ID SLT2_YEAST Reviewed; 484 AA. AC Q00772; D3DKX7; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 27-MAR-2024, entry version 217. DE RecName: Full=Mitogen-activated protein kinase SLT2/MPK1; DE Short=MAP kinase MPK1; DE EC=2.7.11.24; GN Name=SLT2; Synonyms=MPK1; OrderedLocusNames=YHR030C; 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]. RC STRAIN=ATCC 204510 / AB320; RX PubMed=1779770; DOI=10.1111/j.1365-2958.1991.tb01993.x; RA Torres L., Martin H., Garcia-Saez M.I., Arroyo J., Molina M., Sanchez M., RA Nombela C.; RT "A protein kinase gene complements the lytic phenotype of Saccharomyces RT cerevisiae lyt2 mutants."; RL Mol. Microbiol. 5:2845-2854(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091229; DOI=10.1126/science.8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., RA Waterston R., Wilson R., Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). 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 CHARACTERIZATION. RX PubMed=8276900; DOI=10.1083/jcb.123.6.1821; RA Mazzoni C., Zarzov P., Rambourg A., Mann C.; RT "The SLT2 (MPK1) MAP kinase homolog is involved in polarized cell growth in RT Saccharomyces cerevisiae."; RL J. Cell Biol. 123:1821-1833(1993). RN [5] RP FUNCTION, AND INTERACTION WITH RLM1. RX PubMed=9111331; DOI=10.1128/mcb.17.5.2615; RA Watanabe Y., Takaesu G., Hagiwara M., Irie K., Matsumoto K.; RT "Characterization of a serum response factor-like protein in Saccharomyces RT cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 RT (Slt2) mitogen-activated protein kinase pathway."; RL Mol. Cell. Biol. 17:2615-2623(1997). RN [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, AND IDENTIFICATION BY RP 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190, 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). RN [9] RP FUNCTION. RX PubMed=20702584; DOI=10.1091/mbc.e10-03-0182; RA Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.; RT "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein RT kinase A toward some but not all substrates."; RL Mol. Biol. Cell 21:3475-3486(2010). CC -!- FUNCTION: Serine/threonine protein kinase involved in a signal CC transduction pathway that plays a role in yeast cell morphogenesis and CC cell growth. This pathway seems to start by SMP3; then involve the CC kinase PKC1 that may act the BCK1 kinase that then phosphorylates MKK1 CC and MKK2 which themselves phosphorylate the SLT2/MPK1 kinase which CC itself then phosphorylates and activates the transcription factor RLM1. CC Directly phosphorylates BCY1 upon TOR complex 1 (TORC1) inhibition. CC {ECO:0000269|PubMed:20702584, ECO:0000269|PubMed:9111331}. 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 tyrosine and threonine CC phosphorylation by MKK1 and MKK2. {ECO:0000305}. CC -!- SUBUNIT: Interacts with RLM1. {ECO:0000269|PubMed:9111331}. CC -!- INTERACTION: CC Q00772; Q02336: ADA2; NbExp=2; IntAct=EBI-17372, EBI-2186; CC Q00772; Q06697: CDC73; NbExp=2; IntAct=EBI-17372, EBI-29913; CC Q00772; P89105: CTR9; NbExp=2; IntAct=EBI-17372, EBI-5283; CC Q00772; Q03330: GCN5; NbExp=2; IntAct=EBI-17372, EBI-7458; CC Q00772; P02829: HSP82; NbExp=5; IntAct=EBI-17372, EBI-8659; CC Q00772; P38692: KIC1; NbExp=3; IntAct=EBI-17372, EBI-12253; CC Q00772; P38439: LEO1; NbExp=2; IntAct=EBI-17372, EBI-10108; CC Q00772; P32490: MKK1; NbExp=4; IntAct=EBI-17372, EBI-10968; CC Q00772; P32491: MKK2; NbExp=5; IntAct=EBI-17372, EBI-10973; CC Q00772; P38351: PAF1; NbExp=2; IntAct=EBI-17372, EBI-12855; CC Q00772; P53064: RTF1; NbExp=2; IntAct=EBI-17372, EBI-16303; CC Q00772; P53599: SSK2; NbExp=2; IntAct=EBI-17372, EBI-18191; CC Q00772; P13574: STE12; NbExp=2; IntAct=EBI-17372, EBI-18264; CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-190 and Tyr-192, which activates the CC enzyme. CC -!- MISCELLANEOUS: Present with 3230 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59262; CAA41954.1; -; Genomic_DNA. DR EMBL; U00062; AAB68912.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06721.1; -; Genomic_DNA. DR PIR; S43737; S43737. DR RefSeq; NP_011895.1; NM_001179160.1. DR AlphaFoldDB; Q00772; -. DR SMR; Q00772; -. DR BioGRID; 36461; 1047. DR DIP; DIP-1448N; -. DR ELM; Q00772; -. DR IntAct; Q00772; 98. DR MINT; Q00772; -. DR STRING; 4932.YHR030C; -. DR iPTMnet; Q00772; -. DR MaxQB; Q00772; -. DR PaxDb; 4932-YHR030C; -. DR PeptideAtlas; Q00772; -. DR EnsemblFungi; YHR030C_mRNA; YHR030C; YHR030C. DR GeneID; 856425; -. DR KEGG; sce:YHR030C; -. DR AGR; SGD:S000001072; -. DR SGD; S000001072; SLT2. DR VEuPathDB; FungiDB:YHR030C; -. DR eggNOG; KOG0660; Eukaryota. DR GeneTree; ENSGT00940000176702; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; Q00772; -. DR OMA; MDIPRPE; -. DR OrthoDB; 158564at2759; -. DR BioCyc; YEAST:G3O-31090-MONOMER; -. DR BRENDA; 2.7.11.24; 984. DR Reactome; R-SCE-198753; ERK/MAPK targets. DR Reactome; R-SCE-198765; Signalling to ERK5. DR Reactome; R-SCE-202670; ERKs are inactivated. DR Reactome; R-SCE-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-SCE-881907; Gastrin-CREB signalling pathway via PKC and MAPK. DR BioGRID-ORCS; 856425; 5 hits in 13 CRISPR screens. DR PRO; PR:Q00772; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; Q00772; 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; HDA:SGD. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0043332; C:mating projection tip; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central. 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; IDA:SGD. DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IGI:SGD. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:SGD. DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IGI:SGD. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IMP:SGD. DR GO; GO:0000425; P:pexophagy; IMP:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0010973; P:positive regulation of division septum assembly; IGI:SGD. DR GO; GO:0008361; P:regulation of cell size; IMP:SGD. DR GO; GO:0060256; P:regulation of flocculation; IMP:SGD. DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD. DR GO; GO:0090364; P:regulation of proteasome assembly; IMP:SGD. DR GO; GO:0042306; P:regulation of protein import into nucleus; IMP:SGD. DR GO; GO:0010447; P:response to acidic pH; IMP:SGD. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD. DR GO; GO:0007165; P:signal transduction; IMP:SGD. DR CDD; cd07857; STKc_MPK1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF603; MITOGEN-ACTIVATED PROTEIN KINASE SLT2_MPK1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..484 FT /note="Mitogen-activated protein kinase SLT2/MPK1" FT /id="PRO_0000186338" FT DOMAIN 23..318 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 383..403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 426..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 190..192 FT /note="TXY" FT ACT_SITE 153 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 29..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 190 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 192 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17330950" FT CONFLICT 56 FT /note="V -> L (in Ref. 1; CAA41954)" FT /evidence="ECO:0000305" FT CONFLICT 467 FT /note="T -> S (in Ref. 1; CAA41954)" FT /evidence="ECO:0000305" SQ SEQUENCE 484 AA; 55636 MW; 559A3E0D3EBDE5F9 CRC64; MADKIERHTF KVFNQDFSVD KRFQLIKEIG HGAYGIVCSA RFAEAAEDTT VAIKKVTNVF SKTLLCKRSL RELKLLRHFR GHKNITCLYD MDIVFYPDGS INGLYLYEEL MECDMHQIIK SGQPLTDAHY QSFTYQILCG LKYIHSADVL HRDLKPGNLL VNADCQLKIC DFGLARGYSE NPVENSQFLT EYVATRWYRA PEIMLSYQGY TKAIDVWSAG CILAEFLGGK PIFKGKDYVN QLNQILQVLG TPPDETLRRI GSKNVQDYIH QLGFIPKVPF VNLYPNANSQ ALDLLEQMLA FDPQKRITVD EALEHPYLSI WHDPADEPVC SEKFEFSFES VNDMEDLKQM VIQEVQDFRL FVRQPLLEEQ RQLQLQQQQQ QQQQQQQQQQ QPSDVDNGNA AASEENYPKQ MATSNSVAPQ QESFGIHSQN LPRHDADFPP RPQESMMEMR PATGNTADIP PQNDNGTLLD LEKELEFGLD RKYF //