MKK2_YEAST
ID MKK2_YEAST Reviewed; 506 AA.
AC P32491; D6W3M8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=MAP kinase kinase MKK2/SSP33;
DE EC=2.7.12.2;
GN Name=MKK2; Synonyms=SSP33; OrderedLocusNames=YPL140C; ORFNames=LPI6C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RC STRAIN=ATCC 204626 / S288c / A364A;
RA Mallory M.J., Strich R.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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 involves the
CC kinase PKC1 that may act on the BCK1 kinase that then phosphorylates
CC MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.
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 -!- INTERACTION:
CC P32491; Q00772: SLT2; NbExp=5; IntAct=EBI-10973, EBI-17372;
CC -!- MISCELLANEOUS: Present with 1950 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; D13785; BAA02933.1; -; Genomic_DNA.
DR EMBL; U43703; AAB68220.1; -; Genomic_DNA.
DR EMBL; U10280; AAB40938.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11294.1; -; Genomic_DNA.
DR PIR; S69045; S69045.
DR RefSeq; NP_015185.1; NM_001183954.1.
DR AlphaFoldDB; P32491; -.
DR SMR; P32491; -.
DR BioGRID; 36042; 144.
DR DIP; DIP-1447N; -.
DR IntAct; P32491; 53.
DR MINT; P32491; -.
DR STRING; 4932.YPL140C; -.
DR iPTMnet; P32491; -.
DR MaxQB; P32491; -.
DR PaxDb; P32491; -.
DR PRIDE; P32491; -.
DR EnsemblFungi; YPL140C_mRNA; YPL140C; YPL140C.
DR GeneID; 855963; -.
DR KEGG; sce:YPL140C; -.
DR SGD; S000006061; MKK2.
DR VEuPathDB; FungiDB:YPL140C; -.
DR eggNOG; KOG0581; Eukaryota.
DR GeneTree; ENSGT00940000176752; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P32491; -.
DR OMA; MASMFRP; -.
DR BioCyc; YEAST:G3O-34038-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 PRO; PR:P32491; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32491; 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; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; ISS: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:0030242; P:autophagy of peroxisome; IGI:SGD.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IGI:SGD.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS: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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..506
FT /note="MAP kinase kinase MKK2/SSP33"
FT /id="PRO_0000086333"
FT DOMAIN 214..481
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 220..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 252
FT /note="P -> S (in Ref. 1; BAA02933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56758 MW; 8EACED6C742E148B CRC64;
MASMFRPPES NRSHQKTPKL TLPVNLVQNA KSTNDGQHLN RSPYSSVNES PYSNNSTSAT
STTSSMASNS TLLYNRSSTT TIKNRPVPPP LPPLVLTQKK DGIEYRVAGD SQLSERFSNL
HVDITYKELL SSAPISTKLS NIDTTFIKKD LDTPEGEDSY PSTLLSAYDF SSSGSNSAPL
SANNIISCSN LIQGKDVDQL EEEAWRFGHL KDEITTLGIL GEGAGGSVAK CRLKNGKKVF
ALKTINTMNT DPEYQKQIFR ELQFNKSFKS DYIVQYYGMF TDEQSSSIYI AMEYMGGKSL
EATYKNLLKR GGRISERVIG KIAESVLRGL SYLHERKVIH RDIKPQNILL NEKGEIKLCD
FGVSGEAVNS LAMTFTGTSF YMAPERIQGQ PYSVTCDVWS LGLTLLEVAG GRFPFESDKI
TQNVAPIELL TMILTFSPQL KDEPELDISW SKTFRSFIDY CLKKDARERP SPRQMLKHPW
IVGQMKKKVN MERFVKKCWE KEKDGI
