YAK1_YEAST
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 03-AUG-2022, entry version 200.
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<787::aid-yea954>3.0.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=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=2.7.12.1;
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=2.7.12.1;
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=2.7.12.1;
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; 181.
DR DIP; DIP-1374N; -.
DR ELM; P14680; -.
DR IntAct; P14680; 48.
DR MINT; P14680; -.
DR STRING; 4932.YJL141C; -.
DR iPTMnet; P14680; -.
DR MaxQB; P14680; -.
DR PaxDb; P14680; -.
DR PRIDE; P14680; -.
DR EnsemblFungi; YJL141C_mRNA; YJL141C; YJL141C.
DR GeneID; 853300; -.
DR KEGG; sce:YJL141C; -.
DR SGD; S000003677; YAK1.
DR VEuPathDB; FungiDB:YJL141C; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000164472; -.
DR HOGENOM; CLU_000288_88_4_1; -.
DR InParanoid; P14680; -.
DR OMA; TRTVYTY; -.
DR BioCyc; YEAST:G3O-31586-MON; -.
DR BRENDA; 2.7.12.1; 984.
DR Reactome; R-SCE-3899300; SUMOylation of transcription cofactors.
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:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CACAO.
DR GO; GO:0032106; P:positive regulation of response to extracellular stimulus; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IMP:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0010737; P:protein kinase A signaling; IGI: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; 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..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..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
