3.1.26.-) (Dicer-like protein 4) (OsDCL4) (Protein SHOOT ORGANIZATION 1)
[envZ ompB perA tpo b3404 JW3367] Sensor histidine kinase EnvZ (EC 2.7.13.3) (Osmolarity sensor protein EnvZ)
[SLN1 YPD2 YIL147C] Osmosensing histidine protein kinase SLN1 (EC 2.7.13.3) (Osmolarity two-component system protein SLN1) (Tyrosine phosphatase-dependent protein 2)
[STE20 YHL007C] Serine/threonine-protein kinase STE20 (EC 2.7.11.1)
[PBS2 HOG4 SFS4 SSK4 YJL128C J0699] MAP kinase kinase PBS2 (EC 2.7.12.2) (Polymyxin B resistance protein 2) (Suppressor of fluoride sensitivity 4)
[STE11 YLR362W L8039.10] Serine/threonine-protein kinase STE11 (EC 2.7.11.25)
[DGK1 HSD1 YOR311C O6111] CTP-dependent diacylglycerol kinase 1 (EC 2.7.1.174) (Diglyceride kinase 1) (DAG kinase 1) (High-copy suppressor of SLY1 defect protein 1)
[SLC5A7 CHT1] High affinity choline transporter 1 (Hemicholinium-3-sensitive choline transporter) (CHT) (Solute carrier family 5 member 7)
[RGA1 DBM1 THE1 YOR127W O3290 YOR3290W] Rho-type GTPase-activating protein 1
[HMGB1 HMG1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HT1 SUU At1g62400 F24O1.13] Serine/threonine/tyrosine-protein kinase HT1 (EC 2.7.10.1) (EC 2.7.11.1) (High leaf temperature protein 1)
[Hmgb1 Hmg-1 Hmg1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[Hmgb1 Hmg-1 Hmg1] High mobility group protein B1 (Amphoterin) (Heparin-binding protein p30) (High mobility group protein 1) (HMG-1)
[HMGB1 HMG1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1 HMG1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1 HMG1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1 HMG1 RCJMB04_15a21] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1 HMG-1 HMG1] High mobility group protein B1 (High mobility group protein 1) (HMG-1) (Fragment)
[HMGB1 HMG1 QtsA-13487] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[TOR2 DRR2 TSC14 YKL203C] Serine/threonine-protein kinase TOR2 (EC 2.7.1.67) (EC 2.7.11.1) (Dominant rapamycin resistance protein 2) (Phosphatidylinositol 4-kinase TOR2) (PI4-kinase TOR2) (PI4K TOR2) (PtdIns-4-kinase TOR2) (Target of rapamycin kinase 2) (Temperature-sensitive CSG2 suppressor protein 14)
[HMGB1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[HMGB1] High mobility group protein B1 (High mobility group protein 1) (HMG-1)
[NTRK1 MTC TRK TRKA] High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) (TRK1-transforming tyrosine kinase protein) (Tropomyosin-related kinase A) (Tyrosine kinase receptor) (Tyrosine kinase receptor A) (Trk-A) (gp140trk) (p140-TrkA)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :