CDK1_DROME
ID CDK1_DROME Reviewed; 297 AA.
AC P23572; A0ANT1; Q86FT5; Q86FT6; Q86FT7; Q86FT8; Q86FT9; Q9TX68; Q9TX69;
AC Q9TX70; Q9TX71; Q9TX72; Q9TX73; Q9TX74; Q9VKX5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Cyclin-dependent kinase 1;
DE Short=CDK1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Cell division control protein 2 homolog;
DE AltName: Full=Cell division protein kinase 1;
DE AltName: Full=p34 protein kinase;
GN Name=Cdk1 {ECO:0000312|FlyBase:FBgn0004106};
GN Synonyms=cdc2 {ECO:0000312|FlyBase:FBgn0004106};
GN ORFNames=CG5363 {ECO:0000312|FlyBase:FBgn0004106};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2120045; DOI=10.1002/j.1460-2075.1990.tb07568.x;
RA Lehner C.F., O'Farrell P.H.;
RT "Drosophila cdc2 homologs: a functional homolog is coexpressed with a
RT cognate variant.";
RL EMBO J. 9:3573-3581(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=2120044; DOI=10.1002/j.1460-2075.1990.tb07567.x;
RA Jimenez J., Alphey L., Nurse P., Glover D.M.;
RT "Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two
RT cell cycle genes from Drosophila: a cdc2 homologue and string.";
RL EMBO J. 9:3565-3571(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND MUTAGENESIS OF ALA-145;
RP GLY-148; GLU-196; GLY-206 AND PRO-242.
RX PubMed=8223248; DOI=10.1242/dev.117.1.219;
RA Stern B., Ried G., Clegg N.J., Grigliatti T.A., Lehner C.F.;
RT "Genetic analysis of the Drosophila cdc2 homolog.";
RL Development 117:219-232(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL229, ZBMEL377,
RC ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP MUTAGENESIS OF GLY-43; ALA-145; GLY-148; LEU-176; GLU-196; GLY-206 AND
RP PRO-242, AND DEVELOPMENTAL STAGE.
RX PubMed=8405984; DOI=10.1139/g93-091;
RA Clegg N.J., Whitehead I.P., Williams J.A., Spiegelman G.B.,
RA Grigliatti T.A.;
RT "A developmental and molecular analysis of cdc2 mutations in Drosophila
RT melanogaster.";
RL Genome 36:676-685(1993).
RN [9]
RP FUNCTION.
RX PubMed=15581871; DOI=10.1016/j.ydbio.2004.08.043;
RA Fichelson P., Gho M.;
RT "Mother-daughter precursor cell fate transformation after Cdc2 down-
RT regulation in the Drosophila bristle lineage.";
RL Dev. Biol. 276:367-377(2004).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH CYCA AND Z600.
RX PubMed=17431409; DOI=10.1038/sj.embor.7400948;
RA Gawlinski P., Nikolay R., Goursot C., Lawo S., Chaurasia B., Herz H.M.,
RA Kussler-Schneider Y., Ruppert T., Mayer M., Grosshans J.;
RT "The Drosophila mitotic inhibitor Fruehstart specifically binds to the
RT hydrophobic patch of cyclins.";
RL EMBO Rep. 8:490-496(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-160 AND
RP THR-161, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [12]
RP FUNCTION.
RX PubMed=29746464; DOI=10.1371/journal.pbio.2005687;
RA Seller C.A., O'Farrell P.H.;
RT "Rif1 prolongs the embryonic S phase at the Drosophila mid-blastula
RT transition.";
RL PLoS Biol. 16:E2005687-E2005687(2018).
CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle
CC (PubMed:2120044, PubMed:15581871). It is required in higher cells for
CC entry into S-phase and mitosis (PubMed:2120044, PubMed:15581871,
CC PubMed:29746464). In embryos, promotes the release of Rif1 from
CC chromatin during mid-blastula transition (PubMed:29746464). p34 is a
CC component of the kinase complex that phosphorylates the repetitive C-
CC terminus of RNA polymerase II (PubMed:2120044).
CC {ECO:0000269|PubMed:15581871, ECO:0000269|PubMed:2120044,
CC ECO:0000269|PubMed:29746464}.
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-161 activates it.
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
CC subunit and with a cyclin. Component of the Frs-CycA-Cdk1 complex
CC composed of Cdk1, CycA and Z600 (PubMed:17431409).
CC {ECO:0000269|PubMed:17431409}.
CC -!- INTERACTION:
CC P23572; Q9VHN1: Cks85A; NbExp=4; IntAct=EBI-108689, EBI-122930;
CC P23572; Q9I7I0: CycB3; NbExp=2; IntAct=EBI-108689, EBI-150964;
CC P23572; P25008: CycC; NbExp=4; IntAct=EBI-108689, EBI-195485;
CC P23572; P54733: CycE; NbExp=6; IntAct=EBI-108689, EBI-203549;
CC P23572; Q961D1: CycK; NbExp=4; IntAct=EBI-108689, EBI-130995;
CC P23572; Q03019: twe; NbExp=4; IntAct=EBI-108689, EBI-138996;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:2120044, PubMed:8405984). High levels of expression when
CC mitosis is elevated; highest levels of expression are in early embryos
CC with levels decreasing during embryogenesis and remaining low
CC throughout most of larval development, and expression levels are also
CC increased in unfertilized eggs and adult females (PubMed:2120044).
CC {ECO:0000269|PubMed:2120044, ECO:0000269|PubMed:8405984}.
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; X57485; CAA40723.1; -; mRNA.
DR EMBL; X57496; CAA40733.1; -; mRNA.
DR EMBL; S66801; AAP13986.1; -; Genomic_DNA.
DR EMBL; S66804; AAP13987.1; -; Genomic_DNA.
DR EMBL; S66805; AAP13988.1; -; Genomic_DNA.
DR EMBL; S66807; AAP13989.1; -; Genomic_DNA.
DR EMBL; S66810; AAP13990.1; -; Genomic_DNA.
DR EMBL; AM294319; CAL26249.1; -; Genomic_DNA.
DR EMBL; AM294320; CAL26250.1; -; Genomic_DNA.
DR EMBL; AM294321; CAL26251.1; -; Genomic_DNA.
DR EMBL; AM294322; CAL26252.1; -; Genomic_DNA.
DR EMBL; AM294323; CAL26253.1; -; Genomic_DNA.
DR EMBL; AM294324; CAL26254.1; -; Genomic_DNA.
DR EMBL; AM294325; CAL26255.1; -; Genomic_DNA.
DR EMBL; AM294326; CAL26256.1; -; Genomic_DNA.
DR EMBL; AM294327; CAL26257.1; -; Genomic_DNA.
DR EMBL; AM294328; CAL26258.1; -; Genomic_DNA.
DR EMBL; AM294329; CAL26259.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52932.1; -; Genomic_DNA.
DR EMBL; AY061450; AAL28998.1; -; mRNA.
DR PIR; S12009; S12009.
DR RefSeq; NP_476797.1; NM_057449.4.
DR AlphaFoldDB; P23572; -.
DR SMR; P23572; -.
DR BioGRID; 60495; 56.
DR DIP; DIP-649N; -.
DR IntAct; P23572; 25.
DR MINT; P23572; -.
DR STRING; 7227.FBpp0079641; -.
DR iPTMnet; P23572; -.
DR PaxDb; P23572; -.
DR PRIDE; P23572; -.
DR EnsemblMetazoa; FBtr0080051; FBpp0079641; FBgn0004106.
DR GeneID; 34411; -.
DR KEGG; dme:Dmel_CG5363; -.
DR CTD; 983; -.
DR FlyBase; FBgn0004106; Cdk1.
DR VEuPathDB; VectorBase:FBgn0004106; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000153335; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P23572; -.
DR OMA; NNDVWPE; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; P23572; -.
DR Reactome; R-DME-110056; MAPK3 (ERK1) activation.
DR Reactome; R-DME-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DME-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DME-176412; Phosphorylation of the APC/C.
DR Reactome; R-DME-176417; Phosphorylation of Emi1.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DME-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-DME-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-69478; G2/M DNA replication checkpoint.
DR Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-DME-8878166; Transcriptional regulation by RUNX2.
DR SignaLink; P23572; -.
DR BioGRID-ORCS; 34411; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 34411; -.
DR PRO; PR:P23572; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004106; Expressed in secondary oocyte and 51 other tissues.
DR ExpressionAtlas; P23572; baseline and differential.
DR Genevisible; P23572; DM.
DR GO; GO:0045169; C:fusome; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IGI:FlyBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:FlyBase.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0048142; P:germarium-derived cystoblast division; IMP:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
DR GO; GO:0007284; P:spermatogonial cell division; IMP:FlyBase.
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..297
FT /note="Cyclin-dependent kinase 1"
FT /id="PRO_0000085743"
FT DOMAIN 4..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 128
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 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 160
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 161
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000255"
FT MUTAGEN 43
FT /note="G->D: In cdc2-E1-4; larval-pupal lethal with some
FT adult escapers."
FT /evidence="ECO:0000269|PubMed:8405984"
FT MUTAGEN 145
FT /note="A->V: In cdc2-216A; larval-pupal lethal."
FT /evidence="ECO:0000269|PubMed:8223248,
FT ECO:0000269|PubMed:8405984"
FT MUTAGEN 148
FT /note="G->R: In cdc2-D57; embryonic or larval-pupal
FT lethal."
FT /evidence="ECO:0000269|PubMed:8223248,
FT ECO:0000269|PubMed:8405984"
FT MUTAGEN 176
FT /note="L->Q: In cdc2-E10; larval-pupal lethal."
FT /evidence="ECO:0000269|PubMed:8405984"
FT MUTAGEN 196
FT /note="E->K: In cdc2-E1-24; larval-pupal lethal with some
FT adult escapers."
FT /evidence="ECO:0000269|PubMed:8223248,
FT ECO:0000269|PubMed:8405984"
FT MUTAGEN 206
FT /note="G->D: In cdc2-E1-23; larval-pupal lethal."
FT /evidence="ECO:0000269|PubMed:8223248,
FT ECO:0000269|PubMed:8405984"
FT MUTAGEN 242
FT /note="P->S: In cdc2-E1-9; larval-pupal lethal."
FT /evidence="ECO:0000269|PubMed:8223248,
FT ECO:0000269|PubMed:8405984"
SQ SEQUENCE 297 AA; 34439 MW; 952CF136D8AB64C0 CRC64;
MEDFEKIEKI GEGTYGVVYK GRNRLTGQIV AMKKIRLESD DEGVPSTAIR EISLLKELKH
ENIVCLEDVL MEENRIYLIF EFLSMDLKKY MDSLPVDKHM ESELVRSYLY QITSAILFCH
RRRVLHRDLK PQNLLIDKSG LIKVADFGLG RSFGIPVRIY THEIVTLWYR APEVLLGSPR
YSCPVDIWSI GCIFAEMATR KPLFQGDSEI DQLFRMFRIL KTPTEDIWPG VTSLPDYKNT
FPCWSTNQLT NQLKNLDANG IDLIQKMLIY DPVHRISAKD ILEHPYFNGF QSGLVRN
