STE7_YEAST
ID STE7_YEAST Reviewed; 515 AA.
AC P06784; D6VRJ2;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Serine/threonine-protein kinase STE7;
DE EC=2.7.12.2;
GN Name=STE7; OrderedLocusNames=YDL159W; ORFNames=D1525;
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].
RX PubMed=3532111; DOI=10.1073/pnas.83.19.7371;
RA Teague M.A., Chaleff D.T., Errede B.;
RT "Nucleotide sequence of the yeast regulatory gene STE7 predicts a protein
RT homologous to protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7371-7375(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-515.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL Yeast 12:1587-1592(1996).
RN [5]
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 [6]
RP PHOSPHORYLATION AT SER-359 AND THR-363, AND MUTAGENESIS.
RX PubMed=8131746; DOI=10.1002/j.1460-2075.1994.tb06361.x;
RA Zheng C.-F., Guan K.-L.;
RT "Activation of MEK family kinases requires phosphorylation of two conserved
RT Ser/Thr residues.";
RL EMBO J. 13:1123-1131(1994).
RN [7]
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).
CC -!- FUNCTION: Serine/threonine protein kinase required for cell-type-
CC specific transcription and signal transduction in yeast. It is thought
CC that it is phosphorylated by the ste11 protein kinase and that it can
CC phosphorylate the FUS3 and or KSS1 kinases.
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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- ACTIVITY REGULATION: Phosphorylated at multiple sites in response to
CC pheromone.
CC -!- INTERACTION:
CC P06784; Q00684: CDC14; NbExp=2; IntAct=EBI-18389, EBI-4192;
CC P06784; P16892: FUS3; NbExp=15; IntAct=EBI-18389, EBI-7193;
CC P06784; P32485: HOG1; NbExp=2; IntAct=EBI-18389, EBI-8437;
CC P06784; P14681: KSS1; NbExp=17; IntAct=EBI-18389, EBI-9945;
CC P06784; P32917: STE5; NbExp=9; IntAct=EBI-18389, EBI-18373;
CC -!- MISCELLANEOUS: Present with 672 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 subfamily. {ECO:0000305}.
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DR EMBL; M14097; AAA35118.1; -; Genomic_DNA.
DR EMBL; Z67750; CAA91587.1; -; Genomic_DNA.
DR EMBL; Z74207; CAA98732.1; -; Genomic_DNA.
DR EMBL; X97751; CAA66332.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11702.1; -; Genomic_DNA.
DR PIR; A25048; A25048.
DR RefSeq; NP_010122.1; NM_001180219.1.
DR AlphaFoldDB; P06784; -.
DR SMR; P06784; -.
DR BioGRID; 31905; 59.
DR DIP; DIP-9N; -.
DR ELM; P06784; -.
DR IntAct; P06784; 27.
DR MINT; P06784; -.
DR STRING; 4932.YDL159W; -.
DR iPTMnet; P06784; -.
DR MaxQB; P06784; -.
DR PaxDb; P06784; -.
DR PRIDE; P06784; -.
DR EnsemblFungi; YDL159W_mRNA; YDL159W; YDL159W.
DR GeneID; 851396; -.
DR KEGG; sce:YDL159W; -.
DR SGD; S000002318; STE7.
DR VEuPathDB; FungiDB:YDL159W; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P06784; -.
DR OMA; EFRHWCK; -.
DR BioCyc; YEAST:G3O-29553-MON; -.
DR BRENDA; 2.7.12.2; 984.
DR Reactome; R-SCE-110056; MAPK3 (ERK1) activation.
DR Reactome; R-SCE-112411; MAPK1 (ERK2) activation.
DR Reactome; R-SCE-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-2871796; FCERI mediated MAPK activation.
DR Reactome; R-SCE-445144; Signal transduction by L1.
DR Reactome; R-SCE-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-SCE-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-SCE-5674135; MAP2K and MAPK activation.
DR Reactome; R-SCE-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:P06784; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P06784; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
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:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0071507; P:pheromone response MAPK cascade; 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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Pheromone response;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..515
FT /note="Serine/threonine-protein kinase STE7"
FT /id="PRO_0000086688"
FT DOMAIN 191..466
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8131746"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:8131746"
FT MUTAGEN 353
FT /note="S->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8131746"
FT MUTAGEN 359
FT /note="S->A: Inactivation."
FT /evidence="ECO:0000269|PubMed:8131746"
FT MUTAGEN 363
FT /note="T->A: Inactivation."
FT /evidence="ECO:0000269|PubMed:8131746"
SQ SEQUENCE 515 AA; 57709 MW; C8A75899CFBE8BDE CRC64;
MFQRKTLQRR NLKGLNLNLH PDVGNNGQLQ EKTETHQGQS RIEGHVMSNI NAIQNNSNLF
LRRGIKKKLT LDAFGDDQAI SKPNTVVIQQ PQNEPVLVLS SLSQSPCVSS SSSLSTPCII
DAYSNNFGLS PSSTNSTPST IQGLSNIATP VENEHSISLP PLEESLSPAA ADLKDTLSGT
SNGNYIQLQD LVQLGKIGAG NSGTVVKALH VPDSKIVAKK TIPVEQNNST IINQLVRELS
IVKNVKPHEN IITFYGAYYN QHINNEIIIL MEYSDCGSLD KILSVYKRFV QRGTVSSKKT
WFNELTISKI AYGVLNGLDH LYRQYKIIHR DIKPSNVLIN SKGQIKLCDF GVSKKLINSI
ADTFVGTSTY MSPERIQGNV YSIKGDVWSL GLMIIELVTG EFPLGGHNDT PDGILDLLQR
IVNEPSPRLP KDRIYSKEMT DFVNRCCIKN ERERSSIHEL LHHDLIMKYV SPSKDDKFRH
WCRKIKSKIK EDKRIKREAL DRAKLEKKQS ERSTH
