CDK1_CAEEL
ID CDK1_CAEEL Reviewed; 332 AA.
AC P34556;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
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=cdk-1; Synonyms=ncc-1; ORFNames=T05G5.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Ferraz C., Thierry-Mieg D., Le Peuch C.J.;
RT "Complete nucleotide sequence of a cDNA coding for a p34-cdc2-like protein
RT from Caenorhabiditis elegans.";
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7830726; DOI=10.1007/bf00297285;
RA Mori H., Palmer R.E., Sternberg P.W.;
RT "The identification of a Caenorhabditis elegans homolog of p34cdc2
RT kinase.";
RL Mol. Gen. Genet. 245:781-786(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=10207147; DOI=10.1242/dev.126.10.2227;
RA Boxem M., Srinivasan D.G., van den Heuvel S.;
RT "The Caenorhabditis elegans gene ncc-1 encodes a cdc2-related kinase
RT required for M phase in meiotic and mitotic cell divisions, but not for S
RT phase.";
RL Development 126:2227-2239(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [6]
RP INTERACTION WITH CKS-1, ACTIVITY REGULATION, AND MUTAGENESIS OF ILE-173.
RX PubMed=16343905; DOI=10.1016/j.cub.2005.11.070;
RA Shirayama M., Soto M.C., Ishidate T., Kim S., Nakamura K., Bei Y.,
RA van den Heuvel S., Mello C.C.;
RT "The conserved kinases CDK-1, GSK-3, KIN-19, and MBK-2 promote OMA-1
RT destruction to regulate the oocyte-to-embryo transition in C. elegans.";
RL Curr. Biol. 16:47-55(2006).
CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle.
CC It is required in higher cells for entry into S-phase and mitosis. p34
CC is a component of the kinase complex that phosphorylates the repetitive
CC C-terminus of RNA polymerase II (By similarity). {ECO:0000250}.
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 both activates and inactivates the
CC enzyme depending on the site of phosphorylation.
CC {ECO:0000269|PubMed:16343905}.
CC -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
CC subunit and with a cyclin. Interacts with cks-1.
CC {ECO:0000269|PubMed:16343905}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}.
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; X68384; CAA48455.1; -; mRNA.
DR EMBL; S75262; AAC60520.1; -; mRNA.
DR EMBL; AF129109; AAD37119.1; -; mRNA.
DR EMBL; Z27079; CAA81590.1; -; Genomic_DNA.
DR PIR; S41003; S41003.
DR RefSeq; NP_001022747.1; NM_001027576.3.
DR AlphaFoldDB; P34556; -.
DR SMR; P34556; -.
DR BioGRID; 41569; 14.
DR DIP; DIP-26477N; -.
DR IntAct; P34556; 4.
DR STRING; 6239.T05G5.3.2; -.
DR iPTMnet; P34556; -.
DR EPD; P34556; -.
DR PaxDb; P34556; -.
DR PeptideAtlas; P34556; -.
DR EnsemblMetazoa; T05G5.3.1; T05G5.3.1; WBGene00000405.
DR GeneID; 176374; -.
DR KEGG; cel:CELE_T05G5.3; -.
DR UCSC; T05G5.3.1; c. elegans.
DR CTD; 176374; -.
DR WormBase; T05G5.3; CE00315; WBGene00000405; cdk-1.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000153335; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P34556; -.
DR OMA; IWRIRTI; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; P34556; -.
DR BRENDA; 2.7.11.22; 1045.
DR Reactome; R-CEL-110056; MAPK3 (ERK1) activation.
DR Reactome; R-CEL-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-CEL-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-CEL-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-CEL-69478; G2/M DNA replication checkpoint.
DR Reactome; R-CEL-8878166; Transcriptional regulation by RUNX2.
DR SignaLink; P34556; -.
DR PRO; PR:P34556; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000405; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IGI:WormBase.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:WormBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:WormBase.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:WormBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:WormBase.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
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; Cytoplasm; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..332
FT /note="Cyclin-dependent kinase 1"
FT /id="PRO_0000085738"
FT DOMAIN 22..312
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 33
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MUTAGEN 173
FT /note="I->F: No effect on cks-1 binding."
FT /evidence="ECO:0000269|PubMed:16343905"
FT CONFLICT 176
FT /note="R -> P (in Ref. 2; AAC60520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38295 MW; B6297E92949C8206 CRC64;
MDPIREGEVA HEGDSVYTLN DFTKLEKIGE GTYGVVYKGK NRRTNAMVAM KKIRLESEDE
GVPSTAVREI SLLKELQHPN VVGLEAVIMQ ENRLFLIFEF LSFDLKRYMD QLGKDEYLPL
ETLKSYTFQI LQAMCFCHQR RVIHRDLKPQ NLLVDNNGAI KLADFGLARA IGIPIRVYTH
EVVTLWYRAP EILMGAQRYS MGVDMWSIGC IFAEMATKKP LFQGDSEIDE LFRIFRVLGT
PTELEWNGVE SLPDYKATFP KWRENFLRDK FYDKKTGKHL LDDTAFSLLE GLLIYDPSLR
LNAKKALVHP YFDNMDTSKL PAGNYRGELE LF
