ID CDK1A_XENLA Reviewed; 302 AA. AC P35567; Q5D0B3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 149. DE RecName: Full=Cyclin-dependent kinase 1-A; DE Short=CDK1-A; DE EC=2.7.11.22 {ECO:0000250|UniProtKB:P06493}; DE EC=2.7.11.23 {ECO:0000250|UniProtKB:P11440}; DE AltName: Full=Cell division control protein 2 homolog 1; DE AltName: Full=Cell division control protein 2-A; DE AltName: Full=Cell division protein kinase 1-A; DE AltName: Full=p34 protein kinase 1; GN Name=cdk1-a; Synonyms=cdc2-a, cdc2x1.1; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ACTIVITY REGULATION, AND SUBUNIT. RC TISSUE=Oocyte; RX PubMed=1377775; DOI=10.1128/mcb.12.7.3192-3203.1992; RA Pickham K.M., Meyer A.N., Li J., Donoghue D.J.; RT "Requirement of mosXe protein kinase for meiotic maturation of Xenopus RT oocytes induced by a cdc2 mutant lacking regulatory phosphorylation RT sites."; RL Mol. Cell. Biol. 12:3192-3203(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP PHOSPHORYLATION AT THR-161. RX PubMed=8344251; DOI=10.1002/j.1460-2075.1993.tb05980.x; RA Fesquet D., Labbe J.-C., Derancourt J., Capony J.-P., Galas S., Girard F., RA Lorca T., Shuttleworth J., Doree M., Cavadore J.-C.; RT "The MO15 gene encodes the catalytic subunit of a protein kinase that RT activates cdc2 and other cyclin-dependent kinases (CDKs) through RT phosphorylation of Thr161 and its homologues."; RL EMBO J. 12:3111-3121(1993). RN [4] RP PHOSPHORYLATION AT TYR-15. RX PubMed=7749193; DOI=10.1091/mbc.6.1.119; RA Mueller P.R., Coleman T.R., Dunphy W.G.; RT "Cell cycle regulation of a Xenopus Wee1-like kinase."; RL Mol. Biol. Cell 6:119-134(1995). RN [5] RP PHOSPHORYLATION AT TYR-15. RX PubMed=9486797; DOI=10.1242/dev.125.2.237; RA Murakami M.S., Vande Woude G.F.; RT "Analysis of the early embryonic cell cycles of Xenopus; regulation of cell RT cycle length by Xe-wee1 and Mos."; RL Development 125:237-248(1998). RN [6] RP INTERACTION WITH SPDYA. RX PubMed=10465793; DOI=10.1101/gad.13.16.2177; RA Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R.; RT "A novel p34cdc2 binding and activating protein that is necessary and RT sufficient to trigger G2/M progression in Xenopus oocytes."; RL Genes Dev. 13:2177-2189(1999). RN [7] RP INTERACTION WITH SPDYA. RX PubMed=15611625; DOI=10.4161/cc.4.1.1347; RA Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.; RT "Identification and comparative analysis of multiple mammalian Speedy/Ringo RT proteins."; RL Cell Cycle 4:155-165(2005). 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 (By CC similarity). 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. Once CC chromosomes are condensed and aligned at the metaphase plate, CDK1 CC activity is switched off by WEE1- and PKMYT1-mediated phosphorylation CC to allow sister chromatid separation, chromosome decondensation, CC reformation of the nuclear envelope and cytokinesis (By similarity). CC Catalyzes lamin (LMNA, LMNB1 and LMNB2) phosphorylation at the onset of CC mitosis, promoting nuclear envelope breakdown (By similarity). CC {ECO:0000250|UniProtKB:P06493, ECO:0000250|UniProtKB:P13863}. 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:P06493}; 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: Phosphorylation at Thr-14 or Tyr-15 inactivates CC the enzyme, while phosphorylation at Thr-161 activates it. CC {ECO:0000269|PubMed:1377775}. CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory CC subunit and with a cyclin. Interacts with spdya. CC {ECO:0000269|PubMed:10465793, ECO:0000269|PubMed:1377775, CC ECO:0000269|PubMed:15611625}. CC -!- SUBCELLULAR LOCATION: Nucleus {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:0000269|PubMed:7749193, CC ECO:0000269|PubMed:8344251, ECO:0000269|PubMed:9486797}. 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; M60680; AAA63561.1; -; mRNA. DR EMBL; BC045078; AAH45078.1; -; mRNA. DR PIR; A44349; A44349. DR RefSeq; NP_001080554.1; NM_001087085.1. DR RefSeq; XP_018082295.1; XM_018226806.1. DR RefSeq; XP_018082296.1; XM_018226807.1. DR AlphaFoldDB; P35567; -. DR SMR; P35567; -. DR BioGRID; 98488; 20. DR IntAct; P35567; 1. DR MINT; P35567; -. DR iPTMnet; P35567; -. DR MaxQB; P35567; -. DR DNASU; 380246; -. DR GeneID; 380246; -. DR KEGG; xla:380246; -. DR AGR; Xenbase:XB-GENE-482754; -. DR CTD; 380246; -. DR Xenbase; XB-GENE-482754; cdk1.S. DR OMA; SLRDWHE; -. DR OrthoDB; 244018at2759; -. DR BRENDA; 2.7.11.22; 6725. DR Proteomes; UP000186698; Chromosome 7S. DR Bgee; 380246; Expressed in ovary and 16 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. 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:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB. 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; Kinase; Mitosis; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..302 FT /note="Cyclin-dependent kinase 1-A" FT /id="PRO_0000085735" 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:0000250" FT MOD_RES 15 FT /note="Phosphotyrosine; by wee1 and wee2" FT /evidence="ECO:0000269|PubMed:7749193, FT ECO:0000269|PubMed:9486797" FT MOD_RES 161 FT /note="Phosphothreonine; by CAK" FT /evidence="ECO:0000269|PubMed:8344251" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06493" SQ SEQUENCE 302 AA; 34506 MW; 90D2113216DF31DA CRC64; MDEYTKIEKI GEGTYGVVYK GRHKATGQVV AMKKIRLENE EEGVPSTAIR EISLLKELQH PNIVCLLDVL MQDSRLYLIF EFLSMDLKKY LDSIPSGQYI DTMLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDSKG VIKLADFGLA RAFGIPVRVY THEVVTLWYR APEVLLGSVR YSTPVDVWSI GTIFAEIATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNS FPKWKGGSLS ANVKNIDKDG LDLLAKMLIY DPAKRISARK ALLHPYFDDL DKSSLPDNQI RN //