ID CDK2_CARAU Reviewed; 298 AA. AC P43450; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 22-FEB-2023, entry version 103. DE RecName: Full=Cyclin-dependent kinase 2; DE EC=2.7.11.22 {ECO:0000269|PubMed:1339336}; DE AltName: Full=Cell division protein kinase 2; GN Name=cdk2; OS Carassius auratus (Goldfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprininae; Carassius. OX NCBI_TaxID=7957; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY. RC TISSUE=Oocyte; RX PubMed=1339336; DOI=10.1016/0012-1606(92)90161-9; RA Hirai T., Yamashita M., Yoshikuni M., Tokumoto T., Kajiura H., Sakai N., RA Nagahama Y.; RT "Isolation and characterization of goldfish cdk2, a cognate variant of the RT cell cycle regulator cdc2."; RL Dev. Biol. 152:113-120(1992). CC -!- FUNCTION: Involved in the control of the cell cycle. Interacts with CC cyclins A, B1, B3, D, or E. Activity of CDK2 is maximal during S phase CC and G2 (By similarity). {ECO:0000250|UniProtKB:P23437}. 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:1339336}; 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:1339336}; CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates CC the enzyme, while phosphorylation at Thr-160 activates it. CC {ECO:0000250|UniProtKB:P23437}. 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; S40289; AAB22550.1; -; mRNA. DR PIR; A44878; A44878. DR AlphaFoldDB; P43450; -. DR SMR; P43450; -. DR Ensembl; ENSCART00000143187; ENSCARP00000126988; ENSCARG00000066517. DR OrthoDB; 244018at2759; -. DR BRENDA; 2.7.11.22; 1175. DR Proteomes; UP000515129; Genome assembly. 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..298 FT /note="Cyclin-dependent kinase 2" FT /id="PRO_0000085773" 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:0000250" SQ SEQUENCE 298 AA; 33999 MW; 50A93A63A235F9A9 CRC64; MESFQKVEKI GEGTYGVVYK AKNKVTGETV ALKKIRLDTE TEGVPSTAIR EISLLKELNH PNIVKLHDVI HTENKLYLVF EFLHQDLKRF MDSSTVTGIS LPLVKSYLFQ LLQGLAFCHS HRVLHRDLKP QNLLINAQGE IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY STAVDIWSLG CIFAEMITRK ALFPGDSEID QLFRIFRTLG TPDESIWPGV TSMPDYKPSF PKWARQDLSK VVPPLDEDGR DLLGQMLIYD PNKRISAKNA LVHRFFRDVT MPVPPLRL //