(data stored in ACNUC8465 zone)

SWISSPROT: 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   11-DEC-2019, entry version 201.
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<1587::aid-yea46>3.0.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       Q00684:CDC14; NbExp=2; IntAct=EBI-18389, EBI-4192;
CC       P16892:FUS3; NbExp=15; IntAct=EBI-18389, EBI-7193;
CC       P32485:HOG1; NbExp=2; IntAct=EBI-18389, EBI-8437;
CC       P14681:KSS1; NbExp=17; IntAct=EBI-18389, EBI-9945;
CC       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}.
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   SMR; P06784; -.
DR   BioGrid; 31905; 56.
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   EuPathDB; FungiDB:YDL159W; -.
DR   SGD; S000002318; STE7.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; P06784; -.
DR   KO; K11226; -.
DR   OMA; EIIILME; -.
DR   BioCyc; YEAST:G3O-29553-MONOMER; -.
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-170968; Frs2-mediated activation.
DR   Reactome; R-SCE-445144; Signal transduction by L1.
DR   Reactome; R-SCE-5674135; MAP2K and MAPK activation.
DR   Reactome; R-SCE-5674499; Negative feedback regulation of MAPK pathway.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:SGD.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
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:0071507; P:pheromone response MAPK cascade; IDA: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:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
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;
DR   PRODOM; P06784.
DR   SWISS-2DPAGE; P06784.
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   NP_BIND         197..205
FT                   /note="ATP"
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         220
FT                   /note="ATP"
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
//

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