CDK1B_XENLA
ID CDK1B_XENLA Reviewed; 302 AA.
AC P24033; Q7SZ44;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cyclin-dependent kinase 1-B;
DE Short=CDK1-B;
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 2;
DE AltName: Full=Cell division control protein 2-B;
DE AltName: Full=Cell division protein kinase 1;
DE AltName: Full=p34 protein kinase 2;
GN Name=cdk1-b; Synonyms=cdc2, cdc2x1.2;
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=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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, 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: 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}.
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DR EMBL; M60681; AAA63562.1; -; mRNA.
DR EMBL; BC054146; AAH54146.1; -; mRNA.
DR PIR; B44349; B44349.
DR RefSeq; NP_001080093.1; NM_001086624.1.
DR AlphaFoldDB; P24033; -.
DR SMR; P24033; -.
DR BioGRID; 98027; 1.
DR iPTMnet; P24033; -.
DR DNASU; 379785; -.
DR GeneID; 379785; -.
DR KEGG; xla:379785; -.
DR CTD; 379785; -.
DR Xenbase; XB-GENE-6254942; cdk1.L.
DR OrthoDB; 1010560at2759; -.
DR BRENDA; 2.7.11.22; 6725.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 379785; Expressed in ovary and 19 other 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Kinase;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..302
FT /note="Cyclin-dependent kinase 1-B"
FT /id="PRO_0000085736"
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"
FT CONFLICT 87
FT /note="L -> V (in Ref. 1; AAA63562)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="R -> G (in Ref. 1; AAA63562)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="S -> P (in Ref. 1; AAA63562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 34532 MW; FA9DC156392D7CBC CRC64;
MDEYTKIEKI GEGTYGVVYK GRHKATGQVV AMKKIRLENE EEGVPSTAIR EISLLKELQH
PNIVCLLDVL MQDSRLYLIF EFLSMDLKKY LDSIPSGQYI DTMLVKSYLY QILQGIVFCH
SRRVLHRDLK PQNLLIDNKG VIKLADFGLA RAFGIPVRVY THEVVTLWYR ASEVLLGSVR
YSTPVDVWSV GTIFAEIATK KPLFHGDSEI DQLFRIFRSL GTPNNEVWPE VESLQDYKNT
FPKWKGGSLS SNVKNIDEDG LDLLSKMLVY DPAKRISARK AMLHPYFDDL DKSSLPANQI
RN
