ID STE20_YEAST Reviewed; 939 AA.
AC Q03497; D3DKQ8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 27-MAR-2024, entry version 231.
DE RecName: Full=Serine/threonine-protein kinase STE20;
DE EC=2.7.11.1;
GN Name=STE20; OrderedLocusNames=YHL007C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1464311; DOI=10.1002/j.1460-2075.1992.tb05587.x;
RA Leberer E., Dignard D., Harcus D., Thomas D.Y., Whiteway M.;
RT "The protein kinase homologue Ste20p is required to link the yeast
RT pheromone response G-protein beta gamma subunits to downstream signalling
RT components.";
RL EMBO J. 11:4815-4824(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8421676; DOI=10.1073/pnas.90.2.452;
RA Ramer S.W., Davis R.W.;
RT "A dominant truncation allele identifies a gene, STE20, that encodes a
RT putative protein kinase necessary for mating in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:452-456(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 164-169; 583-591 AND 408-431, AND PHOSPHORYLATION AT
RP SER-169; SER-585 AND SER-418.
RX PubMed=16428446; DOI=10.1128/mcb.26.3.912-928.2006;
RA Truckses D.M., Bloomekatz J.E., Thorner J.;
RT "The RA domain of Ste50 adaptor protein is required for delivery of Ste11
RT to the plasma membrane in the filamentous growth signaling pathway of the
RT yeast Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:912-928(2006).
RN [6]
RP AUTOPHOSPHORYLATION, FUNCTION IN PHOSPHORYLATION OF STE11, AND MUTAGENESIS
RP OF LYS-649 AND THR-777.
RX PubMed=7608157; DOI=10.1074/jbc.270.27.15984;
RA Wu C., Whiteway M., Thomas D.Y., Leberer E.;
RT "Molecular characterization of Ste20p, a potential mitogen-activated
RT protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase
RT from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:15984-15992(1995).
RN [7]
RP FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
RX PubMed=9003780; DOI=10.1002/j.1460-2075.1996.tb01096.x;
RA Peter M., Neiman A.M., Park H.-O., van Lohuizen M., Herskowitz I.;
RT "Functional analysis of the interaction between the small GTP binding
RT protein Cdc42 and the Ste20 protein kinase in yeast.";
RL EMBO J. 15:7046-7059(1996).
RN [8]
RP FUNCTION.
RX PubMed=8722766; DOI=10.1093/genetics/143.1.103;
RA Akada R., Kallal L., Johnson D.I., Kurjan J.;
RT "Genetic relationships between the G protein beta gamma complex, Ste5p,
RT Ste20p and Cdc42p: investigation of effector roles in the yeast pheromone
RT response pathway.";
RL Genetics 143:103-117(1996).
RN [9]
RP FUNCTION.
RX PubMed=8643578; DOI=10.1073/pnas.93.11.5352;
RA Moesch H.-U., Roberts R.L., Fink G.R.;
RT "Ras2 signals via the Cdc42/Ste20/mitogen-activated protein kinase module
RT to induce filamentous growth in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5352-5356(1996).
RN [10]
RP INTERACTION WITH BMH1 AND BMH2.
RX PubMed=9215628; DOI=10.1016/s0092-8674(00)80293-7;
RA Roberts R.L., Moesch H.-U., Fink G.R.;
RT "14-3-3 proteins are essential for RAS/MAPK cascade signaling during
RT pseudohyphal development in S. cerevisiae.";
RL Cell 89:1055-1065(1997).
RN [11]
RP FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
RX PubMed=9009270; DOI=10.1093/emboj/16.1.83;
RA Leberer E., Wu C., Leeuw T., Fourest-Lieuvin A., Segall J.E., Thomas D.Y.;
RT "Functional characterization of the Cdc42p binding domain of yeast Ste20p
RT protein kinase.";
RL EMBO J. 16:83-97(1997).
RN [12]
RP FUNCTION IN PHOSPHORYLATION OF MYO3.
RX PubMed=9388196; DOI=10.1074/jbc.272.49.30623;
RA Wu C., Lytvyn V., Thomas D.Y., Leberer E.;
RT "The phosphorylation site for Ste20p-like protein kinases is essential for
RT the function of myosin-I in yeast.";
RL J. Biol. Chem. 272:30623-30626(1997).
RN [13]
RP FUNCTION.
RX PubMed=9742399; DOI=10.1016/s0960-9822(98)00398-4;
RA Eby J.J., Holly S.P., van Drogen F., Grishin A.V., Peter M., Drubin D.G.,
RA Blumer K.J.;
RT "Actin cytoskeleton organization regulated by the PAK family of protein
RT kinases.";
RL Curr. Biol. 8:967-970(1998).
RN [14]
RP PHOSPHORYLATION BY THE CLN2-CDC28 COMPLEX.
RX PubMed=9774429; DOI=10.1074/jbc.273.43.28107;
RA Wu C., Leeuw T., Leberer E., Thomas D.Y., Whiteway M.;
RT "Cell cycle- and Cln2p-Cdc28p-dependent phosphorylation of the yeast Ste20p
RT protein kinase.";
RL J. Biol. Chem. 273:28107-28115(1998).
RN [15]
RP FUNCTION, AND INTERACTION WITH STE4.
RX PubMed=9428767; DOI=10.1038/34448;
RA Leeuw T., Wu C., Schrag J.D., Whiteway M., Thomas D.Y., Leberer E.;
RT "Interaction of a G-protein beta-subunit with a conserved sequence in
RT Ste20/PAK family protein kinases.";
RL Nature 391:191-195(1998).
RN [16]
RP FUNCTION.
RX PubMed=10562285; DOI=10.1083/jcb.147.4.845;
RA Holly S.P., Blumer K.J.;
RT "PAK-family kinases regulate cell and actin polarization throughout the
RT cell cycle of Saccharomyces cerevisiae.";
RL J. Cell Biol. 147:845-856(1999).
RN [17]
RP INTERACTION WITH CLN2, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT SER-547; SER-562; THR-573; SER-585 AND THR-773.
RX PubMed=10359756; DOI=10.1073/pnas.96.12.6591;
RA Oda Y., Huang K., Cross F.R., Cowburn D., Chait B.T.;
RT "Accurate quantitation of protein expression and site-specific
RT phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6591-6596(1999).
RN [18]
RP FUNCTION IN PHOSPHORYLATION OF STE11.
RX PubMed=10837245; DOI=10.1016/s0960-9822(00)00511-x;
RA van Drogen F., O'Rourke S.M., Stucke V.M., Jaquenoud M., Neiman A.M.,
RA Peter M.;
RT "Phosphorylation of the MEKK Ste11p by the PAK-like kinase Ste20p is
RT required for MAP kinase signaling in vivo.";
RL Curr. Biol. 10:630-639(2000).
RN [19]
RP FUNCTION.
RX PubMed=10970855; DOI=10.1093/emboj/19.17.4623;
RA Raitt D.C., Posas F., Saito H.;
RT "Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent
RT activation of the Hog1 MAPK pathway.";
RL EMBO J. 19:4623-4631(2000).
RN [20]
RP FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
RX PubMed=11003652; DOI=10.1128/mcb.20.20.7559-7571.2000;
RA Moskow J.J., Gladfelter A.S., Lamson R.E., Pryciak P.M., Lew D.J.;
RT "Role of Cdc42p in pheromone-stimulated signal transduction in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 20:7559-7571(2000).
RN [21]
RP INTERACTION WITH CDC42.
RX PubMed=11046150; DOI=10.1128/mcb.20.22.8548-8559.2000;
RA Richman T.J., Johnson D.I.;
RT "Saccharomyces cerevisiae cdc42p GTPase is involved in preventing the
RT recurrence of bud emergence during the cell cycle.";
RL Mol. Cell. Biol. 20:8548-8559(2000).
RN [22]
RP INTERACTION WITH CDC42.
RX PubMed=12455995; DOI=10.1128/ec.1.3.469-480.2002;
RA Smith G.R., Givan S.A., Cullen P., Sprague G.F. Jr.;
RT "GTPase-activating proteins for Cdc42.";
RL Eukaryot. Cell 1:469-480(2002).
RN [23]
RP FUNCTION, INTERACTION WITH CDC42, AND MUTAGENESIS OF SER-338 AND HIS-345.
RX PubMed=11940652; DOI=10.1128/mcb.22.9.2939-2951.2002;
RA Lamson R.E., Winters M.J., Pryciak P.M.;
RT "Cdc42 regulation of kinase activity and signaling by the yeast p21-
RT activated kinase Ste20.";
RL Mol. Cell. Biol. 22:2939-2951(2002).
RN [24]
RP INTERACTION WITH CDC42, MUTAGENESIS OF HIS-345 AND HIS-348, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12586692; DOI=10.1093/genetics/163.1.9;
RA Ash J., Wu C., Larocque R., Jamal M., Stevens W., Osborne M., Thomas D.Y.,
RA Whiteway M.;
RT "Genetic analysis of the interface between Cdc42p and the CRIB domain of
RT Ste20p in Saccharomyces cerevisiae.";
RL Genetics 163:9-20(2003).
RN [25]
RP FUNCTION.
RX PubMed=12686605; DOI=10.1091/mbc.e02-06-0348;
RA Goehring A.S., Mitchell D.A., Tong A.H., Keniry M.E., Boone C.,
RA Sprague G.F. Jr.;
RT "Synthetic lethal analysis implicates Ste20p, a p21-activated protein
RT kinase, in polarisome activation.";
RL Mol. Biol. Cell 14:1501-1516(2003).
RN [26]
RP FUNCTION.
RX PubMed=12588977; DOI=10.1128/mcb.23.5.1569-1580.2003;
RA Keniry M.E., Sprague G.F. Jr.;
RT "Identification of p21-activated kinase specificity determinants in budding
RT yeast: a single amino acid substitution imparts Ste20 specificity to
RT Cla4.";
RL Mol. Cell. Biol. 23:1569-1580(2003).
RN [27]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [28]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H2B, MUTAGENESIS OF LYS-649, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15652479; DOI=10.1016/j.cell.2004.11.016;
RA Ahn S.-H., Cheung W.L., Hsu J.-Y., Diaz R.L., Smith M.M., Allis C.D.;
RT "Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen
RT peroxide-induced apoptosis in S. cerevisiae.";
RL Cell 120:25-36(2005).
RN [29]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H2B.
RX PubMed=15970663; DOI=10.4161/cc.4.6.1745;
RA Ahn S.-H., Henderson K.A., Keeney S., Allis C.D.;
RT "H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S.
RT cerevisiae.";
RL Cell Cycle 4:780-783(2005).
RN [30]
RP FUNCTION, INTERACTION WITH BEM1, MUTAGENESIS OF PRO-475 AND PRO-477, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15743816; DOI=10.1128/mcb.25.6.2177-2190.2005;
RA Winters M.J., Pryciak P.M.;
RT "Interaction with the SH3 domain protein Bem1 regulates signaling by the
RT Saccharomyces cerevisiae p21-activated kinase Ste20.";
RL Mol. Cell. Biol. 25:2177-2190(2005).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-203; SER-562 AND
RP SER-585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; THR-167; THR-203;
RP SER-502; SER-924 AND THR-927, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-169; THR-203;
RP SER-502; SER-547 AND SER-562, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: MAP4K component of the MAPK pathway required for the mating
CC pheromone response, haploid invasive growth and diploid pseudohyphal
CC development. Links the pheromone response G-protein beta gamma subunits
CC to downstream signaling components. Needed for mating in haploid cells,
CC induction of a mating-specific gene FUS1, induction of mating-specific
CC morphologies, and pheromone-induced proliferation arrest. Required for
CC the regulation of the actin polarization and bud emergence during cell
CC cycle in G1. Involved in the high osmolarity glycerol (HOG) response.
CC Phosphorylates 'Thr-307' and 'Ser-302' or 'Ser-306' of STE11 and 'Ser-
CC 357' of MYO3. Phosphorylates histone H2B to form H2BS10ph during
CC meiosis and H(2)O(2)-induced apoptosis. Its interaction with CDC42 is
CC required for both invasive growth and the formation of pseudohyphae.
CC Its interaction with STE4 is required for the pheromone signaling.
CC {ECO:0000269|PubMed:10562285, ECO:0000269|PubMed:10837245,
CC ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:11003652,
CC ECO:0000269|PubMed:11940652, ECO:0000269|PubMed:12588977,
CC ECO:0000269|PubMed:12686605, ECO:0000269|PubMed:1464311,
CC ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15743816,
CC ECO:0000269|PubMed:15970663, ECO:0000269|PubMed:7608157,
CC ECO:0000269|PubMed:8421676, ECO:0000269|PubMed:8643578,
CC ECO:0000269|PubMed:8722766, ECO:0000269|PubMed:9003780,
CC ECO:0000269|PubMed:9009270, ECO:0000269|PubMed:9388196,
CC ECO:0000269|PubMed:9428767, ECO:0000269|PubMed:9742399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with BEM1, CDC42, CLN2, STE4 and the 14-3-3 proteins
CC BMH1 and BMH2. {ECO:0000269|PubMed:10359756,
CC ECO:0000269|PubMed:11003652, ECO:0000269|PubMed:11046150,
CC ECO:0000269|PubMed:11940652, ECO:0000269|PubMed:12455995,
CC ECO:0000269|PubMed:12586692, ECO:0000269|PubMed:15743816,
CC ECO:0000269|PubMed:9003780, ECO:0000269|PubMed:9009270,
CC ECO:0000269|PubMed:9215628, ECO:0000269|PubMed:9428767}.
CC -!- INTERACTION:
CC Q03497; P29366: BEM1; NbExp=11; IntAct=EBI-18285, EBI-3508;
CC Q03497; P19073: CDC42; NbExp=6; IntAct=EBI-18285, EBI-4274;
CC Q03497; P36006: MYO3; NbExp=3; IntAct=EBI-18285, EBI-11670;
CC Q03497; Q04439: MYO5; NbExp=4; IntAct=EBI-18285, EBI-11687;
CC Q03497; Q12163: NBP2; NbExp=6; IntAct=EBI-18285, EBI-34713;
CC Q03497; P80667: PEX13; NbExp=3; IntAct=EBI-18285, EBI-13206;
CC Q03497; P18851: STE4; NbExp=3; IntAct=EBI-18285, EBI-7390;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The translocation from
CC the cytoplasm to the nucleus is stimulated by H(2)O(2). Localizes at
CC bud emergence during cell cycle and the shmoo top during mating, both
CC localizations requiring an interaction with CDC42.
CC -!- DOMAIN: The CRIB domain is required for the association with CDC42.
CC -!- PTM: Autophosphorylated and phosphorylated by the CLN2-CDC28 complex in
CC a cell cycle dependent manner.
CC -!- PTM: Autophosphorylated on serine residues.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; M94719; AAA35111.1; -; Genomic_DNA.
DR EMBL; L04655; AAA35038.1; -; Genomic_DNA.
DR EMBL; L04655; AAA35039.1; -; Genomic_DNA.
DR EMBL; U11581; AAB69747.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06681.1; -; Genomic_DNA.
DR PIR; S28394; S28394.
DR RefSeq; NP_011856.1; NM_001179087.1.
DR PDB; 2KYM; NMR; -; B=468-483.
DR PDB; 2LCS; NMR; -; B=468-483.
DR PDB; 2RQW; NMR; -; B=463-486.
DR PDBsum; 2KYM; -.
DR PDBsum; 2LCS; -.
DR PDBsum; 2RQW; -.
DR AlphaFoldDB; Q03497; -.
DR BMRB; Q03497; -.
DR SMR; Q03497; -.
DR BioGRID; 36419; 274.
DR DIP; DIP-712N; -.
DR IntAct; Q03497; 37.
DR MINT; Q03497; -.
DR STRING; 4932.YHL007C; -.
DR GlyGen; Q03497; 18 sites, 1 O-linked glycan (18 sites).
DR iPTMnet; Q03497; -.
DR MaxQB; Q03497; -.
DR PaxDb; 4932-YHL007C; -.
DR PeptideAtlas; Q03497; -.
DR EnsemblFungi; YHL007C_mRNA; YHL007C; YHL007C.
DR GeneID; 856382; -.
DR KEGG; sce:YHL007C; -.
DR AGR; SGD:S000000999; -.
DR SGD; S000000999; STE20.
DR VEuPathDB; FungiDB:YHL007C; -.
DR eggNOG; KOG0578; Eukaryota.
DR GeneTree; ENSGT00940000165560; -.
DR HOGENOM; CLU_000288_26_3_1; -.
DR InParanoid; Q03497; -.
DR OMA; FYQDVTE; -.
DR OrthoDB; 460351at2759; -.
DR BioCyc; YEAST:G3O-31029-MONOMER; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SCE-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-SCE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-SCE-445144; Signal transduction by L1.
DR Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9013406; RHOQ GTPase cycle.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 856382; 0 hits in 13 CRISPR screens.
DR EvolutionaryTrace; Q03497; -.
DR PRO; PR:Q03497; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; Q03497; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044025; F:histone H2BS14 kinase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; HMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IMP:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR GO; GO:0035376; P:sterol import; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR CDD; cd06614; STKc_PAK; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus;
KW Pheromone response; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..939
FT /note="Serine/threonine-protein kinase STE20"
FT /id="PRO_0000086686"
FT DOMAIN 337..350
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 620..871
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..499
FT /note="BEM1-binding"
FT REGION 500..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 739
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 626..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16428446,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16428446"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10359756,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10359756,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 573
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10359756"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10359756,
FT ECO:0000269|PubMed:16428446, ECO:0007744|PubMed:17330950"
FT MOD_RES 773
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10359756"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 927
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 338
FT /note="S->A: Reduces interaction with CDC42."
FT /evidence="ECO:0000269|PubMed:11940652"
FT MUTAGEN 345
FT /note="H->A,D: Reduces interaction with CDC42."
FT /evidence="ECO:0000269|PubMed:11940652,
FT ECO:0000269|PubMed:12586692"
FT MUTAGEN 348
FT /note="H->D: Reduces interaction with CDC42."
FT /evidence="ECO:0000269|PubMed:12586692"
FT MUTAGEN 475
FT /note="P->G: Impairs interaction with BEM1; when associated
FT with A-477."
FT /evidence="ECO:0000269|PubMed:15743816"
FT MUTAGEN 477
FT /note="P->A: Impairs interaction with BEM1; when associated
FT with G-475."
FT /evidence="ECO:0000269|PubMed:15743816"
FT MUTAGEN 649
FT /note="K->R: Impairs phosphorylation of STE11 and histone
FT H2B and mating efficiency."
FT /evidence="ECO:0000269|PubMed:15652479,
FT ECO:0000269|PubMed:7608157"
FT MUTAGEN 777
FT /note="T->A: Impairs autophosphorylation and mating
FT efficiency."
FT /evidence="ECO:0000269|PubMed:7608157"
FT CONFLICT 19
FT /note="N -> S (in Ref. 2; AAA35038)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="I -> M (in Ref. 2; AAA35038)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="P -> S (in Ref. 2; AAA35038)"
FT /evidence="ECO:0000305"
SQ 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
//
