ID CDK1_CHICK Reviewed; 303 AA. AC P13863; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 27-MAR-2024, entry version 158. DE RecName: Full=Cyclin-dependent kinase 1; DE Short=CDK1; DE EC=2.7.11.22 {ECO:0000269|PubMed:2188731}; DE EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440}; 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; Synonyms=CDC2 {ECO:0000303|PubMed:2188731}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2684635; DOI=10.1002/j.1460-2075.1989.tb08458.x; RA Krek W., Nigg E.A.; RT "Structure and developmental expression of the chicken CDC2 kinase."; RL EMBO J. 8:3071-3078(1989). RN [2] RP FUNCTION. RX PubMed=2188731; DOI=10.1016/0092-8674(90)90471-p; RA Peter M., Nakagawa J., Doree M., Labbe J.C., Nigg E.A.; RT "In vitro disassembly of the nuclear lamina and M phase-specific RT phosphorylation of lamins by cdc2 kinase."; RL Cell 61:591-602(1990). RN [3] RP PHOSPHORYLATION AT THR-14; TYR-15 AND SER-277. RX PubMed=1846803; DOI=10.1002/j.1460-2075.1991.tb07951.x; RA Krek W., Nigg E.A.; RT "Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and RT G2/M transitions of the cell cycle: identification of major phosphorylation RT sites."; RL EMBO J. 10:305-316(1991). RN [4] RP PHOSPHORYLATION AT TYR-15 (MICROBIAL INFECTION). RX PubMed=30135207; DOI=10.1074/jbc.ra118.002784; RA Horiuchi M., Kuga T., Saito Y., Nagano M., Adachi J., Tomonaga T., RA Yamaguchi N., Nakayama Y.; RT "The tyrosine kinase v-Src causes mitotic slippage by phosphorylating an RT inhibitory tyrosine residue of Cdk1."; RL J. Biol. Chem. 293:15524-15537(2018). CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle CC by modulating the centrosome cycle as well as mitotic onset; promotes CC G2-M transition via association with multiple interphase cyclins CC (PubMed:2188731). During G2 and early mitosis, CDC25A/B/C-mediated CC dephosphorylation activates CDK1/cyclin complexes which phosphorylate CC several substrates that trigger at least centrosome separation, Golgi CC dynamics, nuclear envelope breakdown and chromosome condensation (By CC similarity). Once chromosomes are condensed and aligned at the CC metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1- CC mediated phosphorylation to allow sister chromatid separation, CC chromosome decondensation, reformation of the nuclear envelope and CC cytokinesis (By similarity). Catalyzes lamin (LMNA, LMNB1 and LMNB2) CC phosphorylation at the onset of mitosis, promoting nuclear envelope CC breakdown (PubMed:2188731). {ECO:0000250|UniProtKB:P06493, CC ECO:0000269|PubMed:2188731}. 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:0000269|PubMed:2188731}; 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:P06493}; 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 Evidence={ECO:0000250|UniProtKB:P11440}; CC -!- ACTIVITY REGULATION: Thr-14 and Tyr-15 are phosphorylated maximally CC during G2 phase, but dephosphorylated abruptly at the G2/M transition. CC Phosphorylation at Thr-14 and Tyr-15 inactivates the enzyme. During M CC phase it is also phosphorylated on Thr-161. Finally during G1 phase it CC is phosphorylated on Ser-277. {ECO:0000250|UniProtKB:P06493}. CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory CC subunit and with a cyclin. Interacts with catalytically active CCNB1 CC and RALBP1 during mitosis to form an endocytotic complex during CC interphase. {ECO:0000250|UniProtKB:P06493}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06493}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:P06493}. CC -!- PTM: Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein CC kinase activity and acts negative regulator of entry into mitosis (G2 CC to M transition). {ECO:0000250|UniProtKB:P06493}. CC -!- PTM: (Microbial infection) Phosphorylated at Tyr-15 by Rous sarcoma CC virus v-oncogene Src, possibly causing mitotic slippage. CC {ECO:0000269|PubMed:30135207}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X16881; CAA34764.1; -; mRNA. DR PIR; S06011; S06011. DR RefSeq; NP_990645.1; NM_205314.1. DR AlphaFoldDB; P13863; -. DR SMR; P13863; -. DR BioGRID; 676512; 5. DR STRING; 9031.ENSGALP00000004867; -. DR iPTMnet; P13863; -. DR PaxDb; 9031-ENSGALP00000042598; -. DR GeneID; 396252; -. DR KEGG; gga:396252; -. DR CTD; 983; -. DR VEuPathDB; HostDB:geneid_396252; -. DR eggNOG; KOG0594; Eukaryota. DR InParanoid; P13863; -. DR PhylomeDB; P13863; -. DR BRENDA; 2.7.11.22; 1306. DR Reactome; R-GGA-265976; Homologous DNA pairing and strand exchange. DR Reactome; R-GGA-351451; Homologous recombination repair of replication-dependent double-strand breaks. DR PRO; PR:P13863; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 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; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome. 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:0034605; P:cellular response to heat; IDA:AgBase. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR CDD; cd07861; STKc_CDK1_euk; 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:SF334; CYCLIN-DEPENDENT KINASE 1; 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; Cytoplasm; Cytoskeleton; Kinase; KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..303 FT /note="Cyclin-dependent kinase 1" FT /id="PRO_0000085728" 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:1846803" FT MOD_RES 15 FT /note="Phosphotyrosine; by WEE1 and WEE2" FT /evidence="ECO:0000269|PubMed:1846803" FT MOD_RES 161 FT /note="Phosphothreonine; by CAK" FT /evidence="ECO:0000250|UniProtKB:P06493" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:1846803" SQ SEQUENCE 303 AA; 34688 MW; 976740ECC4741D69 CRC64; MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELHH PNIVCLQDVL MQDARLYLIF EFLSMDLKKY LDTIPSGQYL DRSRVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDDKG VIKLADFGLA RAFGIPVRVY THEVVTLWYR SPEVLLGSAL YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNDVWPD VESLQDYKNT FPKWKPGSLG THVQNLDEDG LDLLSKMLIY DPAKRISGKM ALNHPYFDDL DKSTLPANLI KKF //