CKB11_ARATH
ID CKB11_ARATH Reviewed; 309 AA.
AC P25859; Q147L4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cyclin-dependent kinase B1-1;
DE Short=CDKB1;1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Cell division control protein 2 homolog B;
GN Name=CDKB1-1; Synonyms=CDC2B; OrderedLocusNames=At3g54180;
GN ORFNames=F24B22.140;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=1618302; DOI=10.1016/0014-5793(92)80592-5;
RA Imajuku Y., Hirayama T., Endoh H., Oka A.;
RT "Exon-intron organization of the Arabidopsis thaliana protein kinase genes
RT CDC2a and CDC2b.";
RL FEBS Lett. 304:73-77(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-309.
RC STRAIN=cv. Columbia;
RX PubMed=1937013; DOI=10.1016/0378-1119(91)90146-3;
RA Hirayama T., Imajuku Y., Anai T., Matsui M., Oka A.;
RT "Identification of two cell-cycle-controlling cdc2 gene homologs in
RT Arabidopsis thaliana.";
RL Gene 105:159-165(1991).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8893539; DOI=10.1046/j.1365-313x.1996.10040601.x;
RA Segers G., Gadisseur I., Bergounioux C., de Almeida Engler J., Jacqmard A.,
RA van Montagu M., Inze D.;
RT "The Arabidopsis cyclin-dependent kinase gene cdc2bAt is preferentially
RT expressed during S and G2 phases of the cell cycle.";
RL Plant J. 10:601-612(1996).
RN [8]
RP INTERACTION WITH CKS1.
RX PubMed=9276444; DOI=10.1016/s0014-5793(97)00822-3;
RA de Veylder L., Segers G., Glab N., Casteels P., van Montagu M., Inze D.;
RT "The Arabidopsis Cks1At protein binds the cyclin-dependent kinases Cdc2aAt
RT and Cdc2bAt.";
RL FEBS Lett. 412:446-452(1997).
RN [9]
RP MUTAGENESIS OF THR-14; TYR-15; ASP-161; PRO-171; THR-181 AND
RP 249-LEU--ASP-251.
RX PubMed=10100639; DOI=10.1016/s0014-5793(99)00211-2;
RA Porceddu A., de Veylder L., Hayles J., van Montagu M., Inze D., Mironov V.;
RT "Mutational analysis of two Arabidopsis thaliana cyclin-dependent kinases
RT in fission yeast.";
RL FEBS Lett. 446:182-188(1999).
RN [10]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10521519; DOI=10.2307/3871084;
RA Yoshizumi T., Nagata N., Shimada H., Matsui M.;
RT "An Arabidopsis cell cycle-dependent kinase-related gene, CDC2b, plays a
RT role in regulating seedling growth in darkness.";
RL Plant Cell 11:1883-1896(1999).
RN [11]
RP FUNCTION.
RX PubMed=11442060; DOI=10.1023/a:1010665831955;
RA Imajuku Y., Ohashi Y., Aoyama T., Goto K., Oka A.;
RT "An upstream region of the Arabidopsis thaliana CDKA;1 (CDC2aAt) gene
RT directs transcription during trichome development.";
RL Plant Mol. Biol. 46:205-213(2001).
RN [12]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ASP-161.
RX PubMed=11477067; DOI=10.1074/jbc.m011060200;
RA Porceddu A., Stals H., Reichheld J.-P., Segers G., de Veylder L.,
RA Barroco R.M., Casteels P., van Montagu M., Inze D., Mironov V.;
RT "A plant-specific cyclin-dependent kinase is involved in the control of
RT G2/M progression in plants.";
RL J. Biol. Chem. 276:36354-36360(2001).
RN [13]
RP INTERACTION WITH CKS1.
RX PubMed=11319029; DOI=10.1046/j.1365-313x.2001.00996.x;
RA de Veylder L., Beemster G.T.S., Beeckman T., Inze D.;
RT "CKS1At overexpression in Arabidopsis thaliana inhibits growth by reducing
RT meristem size and inhibiting cell-cycle progression.";
RL Plant J. 25:617-626(2001).
RN [14]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [15]
RP INTERACTION WITH CYCU3-1.
RX PubMed=15197472; DOI=10.1007/s00018-004-4057-4;
RA Torres Acosta J.A., de Almeida Engler J., Raes J., Magyar Z., de Groodt R.,
RA Inze D., de Veylder L.;
RT "Molecular characterization of Arabidopsis PHO80-like proteins, a novel
RT class of CDKA;1-interacting cyclins.";
RL Cell. Mol. Life Sci. 61:1485-1497(2004).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-161.
RX PubMed=15031414; DOI=10.1105/tpc.021774;
RA Boudolf V., Barroco R.M., de Almeida Engler J., Verkest A., Beeckman T.,
RA Naudts M., Inze D., de Veylder L.;
RT "B1-type cyclin-dependent kinases are essential for the formation of
RT stomatal complexes in Arabidopsis thaliana.";
RL Plant Cell 16:945-955(2004).
RN [17]
RP FUNCTION.
RX PubMed=15377755; DOI=10.1105/tpc.104.024398;
RA Boudolf V., Vlieghe K., Beemster G.T.S., Magyar Z., Torres Acosta J.A.,
RA Maes S., Van Der Schueren E., Inze D., De Veylder L.;
RT "The plant-specific cyclin-dependent kinase CDKB1;1 and transcription
RT factor E2Fa-DPa control the balance of mitotically dividing and
RT endoreduplicating cells in Arabidopsis.";
RL Plant Cell 16:2683-2692(2004).
RN [18]
RP REVIEW.
RX PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
RA Inze D., de Veylder L.;
RT "Cell cycle regulation in plant development.";
RL Annu. Rev. Genet. 40:77-105(2006).
RN [19]
RP INTERACTION WITH SIM; SMR1 AND SMR2.
RX PubMed=20706207; DOI=10.1038/msb.2010.53;
RA Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
RA Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y., De Bodt S.,
RA Maere S., Laukens K., Pharazyn A., Ferreira P.C.G., Eloy N., Renne C.,
RA Meyer C., Faure J.-D., Steinbrenner J., Beynon J., Larkin J.C.,
RA Van de Peer Y., Hilson P., Kuiper M., De Veylder L., Van Onckelen H.,
RA Inze D., Witters E., De Jaeger G.;
RT "Targeted interactomics reveals a complex core cell cycle machinery in
RT Arabidopsis thaliana.";
RL Mol. Syst. Biol. 6:397-397(2010).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND REGULATION BY MYB88 AND MYB124.
RC STRAIN=cv. Columbia;
RX PubMed=20675570; DOI=10.1105/tpc.110.074609;
RA Xie Z., Lee E., Lucas J.R., Morohashi K., Li D., Murray J.A., Sack F.D.,
RA Grotewold E.;
RT "Regulation of cell proliferation in the stomatal lineage by the
RT Arabidopsis MYB FOUR LIPS via direct targeting of core cell cycle genes.";
RL Plant Cell 22:2306-2321(2010).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24123248; DOI=10.1093/jxb/ert313;
RA Lee E., Liu X., Eglit Y., Sack F.;
RT "FOUR LIPS and MYB88 conditionally restrict the G1/S transition during
RT stomatal formation.";
RL J. Exp. Bot. 64:5207-5219(2013).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24687979; DOI=10.1093/jxb/eru139;
RA Yang K., Wang H., Xue S., Qu X., Zou J., Le J.;
RT "Requirement for A-type cyclin-dependent kinase and cyclins for the
RT terminal division in the stomatal lineage of Arabidopsis.";
RL J. Exp. Bot. 65:2449-2461(2014).
CC -!- FUNCTION: May control G2/M (mitosis) phase progression. Plays a role in
CC regulating seedling growth in darkness via regulation of hypocotyl cell
CC elongation and cotyledon cell development. Plays a role in stomatal
CC development. Required to suppress endoreduplication. Together with
CC CDKB1-2, promotes both the last division in the stomatal cell lineage
CC as well as the number of stomata (PubMed:20675570). In collaboration
CC with MYB124 and MYB88, restrict the G1/S transition and chloroplast and
CC nuclear number during stomatal formation, and normally maintain fate
CC and developmental progression throughout the stomatal cell lineage
CC (PubMed:24123248, PubMed:24687979). {ECO:0000269|PubMed:10521519,
CC ECO:0000269|PubMed:11442060, ECO:0000269|PubMed:11477067,
CC ECO:0000269|PubMed:15031414, ECO:0000269|PubMed:15377755,
CC ECO:0000269|PubMed:20675570, ECO:0000269|PubMed:24123248,
CC ECO:0000269|PubMed:24687979}.
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 -!- 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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-176 activates it.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CKS1 (PubMed:9276444, PubMed:11319029).
CC Interacts with CYCU3-1 (PubMed:15197472). Interacts with SIM, SMR1 and
CC SMR2 (PubMed:20706207). {ECO:0000269|PubMed:11319029,
CC ECO:0000269|PubMed:15197472, ECO:0000269|PubMed:9276444}.
CC -!- INTERACTION:
CC P25859; O23249: CKS1; NbExp=7; IntAct=EBI-1253311, EBI-1253127;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20675570}.
CC -!- TISSUE SPECIFICITY: Highly expressed in guard cells and stomatal
CC precursor cells of cotyledons. Expressed in roots, stems, flowers and
CC siliques. {ECO:0000269|PubMed:15031414, ECO:0000269|PubMed:8893539}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in the S and G2 phases.
CC Expressed in actively dividing cells: root and shoot apical meristems,
CC leaf primordia and emerging lateral root meristem. Expressed in light-
CC grown seedlings from 1 up to 7 days after germination with a peak at 2
CC and 3 days. Observed in late guard mother cells (GMC), newly formed
CC guard cells, and immature stomata, thus being expressed just before and
CC after the symmetric division of stomatal differentiation
CC (PubMed:20675570). {ECO:0000269|PubMed:10521519,
CC ECO:0000269|PubMed:11477067, ECO:0000269|PubMed:20675570,
CC ECO:0000269|PubMed:8893539}.
CC -!- INDUCTION: Repressed by MYB88 and MYB124 during stomatal development.
CC {ECO:0000269|PubMed:20675570}.
CC -!- DISRUPTION PHENOTYPE: No apparent stomatal abnormalities. The double
CC mutant cdkb1;1 cdkb1;2 has a reduced number of abnormal stomata
CC consisting in single guard cells (GC) (PubMed:20675570,
CC PubMed:24123248, PubMed:24687979). CDKA-1 partially rescue abnormal
CC stomata phenotype of cdkb1;1 cdkb1;2 (PubMed:24687979). The quadruple
CC mutant flp-1 myb88 cdkb1;1 cdkb1;2 has a reduced number of large single
CC guard cells blocked at mitosis, with strongly altered shape and size
CC and characterized by enlarged nucleus due to endomitosis and
CC endocycling, as well as extensive chloroplast replication
CC (PubMed:24123248). {ECO:0000269|PubMed:20675570,
CC ECO:0000269|PubMed:24123248, ECO:0000269|PubMed:24687979}.
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; D10851; BAA01624.1; -; Genomic_DNA.
DR EMBL; AL132957; CAB70992.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79196.1; -; Genomic_DNA.
DR EMBL; BT026079; ABG48435.1; -; mRNA.
DR EMBL; AY084810; AAM61376.1; -; mRNA.
DR EMBL; X57840; CAA40972.1; -; mRNA.
DR PIR; S23096; S23096.
DR RefSeq; NP_190986.1; NM_115278.3.
DR AlphaFoldDB; P25859; -.
DR SMR; P25859; -.
DR BioGRID; 9902; 50.
DR IntAct; P25859; 25.
DR STRING; 3702.AT3G54180.1; -.
DR iPTMnet; P25859; -.
DR PaxDb; P25859; -.
DR PRIDE; P25859; -.
DR ProteomicsDB; 246700; -.
DR EnsemblPlants; AT3G54180.1; AT3G54180.1; AT3G54180.
DR GeneID; 824585; -.
DR Gramene; AT3G54180.1; AT3G54180.1; AT3G54180.
DR KEGG; ath:AT3G54180; -.
DR Araport; AT3G54180; -.
DR TAIR; locus:2080290; AT3G54180.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; P25859; -.
DR OMA; LYCHARR; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; P25859; -.
DR BRENDA; 2.7.11.22; 399.
DR PRO; PR:P25859; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P25859; baseline and differential.
DR Genevisible; P25859; AT.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; ISS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048825; P:cotyledon development; IEP:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; TAS:TAIR.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010444; P:guard mother cell differentiation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; IMP:UniProtKB.
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:2000037; P:regulation of stomatal complex patterning; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0010376; P:stomatal complex formation; IEP:UniProtKB.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..309
FT /note="Cyclin-dependent kinase B1-1"
FT /id="PRO_0000085750"
FT DOMAIN 4..301
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 176
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT MUTAGEN 14
FT /note="T->A: Decreased kinase activity and disturbed cell
FT cycle; when associated with F-15."
FT /evidence="ECO:0000269|PubMed:10100639"
FT MUTAGEN 15
FT /note="Y->F: Decreased kinase activity and disturbed cell
FT cycle; when associated with A-14."
FT /evidence="ECO:0000269|PubMed:10100639"
FT MUTAGEN 161
FT /note="D->N: Dominant negative. Decreased kinase activity
FT and disturbed cell cycle."
FT /evidence="ECO:0000269|PubMed:10100639,
FT ECO:0000269|PubMed:11477067, ECO:0000269|PubMed:15031414"
FT MUTAGEN 171
FT /note="P->L: Decreased kinase activity and disturbed cell
FT cycle."
FT /evidence="ECO:0000269|PubMed:10100639"
FT MUTAGEN 181
FT /note="T->I: Decreased kinase activity and disturbed cell
FT cycle."
FT /evidence="ECO:0000269|PubMed:10100639"
FT MUTAGEN 249..251
FT /note="Missing: Decreased kinase activity and disturbed
FT cell cycle."
FT /evidence="ECO:0000269|PubMed:10100639"
FT CONFLICT 226
FT /note="Q -> R (in Ref. 6; CAA40972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35318 MW; 8FFCD006A9A4A75B CRC64;
MEKYEKLEKV GEGTYGKVYK AMEKGTGKLV ALKKTRLEMD EEGIPPTALR EISLLQMLST
SIYVVRLLCV EHVHQPSTKS QSTKSNLYLV FEYLDTDLKK FIDSYRKGPN PKPLEPFLIQ
KLMFQLCKGV AHCHSHGVLH RDLKPQNLLL VKDKELLKIA DLGLGRAFTV PLKSYTHEIV
TLWYRAPEVL LGSTHYSTGV DMWSVGCIFA EMVRRQALFP GDSEFQQLLH IFRLLGTPTE
QQWPGVSTLR DWHVYPKWEP QDLTLAVPSL SPQGVDLLTK MLKYNPAERI SAKTALDHPY
FDSLDKSQF
