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 27-MAR-2024, entry version 132. 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}. 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; 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 AGR; Xenbase:XB-GENE-1001995; -. DR CTD; 399314; -. DR Xenbase; XB-GENE-1001995; cdk2.S. DR OMA; HCHENRI; -. DR OrthoDB; 244018at2759; -. DR BRENDA; 2.7.11.22; 6725. DR Proteomes; UP000186698; Chromosome 2S. DR Bgee; 399314; Expressed in egg cell and 18 other cell types or 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 CDD; cd07860; STKc_CDK2_3; 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:SF254; CYCLIN-DEPENDENT KINASE 2; 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; 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 //