CDK2_XENLA
ID CDK2_XENLA Reviewed; 297 AA.
AC P23437; Q3KPN7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cyclin-dependent kinase 2;
DE EC=2.7.11.22 {ECO:0000269|PubMed:10202150};
DE AltName: Full=CDC2 homolog Eg1 protein kinase;
DE AltName: Full=Cell division protein kinase 2;
GN Name=cdk2; Synonyms=eg1;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=1704128; DOI=10.1073/pnas.88.3.1039;
RA Paris J., le Guellec R., Couturier A., le Guellec K., Omilli F.,
RA Camonis J., Macneill S., Philippe M.;
RT "Cloning by differential screening of a Xenopus cDNA coding for a protein
RT highly homologous to cdc2.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1039-1043(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT THR-160.
RX PubMed=8393783; DOI=10.1002/j.1460-2075.1993.tb05981.x;
RA Poon R.Y.C., Yamashita K., Adamczewski J.P., Hunt T., Shuttleworth J.;
RT "The cdc2-related protein p40MO15 is the catalytic subunit of a protein
RT kinase that can activate p33cdk2 and p34cdc2.";
RL EMBO J. 12:3123-3132(1993).
RN [4]
RP INTERACTION WITH SPDYA, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC TISSUE=Ovary;
RX PubMed=10202150; DOI=10.1093/emboj/18.7.1869;
RA Lenormand J.-L., Dellinger R.W., Knudsen K.E., Subramani S., Donoghue D.J.;
RT "Speedy: a novel cell cycle regulator of the G2/M transition.";
RL EMBO J. 18:1869-1877(1999).
CC -!- FUNCTION: Involved in the control of the cell cycle. Interacts with
CC cyclins A, B, D, or E. Activity of CDK2 is maximal during S phase and
CC G2. {ECO:0000269|PubMed:1704128}.
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:10202150};
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:0000269|PubMed:10202150};
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-160 activates it (By
CC similarity). Activated by spdya. {ECO:0000250,
CC ECO:0000269|PubMed:10202150}.
CC -!- SUBUNIT: Interacts with spdya. {ECO:0000269|PubMed:10202150}.
CC -!- DEVELOPMENTAL STAGE: Synthesized in unfertilized egg, but no longer
CC made in the early embryo. {ECO:0000269|PubMed:1704128}.
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; X14227; CAA32443.1; -; mRNA.
DR EMBL; BC106636; AAI06637.1; -; mRNA.
DR PIR; A37871; A37871.
DR RefSeq; NP_001084120.1; NM_001090651.1.
DR AlphaFoldDB; P23437; -.
DR SMR; P23437; -.
DR BioGRID; 100639; 6.
DR DIP; DIP-60879N; -.
DR IntAct; P23437; 1.
DR iPTMnet; P23437; -.
DR DNASU; 399314; -.
DR GeneID; 399314; -.
DR KEGG; xla:399314; -.
DR CTD; 399314; -.
DR Xenbase; XB-GENE-1001995; cdk2.S.
DR OMA; HYTHEVV; -.
DR OrthoDB; 1010560at2759; -.
DR BRENDA; 2.7.11.22; 6725.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 399314; Expressed in egg cell and 18 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..297
FT /note="Cyclin-dependent kinase 2"
FT /id="PRO_0000085774"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 127
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 BINDING 81..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 129..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 145
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"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000269|PubMed:8393783"
FT CONFLICT 93
FT /note="G -> R (in Ref. 1; CAA32443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33870 MW; 173ED4E4C12DA397 CRC64;
MENFQKVEKI GEGTYGVVYK ARNRETGEIV ALKKIRLDTE TEGVPSTAIR EISLLKELNH
PNIVKLLDVI HTENKLYLVF EFLNQDLKKF MDGSNISGIS LALVKSYLFQ LLQGLAFCHS
HRVLHRDLKP QNLLINSDGA IKLADFGLAR AFGVPVRTFT HEVVTLWYRA PEILLGCKFY
STAVDIWSLG CIFAEMITRR ALFPGDSEID QLFRIFRTLG TPDEVSWPGV TTMPDYKSTF
PKWIRQDFSK VVPPLDEDGR DLLAQMLQYD SNKRISAKVA LTHPFFRDVS RPTPHLI
