STE50_YEAST
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 03-AUG-2022, entry version 187.
DE RecName: Full=Protein STE50;
GN Name=STE50; OrderedLocusNames=YCL032W; 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=5; IntAct=EBI-18305, EBI-18259;
CC -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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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 PDBsum; 1UQV; -.
DR PDBsum; 1Z1V; -.
DR AlphaFoldDB; P25344; -.
DR SMR; P25344; -.
DR BioGRID; 30951; 733.
DR DIP; DIP-667N; -.
DR IntAct; P25344; 40.
DR MINT; P25344; -.
DR STRING; 4932.YCL032W; -.
DR iPTMnet; P25344; -.
DR MaxQB; P25344; -.
DR PaxDb; P25344; -.
DR PRIDE; P25344; -.
DR EnsemblFungi; YCL032W_mRNA; YCL032W; YCL032W.
DR GeneID; 850325; -.
DR KEGG; sce:YCL032W; -.
DR SGD; S000000537; STE50.
DR VEuPathDB; FungiDB:YCL032W; -.
DR eggNOG; ENOG502RXZB; Eukaryota.
DR HOGENOM; CLU_051042_0_0_1; -.
DR InParanoid; P25344; -.
DR OMA; WRQYVLV; -.
DR BioCyc; YEAST:G3O-29292-MON; -.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IGI: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:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR CDD; cd09536; SAM_Ste50_fungal; 1.
DR DisProt; DP01515; -.
DR Gene3D; 1.10.150.50; -; 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; SSF47769; 1.
DR SUPFAM; SSF54236; SSF54236; 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 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..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..250
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
