CDK1_CHICK
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 03-AUG-2022, entry version 153.
DE RecName: Full=Cyclin-dependent kinase 1;
DE Short=CDK1;
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;
DE AltName: Full=Cell division protein kinase 1;
DE AltName: Full=p34 protein kinase;
GN Name=CDK1; Synonyms=CDC2;
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 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).
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, and regulates G1 progress and G1-S transition via
CC association with multiple interphase cyclins. Required in higher cells
CC for entry into S-phase and mitosis. May play a role in regulating the
CC amplitude of the cyclic expression of circadian clock genes.
CC {ECO:0000250|UniProtKB:P06493}.
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: 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 -!- 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; 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; 1.
DR STRING; 9031.ENSGALP00000042598; -.
DR iPTMnet; P13863; -.
DR PaxDb; P13863; -.
DR GeneID; 396252; -.
DR KEGG; gga:396252; -.
DR CTD; 983; -.
DR VEuPathDB; HostDB:geneid_396252; -.
DR eggNOG; KOG0594; Eukaryota.
DR InParanoid; P13863; -.
DR OrthoDB; 1010560at2759; -.
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; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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; ISS: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; IBA:GO_Central.
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; IMP:AgBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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; Biological rhythms; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; 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
