ID   YAK1_YEAST              Reviewed;         807 AA.
AC   P14680; D6VW43;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   02-SEP-2026, entry version 218.
DE   RecName: Full=Dual specificity protein kinase YAK1;
DE            EC=2.7.12.1;
GN   Name=YAK1; OrderedLocusNames=YJL141C; ORFNames=J0652;
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=2558053; DOI=10.1101/gad.3.9.1336;
RA   Garrett S., Broach J.;
RT   "Loss of Ras activity in Saccharomyces cerevisiae is suppressed by
RT   disruptions of a new kinase gene, YAKI, whose product may act downstream of
RT   the cAMP-dependent protein kinase.";
RL   Genes Dev. 3:1336-1348(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8813765;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8%3c787::aid-yea954%3e3.0.co;2-4;
RA   Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT   "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT   chromosome X reveals 14 known genes and 13 new open reading frames
RT   including homologues of genes clustered on the right arm of chromosome
RT   XI.";
RL   Yeast 12:787-797(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   FUNCTION.
RX   PubMed=11358866; DOI=10.1101/gad.884001;
RA   Moriya H., Shimizu-Yoshida Y., Omori A., Iwashita S., Katoh M., Sakai A.;
RT   "Yak1p, a DYRK family kinase, translocates to the nucleus and
RT   phosphorylates yeast Pop2p in response to a glucose signal.";
RL   Genes Dev. 15:1217-1228(2001).
RN   [6]
RP   PHOSPHORYLATION AT TYR-530.
RX   PubMed=10816418; DOI=10.1042/bj3480263;
RA   Kassis S., Melhuish T., Annan R.S., Chen S.L., Lee J.C., Livi G.P.,
RA   Creasy C.L.;
RT   "Saccharomyces cerevisiae Yak1p protein kinase autophosphorylates on
RT   tyrosine residues and phosphorylates myelin basic protein on a C-terminal
RT   serine residue.";
RL   Biochem. J. 348:263-272(2000).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND TYR-530, AND
RP   IDENTIFICATION BY 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND THR-288, AND
RP   IDENTIFICATION BY 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-118; SER-127;
RP   SER-206; SER-240; SER-245; SER-247; THR-288 AND TYR-530, AND IDENTIFICATION
RP   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: Negative regulator of the cell cycle acting downstream of the
CC       cAMP-dependent protein kinase. Part of a glucose-sensing system
CC       involved in growth control in response to glucose availability.
CC       Phosphorylates POP2. {ECO:0000269|PubMed:11358866}.
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=2.7.12.1;
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=2.7.12.1;
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=2.7.12.1;
CC   -!- INTERACTION:
CC       P14680; Q08273: HRT1; NbExp=3; IntAct=EBI-20777, EBI-31686;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between both
CC       compartments in response to glucose.
CC   -!- PTM: Phosphorylated; highly. {ECO:0000269|PubMed:10816418}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR   EMBL; X16056; CAA34192.1; -; Genomic_DNA.
DR   EMBL; X87371; CAA60814.1; -; Genomic_DNA.
DR   EMBL; Z49417; CAA89437.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08659.1; -; Genomic_DNA.
DR   PIR; A32582; A32582.
DR   RefSeq; NP_012394.1; NM_001181574.1.
DR   AlphaFoldDB; P14680; -.
DR   SMR; P14680; -.
DR   BioGRID; 33616; 191.
DR   DIP; DIP-1374N; -.
DR   ELM; P14680; -.
DR   FunCoup; P14680; 535.
DR   IntAct; P14680; 49.
DR   MINT; P14680; -.
DR   STRING; 4932.YJL141C; -.
DR   GlyGen; P14680; 7 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P14680; -.
DR   PaxDb; 4932-YJL141C; -.
DR   PeptideAtlas; P14680; -.
DR   EnsemblFungi; YJL141C_mRNA; YJL141C; YJL141C.
DR   GeneID; 853300; -.
DR   KEGG; sce:YJL141C; -.
DR   AGR; SGD:S000003677; -.
DR   SGD; S000003677; YAK1.
DR   VEuPathDB; FungiDB:YJL141C; -.
DR   eggNOG; KOG0667; Eukaryota.
DR   HOGENOM; CLU_000288_88_4_1; -.
DR   InParanoid; P14680; -.
DR   OMA; TRTVYTY; -.
DR   OrthoDB; 9332038at2759; -.
DR   BioCyc; YEAST:G3O-31586-MONOMER; -.
DR   BRENDA; 2.7.12.1; 984.
DR   Reactome; R-SCE-3899300; SUMOylation of transcription cofactors.
DR   BioGRID-ORCS; 853300; 8 hits in 13 CRISPR screens.
DR   PRO; PR:P14680; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P14680; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:SGD.
DR   GO; GO:0141156; P:cAMP/PKA signal transduction; IGI:SGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CACAO.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:CACAO.
DR   CDD; cd14212; PKc_YAK1; 1.
DR   FunFam; 3.30.200.20:FF:000087; Dual specificity tyrosine-phosphorylation-regulated kinase 1A; 1.
DR   FunFam; 1.10.510.10:FF:000380; Serine/threonine-protein kinase ppk15; 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   InterPro; IPR050494; Ser_Thr_dual-spec_kinase.
DR   PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR   PANTHER; PTHR24058:SF17; HOMEODOMAIN INTERACTING PROTEIN KINASE, ISOFORM D; 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; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..807
FT                   /note="Dual specificity protein kinase YAK1"
FT                   /id="PRO_0000086828"
FT   DOMAIN          369..704
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..84
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..180
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..224
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        496
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         375..383
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         398
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         288
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         530
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10816418,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   807 AA;  91245 MW;  E0B7C56FAA35E056 CRC64;
     MNSSNNNDSS SSNSNMNNSL SPTLVTHSDA SMGSGRASPD NSHMGRGIWN PSYVNQGSQR
     SPQQQHQNHH QQQQQQQQQQ QQNSQFCFVN PWNEEKVTNS QQNLVYPPQY DDLNSNESLD
     AYRRRKSSLV VPPARAPAPN PFQYDSYPAY TSSNTSLAGN SSGQYPSGYQ QQQQQVYQQG
     AIHPSQFGSR FVPSLYDRQD FQRRQSLAAT NYSSNFSSLN SNTNQGTNSI PVMSPYRRLS
     AYPPSTSPPL QPPFKQLRRD EVQGQKLSIP QMQLCNSKND LQPVLNATPK FRRASLNSKT
     ISPLVSVTKS LITTYSLCSP EFTYQTSKNP KRVLTKPSEG KCNNGFDNIN SDYILYVNDV
     LGVEQNRKYL VLDILGQGTF GQVVKCQNLL TKEILAVKVV KSRTEYLTQS ITEAKILELL
     NQKIDPTNKH HFLRMYDSFV HKNHLCLVFE LLSNNLYELL KQNKFHGLSI QLIRTFTTQI
     LDSLCVLKES KLIHCDLKPE NILLCAPDKP ELKIIDFGSS CEEARTVYTY IQSRFYRAPE
     IILGIPYSTS IDMWSLGCIV AELFLGIPIF PGASEYNQLT RIIDTLGYPP SWMIDMGKNS
     GKFMKKLAPE ESSSSTQKHR MKTIEEFCRE YNIVEKPSKQ YFKWRKLPDI IRNYRYPKSI
     QNSQELIDQE MQNRECLIHF LGGVLNLNPL ERWTPQQAML HPFITKQEFT GEWFPPGSSL
     PGPSEKHDDA KGQQSEYGSA NDSSNNAGHN YVYNPSSATG GADSVDIGAI SKRKENTSGD
     ISNNFAVTHS VQEGPTSAFN KLHIVEE
//