ID   CDK1_YEAST              Reviewed;         298 AA.
AC   P00546; D6VQF5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 238.
DE   RecName: Full=Cyclin-dependent kinase 1 {ECO:0000303|PubMed:14574415};
DE            Short=CDK1 {ECO:0000303|PubMed:14574415};
DE            EC=2.7.11.22 {ECO:0000250|UniProtKB:P04551};
DE   AltName: Full=Cell division control protein 28;
DE   AltName: Full=Cell division protein kinase 1;
GN   Name=CDC28 {ECO:0000303|PubMed:6361575}; Synonyms=CDK1, HSL5, SRM5;
GN   OrderedLocusNames=YBR160W {ECO:0000312|SGD:S000000364};
GN   ORFNames=YBR1211;
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=6361575; DOI=10.1038/307183a0;
RA   Lorincz A.T., Reed S.I.;
RT   "Primary structure homology between the product of yeast cell division
RT   control gene CDC28 and vertebrate oncogenes.";
RL   Nature 307:183-185(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7597849; DOI=10.1002/yea.320110508;
RA   Baur S., Becker J., Li Z., Niegemann E., Wehner E., Wolter R., Brendel M.;
RT   "Sequence analysis of a 5.6 kb fragment of chromosome II from Saccharomyces
RT   cerevisiae reveals two new open reading frames next to CDC28.";
RL   Yeast 11:455-458(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   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   [6]
RP   FUNCTION, AND INTERACTION WITH CKS1.
RX   PubMed=2664468; DOI=10.1128/mcb.9.5.2034-2041.1989;
RA   Hadwiger J.A., Wittenberg C., Mendenhall M.D., Reed S.I.;
RT   "The Saccharomyces cerevisiae CKS1 gene, a homolog of the
RT   Schizosaccharomyces pombe suc1+ gene, encodes a subunit of the Cdc28
RT   protein kinase complex.";
RL   Mol. Cell. Biol. 9:2034-2041(1989).
RN   [7]
RP   FUNCTION.
RX   PubMed=14574415; DOI=10.1038/nature02062;
RA   Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA   Shokat K.M., Morgan D.O.;
RT   "Targets of the cyclin-dependent kinase Cdk1.";
RL   Nature 425:859-864(2003).
RN   [8]
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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19 AND THR-169, AND
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).
RN   [11]
RP   FUNCTION.
RX   PubMed=22156209; DOI=10.1101/gad.173427.111;
RA   Kurat C.F., Lambert J.P., van Dyk D., Tsui K., van Bakel H.,
RA   Kaluarachchi S., Friesen H., Kainth P., Nislow C., Figeys D.,
RA   Fillingham J., Andrews B.J.;
RT   "Restriction of histone gene transcription to S phase by phosphorylation of
RT   a chromatin boundary protein.";
RL   Genes Dev. 25:2489-2501(2011).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Cyclin-dependent kinase that acts as a master regulator of
CC       the mitotic and meiotic cell cycles (By similarity). Required to drive
CC       the G1-S transition (PubMed:2664468). More than 200 substrates have
CC       been identified (PubMed:14574415). Substrate specificity is in part
CC       regulated by the bound cyclin protein (By similarity). Phosphorylates
CC       YTA7 during S-phase to promote transcription of histones
CC       (PubMed:22156209). {ECO:0000250|UniProtKB:P04551,
CC       ECO:0000269|PubMed:14574415, ECO:0000269|PubMed:22156209,
CC       ECO:0000269|PubMed:2664468}.
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=2.7.11.22;
CC         Evidence={ECO:0000250|UniProtKB:P24941};
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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P04551};
CC   -!- ACTIVITY REGULATION: Phosphorylation at Thr-18 or Tyr-19 inactivates
CC       the enzyme, while phosphorylation at Thr-169 activates it.
CC       {ECO:0000250|UniProtKB:P06493}.
CC   -!- SUBUNIT: Forms a stable but non-covalent complex with the CKS1 protein
CC       and with a cyclin. {ECO:0000269|PubMed:2664468}.
CC   -!- INTERACTION:
CC       P00546; P43568: CAK1; NbExp=3; IntAct=EBI-4253, EBI-3953;
CC       P00546; P09119: CDC6; NbExp=2; IntAct=EBI-4253, EBI-4447;
CC       P00546; P20486: CKS1; NbExp=9; IntAct=EBI-4253, EBI-4746;
CC       P00546; P30283: CLB5; NbExp=5; IntAct=EBI-4253, EBI-4538;
CC       P00546; P32943: CLB6; NbExp=3; IntAct=EBI-4253, EBI-2049771;
CC       P00546; P20437: CLN1; NbExp=7; IntAct=EBI-4253, EBI-4479;
CC       P00546; P20438: CLN2; NbExp=10; IntAct=EBI-4253, EBI-4483;
CC       P00546; P13365: CLN3; NbExp=6; IntAct=EBI-4253, EBI-4490;
CC       P00546; P03070; Xeno; NbExp=3; IntAct=EBI-4253, EBI-617698;
CC   -!- MISCELLANEOUS: Present with 6670 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. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; X00257; CAA25065.1; -; Genomic_DNA.
DR   EMBL; Z36029; CAA85119.1; -; Genomic_DNA.
DR   EMBL; X80224; CAA56509.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07275.1; -; Genomic_DNA.
DR   PIR; A00657; TVBY8.
DR   RefSeq; NP_009718.3; NM_001178508.3.
DR   AlphaFoldDB; P00546; -.
DR   SMR; P00546; -.
DR   BioGRID; 32859; 1574.
DR   ComplexPortal; CPX-1699; CLN1-CDC28 kinase complex.
DR   ComplexPortal; CPX-1700; CLN3-CDC28 kinase complex.
DR   ComplexPortal; CPX-1701; CLB2-CDC28 kinase complex.
DR   ComplexPortal; CPX-1702; CLB5-CDC28 kinase complex.
DR   ComplexPortal; CPX-335; CLB1-CDC28 kinase complex.
DR   ComplexPortal; CPX-336; CLB3-CDC28 kinase complex.
DR   ComplexPortal; CPX-337; CLB4-CDC28 kinase complex.
DR   ComplexPortal; CPX-339; CLB6-CDC28 kinase complex.
DR   ComplexPortal; CPX-342; CLN2-CDC28 kinase complex.
DR   DIP; DIP-1039N; -.
DR   IntAct; P00546; 87.
DR   MINT; P00546; -.
DR   STRING; 4932.YBR160W; -.
DR   BindingDB; P00546; -.
DR   ChEMBL; CHEMBL5213; -.
DR   MoonDB; P00546; Predicted.
DR   iPTMnet; P00546; -.
DR   MaxQB; P00546; -.
DR   PaxDb; 4932-YBR160W; -.
DR   PeptideAtlas; P00546; -.
DR   EnsemblFungi; YBR160W_mRNA; YBR160W; YBR160W.
DR   GeneID; 852457; -.
DR   KEGG; sce:YBR160W; -.
DR   AGR; SGD:S000000364; -.
DR   SGD; S000000364; CDC28.
DR   VEuPathDB; FungiDB:YBR160W; -.
DR   eggNOG; KOG0594; Eukaryota.
DR   GeneTree; ENSGT00940000153335; -.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; P00546; -.
DR   OMA; YLYQITR; -.
DR   OrthoDB; 244018at2759; -.
DR   BioCyc; YEAST:G3O-29110-MONOMER; -.
DR   BRENDA; 2.7.11.22; 984.
DR   Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR   BioGRID-ORCS; 852457; 1 hit in 13 CRISPR screens.
DR   PRO; PR:P00546; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P00546; Protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR   GO; GO:0042393; F:histone binding; IDA: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:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IDA:SGD.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IMP:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:DNA damage response; IDA:ComplexPortal.
DR   GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:ComplexPortal.
DR   GO; GO:0000706; P:meiotic DNA double-strand break processing; IGI:SGD.
DR   GO; GO:1990758; P:mitotic sister chromatid biorientation; IGI:SGD.
DR   GO; GO:0090307; P:mitotic spindle assembly; IGI:SGD.
DR   GO; GO:1902596; P:negative regulation of DNA replication origin binding; IGI:SGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:SGD.
DR   GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IMP:SGD.
DR   GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:SGD.
DR   GO; GO:1903500; P:negative regulation of mitotic actomyosin contractile ring assembly; IMP:SGD.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:SGD.
DR   GO; GO:0045875; P:negative regulation of sister chromatid cohesion; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:SGD.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:SGD.
DR   GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:SGD.
DR   GO; GO:0051446; P:positive regulation of meiotic cell cycle; IDA:SGD.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:SGD.
DR   GO; GO:1904291; P:positive regulation of mitotic DNA damage checkpoint; IMP:SGD.
DR   GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IMP:SGD.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:1901319; P:positive regulation of trehalose catabolic process; IMP:SGD.
DR   GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IMP:SGD.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR   GO; GO:1990139; P:protein localization to nuclear periphery; IMP:SGD.
DR   GO; GO:0034504; P:protein localization to nucleus; IMP:SGD.
DR   GO; GO:1902889; P:protein localization to spindle microtubule; IMP:SGD.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:CACAO.
DR   GO; GO:0010568; P:regulation of budding cell apical bud growth; IMP:SGD.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; NAS:ComplexPortal.
DR   GO; GO:1902275; P:regulation of chromatin organization; IPI:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:ComplexPortal.
DR   GO; GO:0010570; P:regulation of filamentous growth; IMP:SGD.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR   GO; GO:1905634; P:regulation of protein localization to chromatin; IDA:SGD.
DR   GO; GO:0090169; P:regulation of spindle assembly; IMP:SGD.
DR   GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IGI:SGD.
DR   GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007130; P:synaptonemal complex assembly; IMP:SGD.
DR   CDD; cd07835; STKc_CDK1_CdkB_like; 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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF254; CYCLIN-DEPENDENT KINASE 2; 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   Acetylation; ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..298
FT                   /note="Cyclin-dependent kinase 1"
FT                   /id="PRO_0000085722"
FT   DOMAIN          8..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         14..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         19
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         169
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   298 AA;  34061 MW;  57A7A2B97A90DC6C CRC64;
     MSGELANYKR LEKVGEGTYG VVYKALDLRP GQGQRVVALK KIRLESEDEG VPSTAIREIS
     LLKELKDDNI VRLYDIVHSD AHKLYLVFEF LDLDLKRYME GIPKDQPLGA DIVKKFMMQL
     CKGIAYCHSH RILHRDLKPQ NLLINKDGNL KLGDFGLARA FGVPLRAYTH EIVTLWYRAP
     EVLLGGKQYS TGVDTWSIGC IFAEMCNRKP IFSGDSEIDQ IFKIFRVLGT PNEAIWPDIV
     YLPDFKPSFP QWRRKDLSQV VPSLDPRGID LLDKLLAYDP INRISARRAA IHPYFQES
//