ID   STE50_YEAST             Reviewed;         346 AA.
AC   P25344; D6VQY3; Q3S1N2;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   04-NOV-2026, entry version 205.
DE   RecName: Full=Protein kinase regulator STE50 {ECO:0000303|PubMed:14573615};
GN   Name=STE50 {ECO:0000303|PubMed:14573615}; OrderedLocusNames=YCL032W;
GN   ORFNames=YCL32W;
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=1494345; DOI=10.1007/bf00279653;
RA   Rad M.R., Xu G., Hollenberg C.P.;
RT   "STE50, a novel gene required for activation of conjugation at an early
RT   step in mating in Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 236:145-154(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1897318; DOI=10.1002/yea.320070513;
RA   Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
RT   "The complete sequence of a 11,953 bp fragment from C1G on chromosome III
RT   encompasses four new open reading frames.";
RL   Yeast 7:533-538(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-248, AND
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; THR-244 AND SER-248, AND
RP   IDENTIFICATION BY 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   [9]
RP   STRUCTURE BY NMR OF 27-108, AND INTERACTION WITH STE11.
RX   PubMed=14573615; DOI=10.1074/jbc.m305605200;
RA   Grimshaw S.J., Mott H.R., Stott K.M., Nielsen P.R., Evetts K.A.,
RA   Hopkins L.J., Nietlispach D., Owen D.;
RT   "Structure of the sterile alpha motif (SAM) domain of the Saccharomyces
RT   cerevisiae mitogen-activated protein kinase pathway-modulating protein
RT   STE50 and analysis of its interaction with the STE11 SAM.";
RL   J. Biol. Chem. 279:2192-2201(2004).
RN   [10]
RP   STRUCTURE BY NMR OF 32-107, AND INTERACTION WITH STE11.
RX   PubMed=16337230; DOI=10.1016/j.jmb.2005.11.012;
RA   Kwan J.J., Warner N., Maini J., Chan Tung K.W., Zakaria H., Pawson T.,
RA   Donaldson L.W.;
RT   "Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-
RT   tail SAM domain interaction.";
RL   J. Mol. Biol. 356:142-154(2006).
CC   -!- FUNCTION: Involved in growth arrest during conjugation. May interact
CC       with the G protein alpha subunit.
CC   -!- SUBUNIT: Interacts with STE11 through the respective SAM domains.
CC       {ECO:0000269|PubMed:14573615, ECO:0000269|PubMed:16337230}.
CC   -!- INTERACTION:
CC       P25344; P40073: SHO1; NbExp=3; IntAct=EBI-18305, EBI-18140;
CC       P25344; P23561: STE11; NbExp=6; IntAct=EBI-18305, EBI-18259;
CC   -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the STE50 family. {ECO:0000305}.
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DR   EMBL; Z11116; CAA77462.1; -; Genomic_DNA.
DR   EMBL; S54312; AAA13629.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42384.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07452.1; -; Genomic_DNA.
DR   PIR; S17475; S17475.
DR   RefSeq; NP_009898.1; NM_001178677.1.
DR   PDB; 1UQV; NMR; -; A=27-108.
DR   PDB; 1Z1V; NMR; -; A=32-107.
DR   AlphaFoldDB; P25344; -.
DR   MDposit; P25344; -.
DR   SMR; P25344; -.
DR   BioGRID; 30951; 743.
DR   DIP; DIP-667N; -.
DR   FunCoup; P25344; 163.
DR   IntAct; P25344; 41.
DR   STRING; 4932.YCL032W; -.
DR   GlyCosmos; P25344; 1 site, No reported glycans.
DR   GlyGen; P25344; 10 sites, 1 O-linked glycan (9 sites).
DR   iPTMnet; P25344; -.
DR   PaxDb; 4932-YCL032W; -.
DR   PeptideAtlas; P25344; -.
DR   EnsemblFungi; YCL032W_mRNA; YCL032W; YCL032W.
DR   GeneID; 850325; -.
DR   KEGG; sce:YCL032W; -.
DR   AGR; SGD:S000000537; -.
DR   SGD; S000000537; STE50.
DR   VEuPathDB; FungiDB:YCL032W; -.
DR   eggNOG; ENOG502RXZB; Eukaryota.
DR   HOGENOM; CLU_051042_0_0_1; -.
DR   InParanoid; P25344; -.
DR   OMA; ADQDWRQ; -.
DR   OrthoDB; 445896at2759; -.
DR   BioCyc; YEAST:G3O-29292-MONOMER; -.
DR   BioGRID-ORCS; 850325; 5 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P25344; -.
DR   PRO; PR:P25344; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25344; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0019887; F:protein kinase regulator activity; IDA:SGD.
DR   GO; GO:0032093; F:SAM domain binding; IDA:SGD.
DR   GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR   GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IMP:SGD.
DR   GO; GO:0038066; P:p38MAPK cascade; IGI:SGD.
DR   GO; GO:0071507; P:pheromone response MAPK cascade; IMP:SGD.
DR   GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR   CDD; cd01786; RA_STE50; 1.
DR   CDD; cd09536; SAM_Ste50_fungal; 1.
DR   DisProt; DP01515; -.
DR   FunFam; 3.10.20.90:FF:000314; Ste50p; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR015316; SAM_Ste50.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF09235; SAM_Ste50p; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50200; RA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Growth arrest; Pheromone response;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..346
FT                   /note="Protein kinase regulator STE50"
FT                   /id="PRO_0000072265"
FT   DOMAIN          24..108
FT                   /note="SAM"
FT   DOMAIN          233..327
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   REGION          151..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         244
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:1UQV"
FT   HELIX           37..48
FT                   /evidence="ECO:0007829|PDB:1UQV"
FT   HELIX           56..62
FT                   /evidence="ECO:0007829|PDB:1UQV"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:1UQV"
FT   HELIX           70..80
FT                   /evidence="ECO:0007829|PDB:1UQV"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:1UQV"
FT   HELIX           86..101
FT                   /evidence="ECO:0007829|PDB:1UQV"
SQ   SEQUENCE   346 AA;  38971 MW;  EFC7D14F2940C779 CRC64;
     MEDGKQAINE GSNDASPDLD VNGTILMNNE DFSQWSVDDV ITWCISTLEV EETDPLCQRL
     RENDIVGDLL PELCLQDCQD LCDGDLNKAI KFKILINKMR DSKLEWKDDK TQEDMITVLK
     NLYTTTSAKL QEFQSQYTRL RMDVLDVMKT SSSSSPINTH GVSTTVPSSN NTIIPSSDGV
     SLSQTDYFDT VHNRQSPSRR ESPVTVFRQP SLSHSKSLHK DSKNKVPQIS TNQSHPSAVS
     TANTPGPSPN EALKQLRASK EDSCERILKN AMKRHNLADQ DWRQYVLVIC YGDQERLLEL
     NEKPVIIFKN LKQQGLHPAI MLRRRGDFEE VAMMNGSDNV TPGGRL
//