ID   MKK1_YEAST              Reviewed;         508 AA.
AC   P32490; D6W2T5; Q2VQW6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 212.
DE   RecName: Full=MAP kinase kinase MKK1/SSP32;
DE            EC=2.7.12.2;
GN   Name=MKK1; Synonyms=SSP32; OrderedLocusNames=YOR231W; ORFNames=O5095;
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=8386320; DOI=10.1128/mcb.13.5.3076-3083.1993;
RA   Irie K., Takase M., Lee K.S., Levin D.E., Araki H., Matsumoto K.,
RA   Oshima Y.;
RT   "MKK1 and MKK2, which encode Saccharomyces cerevisiae mitogen-activated
RT   protein kinase-kinase homologs, function in the pathway mediated by protein
RT   kinase C.";
RL   Mol. Cell. Biol. 13:3076-3083(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972580;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15%3c1575::aid-yea45%3e3.0.co;2-e;
RA   Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT   "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT   yeast Saccharomyces cerevisiae.";
RL   Yeast 12:1575-1586(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874; DOI=10.1038/387s098;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-74.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=15905473; DOI=10.1093/nar/gki583;
RA   Zhang Z., Dietrich F.S.;
RT   "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT   SAGE.";
RL   Nucleic Acids Res. 33:2838-2851(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12361575; DOI=10.1016/s0960-9822(02)01186-7;
RA   van Drogen F., Peter M.;
RT   "Spa2p functions as a scaffold-like protein to recruit the Mpk1p MAP kinase
RT   module to sites of polarized growth.";
RL   Curr. Biol. 12:1698-1703(2002).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, 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   [9]
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).
CC   -!- FUNCTION: Involved in a signal transduction pathway that play a role in
CC       yeast cell morphogenesis and cell growth. This pathway seems to start
CC       by SMP3; then involve the kinase PKC1 that may act on the BCK1 kinase
CC       that then phosphorylates MKK1 and MKK2 which themselves phosphorylate
CC       the MPK1 kinase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- INTERACTION:
CC       P32490; Q12263: GIN4; NbExp=2; IntAct=EBI-10968, EBI-7595;
CC       P32490; Q00772: SLT2; NbExp=4; IntAct=EBI-10968, EBI-17372;
CC       P32490; P23561: STE11; NbExp=2; IntAct=EBI-10968, EBI-18259;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12361575}.
CC       Cell tip {ECO:0000269|PubMed:12361575}. Note=Localizes to sites of
CC       polarized cell growth including the tip of small buds and the tips of
CC       mating projections (PubMed:12361575). Also localizes to the cell
CC       division site (PubMed:12361575). {ECO:0000269|PubMed:12361575}.
CC   -!- MISCELLANEOUS: Present with 1040 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; D13001; BAA02364.1; -; Genomic_DNA.
DR   EMBL; Z75139; CAA99451.1; -; Genomic_DNA.
DR   EMBL; AY899252; AAX83937.1; -; mRNA.
DR   EMBL; BK006948; DAA11001.1; -; Genomic_DNA.
DR   PIR; A48069; A48069.
DR   RefSeq; NP_014874.1; NM_001183650.1.
DR   AlphaFoldDB; P32490; -.
DR   SMR; P32490; -.
DR   BioGRID; 34624; 178.
DR   DIP; DIP-2224N; -.
DR   FunCoup; P32490; 680.
DR   IntAct; P32490; 21.
DR   MINT; P32490; -.
DR   STRING; 4932.YOR231W; -.
DR   iPTMnet; P32490; -.
DR   PaxDb; 4932-YOR231W; -.
DR   PeptideAtlas; P32490; -.
DR   EnsemblFungi; YOR231W_mRNA; YOR231W; YOR231W.
DR   GeneID; 854406; -.
DR   KEGG; sce:YOR231W; -.
DR   AGR; SGD:S000005757; -.
DR   SGD; S000005757; MKK1.
DR   VEuPathDB; FungiDB:YOR231W; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   HOGENOM; CLU_000288_63_23_1; -.
DR   InParanoid; P32490; -.
DR   OMA; ELNIVWS; -.
DR   OrthoDB; 10252354at2759; -.
DR   BioCyc; YEAST:G3O-33729-MONOMER; -.
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-6811555; PI5P Regulates TP53 Acetylation.
DR   BioGRID-ORCS; 854406; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P32490; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P32490; 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:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004708; F:MAP kinase kinase activity; ISS:SGD.
DR   GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR   GO; GO:0000196; P:cell integrity MAPK cascade; IGI:SGD.
DR   GO; GO:0000425; P:pexophagy; IGI:SGD.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IGI:SGD.
DR   GO; GO:0007165; P:signal transduction; IMP:SGD.
DR   FunFam; 3.30.200.20:FF:000294; Map kinase kinase; 1.
DR   FunFam; 1.10.510.10:FF:000263; MAP kinase skh1/pek1; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48013; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED; 1.
DR   PANTHER; PTHR48013:SF6; MAP KINASE KINASE MKK1_SSP32-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..508
FT                   /note="MAP kinase kinase MKK1/SSP32"
FT                   /id="PRO_0000086332"
FT   DOMAIN          221..488
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..66
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         227..235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   508 AA;  56720 MW;  4FE62CDD185CDAA2 CRC64;
     MASLFRPPES AKCNPNSPRL KLPLLRNNQV DENNIYLTSN GSSTTAYSSH TPEPLTSSTS
     TLFSQTRLHP SDSSMTLNTM KKRPAPPSLP SLSINSQSKC KTLPELVPIA DVSDGKHDLG
     LKQRVIAENE LSGNSDLTPS SMASPFSHTN TSSPYLRNDL SNSVGSDFSN LISAYEQSSS
     PIKSSSQPKS SSESYIDLNS VRDVDQLDEN GWKYANLKDR IETLGILGEG AGGSVSKCKL
     KNGSKIFALK VINTLNTDPE YQKQIFRELQ FNRSFQSEYI VRYYGMFTDD ENSSIYIAME
     YMGGRSLDAI YKNLLERGGR ISEKVLGKIA EAVLRGLSYL HEKKVIHRDI KPQNILLNEN
     GQVKLCDFGV SGEAVNSLAT TFTGTSFYMA PERIQGQPYS VTSDVWSLGL TILEVANGKF
     PCSSEKMAAN IAPFELLMWI LTFTPELKDE PESNIIWSPS FKSFIDYCLK KDSRERPSPR
     QMINHPWIKG QMKKNVNMEK FVRKCWKD
//