SLT2_YEAST
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 03-AUG-2022, entry version 211.
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; 1041.
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; Q00772; -.
DR PRIDE; Q00772; -.
DR EnsemblFungi; YHR030C_mRNA; YHR030C; YHR030C.
DR GeneID; 856425; -.
DR KEGG; sce:YHR030C; -.
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 BioCyc; YEAST:G3O-31090-MON; -.
DR BRENDA; 2.7.11.24; 984.
DR Reactome; R-SCE-110056; MAPK3 (ERK1) activation.
DR Reactome; R-SCE-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-SCE-170968; Frs2-mediated activation.
DR Reactome; R-SCE-198753; ERK/MAPK targets.
DR Reactome; R-SCE-202670; ERKs are inactivated.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SCE-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-SCE-445144; Signal transduction by L1.
DR Reactome; R-SCE-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-SCE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-SCE-5674135; MAP2K and MAPK activation.
DR Reactome; R-SCE-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
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:0030242; P:autophagy of peroxisome; IMP: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:0010973; P:positive regulation of division septum assembly; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP: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 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 Pfam; PF00069; Pkinase; 1.
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 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
