CSK21_MOUSE
ID CSK21_MOUSE Reviewed; 391 AA.
AC Q60737; Q8R0X4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II alpha;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P68400};
GN Name=Csnk2a1; Synonyms=Ckiia;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N; TISSUE=Spleen;
RX PubMed=7846532; DOI=10.1126/science.7846532;
RA Seldin D.C., Leder P.;
RT "Casein kinase II alpha transgene-induced murine lymphoma: relation to
RT theileriosis in cattle.";
RL Science 267:894-897(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=10806215; DOI=10.1074/jbc.m909107199;
RA Song D.H., Sussman D.J., Seldin D.C.;
RT "Endogenous protein kinase CK2 participates in Wnt signaling in mammary
RT epithelial cells.";
RL J. Biol. Chem. 275:23790-23797(2000).
RN [7]
RP FUNCTION IN APOPTOSIS.
RX PubMed=18467326; DOI=10.1074/jbc.m802846200;
RA McDonnell M.A., Abedin M.J., Melendez M., Platikanova T.N., Ecklund J.R.,
RA Ahmed K., Kelekar A.;
RT "Phosphorylation of murine caspase-9 by the protein kinase casein kinase 2
RT regulates its cleavage by caspase-8.";
RL J. Biol. Chem. 283:20149-20158(2008).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=17954558; DOI=10.1128/mcb.01119-07;
RA Lou D.Y., Dominguez I., Toselli P., Landesman-Bollag E., O'Brien C.,
RA Seldin D.C.;
RT "The alpha catalytic subunit of protein kinase CK2 is required for mouse
RT embryonic development.";
RL Mol. Cell. Biol. 28:131-139(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH SNAI1.
RX PubMed=19923321; DOI=10.1091/mbc.e09-06-0504;
RA MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
RA Martin-Perez J., Portillo F., Cano A.;
RT "Phosphorylation of serine 11 and serine 92 as new positive regulators of
RT human Snail1 function: potential involvement of casein kinase-2 and the
RT cAMP-activated kinase protein kinase A.";
RL Mol. Biol. Cell 21:244-253(2010).
CC -!- FUNCTION: Catalytic subunit of a constitutively active
CC serine/threonine-protein kinase complex that phosphorylates a large
CC number of substrates containing acidic residues C-terminal to the
CC phosphorylated serine or threonine (By similarity). Regulates numerous
CC cellular processes, such as cell cycle progression, apoptosis and
CC transcription, as well as viral infection (By similarity). May act as a
CC regulatory node which integrates and coordinates numerous signals
CC leading to an appropriate cellular response (By similarity). During
CC mitosis, functions as a component of the p53/TP53-dependent spindle
CC assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2
CC arrest in response to spindle damage (By similarity). Also required for
CC p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53
CC following UV irradiation (By similarity). Can also negatively regulate
CC apoptosis (PubMed:18467326). Phosphorylates the caspases CASP9 and
CC CASP2 and the apoptotic regulator NOL3 (PubMed:18467326).
CC Phosphorylation protects CASP9 from cleavage and activation by CASP8,
CC and inhibits the dimerization of CASP2 and activation of CASP8
CC (PubMed:18467326). Regulates transcription by direct phosphorylation of
CC RNA polymerases I, II, III and IV (By similarity). Also phosphorylates
CC and regulates numerous transcription factors including NF-kappa-B,
CC STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB
CC (By similarity). Phosphorylates Hsp90 and its co-chaperones FKBP4 and
CC CDC37, which is essential for chaperone function (By similarity).
CC Mediates sequential phosphorylation of FNIP1, promoting its gradual
CC interaction with Hsp90, leading to activate both kinase and non-kinase
CC client proteins of Hsp90 (By similarity). Regulates Wnt signaling by
CC phosphorylating CTNNB1 and the transcription factor LEF1
CC (PubMed:10806215). Acts as an ectokinase that phosphorylates several
CC extracellular proteins (By similarity). During viral infection,
CC phosphorylates various proteins involved in the viral life cycles of
CC EBV, HSV, HBV, HCV, HIV, CMV and HPV (By similarity). Phosphorylates
CC PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (By
CC similarity). Plays an important role in the circadian clock function by
CC phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its
CC interaction with CLOCK and which controls CLOCK nuclear entry (By
CC similarity). {ECO:0000250|UniProtKB:P19139,
CC ECO:0000250|UniProtKB:P68400, ECO:0000269|PubMed:10806215,
CC ECO:0000269|PubMed:18467326}.
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P68400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:P68400};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P68400};
CC -!- ACTIVITY REGULATION: Constitutively active protein kinase whose
CC activity is not directly affected by phosphorylation. Seems to be
CC regulated by level of expression and localization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain
CC and/or alpha' chain) and two regulatory subunits (beta chains). The
CC tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta
CC or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1
CC complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which
CC forms following UV irradiation (By similarity). Interacts with RNPS1
CC (By similarity). Interacts with SNAI1 (PubMed:19923321). Interacts with
CC PML and CCAR2 (By similarity). {ECO:0000250|UniProtKB:P68400,
CC ECO:0000269|PubMed:19923321}.
CC -!- INTERACTION:
CC Q60737; Q9WTL8: Arntl; NbExp=5; IntAct=EBI-771698, EBI-644534;
CC Q60737; P67871: Csnk2b; NbExp=5; IntAct=EBI-771698, EBI-348179;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P68400}.
CC -!- PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in
CC prophase and metaphase and dephosphorylated during anaphase.
CC Phosphorylation does not directly affect casein kinase 2 activity, but
CC may contribute to its regulation by forming binding sites for
CC interacting proteins and/or targeting it to different compartments (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at 10.5 dpc.
CC {ECO:0000269|PubMed:17954558}.
CC -!- MISCELLANEOUS: Can use both ATP and GTP as phosphoryl donors.
CC Phosphorylation by casein kinase 2 has been estimated to represent up
CC to one quarter of the eukaryotic phosphoproteome.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U17112; AAA64563.1; -; mRNA.
DR EMBL; AK146032; BAE26845.1; -; mRNA.
DR EMBL; AK158077; BAE34350.1; -; mRNA.
DR EMBL; AL831735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL05953.1; -; Genomic_DNA.
DR EMBL; BC026149; AAH26149.1; -; mRNA.
DR EMBL; BC060742; AAH60742.1; -; mRNA.
DR EMBL; BC089343; AAH89343.1; -; mRNA.
DR CCDS; CCDS16879.1; -.
DR PIR; I49141; I49141.
DR RefSeq; NP_031814.2; NM_007788.3.
DR RefSeq; XP_006498720.1; XM_006498657.3.
DR RefSeq; XP_011237574.1; XM_011239272.2.
DR AlphaFoldDB; Q60737; -.
DR SMR; Q60737; -.
DR BioGRID; 198942; 21.
DR CORUM; Q60737; -.
DR DIP; DIP-32409N; -.
DR IntAct; Q60737; 19.
DR MINT; Q60737; -.
DR STRING; 10090.ENSMUSP00000096829; -.
DR ChEMBL; CHEMBL3537; -.
DR iPTMnet; Q60737; -.
DR PhosphoSitePlus; Q60737; -.
DR EPD; Q60737; -.
DR jPOST; Q60737; -.
DR MaxQB; Q60737; -.
DR PaxDb; Q60737; -.
DR PeptideAtlas; Q60737; -.
DR PRIDE; Q60737; -.
DR ProteomicsDB; 279286; -.
DR TopDownProteomics; Q60737; -.
DR DNASU; 12995; -.
DR Ensembl; ENSMUST00000099224; ENSMUSP00000096829; ENSMUSG00000074698.
DR GeneID; 12995; -.
DR KEGG; mmu:12995; -.
DR UCSC; uc008nfa.2; mouse.
DR CTD; 1457; -.
DR MGI; MGI:88543; Csnk2a1.
DR VEuPathDB; HostDB:ENSMUSG00000074698; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; Q60737; -.
DR OMA; ACEKRPQ; -.
DR OrthoDB; 1098380at2759; -.
DR PhylomeDB; Q60737; -.
DR TreeFam; TF300483; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-201688; WNT mediated activation of DVL.
DR Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR BioGRID-ORCS; 12995; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Csnk2a1; mouse.
DR PRO; PR:Q60737; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60737; protein.
DR Bgee; ENSMUSG00000074698; Expressed in undifferentiated genital tubercle and 273 other tissues.
DR ExpressionAtlas; Q60737; baseline and differential.
DR Genevisible; Q60737; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016581; C:NuRD complex; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005956; C:protein kinase CK2 complex; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:1905818; P:regulation of chromosome separation; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
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; PTHR24054; PTHR24054; 1.
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 Apoptosis; ATP-binding; Biological rhythms; Cell cycle; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..391
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085884"
FT DOMAIN 39..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..41
FT /note="Interaction with beta subunit"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 344
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P68400"
FT MOD_RES 360
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P68400"
FT MOD_RES 362
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P68400"
FT MOD_RES 370
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P68400"
FT CONFLICT 315
FT /note="A -> V (in Ref. 1; AAA64563)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="Y -> F (in Ref. 1; AAA64563)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="D -> N (in Ref. 1; AAA64563)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="T -> S (in Ref. 1; AAA64563)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="P -> Q (in Ref. 1; AAA64563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 45134 MW; C7A5F7CC8099230D CRC64;
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMSSTSMA GGSTPVSSAN MMSGISSVPT
PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q
