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Serine/threonine-protein kinase STE20 (EC 2.7.11.1)

 STE20_YEAST             Reviewed;         939 AA.
Q03497; D3DKQ8;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
28-MAR-2018, entry version 196.
RecName: Full=Serine/threonine-protein kinase STE20;
EC=2.7.11.1;
Name=STE20; OrderedLocusNames=YHL007C;
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], AND FUNCTION.
PubMed=1464311;
Leberer E., Dignard D., Harcus D., Thomas D.Y., Whiteway M.;
"The protein kinase homologue Ste20p is required to link the yeast
pheromone response G-protein beta gamma subunits to downstream
signalling components.";
EMBO J. 11:4815-4824(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=8421676; DOI=10.1073/pnas.90.2.452;
Ramer S.W., Davis R.W.;
"A dominant truncation allele identifies a gene, STE20, that encodes a
putative protein kinase necessary for mating in Saccharomyces
cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 90:452-456(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[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]
PROTEIN SEQUENCE OF 164-169; 583-591 AND 408-431, AND PHOSPHORYLATION
AT SER-169; SER-585 AND SER-418.
PubMed=16428446; DOI=10.1128/MCB.26.3.912-928.2006;
Truckses D.M., Bloomekatz J.E., Thorner J.;
"The RA domain of Ste50 adaptor protein is required for delivery of
Ste11 to the plasma membrane in the filamentous growth signaling
pathway of the yeast Saccharomyces cerevisiae.";
Mol. Cell. Biol. 26:912-928(2006).
[6]
AUTOPHOSPHORYLATION, FUNCTION IN PHOSPHORYLATION OF STE11, AND
MUTAGENESIS OF LYS-649 AND THR-777.
PubMed=7608157; DOI=10.1074/jbc.270.27.15984;
Wu C., Whiteway M., Thomas D.Y., Leberer E.;
"Molecular characterization of Ste20p, a potential mitogen-activated
protein or extracellular signal-regulated kinase kinase (MEK) kinase
kinase from Saccharomyces cerevisiae.";
J. Biol. Chem. 270:15984-15992(1995).
[7]
FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
PubMed=9003780;
Peter M., Neiman A.M., Park H.-O., van Lohuizen M., Herskowitz I.;
"Functional analysis of the interaction between the small GTP binding
protein Cdc42 and the Ste20 protein kinase in yeast.";
EMBO J. 15:7046-7059(1996).
[8]
FUNCTION.
PubMed=8722766;
Akada R., Kallal L., Johnson D.I., Kurjan J.;
"Genetic relationships between the G protein beta gamma complex,
Ste5p, Ste20p and Cdc42p: investigation of effector roles in the yeast
pheromone response pathway.";
Genetics 143:103-117(1996).
[9]
FUNCTION.
PubMed=8643578; DOI=10.1073/pnas.93.11.5352;
Moesch H.-U., Roberts R.L., Fink G.R.;
"Ras2 signals via the Cdc42/Ste20/mitogen-activated protein kinase
module to induce filamentous growth in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 93:5352-5356(1996).
[10]
INTERACTION WITH BMH1 AND BMH2.
PubMed=9215628; DOI=10.1016/S0092-8674(00)80293-7;
Roberts R.L., Moesch H.-U., Fink G.R.;
"14-3-3 proteins are essential for RAS/MAPK cascade signaling during
pseudohyphal development in S. cerevisiae.";
Cell 89:1055-1065(1997).
[11]
FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
PubMed=9009270; DOI=10.1093/emboj/16.1.83;
Leberer E., Wu C., Leeuw T., Fourest-Lieuvin A., Segall J.E.,
Thomas D.Y.;
"Functional characterization of the Cdc42p binding domain of yeast
Ste20p protein kinase.";
EMBO J. 16:83-97(1997).
[12]
FUNCTION IN PHOSPHORYLATION OF MYO3.
PubMed=9388196; DOI=10.1074/jbc.272.49.30623;
Wu C., Lytvyn V., Thomas D.Y., Leberer E.;
"The phosphorylation site for Ste20p-like protein kinases is essential
for the function of myosin-I in yeast.";
J. Biol. Chem. 272:30623-30626(1997).
[13]
FUNCTION.
PubMed=9742399; DOI=10.1016/S0960-9822(98)00398-4;
Eby J.J., Holly S.P., van Drogen F., Grishin A.V., Peter M.,
Drubin D.G., Blumer K.J.;
"Actin cytoskeleton organization regulated by the PAK family of
protein kinases.";
Curr. Biol. 8:967-970(1998).
[14]
PHOSPHORYLATION BY THE CLN2-CDC28 COMPLEX.
PubMed=9774429; DOI=10.1074/jbc.273.43.28107;
Wu C., Leeuw T., Leberer E., Thomas D.Y., Whiteway M.;
"Cell cycle- and Cln2p-Cdc28p-dependent phosphorylation of the yeast
Ste20p protein kinase.";
J. Biol. Chem. 273:28107-28115(1998).
[15]
FUNCTION, AND INTERACTION WITH STE4.
PubMed=9428767; DOI=10.1038/34448;
Leeuw T., Wu C., Schrag J.D., Whiteway M., Thomas D.Y., Leberer E.;
"Interaction of a G-protein beta-subunit with a conserved sequence in
Ste20/PAK family protein kinases.";
Nature 391:191-195(1998).
[16]
FUNCTION.
PubMed=10562285; DOI=10.1083/jcb.147.4.845;
Holly S.P., Blumer K.J.;
"PAK-family kinases regulate cell and actin polarization throughout
the cell cycle of Saccharomyces cerevisiae.";
J. Cell Biol. 147:845-856(1999).
[17]
INTERACTION WITH CLN2, IDENTIFICATION BY MASS SPECTROMETRY, AND
PHOSPHORYLATION AT SER-547; SER-562; THR-573; SER-585 AND THR-773.
PubMed=10359756; DOI=10.1073/pnas.96.12.6591;
Oda Y., Huang K., Cross F.R., Cowburn D., Chait B.T.;
"Accurate quantitation of protein expression and site-specific
phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 96:6591-6596(1999).
[18]
FUNCTION IN PHOSPHORYLATION OF STE11.
PubMed=10837245; DOI=10.1016/S0960-9822(00)00511-X;
van Drogen F., O'Rourke S.M., Stucke V.M., Jaquenoud M., Neiman A.M.,
Peter M.;
"Phosphorylation of the MEKK Ste11p by the PAK-like kinase Ste20p is
required for MAP kinase signaling in vivo.";
Curr. Biol. 10:630-639(2000).
[19]
FUNCTION.
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).
[20]
FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
PubMed=11003652; DOI=10.1128/MCB.20.20.7559-7571.2000;
Moskow J.J., Gladfelter A.S., Lamson R.E., Pryciak P.M., Lew D.J.;
"Role of Cdc42p in pheromone-stimulated signal transduction in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 20:7559-7571(2000).
[21]
INTERACTION WITH CDC42.
PubMed=11046150; DOI=10.1128/MCB.20.22.8548-8559.2000;
Richman T.J., Johnson D.I.;
"Saccharomyces cerevisiae cdc42p GTPase is involved in preventing the
recurrence of bud emergence during the cell cycle.";
Mol. Cell. Biol. 20:8548-8559(2000).
[22]
INTERACTION WITH CDC42.
PubMed=12455995; DOI=10.1128/EC.1.3.469-480.2002;
Smith G.R., Givan S.A., Cullen P., Sprague G.F. Jr.;
"GTPase-activating proteins for Cdc42.";
Eukaryot. Cell 1:469-480(2002).
[23]
FUNCTION, INTERACTION WITH CDC42, AND MUTAGENESIS OF SER-338 AND
HIS-345.
PubMed=11940652; DOI=10.1128/MCB.22.9.2939-2951.2002;
Lamson R.E., Winters M.J., Pryciak P.M.;
"Cdc42 regulation of kinase activity and signaling by the yeast p21-
activated kinase Ste20.";
Mol. Cell. Biol. 22:2939-2951(2002).
[24]
INTERACTION WITH CDC42, MUTAGENESIS OF HIS-345 AND HIS-348, AND
SUBCELLULAR LOCATION.
PubMed=12586692;
Ash J., Wu C., Larocque R., Jamal M., Stevens W., Osborne M.,
Thomas D.Y., Whiteway M.;
"Genetic analysis of the interface between Cdc42p and the CRIB domain
of Ste20p in Saccharomyces cerevisiae.";
Genetics 163:9-20(2003).
[25]
FUNCTION.
PubMed=12686605; DOI=10.1091/mbc.E02-06-0348;
Goehring A.S., Mitchell D.A., Tong A.H., Keniry M.E., Boone C.,
Sprague G.F. Jr.;
"Synthetic lethal analysis implicates Ste20p, a p21-activated protein
kinase, in polarisome activation.";
Mol. Biol. Cell 14:1501-1516(2003).
[26]
FUNCTION.
PubMed=12588977; DOI=10.1128/MCB.23.5.1569-1580.2003;
Keniry M.E., Sprague G.F. Jr.;
"Identification of p21-activated kinase specificity determinants in
budding yeast: a single amino acid substitution imparts Ste20
specificity to Cla4.";
Mol. Cell. Biol. 23:1569-1580(2003).
[27]
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).
[28]
FUNCTION IN PHOSPHORYLATION OF HISTONE H2B, MUTAGENESIS OF LYS-649,
AND SUBCELLULAR LOCATION.
PubMed=15652479; DOI=10.1016/j.cell.2004.11.016;
Ahn S.-H., Cheung W.L., Hsu J.-Y., Diaz R.L., Smith M.M., Allis C.D.;
"Sterile 20 kinase phosphorylates histone H2B at serine 10 during
hydrogen peroxide-induced apoptosis in S. cerevisiae.";
Cell 120:25-36(2005).
[29]
FUNCTION IN PHOSPHORYLATION OF HISTONE H2B.
PubMed=15970663; DOI=10.4161/cc.4.6.1745;
Ahn S.-H., Henderson K.A., Keeney S., Allis C.D.;
"H2B (Ser10) phosphorylation is induced during apoptosis and meiosis
in S. cerevisiae.";
Cell Cycle 4:780-783(2005).
[30]
FUNCTION, INTERACTION WITH BEM1, MUTAGENESIS OF PRO-475 AND PRO-477,
AND SUBCELLULAR LOCATION.
PubMed=15743816; DOI=10.1128/MCB.25.6.2177-2190.2005;
Winters M.J., Pryciak P.M.;
"Interaction with the SH3 domain protein Bem1 regulates signaling by
the Saccharomyces cerevisiae p21-activated kinase Ste20.";
Mol. Cell. Biol. 25:2177-2190(2005).
[31]
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).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-203; SER-562
AND SER-585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; THR-167; THR-203;
SER-502; SER-924 AND THR-927, AND 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).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-169; THR-203;
SER-502; SER-547 AND SER-562, 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).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: MAP4K component of the MAPK pathway required for the
mating pheromone response, haploid invasive growth and diploid
pseudohyphal development. Links the pheromone response G-protein
beta gamma subunits to downstream signaling components. Needed for
mating in haploid cells, induction of a mating-specific gene FUS1,
induction of mating-specific morphologies, and pheromone-induced
proliferation arrest. Required for the regulation of the actin
polarization and bud emergence during cell cycle in G1. Involved
in the high osmolarity glycerol (HOG) response. Phosphorylates
'Thr-307' and 'Ser-302' or 'Ser-306' of STE11 and 'Ser-357' of
MYO3. Phosphorylates histone H2B to form H2BS10ph during meiosis
and H(2)O(2)-induced apoptosis. Its interaction with CDC42 is
required for both invasive growth and the formation of
pseudohyphae. Its interaction with STE4 is required for the
pheromone signaling. {ECO:0000269|PubMed:10562285,
ECO:0000269|PubMed:10837245, ECO:0000269|PubMed:10970855,
ECO:0000269|PubMed:11003652, ECO:0000269|PubMed:11940652,
ECO:0000269|PubMed:12588977, ECO:0000269|PubMed:12686605,
ECO:0000269|PubMed:1464311, ECO:0000269|PubMed:15652479,
ECO:0000269|PubMed:15743816, ECO:0000269|PubMed:15970663,
ECO:0000269|PubMed:7608157, ECO:0000269|PubMed:8421676,
ECO:0000269|PubMed:8643578, ECO:0000269|PubMed:8722766,
ECO:0000269|PubMed:9003780, ECO:0000269|PubMed:9009270,
ECO:0000269|PubMed:9388196, ECO:0000269|PubMed:9428767,
ECO:0000269|PubMed:9742399}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with BEM1, CDC42, CLN2, STE4 and the 14-3-3
proteins BMH1 and BMH2. {ECO:0000269|PubMed:10359756,
ECO:0000269|PubMed:11003652, ECO:0000269|PubMed:11046150,
ECO:0000269|PubMed:11940652, ECO:0000269|PubMed:12455995,
ECO:0000269|PubMed:12586692, ECO:0000269|PubMed:15743816,
ECO:0000269|PubMed:9003780, ECO:0000269|PubMed:9009270,
ECO:0000269|PubMed:9215628, ECO:0000269|PubMed:9428767}.
-!- INTERACTION:
P29366:BEM1; NbExp=11; IntAct=EBI-18285, EBI-3508;
P34730:BMH2; NbExp=2; IntAct=EBI-18285, EBI-3672;
P19073:CDC42; NbExp=6; IntAct=EBI-18285, EBI-4274;
Q04660:ERB1; NbExp=3; IntAct=EBI-18285, EBI-28098;
P36006:MYO3; NbExp=3; IntAct=EBI-18285, EBI-11670;
Q04439:MYO5; NbExp=4; IntAct=EBI-18285, EBI-11687;
Q12163:NBP2; NbExp=6; IntAct=EBI-18285, EBI-34713;
P80667:PEX13; NbExp=3; IntAct=EBI-18285, EBI-13206;
P11484:SSB1; NbExp=3; IntAct=EBI-18285, EBI-8627;
P18851:STE4; NbExp=3; IntAct=EBI-18285, EBI-7390;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The translocation
from the cytoplasm to the nucleus is stimulated by H(2)O(2).
Localizes at bud emergence during cell cycle and the shmoo top
during mating, both localizations requiring an interaction with
CDC42.
-!- DOMAIN: The CRIB domain is required for the association with
CDC42.
-!- PTM: Autophosphorylated and phosphorylated by the CLN2-CDC28
complex in a cell cycle dependent manner.
-!- PTM: Autophosphorylated on serine residues.
-!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
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EMBL; M94719; AAA35111.1; -; Genomic_DNA.
EMBL; L04655; AAA35038.1; -; Genomic_DNA.
EMBL; L04655; AAA35039.1; -; Genomic_DNA.
EMBL; U11581; AAB69747.1; -; Genomic_DNA.
EMBL; BK006934; DAA06681.1; -; Genomic_DNA.
PIR; S28394; S28394.
RefSeq; NP_011856.1; NM_001179087.1.
PDB; 2KYM; NMR; -; B=468-483.
PDB; 2LCS; NMR; -; B=468-483.
PDB; 2RQW; NMR; -; B=463-486.
PDBsum; 2KYM; -.
PDBsum; 2LCS; -.
PDBsum; 2RQW; -.
ProteinModelPortal; Q03497; -.
SMR; Q03497; -.
BioGrid; 36419; 243.
DIP; DIP-712N; -.
IntAct; Q03497; 45.
MINT; Q03497; -.
STRING; 4932.YHL007C; -.
iPTMnet; Q03497; -.
MaxQB; Q03497; -.
PaxDb; Q03497; -.
PRIDE; Q03497; -.
EnsemblFungi; YHL007C; YHL007C; YHL007C.
GeneID; 856382; -.
KEGG; sce:YHL007C; -.
EuPathDB; FungiDB:YHL007C; -.
SGD; S000000999; STE20.
GeneTree; ENSGT00910000143994; -.
HOGENOM; HOG000234202; -.
InParanoid; Q03497; -.
KO; K04409; -.
OMA; FNIMTEG; -.
OrthoDB; EOG092C2E30; -.
BioCyc; YEAST:G3O-31029-MONOMER; -.
BRENDA; 2.7.11.1; 984.
Reactome; R-SCE-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-SCE-389359; CD28 dependent Vav1 pathway.
Reactome; R-SCE-3928662; EPHB-mediated forward signaling.
Reactome; R-SCE-445144; Signal transduction by L1.
Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
EvolutionaryTrace; Q03497; -.
PRO; PR:Q03497; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
GO; GO:0043332; C:mating projection tip; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044025; F:histone kinase activity (H2B-S14 specific); IDA:SGD.
GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IDA:SGD.
GO; GO:0048365; F:Rac GTPase binding; IBA:GO_Central.
GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
GO; GO:0000185; P:activation of MAPKKK activity; IDA:SGD.
GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:SGD.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
GO; GO:1990872; P:negative regulation of sterol import by negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IMP:SGD.
GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
GO; GO:0035376; P:sterol import; IMP:SGD.
GO; GO:0034063; P:stress granule assembly; IMP:SGD.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
CDD; cd01093; CRIB_PAK_like; 1.
Gene3D; 3.90.810.10; -; 1.
InterPro; IPR000095; CRIB_dom.
InterPro; IPR036936; CRIB_dom_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033923; PAK_BD.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00786; PBD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00285; PBD; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50108; CRIB; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Complete proteome;
Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding;
Nucleus; Pheromone response; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 939 Serine/threonine-protein kinase STE20.
/FTId=PRO_0000086686.
DOMAIN 337 350 CRIB. {ECO:0000255|PROSITE-
ProRule:PRU00057}.
DOMAIN 620 871 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 626 634 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 434 499 BEM1-binding.
ACT_SITE 739 739 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 649 649 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 167 167 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:16428446}.
MOD_RES 203 203 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000269|PubMed:16428446}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:10359756}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:10359756}.
MOD_RES 573 573 Phosphothreonine.
{ECO:0000269|PubMed:10359756}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000269|PubMed:10359756,
ECO:0000269|PubMed:16428446}.
MOD_RES 773 773 Phosphothreonine.
{ECO:0000269|PubMed:10359756}.
MOD_RES 924 924 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 927 927 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 338 338 S->A: Reduces interaction with CDC42.
{ECO:0000269|PubMed:11940652}.
MUTAGEN 345 345 H->A,D: Reduces interaction with CDC42.
{ECO:0000269|PubMed:11940652,
ECO:0000269|PubMed:12586692}.
MUTAGEN 348 348 H->D: Reduces interaction with CDC42.
{ECO:0000269|PubMed:12586692}.
MUTAGEN 475 475 P->G: Impairs interaction with BEM1; when
associated with A-477.
{ECO:0000269|PubMed:15743816}.
MUTAGEN 477 477 P->A: Impairs interaction with BEM1; when
associated with G-475.
{ECO:0000269|PubMed:15743816}.
MUTAGEN 649 649 K->R: Impairs phosphorylation of STE11
and histone H2B and mating efficiency.
{ECO:0000269|PubMed:15652479,
ECO:0000269|PubMed:7608157}.
MUTAGEN 777 777 T->A: Impairs autophosphorylation and
mating efficiency.
{ECO:0000269|PubMed:7608157}.
CONFLICT 19 19 N -> S (in Ref. 2; AAA35038).
{ECO:0000305}.
CONFLICT 134 134 I -> M (in Ref. 2; AAA35038).
{ECO:0000305}.
CONFLICT 271 271 P -> S (in Ref. 2; AAA35038).
{ECO:0000305}.
SEQUENCE 939 AA; 102362 MW; 69C1C12F5B87733C CRC64;
MSNDPSAVSE LPDKDSLDNG ISNDNERAMG GNGDGGDGLR LPRTTGTLNV NALQKGTNAA
HEAGGYKSMD PAKNAETTND DDNNVVSLDD PIQFTRVSSS SVISGMSSSM SPHSNIDETK
SLEAVTPNIN TSNITPDHSA DNTFSTINAS ESDHQFNDTL LSKLSLTDST ETIENNATVK
HQQPVASSTV NSNKSSTDIR RATPVSTPVI SKPSMTTTPR QINSASHSLS NPKHKQHKPK
VKPSKPEAKS KPVSVKKSFP SKNPLKNSSP PKKQTEKSYY SSSSKKRKSG SNSGTLRMKD
VFTSFVQNIK RNSQDDKRAS SSSNNSSSSS ITTALRISTP YNAKHIHHVG VDSKTGEYTG
LPEEWEKLLT SSGISKREQQ QNMQAVMDIV KFYQDVTETN GEDKMFKTFN TTTGLPGSPQ
VSTPPANSFN KFPPSTSDSH NYGSRTGTPM SNHVMSPTLN TDSSSANGKF IPSRPAPKPP
SSASASAPII KSPVMNSAAN VSPLKQTHAP TTPNRTSPNR SSISRNATLK KEEQPLPPIP
PTKSKTSPII STAHTPQQVA QSPKAPAQET VTTPTSKPAQ ARSLSKELNE KKREERERRK
KQLYAKLNEI CSDGDPSTKY ANLVKIGQGA SGGVYTAYEI GTNVSVAIKQ MNLEKQPKKE
LIINEILVMK GSKHPNIVNF IDSYVLKGDL WVIMEYMEGG SLTDVVTHCI LTEGQIGAVC
RETLSGLEFL HSKGVLHRDI KSDNILLSME GDIKLTDFGF CAQINELNLK RTTMVGTPYW
MAPEVVSRKE YGPKVDIWSL GIMIIEMIEG EPPYLNETPL RALYLIATNG TPKLKEPENL
SSSLKKFLDW CLCVEPEDRA SATELLHDEY ITEIAEANSS LAPLVKLARL KKVAENMDAD
EDNDDDNDNE HINKTNNCDD NNDSKETVNL DVTEDDKQK


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