HOG1_SCHPO
ID HOG1_SCHPO Reviewed; 349 AA.
AC Q09892;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Mitogen-activated protein kinase sty1;
DE Short=MAP kinase sty1;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase spc1;
GN Name=sty1; Synonyms=hog1, phh1, spc1; ORFNames=SPAC24B11.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7657164; DOI=10.1101/gad.9.17.2117;
RA Millar J.B.A., Buck V., Wilkinson M.G.;
RT "Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase
RT controlling cell size at division in fission yeast.";
RL Genes Dev. 9:2117-2130(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, AND ACTIVITY
RP REGULATION.
RX PubMed=7501024; DOI=10.1038/378739a0;
RA Shiozaki K., Russell P.;
RT "Cell-cycle control linked to extracellular environment by MAP kinase
RT pathway in fission yeast.";
RL Nature 378:739-743(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8557102; DOI=10.1016/0014-5793(95)01442-x;
RA Kato T. Jr., Okazaki K., Murakami H., Stettler S., Fantes P.A., Okayama H.;
RT "Stress signal, mediated by a Hog1-like MAP kinase, controls sexual
RT development in fission yeast.";
RL FEBS Lett. 378:207-212(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [5]
RP FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8824587; DOI=10.1101/gad.10.18.2276;
RA Shiozaki K., Russell P.;
RT "Conjugation, meiosis, and the osmotic stress response are regulated by
RT Spc1 kinase through Atf1 transcription factor in fission yeast.";
RL Genes Dev. 10:2276-2288(1996).
RN [6]
RP ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=8649397; DOI=10.1128/mcb.16.6.2870;
RA Degols G., Shiozaki K., Russell P.;
RT "Activation and regulation of the Spc1 stress-activated protein kinase in
RT Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 16:2870-2877(1996).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9251044; DOI=10.1016/s0076-6879(97)83040-6;
RA Shiozaki K., Russell P.;
RT "Stress-activated protein kinase pathway in cell cycle control of fission
RT yeast.";
RL Methods Enzymol. 283:506-520(1997).
RN [8]
RP ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=9188094; DOI=10.1091/mbc.8.3.409;
RA Shiozaki K., Shiozaki M., Russell P.;
RT "Mcs4 mitotic catastrophe suppressor regulates the fission yeast cell cycle
RT through the Wik1-Wis1-Spc1 kinase cascade.";
RL Mol. Biol. Cell 8:409-419(1997).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=9443913; DOI=10.1016/s0960-9822(98)00060-8;
RA Bone N., Millar J.B.A., Toda T., Armstrong J.;
RT "Regulated vacuole fusion and fission in Schizosaccharomyces pombe: an
RT osmotic response dependent on MAP kinases.";
RL Curr. Biol. 8:135-144(1998).
RN [10]
RP FUNCTION.
RX PubMed=9585505; DOI=10.1101/gad.12.10.1453;
RA Toone W.M., Kuge S., Samuels M., Morgan B.A., Toda T., Jones N.;
RT "Regulation of the fission yeast transcription factor Pap1 by oxidative
RT stress: requirement for the nuclear export factor Crm1 (Exportin) and the
RT stress-activated MAP kinase Sty1/Spc1.";
RL Genes Dev. 12:1453-1463(1998).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=9585506; DOI=10.1101/gad.12.10.1464;
RA Gaits F., Degols G., Shiozaki K., Russell P.;
RT "Phosphorylation and association with the transcription factor Atf1
RT regulate localization of Spc1/Sty1 stress-activated kinase in fission
RT yeast.";
RL Genes Dev. 12:1464-1473(1998).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH SRK1.
RX PubMed=12080074; DOI=10.1074/jbc.m204593200;
RA Smith D.A., Toone W.M., Chen D., Baehler J., Jones N., Morgan B.A.,
RA Quinn J.;
RT "The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in
RT fission yeast.";
RL J. Biol. Chem. 277:33411-33421(2002).
RN [13]
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=12181336; DOI=10.1091/mbc.02-03-0043;
RA Nguyen A.N., Ikner A.D., Shiozaki M., Warren S.M., Shiozaki K.;
RT "Cytoplasmic localization of Wis1 MAPKK by nuclear export signal is
RT important for nuclear targeting of Spc1/Sty1 MAPK in fission yeast.";
RL Mol. Biol. Cell 13:2651-2663(2002).
RN [14]
RP INTERACTION WITH CDC37, AND ACTIVITY REGULATION.
RX PubMed=12861001; DOI=10.1128/mcb.23.15.5132-5142.2003;
RA Tatebe H., Shiozaki K.;
RT "Identification of cdc37 as a novel regulator of the stress-responsive
RT mitogen-activated protein kinase.";
RL Mol. Cell. Biol. 23:5132-5142(2003).
RN [15]
RP FUNCTION, AND INTERACTION WITH CMK2 AND SRK1.
RX PubMed=12589433; DOI=10.1007/s00438-002-0786-y;
RA Asp E., Sunnerhagen P.;
RT "Mkp1 and Mkp2, two MAPKAP-kinase homologues in Schizosaccharomyces pombe,
RT interact with the MAP kinase Sty1.";
RL Mol. Genet. Genomics 268:585-597(2003).
RN [16]
RP FUNCTION.
RX PubMed=15840944; DOI=10.1247/csf.29.125;
RA Yoshida J., Tani T.;
RT "Hsp16p is required for thermotolerance in nuclear mRNA export in fission
RT yeast Schizosaccharomyces pombe.";
RL Cell Struct. Funct. 29:125-138(2005).
RN [17]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16087744; DOI=10.1128/ec.4.8.1396-1402.2005;
RA Rodriguez-Gabriel M.A., Russell P.;
RT "Distinct signaling pathways respond to arsenite and reactive oxygen
RT species in Schizosaccharomyces pombe.";
RL Eukaryot. Cell 4:1396-1402(2005).
RN [18]
RP FUNCTION.
RX PubMed=16278445; DOI=10.1128/ec.4.11.1785-1793.2005;
RA Dunand-Sauthier I., Walker C.A., Narasimhan J., Pearce A.K., Wek R.C.,
RA Humphrey T.C.;
RT "Stress-activated protein kinase pathway functions to support protein
RT synthesis and translational adaptation in response to environmental stress
RT in fission yeast.";
RL Eukaryot. Cell 4:1785-1793(2005).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=16141205; DOI=10.1074/jbc.m508400200;
RA Zuin A., Vivancos A.P., Sanso M., Takatsume Y., Ayte J., Inoue Y.,
RA Hidalgo E.;
RT "The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress
RT responses in Schizosaccharomyces pombe.";
RL J. Biol. Chem. 280:36708-36713(2005).
RN [20]
RP FUNCTION, AND INTERACTION WITH HAL4.
RX PubMed=15870269; DOI=10.1128/mcb.25.10.3945-3955.2005;
RA Wang L.-Y., Shimada K., Morishita M., Shiozaki K.;
RT "Response of fission yeast to toxic cations involves cooperative action of
RT the stress-activated protein kinase Spc1/Sty1 and the Hal4 protein
RT kinase.";
RL Mol. Cell. Biol. 25:3945-3955(2005).
RN [21]
RP FUNCTION.
RX PubMed=16603158; DOI=10.1016/j.febslet.2006.03.065;
RA Wang L.-Y., Shiozaki K.;
RT "The fission yeast stress MAPK cascade regulates the pmp3+ gene that
RT encodes a highly conserved plasma membrane protein.";
RL FEBS Lett. 580:2409-2413(2006).
RN [22]
RP PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=16464860; DOI=10.1074/jbc.m511037200;
RA Takatsume Y., Izawa S., Inoue Y.;
RT "Methylglyoxal as a signal initiator for activation of the stress-activated
RT protein kinase cascade in the fission yeast Schizosaccharomyces pombe.";
RL J. Biol. Chem. 281:9086-9092(2006).
RN [23]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [24]
RP FUNCTION.
RX PubMed=17182615; DOI=10.1074/jbc.m608526200;
RA Lawrence C.L., Maekawa H., Worthington J.L., Reiter W., Wilkinson C.R.M.,
RA Jones N.;
RT "Regulation of Schizosaccharomyces pombe Atf1 protein levels by Sty1-
RT mediated phosphorylation and heterodimerization with Pcr1.";
RL J. Biol. Chem. 282:5160-5170(2007).
RN [25]
RP FUNCTION.
RX PubMed=17272281; DOI=10.1074/jbc.m609282200;
RA Taricani L., Wang T.S.F.;
RT "Rad4TopBP1 associates with Srr2, an Spc1 MAPK-regulated protein, in
RT response to environmental stress.";
RL J. Biol. Chem. 282:8793-8800(2007).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-171; TYR-173; SER-175 AND
RP THR-176, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [27]
RP DISRUPTION PHENOTYPE.
RX PubMed=28775286; DOI=10.1038/s41598-017-07647-1;
RA Villahermosa D., Fleck O.;
RT "Elp3 and Dph3 of Schizosaccharomyces pombe mediate cellular stress
RT responses through tRNALysUUU modifications.";
RL Sci. Rep. 7:7225-7225(2017).
CC -!- FUNCTION: Mitogen-activated protein kinase involved in a signal
CC transduction pathway that is activated by changes in the osmolarity of
CC the extracellular environment. Controls osmotic regulation of
CC transcription of target genes. Involved in osmoregulation and stress
CC response pathways leading to an efficient start of sexual
CC differentiation. Supports translation initiation and facilitates
CC adaptation to environmental stress in part through reducing eIF2-alpha
CC phosphorylation. Links the cell-cycle G2/M control with changes in the
CC extracellular environment that affect cell physiology. Phosphorylates
CC atf1 and mkp1. In conjunction with hal4, has a role in the cellular
CC resistance to toxic cations such as Na(+), Li(+) and Ca(2+). Involved
CC in resistance to arsenite, methylglyoxal and hydrogen peroxide.
CC Involved in induction of thermotolerance in mRNA export, as well as in
CC vacuolar fission. {ECO:0000269|PubMed:12080074,
CC ECO:0000269|PubMed:12589433, ECO:0000269|PubMed:15840944,
CC ECO:0000269|PubMed:15870269, ECO:0000269|PubMed:16087744,
CC ECO:0000269|PubMed:16141205, ECO:0000269|PubMed:16278445,
CC ECO:0000269|PubMed:16603158, ECO:0000269|PubMed:17182615,
CC ECO:0000269|PubMed:17272281, ECO:0000269|PubMed:7501024,
CC ECO:0000269|PubMed:7657164, ECO:0000269|PubMed:8557102,
CC ECO:0000269|PubMed:8824587, ECO:0000269|PubMed:9443913,
CC ECO:0000269|PubMed:9585505}.
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=2.7.11.24;
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=2.7.11.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by the MAPK kinase wisl, and negatively
CC regulated by pypl and pyp2 tyrosine phosphatases.
CC {ECO:0000269|PubMed:12181336, ECO:0000269|PubMed:12861001,
CC ECO:0000269|PubMed:16464860, ECO:0000269|PubMed:7501024,
CC ECO:0000269|PubMed:8649397, ECO:0000269|PubMed:9188094}.
CC -!- SUBUNIT: Interacts with cdc37, cmk2, hal4, sin1 and srk1.
CC {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:12589433,
CC ECO:0000269|PubMed:12861001, ECO:0000269|PubMed:15870269}.
CC -!- INTERACTION:
CC Q09892; P52890: atf1; NbExp=2; IntAct=EBI-3648525, EBI-3861527;
CC Q09892; O74802: ehd3; NbExp=3; IntAct=EBI-3648525, EBI-16823313;
CC Q09892; O14156: ptc4; NbExp=4; IntAct=EBI-3648525, EBI-7593590;
CC Q09892; O94547: srk1; NbExp=3; IntAct=EBI-3648525, EBI-3648527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic in unstressed cells but rapidly concentrates within the
CC nucleus in response to hyperosmotic conditions and phosphorylation.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the
CC enzyme (By similarity). Phosphorylated by wis1 in response to osmotic
CC stress, nutrient limitation, hydrogen peroxide and arsenite.
CC Dephosphorylated by pyp1 and pyp2. {ECO:0000250,
CC ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:16087744,
CC ECO:0000269|PubMed:16141205, ECO:0000269|PubMed:16464860,
CC ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:7501024,
CC ECO:0000269|PubMed:8649397, ECO:0000269|PubMed:9188094,
CC ECO:0000269|PubMed:9443913}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to methyl methanesulfonate (MMS, causes
CC DNA breaks), hydroxyurea (HU, ribonucleotide reductase inhibitor),
CC thiabendazole (TBZ), sirolimus (TORC1 inhibitor), and cold.
CC {ECO:0000269|PubMed:28775286}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. HOG1 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X89262; CAA61537.1; -; Genomic_DNA.
DR EMBL; U26739; AAA91020.1; -; mRNA.
DR EMBL; CU329670; CAA91771.1; -; Genomic_DNA.
DR PIR; S68675; S68675.
DR RefSeq; NP_592843.1; NM_001018244.2.
DR AlphaFoldDB; Q09892; -.
DR SMR; Q09892; -.
DR BioGRID; 278148; 313.
DR IntAct; Q09892; 10.
DR MINT; Q09892; -.
DR STRING; 4896.SPAC24B11.06c.1; -.
DR iPTMnet; Q09892; -.
DR MaxQB; Q09892; -.
DR PaxDb; Q09892; -.
DR PRIDE; Q09892; -.
DR EnsemblFungi; SPAC24B11.06c.1; SPAC24B11.06c.1:pep; SPAC24B11.06c.
DR GeneID; 2541652; -.
DR KEGG; spo:SPAC24B11.06c; -.
DR PomBase; SPAC24B11.06c; sty1.
DR VEuPathDB; FungiDB:SPAC24B11.06c; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q09892; -.
DR OMA; YTDLNPV; -.
DR PhylomeDB; Q09892; -.
DR BRENDA; 2.7.11.24; 5613.
DR Reactome; R-SPO-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-SPO-198753; ERK/MAPK targets.
DR Reactome; R-SPO-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-SPO-432142; Platelet sensitization by LDL.
DR Reactome; R-SPO-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-SPO-525793; Myogenesis.
DR Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:Q09892; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:PomBase.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004707; F:MAP kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:PomBase.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IPI:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0007231; P:osmosensory signaling pathway; IBA:GO_Central.
DR GO; GO:0038066; P:p38MAPK cascade; IDA:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:PomBase.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:PomBase.
DR GO; GO:1904789; P:regulation of mitotic actomyosin contractile ring maintenance; EXP:PomBase.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:PomBase.
DR CDD; cd07856; STKc_Sty1_Hog1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008352; MAPK_p38-like.
DR InterPro; IPR038783; MAPK_Sty1/Hog1.
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 PRINTS; PR01773; P38MAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 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 Activator; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..349
FT /note="Mitogen-activated protein kinase sty1"
FT /id="PRO_0000186342"
FT DOMAIN 20..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 171..173
FT /note="TXY"
FT MOTIF 176..178
FT /note="TXY"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 173
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 349 AA; 40222 MW; 9A10835FFD381AC0 CRC64;
MAEFIRTQIF GTCFEITTRY SDLQPIGMGA FGLVCSAKDQ LTGMNVAVKK IMKPFSTPVL
AKRTYRELKL LKHLRHENII SLSDIFISPF EDIYFVTELL GTDLHRLLTS RPLETQFIQY
FLYQILRGLK FVHSAGVIHR DLKPSNILIN ENCDLKICDF GLARIQDPQM TGYVSTRYYR
APEIMLTWQK YNVEVDIWSA GCIFAEMIEG KPLFPGRDHV NQFSIITELL GTPPMEVIET
ICSKNTLRFV QSLPQKEKVP FAEKFKNADP DAIDLLEKML VFDPRKRISA ADALAHNYLA
PYHDPTDEPV ADEVFDWSFQ DNDLPVETWK VMMYSEVLSF HNMDNELQS
