STE11_YEAST
ID STE11_YEAST Reviewed; 717 AA.
AC P23561; D6VZ00;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Serine/threonine-protein kinase STE11;
DE EC=2.7.11.25;
GN Name=STE11; OrderedLocusNames=YLR362W; ORFNames=L8039.10;
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 IDENTIFICATION OF INITIATION SITE.
RX PubMed=2276621; DOI=10.1101/gad.4.11.1862;
RA Rhodes N., Connell L., Errede B.;
RT "STE11 is a protein kinase required for cell-type-specific transcription
RT and signal transduction in yeast.";
RL Genes Dev. 4:1862-1874(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP POSSIBLE FUNCTION.
RX PubMed=1628833; DOI=10.1101/gad.6.7.1305;
RA Cairns B.R., Ramer S.W., Kornberg K.D.;
RT "Order of action of components in the yeast pheromone response pathway
RT revealed with a dominant allele of the STE11 kinase and the multiple
RT phosphorylation of the STE7 kinase.";
RL Genes Dev. 6:1305-1318(1992).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH PBS2 AND SHO1.
RX PubMed=15200959; DOI=10.1016/j.molcel.2004.06.011;
RA Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A.;
RT "Sho1 and Pbs2 act as coscaffolds linking components in the yeast high
RT osmolarity MAP kinase pathway.";
RL Mol. Cell 14:825-832(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [10]
RP STRUCTURE BY NMR OF 15-92, INTERACTION WITH STE50, AND MUTAGENESIS OF
RP ILE-59.
RX PubMed=15327964; DOI=10.1016/j.jmb.2004.06.064;
RA Kwan J.J., Warner N., Pawson T., Donaldson L.W.;
RT "The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its
RT partnership with Ste50.";
RL J. Mol. Biol. 342:681-693(2004).
RN [11]
RP STRUCTURE BY NMR OF 16-83, SUBUNIT, AND INTERACTION WITH STE50.
RX PubMed=15544813; DOI=10.1016/j.jmb.2004.09.018;
RA Bhattacharjya S., Xu P., Gingras R., Shaykhutdinov R., Wu C., Whiteway M.,
RA Ni F.;
RT "Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its
RT interactions with the adaptor protein Ste50 from the budding yeast:
RT implications for Ste11 activation and signal transmission through the
RT Ste50-Ste11 complex.";
RL J. Mol. Biol. 344:1071-1087(2004).
CC -!- FUNCTION: Serine/threonine protein kinase required for cell-type-
CC specific transcription and signal transduction in yeast. It is thought
CC that it phosphorylates the STE7 protein kinase which itself,
CC phosphorylates the FUS3 and or KSS1 kinases.
CC {ECO:0000269|PubMed:15200959}.
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=2.7.11.25;
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=2.7.11.25;
CC -!- SUBUNIT: Homodimer (Probable). Interacts (via SAM domain) with STE50
CC (via SAM domain). Interacts with PBS2 and SHO1.
CC {ECO:0000269|PubMed:15200959, ECO:0000269|PubMed:15327964,
CC ECO:0000269|PubMed:15544813, ECO:0000305}.
CC -!- INTERACTION:
CC P23561; P16892: FUS3; NbExp=6; IntAct=EBI-18259, EBI-7193;
CC P23561; P14681: KSS1; NbExp=6; IntAct=EBI-18259, EBI-9945;
CC P23561; P32490: MKK1; NbExp=2; IntAct=EBI-18259, EBI-10968;
CC P23561; P40073: SHO1; NbExp=3; IntAct=EBI-18259, EBI-18140;
CC P23561; P23561: STE11; NbExp=3; IntAct=EBI-18259, EBI-18259;
CC P23561; P32917: STE5; NbExp=8; IntAct=EBI-18259, EBI-18373;
CC P23561; P25344: STE50; NbExp=5; IntAct=EBI-18259, EBI-18305;
CC -!- MISCELLANEOUS: Present with 736 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. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67571.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X53431; CAA37522.1; -; Genomic_DNA.
DR EMBL; U19103; AAB67571.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006945; DAA09666.1; -; Genomic_DNA.
DR PIR; S51380; S51380.
DR RefSeq; NP_013466.1; NM_001182251.1.
DR PDB; 1OW5; NMR; -; A=15-92.
DR PDB; 1X9X; NMR; -; A/B=16-83.
DR PDBsum; 1OW5; -.
DR PDBsum; 1X9X; -.
DR AlphaFoldDB; P23561; -.
DR BMRB; P23561; -.
DR SMR; P23561; -.
DR BioGRID; 31623; 124.
DR DIP; DIP-861N; -.
DR IntAct; P23561; 25.
DR MINT; P23561; -.
DR STRING; 4932.YLR362W; -.
DR CarbonylDB; P23561; -.
DR iPTMnet; P23561; -.
DR MaxQB; P23561; -.
DR PaxDb; P23561; -.
DR PRIDE; P23561; -.
DR EnsemblFungi; YLR362W_mRNA; YLR362W; YLR362W.
DR GeneID; 851076; -.
DR KEGG; sce:YLR362W; -.
DR SGD; S000004354; STE11.
DR VEuPathDB; FungiDB:YLR362W; -.
DR eggNOG; KOG0198; Eukaryota.
DR GeneTree; ENSGT00940000160383; -.
DR HOGENOM; CLU_003051_2_1_1; -.
DR InParanoid; P23561; -.
DR OMA; VTICHSS; -.
DR BioCyc; YEAST:G3O-32433-MON; -.
DR BRENDA; 2.7.11.25; 984.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR EvolutionaryTrace; P23561; -.
DR PRO; PR:P23561; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P23561; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA: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:0032093; F:SAM domain binding; IDA:SGD.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IGI:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IMP:SGD.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IGI:SGD.
DR GO; GO:0071507; P:pheromone response MAPK cascade; IDA:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0010525; P:regulation of transposition, RNA-mediated; IMP:SGD.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Pheromone response;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..717
FT /note="Serine/threonine-protein kinase STE11"
FT /id="PRO_0000086684"
FT DOMAIN 20..84
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 415..712
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 452..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 421..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 59
FT /note="I->R: Disrupts interaction with STE50 and abolishes
FT signal transduction."
FT /evidence="ECO:0000269|PubMed:15327964"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:1OW5"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:1OW5"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1OW5"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:1OW5"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1OW5"
SQ SEQUENCE 717 AA; 80721 MW; E9E0DF27114EEEEF CRC64;
MEQTQTAEGT DLLIGDEKTN DLPFVQLFLE EIGCTQYLDS FIQCNLVTEE EIKYLDKDIL
IALGVNKIGD RLKILRKSKS FQRDKRIEQV NRLKNLMEKV SSLSTATLSM NSELIPEKHC
VIFILNDGSA KKVNVNGCFN ADSIKKRLIR RLPHELLATN SNGEVTKMVQ DYDVFVLDYT
KNVLHLLYDV ELVTICHAND RVEKNRLIFV SKDQTPSDKA ISTSKKLYLR TLSALSQVGP
SSSNLLAQNK GISHNNAEGK LRIDNTEKDR IRQIFNQRPP SEFISTNLAG YFPHTDMKRL
QKTMRESFRH SARLSIAQRR PLSAESNNIG DILLKHSNAV DMALLQGLDQ TRLSSKLDTT
KIPKLAHKRP EDNDAISNQL ELLSVESGEE EDHDFFGEDS DIVSLPTKIA TPKNWLKGAC
IGSGSFGSVY LGMNAHTGEL MAVKQVEIKN NNIGVPTDNN KQANSDENNE QEEQQEKIED
VGAVSHPKTN QNIHRKMVDA LQHEMNLLKE LHHENIVTYY GASQEGGNLN IFLEYVPGGS
VSSMLNNYGP FEESLITNFT RQILIGVAYL HKKNIIHRDI KGANILIDIK GCVKITDFGI
SKKLSPLNKK QNKRASLQGS VFWMSPEVVK QTATTAKADI WSTGCVVIEM FTGKHPFPDF
SQMQAIFKIG TNTTPEIPSW ATSEGKNFLR KAFELDYQYR PSALELLQHP WLDAHII
