ID CDK1_CANAL Reviewed; 317 AA.
AC P43063; A0A1D8PT63; Q59V96;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Cyclin-dependent kinase 1 {ECO:0000250|UniProtKB:P00546};
DE Short=CDK1 {ECO:0000250|UniProtKB:P00546};
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 2;
GN Name=CDC28 {ECO:0000303|PubMed:7830719}; Synonyms=CDK1;
GN OrderedLocusNames=CAALFM_CR06050WA; ORFNames=CaO19.11337, CaO19.3856;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=SGY126;
RX PubMed=7830719; DOI=10.1007/bf00297278;
RA Sherlock G., Bahman A.M., Mahal A., Shieh J.C., Ferreira M., Rosamond J.;
RT "Molecular cloning and analysis of CDC28 and cyclin homologues from the
RT human fungal pathogen Candida albicans.";
RL Mol. Gen. Genet. 245:716-723(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8654974; DOI=10.1016/0378-1119(95)00893-4;
RA Damagnez V., Cottarel G.;
RT "Candida albicans CDK1 and CYB1: cDNA homologues of the cdc2/CDC28 and
RT cdc13/CLB1/CLB2 cell cycle control genes.";
RL Gene 172:137-141(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-18.
RX PubMed=11809828; DOI=10.1091/mbc.01-03-0116;
RA Hazan I., Sepulveda-Becerra M., Liu H.;
RT "Hyphal elongation is regulated independently of cell cycle in Candida
RT albicans.";
RL Mol. Biol. Cell 13:134-145(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH HGC1.
RX PubMed=15071502; DOI=10.1038/sj.emboj.7600195;
RA Zheng X., Wang Y., Wang Y.;
RT "Hgc1, a novel hypha-specific G1 cyclin-related protein regulates Candida
RT albicans hyphal morphogenesis.";
RL EMBO J. 23:1845-1856(2004).
RN [8]
RP PHOSPHORYLATION AT TYR-18 BY SWE1, AND FUNCTION.
RX PubMed=15659158; DOI=10.1111/j.1365-2958.2004.04405.x;
RA Umeyama T., Kaneko A., Nagai Y., Hanaoka N., Tanabe K., Takano Y.,
RA Niimi M., Uehara Y.;
RT "Candida albicans protein kinase CaHsl1p regulates cell elongation and
RT virulence.";
RL Mol. Microbiol. 55:381-395(2005).
RN [9]
RP FUNCTION.
RX PubMed=16710830; DOI=10.1002/yea.1373;
RA Umeyama T., Kaneko A., Niimi M., Uehara Y.;
RT "Repression of CDC28 reduces the expression of the morphology-related
RT transcription factors, Efg1p, Nrg1p, Rbf1p, Rim101p, Fkh2p and Tec1p and
RT induces cell elongation in Candida albicans.";
RL Yeast 23:537-552(2006).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF RGA2.
RX PubMed=17673907; DOI=10.1038/sj.emboj.7601814;
RA Zheng X.D., Lee R.T., Wang Y.M., Lin Q.S., Wang Y.;
RT "Phosphorylation of Rga2, a Cdc42 GAP, by CDK/Hgc1 is crucial for Candida
RT albicans hyphal growth.";
RL EMBO J. 26:3760-3769(2007).
RN [11]
RP INTERACTION WITH HGC1; CCN1 AND CDC11, AND FUNCTION IN PHOSPHORYLATION OF
RP CDC11.
RX PubMed=17765684; DOI=10.1016/j.devcel.2007.06.011;
RA Sinha I., Wang Y.M., Philp R., Li C.R., Yap W.H., Wang Y.;
RT "Cyclin-dependent kinases control septin phosphorylation in Candida
RT albicans hyphal development.";
RL Dev. Cell 13:421-432(2007).
RN [12]
RP INDUCTION.
RX PubMed=17555439; DOI=10.1111/j.1365-2958.2007.05760.x;
RA Uppuluri P., Chaffin W.L.;
RT "Defining Candida albicans stationary phase by cellular and DNA
RT replication, gene expression and regulation.";
RL Mol. Microbiol. 64:1572-1586(2007).
RN [13]
RP INTERACTION WITH CLB2 AND IQG1, AND FUNCTION IN PHOSPHORYLATION OF IQG1.
RX PubMed=18923418; DOI=10.1038/emboj.2008.219;
RA Li C.R., Wang Y.M., Wang Y.;
RT "The IQGAP Iqg1 is a regulatory target of CDK for cytokinesis in Candida
RT albicans.";
RL EMBO J. 27:2998-3010(2008).
RN [14]
RP FUNCTION IN PHOSPHORYLATION OF EFG1.
RX PubMed=19528234; DOI=10.1128/mcb.01502-08;
RA Wang A., Raniga P.P., Lane S., Lu Y., Liu H.;
RT "Hyphal chain formation in Candida albicans: Cdc28-Hgc1 phosphorylation of
RT Efg1 represses cell separation genes.";
RL Mol. Cell. Biol. 29:4406-4416(2009).
RN [15]
RP INDUCTION.
RX PubMed=20064588; DOI=10.1016/j.bbagen.2010.01.001;
RA Wu X.Z., Chang W.Q., Cheng A.X., Sun L.M., Lou H.X.;
RT "Plagiochin E, an antifungal active macrocyclic bis(bibenzyl), induced
RT apoptosis in Candida albicans through a metacaspase-dependent apoptotic
RT pathway.";
RL Biochim. Biophys. Acta 1800:439-447(2010).
RN [16]
RP FUNCTION IN PHOSPHORYLATION OF SEC2.
RX PubMed=20639857; DOI=10.1038/emboj.2010.158;
RA Bishop A., Lane R., Beniston R., Chapa-y-Lazo B., Smythe C., Sudbery P.;
RT "Hyphal growth in Candida albicans requires the phosphorylation of Sec2 by
RT the Cdc28-Ccn1/Hgc1 kinase.";
RL EMBO J. 29:2930-2942(2010).
RN [17]
RP FUNCTION IN PHOSPHORYLATION OF MOB2.
RX PubMed=21593210; DOI=10.1091/mbc.e11-03-0205;
RA Gutierrez-Escribano P., Gonzalez-Novo A., Suarez M.B., Li C.R., Wang Y.,
RA de Aldana C.R., Correa-Bordes J.;
RT "CDK-dependent phosphorylation of Mob2 is essential for hyphal development
RT in Candida albicans.";
RL Mol. Biol. Cell 22:2458-2469(2011).
RN [18]
RP FUNCTION IN PHOSPHORYLATION OF GIN4.
RX PubMed=22366454; DOI=10.1242/jcs.104497;
RA Li C.R., Yong J.Y., Wang Y.M., Wang Y.;
RT "CDK regulates septin organization through cell-cycle-dependent
RT phosphorylation of the Nim1-related kinase Gin4.";
RL J. Cell Sci. 125:2533-2543(2012).
RN [19]
RP FUNCTION, AND INTERACTION WITH HSP90.
RX PubMed=22090345; DOI=10.1091/mbc.e11-08-0729;
RA Senn H., Shapiro R.S., Cowen L.E.;
RT "Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell
RT cycle progression in Candida albicans.";
RL Mol. Biol. Cell 23:268-283(2012).
RN [20]
RP INTERACTION WITH CLN3, AND FUNCTION IN PHOSPHORYLATION OF SLA1.
RX PubMed=22787279; DOI=10.1091/mbc.e12-03-0231;
RA Zeng G., Wang Y.M., Wang Y.;
RT "Cdc28-Cln3 phosphorylation of Sla1 regulates actin patch dynamics in
RT different modes of fungal growth.";
RL Mol. Biol. Cell 23:3485-3497(2012).
RN [21]
RP INTERACTION WITH RFA2, AND FUNCTION IN PHOSPHORYLATION OF RFA2.
RX PubMed=23140133; DOI=10.1042/bj20120952;
RA Wang H., Gao J., Wong A.H., Hu K., Li W., Wang Y., Sang J.;
RT "Rfa2 is specifically dephosphorylated by Pph3 in Candida albicans.";
RL Biochem. J. 449:673-681(2013).
CC -!- FUNCTION: Cyclin-dependent kinase that acts as a master regulator of
CC the mitotic and meiotic cell cycles (By similarity). May drive the G1-S
CC transition (PubMed:7830719). Plays a role in mitotic exit
CC (PubMed:22090345). Plays a role in the expression of morphology-related
CC transcription factors, and especially hyphae-specific genes
CC (PubMed:16710830, PubMed:11809828, PubMed:15659158). Binds distinct
CC cyclin subunits as cells progress through the division cycle or
CC flamentous growth (PubMed:15071502, PubMed:17765684, PubMed:18923418,
CC PubMed:22787279). The CDC28-CLB2 complex regulates cytokinesis partly
CC by phosphorylating the actomyosin ring component IQG1
CC (PubMed:18923418). The CDC28-CLN3 complex phosphorylates SLA1 which
CC regulates cortical actin patch dynamics (PubMed:22787279). The CDC28-
CC CCN1 complex phosphorylates CDC11 and SEC2 upon induction of
CC filamentous growth (PubMed:17765684). The CDC28-HGC1 complex also
CC phosphorylates SEC2 and maintains CDC11 phosphorylation throughout
CC hyphal growth (PubMed:20639857). Moreover, the CDC28-HGC1 complex
CC phosphorylates and prevents RGA2 from localizing to hyphal tips,
CC leading to localized CDC42 activation for hyphal extension
CC (PubMed:17673907). CDC28-HGC1 phosphorylation of EFG1 represses cell
CC separation genes during hyphal growth (PubMed:19528234). Additional
CC substrates for CDC28 are RFA2 in G1-phase; MOB2, which is required for
CC the maintenance of polarisome components and for inhibition of cell
CC separation in hyphae; and GIN4 to regulate its association to SEP7 and
CC subsequent septin ring assembly (PubMed:23140133, PubMed:22366454,
CC PubMed:21593210). {ECO:0000250|UniProtKB:P04551,
CC ECO:0000269|PubMed:11809828, ECO:0000269|PubMed:15071502,
CC ECO:0000269|PubMed:15659158, ECO:0000269|PubMed:16710830,
CC ECO:0000269|PubMed:17673907, ECO:0000269|PubMed:17765684,
CC ECO:0000269|PubMed:18923418, ECO:0000269|PubMed:19528234,
CC ECO:0000269|PubMed:20639857, ECO:0000269|PubMed:21593210,
CC ECO:0000269|PubMed:22090345, ECO:0000269|PubMed:22366454,
CC ECO:0000269|PubMed:22787279, ECO:0000269|PubMed:23140133,
CC ECO:0000269|PubMed:7830719}.
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-17 or Tyr-18 inactivates
CC the enzyme, while phosphorylation at Thr-166 activates it.
CC {ECO:0000250|UniProtKB:P06493}.
CC -!- SUBUNIT: Forms several complexes with cyclins CCN1, CLB2, CLN3, and
CC HGC1. The CDC28-CCN1 complex associates with septin CDC11 upon hyphal
CC induction. Interacts with IQG1, RFA2, and HSP90.
CC {ECO:0000269|PubMed:15071502, ECO:0000269|PubMed:17765684,
CC ECO:0000269|PubMed:18923418, ECO:0000269|PubMed:22090345,
CC ECO:0000269|PubMed:22787279, ECO:0000269|PubMed:23140133}.
CC -!- INDUCTION: Expression is increased during exponential growth and
CC repressed by the antifungal drug plagiochin E (PLE).
CC {ECO:0000269|PubMed:17555439, ECO:0000269|PubMed:20064588}.
CC -!- PTM: Phosphorylated at Tyr-18 by SWE1 in a cell cycle-dependent manner.
CC Yeast-form and hyphal cells display similar dynamics of phosphorylation
CC and dephosphorylation of Tyr-18. Tyr-18 phosphorylation leads to
CC inhibition of CDC28 kinase activity. {ECO:0000269|PubMed:11809828,
CC ECO:0000269|PubMed:15659158}.
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; X80034; CAA56338.1; -; Genomic_DNA.
DR EMBL; U40405; AAC49450.1; -; mRNA.
DR EMBL; CP017630; AOW31316.1; -; Genomic_DNA.
DR PIR; JC4827; JC4827.
DR RefSeq; XP_713486.1; XM_708393.1.
DR AlphaFoldDB; P43063; -.
DR SMR; P43063; -.
DR BioGRID; 1227914; 19.
DR DIP; DIP-497N; -.
DR IntAct; P43063; 3.
DR MINT; P43063; -.
DR STRING; 237561.P43063; -.
DR iPTMnet; P43063; -.
DR EnsemblFungi; CR_06050W_A-T; CR_06050W_A-T-p1; CR_06050W_A.
DR GeneID; 3644838; -.
DR KEGG; cal:CAALFM_CR06050WA; -.
DR CGD; CAL0000191263; CDC28.
DR VEuPathDB; FungiDB:CR_06050W_A; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P43063; -.
DR OMA; YLYQITR; -.
DR OrthoDB; 244018at2759; -.
DR BRENDA; 2.7.11.22; 1096.
DR PRO; PR:P43063; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:CGD.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0004672; F:protein kinase activity; IMP:CGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IEA:EnsemblFungi.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:CGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IEA:EnsemblFungi.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR GO; GO:0060258; P:negative regulation of filamentous growth; IMP:CGD.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:1903500; P:negative regulation of mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0045875; P:negative regulation of sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0045819; P:positive regulation of glycogen catabolic process; IEA:EnsemblFungi.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:1904291; P:positive regulation of mitotic DNA damage checkpoint; IEA:EnsemblFungi.
DR GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IEA:EnsemblFungi.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:1901319; P:positive regulation of trehalose catabolic process; IEA:EnsemblFungi.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0030163; P:protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:1990139; P:protein localization to nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:1902889; P:protein localization to spindle microtubule; IEA:EnsemblFungi.
DR GO; GO:0010568; P:regulation of budding cell apical bud growth; IEA:EnsemblFungi.
DR GO; GO:0051726; P:regulation of cell cycle; IGI:CGD.
DR GO; GO:1902275; P:regulation of chromatin organization; IEA:EnsemblFungi.
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:1905634; P:regulation of protein localization to chromatin; IEA:EnsemblFungi.
DR GO; GO:0090169; P:regulation of spindle assembly; IEA:EnsemblFungi.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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 ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..317
FT /note="Cyclin-dependent kinase 1"
FT /id="PRO_0000085721"
FT DOMAIN 7..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Phosphotyrosine; by SWE1"
FT /evidence="ECO:0000269|PubMed:11809828,
FT ECO:0000269|PubMed:15659158"
FT MOD_RES 166
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 36647 MW; 2B91EABE5E5C028B CRC64;
MVELSDYQRQ EKVGEGTYGV VYKALDTKHN NRVVALKKIR LESEDEGVPS TAIREISLLK
EMKDDNIVRL YDIIHSDSHK LYLVFEFLDL DLKKYMESIP QGVGLGANMI KRFMNQLIRG
IKHCHSHRVL HRDLKPQNLL IDKEGNLKLA DFGLARAFGV PLRAYTHEVV TLWYRAPEIL
LGGKQYSTGV DMWSVGCIFA EMCNRKPLFP GDSEIDEIFR IFRILGTPNE EIWPDVNYLP
DFKSSFPQWK KKPLSEAVPS LDANGIDLLD QMLVYDPSRR ISAKRALIHP YFNDNDDRDH
NNYNEDNIGI DKHQNMQ
//
