PBS2_YEAST
ID PBS2_YEAST Reviewed; 668 AA.
AC P08018; D6VW57;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=MAP kinase kinase PBS2;
DE EC=2.7.12.2;
DE AltName: Full=Polymyxin B resistance protein 2;
DE AltName: Full=Suppressor of fluoride sensitivity 4;
GN Name=PBS2; Synonyms=HOG4, SFS4, SSK4; OrderedLocusNames=YJL128C;
GN ORFNames=J0699;
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.
RX PubMed=3039511; DOI=10.1073/pnas.84.16.5848;
RA Boguslawski G., Polazzi J.O.;
RT "Complete nucleotide sequence of a gene conferring polymyxin B resistance
RT on yeast: similarity of the predicted polypeptide to protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5848-5852(1987).
RN [2]
RP SEQUENCE REVISION TO 222-223 AND 668.
RX PubMed=1479360; DOI=10.1099/00221287-138-11-2425;
RA Boguslawski G.;
RT "PBS2, a yeast gene encoding a putative protein kinase, interacts with the
RT RAS2 pathway and affects osmotic sensitivity of Saccharomyces cerevisiae.";
RL J. Gen. Microbiol. 138:2425-2432(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7814365; DOI=10.1074/jbc.270.1.143;
RA Kahn R.A., Clark J., Rulka C., Stearns T., Zhang C.J., Randazzo P.A.,
RA Terui T., Cavenagh M.;
RT "Mutational analysis of Saccharomyces cerevisiae ARF1.";
RL J. Biol. Chem. 270:143-150(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 222-223.
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 [7]
RP NUCLEOTIDE SEQUENCE OF 91-101, DOMAIN, PHOSPHORYLATION AT SER-514 AND
RP THR-518, AND MUTAGENESIS OF PRO-96; LYS-389; SER-514 AND THR-518.
RX PubMed=7624781; DOI=10.1126/science.7624781;
RA Maeda T., Takekawa M., Saito H.;
RT "Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-
RT containing osmosensor.";
RL Science 269:554-558(1995).
RN [8]
RP FUNCTION.
RX PubMed=7681220; DOI=10.1126/science.7681220;
RA Brewster J.L., de Valoir T., Dwyer N.D., Winter E., Gustin M.C.;
RT "An osmosensing signal transduction pathway in yeast.";
RL Science 259:1760-1763(1993).
RN [9]
RP FUNCTION, AND INTERACTION WITH SHO1.
RX PubMed=10970855; DOI=10.1093/emboj/19.17.4623;
RA Raitt D.C., Posas F., Saito H.;
RT "Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent
RT activation of the Hog1 MAPK pathway.";
RL EMBO J. 19:4623-4631(2000).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
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 [12]
RP INTERACTION WITH NBP2 AND PTC1.
RX PubMed=14685261; DOI=10.1038/sj.emboj.7600036;
RA Mapes J., Ota I.M.;
RT "Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK
RT pathway.";
RL EMBO J. 23:302-311(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH SHO1.
RX PubMed=15256499; DOI=10.1101/gad.1178604;
RA Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K.,
RA Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.;
RT "A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous
RT growth pathway in yeast.";
RL Genes Dev. 18:1695-1708(2004).
RN [14]
RP INTERACTION WITH SHO1 AND STE11.
RX PubMed=15200958; DOI=10.1016/j.molcel.2004.05.024;
RA Marles J.A., Dahesh S., Haynes J., Andrews B.J., Davidson A.R.;
RT "Protein-protein interaction affinity plays a crucial role in controlling
RT the Sho1p-mediated signal transduction pathway in yeast.";
RL Mol. Cell 14:813-823(2004).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, 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).
CC -!- FUNCTION: Kinase involved in a signal transduction pathway that is
CC activated by changes in the osmolarity of the extracellular
CC environment. Seems to phosphorylate HOG1 on a tyrosine residue.
CC {ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:15256499,
CC ECO:0000269|PubMed:7681220}.
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 -!- SUBUNIT: Interacts with NBP2, PTC1, SHO1 AND STE11.
CC {ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:14685261,
CC ECO:0000269|PubMed:15200958, ECO:0000269|PubMed:15256499}.
CC -!- INTERACTION:
CC P08018; Q12163: NBP2; NbExp=3; IntAct=EBI-12972, EBI-34713;
CC P08018; P40073: SHO1; NbExp=8; IntAct=EBI-12972, EBI-18140;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: Alternative way of activation involves binding the proline-rich
CC motif to the SH3 domain of SHO1. {ECO:0000269|PubMed:7624781}.
CC -!- PTM: Activated by phosphorylation by SSK2 or SSK22. Ser/Thr
CC phosphorylation is also necessary for SHO1-mediated activation.
CC {ECO:0000269|PubMed:7624781}.
CC -!- MISCELLANEOUS: Present with 2160 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; J02946; AAA16819.1; -; Unassigned_DNA.
DR EMBL; U12237; AAA20392.1; -; Genomic_DNA.
DR EMBL; Z49403; CAA89423.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08673.2; -; Genomic_DNA.
DR PIR; S56909; S56909.
DR RefSeq; NP_012407.2; NM_001181561.2.
DR PDB; 2VKN; X-ray; 2.05 A; C=92-103.
DR PDBsum; 2VKN; -.
DR AlphaFoldDB; P08018; -.
DR SMR; P08018; -.
DR BioGRID; 33628; 509.
DR DIP; DIP-2368N; -.
DR ELM; P08018; -.
DR IntAct; P08018; 45.
DR MINT; P08018; -.
DR STRING; 4932.YJL128C; -.
DR iPTMnet; P08018; -.
DR MaxQB; P08018; -.
DR PaxDb; P08018; -.
DR PRIDE; P08018; -.
DR EnsemblFungi; YJL128C_mRNA; YJL128C; YJL128C.
DR GeneID; 853313; -.
DR KEGG; sce:YJL128C; -.
DR SGD; S000003664; PBS2.
DR VEuPathDB; FungiDB:YJL128C; -.
DR eggNOG; KOG0581; Eukaryota.
DR GeneTree; ENSGT00940000158914; -.
DR HOGENOM; CLU_000288_79_1_1; -.
DR InParanoid; P08018; -.
DR OMA; NILCSAK; -.
DR BioCyc; YEAST:G3O-31578-MON; -.
DR BRENDA; 2.7.12.2; 984.
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-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-6811555; PI5P Regulates TP53 Acetylation.
DR EvolutionaryTrace; P08018; -.
DR PRO; PR:P08018; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P08018; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0031416; C:NatB complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IMP:SGD.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IPI:SGD.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IMP:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; HDA: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:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0071474; P:cellular hyperosmotic response; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IMP:SGD.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0007231; P:osmosensory signaling pathway; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..668
FT /note="MAP kinase kinase PBS2"
FT /id="PRO_0000086483"
FT DOMAIN 360..623
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 485
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 366..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7624781,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:7624781"
FT MUTAGEN 96
FT /note="P->S: In PBS2-13; loss of SH3-domain interaction."
FT /evidence="ECO:0000269|PubMed:7624781"
FT MUTAGEN 389
FT /note="K->M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7624781"
FT MUTAGEN 514
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:7624781"
FT MUTAGEN 518
FT /note="T->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:7624781"
FT CONFLICT 222..223
FT /note="GL -> AV (in Ref. 4 and 5; CAA89423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 72720 MW; 9BC3435BDAFE8019 CRC64;
MEDKFANLSL HEKTGKSSIQ LNEQTGSDNG SAVKRTSSTS SHYNNINADL HARVKAFQEQ
RALKRSASVG SNQSEQDKGS SQSPKHIQQI VNKPLPPLPV AGSSKVSQRM SSQVVQASSK
STLKNVLDNQ ETQNITDVNI NIDTTKITAT TIGVNTGLPA TDITPSVSNT ASATHKAQLL
NPNRRAPRRP LSTQHPTRPN VAPHKAPAII NTPKQSLSAR RGLKLPPGGM SLKMPTKTAQ
QPQQFAPSPS NKKHIETLSN SKVVEGKRSN PGSLINGVQS TSTSSSTEGP HDTVGTTPRT
GNSNNSSNSG SSGGGGLFAN FSKYVDIKSG SLNFAGKLSL SSKGIDFSNG SSSRITLDEL
EFLDELGHGN YGNVSKVLHK PTNVIMATKE VRLELDEAKF RQILMELEVL HKCNSPYIVD
FYGAFFIEGA VYMCMEYMDG GSLDKIYDES SEIGGIDEPQ LAFIANAVIH GLKELKEQHN
IIHRDVKPTN ILCSANQGTV KLCDFGVSGN LVASLAKTNI GCQSYMAPER IKSLNPDRAT
YTVQSDIWSL GLSILEMALG RYPYPPETYD NIFSQLSAIV DGPPPRLPSD KFSSDAQDFV
SLCLQKIPER RPTYAALTEH PWLVKYRNQD VHMSEYITER LERRNKILRE RGENGLSKNV
PALHMGGL
