CDK2_MOUSE
ID CDK2_MOUSE Reviewed; 346 AA.
AC P97377; O55105;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Cyclin-dependent kinase 2;
DE EC=2.7.11.22 {ECO:0000269|PubMed:23853094};
DE AltName: Full=Cell division protein kinase 2;
GN Name=Cdk2; Synonyms=Cdkn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDK2-ALPHA).
RC STRAIN=C57BL/6J;
RA Jun D., Lee Y.H., Park H.K., Kim Y.H.;
RT "Exon-intron organization of the murine cyclin-dependent kinase-2 genes
RT Cdk2-alpha and Cdk2-beta.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RA Ellenrieder C., Bartosch B., Lee G.Y., Murphy M., Sweeney C.,
RA Hergersberg M., Hunt T., Carrington M., Jaussi R.;
RT "The 39 kDa form of CDK2 arises through alternative splicing, is expressed
RT in many but not all mammals, and is an active kinase.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CDK2-BETA).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION AT TYR-15, MUTAGENESIS OF TYR-15, IDENTIFICATION IN A
RP COMPLEX WITH CABLES1; CCNA1 AND CCNE1, AND INTERACTION WITH CABLES1.
RX PubMed=11585773;
RA Wu C.-L., Kirley S.D., Xiao H., Chuang Y., Chung D.C., Zukerberg L.R.;
RT "Cables enhances cdk2 tyrosine 15 phosphorylation by Wee1, inhibits cell
RT growth, and is lost in many human colon and squamous cancers.";
RL Cancer Res. 61:7325-7332(2001).
RN [5]
RP FUNCTION AS CABLES1 KINASE.
RX PubMed=11733001; DOI=10.1046/j.0014-2956.2001.02555.x;
RA Yamochi T., Semba K., Tsuji K., Mizumoto K., Sato H., Matsuura Y.,
RA Nishimoto I., Matsuoka M.;
RT "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3).";
RL Eur. J. Biochem. 268:6076-6082(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14561402; DOI=10.1016/j.cub.2003.09.024;
RA Berthet C., Aleem E., Coppola V., Tessarollo L., Kaldis P.;
RT "Cdk2 knockout mice are viable.";
RL Curr. Biol. 13:1775-1785(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12923533; DOI=10.1038/ng1232;
RA Ortega S., Prieto I., Odajima J., Martin A., Dubus P., Sotillo R.,
RA Barbero J.L., Malumbres M., Barbacid M.;
RT "Cyclin-dependent kinase 2 is essential for meiosis but not for mitotic
RT cell division in mice.";
RL Nat. Genet. 35:25-31(2003).
RN [8]
RP INTERACTION WITH CEBPA.
RX PubMed=15107404; DOI=10.1101/gad.1183304;
RA Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
RT "Liver tumors escape negative control of proliferation via PI3K/Akt-
RT mediated block of C/EBP alpha growth inhibitory activity.";
RL Genes Dev. 18:912-925(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17942597; DOI=10.1091/mbc.e07-06-0525;
RA Satyanarayana A., Hilton M.B., Kaldis P.;
RT "p21 Inhibits Cdk1 in the absence of Cdk2 to maintain the G1/S phase DNA
RT damage checkpoint.";
RL Mol. Biol. Cell 19:65-77(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23853094; DOI=10.1074/jbc.m113.467704;
RA Morawski P.A., Mehra P., Chen C., Bhatti T., Wells A.D.;
RT "Foxp3 protein stability is regulated by cyclin-dependent kinase 2.";
RL J. Biol. Chem. 288:24494-24502(2013).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC the cell cycle; essential for meiosis, but dispensable for mitosis.
CC Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC,
CC NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the
CC G1-S transition to promote the E2F transcriptional program and the
CC initiation of DNA synthesis, and modulates G2 progression; controls the
CC timing of entry into mitosis/meiosis by controlling the subsequent
CC activation of cyclin B/CDK1 by phosphorylation, and coordinates the
CC activation of cyclin B/CDK1 at the centrosome and in the nucleus.
CC Crucial role in orchestrating a fine balance between cellular
CC proliferation, cell death, and DNA repair in human embryonic stem cells
CC (hESCs). Activity of CDK2 is maximal during S phase and G2; activated
CC by interaction with cyclin E during the early stages of DNA synthesis
CC to permit G1-S transition, and subsequently activated by cyclin A2
CC (cyclin A1 in germ cells) during the late stages of DNA replication to
CC drive the transition from S phase to mitosis, the G2 phase. EZH2
CC phosphorylation promotes H3K27me3 maintenance and epigenetic gene
CC silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2
CC prevents oxidative stress-mediated Ras-induced senescence by
CC phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that
CC prevents cells with damaged DNA from initiating mitosis; regulates
CC homologous recombination-dependent repair by phosphorylating BRCA2,
CC this phosphorylation is low in S phase when recombination is active,
CC but increases as cells progress towards mitosis. In response to DNA
CC damage, double-strand break repair by homologous recombination a
CC reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of
CC RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin
CC E/CDK2 promotes its dissociates from unduplicated centrosomes, thus
CC initiating centrosome duplication. Cyclin E/CDK2-mediated
CC phosphorylation of NPAT at G1-S transition and until prophase
CC stimulates the NPAT-mediated activation of histone gene transcription
CC during S phase. Required for vitamin D-mediated growth inhibition by
CC being itself inactivated. Involved in the nitric oxide- (NO) mediated
CC signaling in a nitrosylation/activation-dependent manner. USP37 is
CC activated by phosphorylation and thus triggers G1-S transition. CTNNB1
CC phosphorylation regulates insulin internalization. Phosphorylates FOXP3
CC and negatively regulates its transcriptional activity and protein
CC stability (PubMed:23853094). Phosphorylates CDK2AP2 (By similarity).
CC Phosphorylates ERCC6 which is essential for its chromatin remodeling
CC activity at DNA double-strand breaks (By similarity).
CC {ECO:0000250|UniProtKB:P24941, ECO:0000269|PubMed:11733001,
CC ECO:0000269|PubMed:12923533, ECO:0000269|PubMed:14561402,
CC ECO:0000269|PubMed:17942597, ECO:0000269|PubMed:23853094}.
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:23853094};
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:23853094};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P24941};
CC Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941};
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-160 activates it. Stimulated
CC by MYC. Inactivated by CDKN1A (p21) (By similarity).
CC {ECO:0000250|UniProtKB:P24941}.
CC -!- SUBUNIT: Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts
CC with CABLES1 (PubMed:11585773). Interacts with UHRF2. Part of a complex
CC consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo
CC proteins SPDYA and SPDYC. Interaction with SPDYA promotes kinase
CC activation via a conformation change that alleviates obstruction of the
CC substrate-binding cleft by the T-loop. Found in a complex with both
CC SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to CDKN1A (p21)
CC leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage
CC checkpoint, thereby arresting cells at the G1-S transition during DNA
CC repair. Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with
CC CACUL1. May interact with CEP63. Interacts with ANKRD17 (By
CC similarity). Interacts with CEBPA (when phosphorylated)
CC (PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B;
CC CDKN1B inhibits the kinase activity of CDK2 through conformational
CC rearrangements. Interacts with cyclins A, B1, B3, D, or E. Interacts
CC with CDK2AP2 (By similarity). {ECO:0000250|UniProtKB:P24941,
CC ECO:0000250|UniProtKB:Q63699, ECO:0000269|PubMed:11585773,
CC ECO:0000269|PubMed:15107404}.
CC -!- INTERACTION:
CC P97377; P51943: Ccna2; NbExp=3; IntAct=EBI-847048, EBI-846980;
CC P97377; Q61457: Ccne1; NbExp=3; IntAct=EBI-847048, EBI-643090;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Note=Localized at the
CC centrosomes in late G2 phase after separation of the centrosomes but
CC before the start of prophase. Nuclear-cytoplasmic trafficking is
CC mediated during the inhibition by 1,25-(OH)(2)D(3) (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=CDK2-beta;
CC IsoId=P97377-1; Sequence=Displayed;
CC Name=CDK2-alpha;
CC IsoId=P97377-2; Sequence=VSP_004800;
CC -!- PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex.
CC Phosphorylation at Thr-160 promotes kinase activity, whereas
CC phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity.
CC Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being
CC dephosphorylated by CDC25A. {ECO:0000250|UniProtKB:P24941}.
CC -!- PTM: Nitrosylated after treatment with nitric oxide (DETA-NO).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced body size and impaired neural progenitor
CC cell proliferation. Sterility due to defective meiosis; no effect on
CC mitotic cells. Premature translocation of CDK1 from the cytoplasm to
CC the nucleus compensating CDK2 loss. Prolonged and impaired DNA repair
CC activity upon DNA damage by gamma-irradiation.
CC {ECO:0000269|PubMed:12923533, ECO:0000269|PubMed:14561402,
CC ECO:0000269|PubMed:17942597}.
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; U63337; AAB37128.1; -; mRNA.
DR EMBL; AJ223732; CAA11533.1; -; mRNA.
DR EMBL; AJ223733; CAA11534.1; -; Genomic_DNA.
DR EMBL; AJ223733; CAA11535.1; -; Genomic_DNA.
DR EMBL; BC005654; AAH05654.1; -; mRNA.
DR CCDS; CCDS24288.1; -. [P97377-2]
DR CCDS; CCDS24289.1; -. [P97377-1]
DR RefSeq; NP_058036.1; NM_016756.4. [P97377-2]
DR RefSeq; NP_904326.1; NM_183417.3. [P97377-1]
DR AlphaFoldDB; P97377; -.
DR SMR; P97377; -.
DR BioGRID; 198644; 33.
DR ComplexPortal; CPX-2065; Cyclin A1-CDK2 complex.
DR ComplexPortal; CPX-2066; Cyclin A2-CDK2 complex.
DR ComplexPortal; CPX-2071; Cyclin B3-CDK2 complex.
DR ComplexPortal; CPX-2081; Cyclin E1-CDK2 complex.
DR ComplexPortal; CPX-2082; Cyclin E2-CDK2 complex.
DR CORUM; P97377; -.
DR DIP; DIP-24176N; -.
DR ELM; P97377; -.
DR IntAct; P97377; 7.
DR MINT; P97377; -.
DR STRING; 10090.ENSMUSP00000026416; -.
DR ChEMBL; CHEMBL4106185; -.
DR ChEMBL; CHEMBL4106186; -.
DR iPTMnet; P97377; -.
DR PhosphoSitePlus; P97377; -.
DR SwissPalm; P97377; -.
DR EPD; P97377; -.
DR jPOST; P97377; -.
DR PaxDb; P97377; -.
DR PeptideAtlas; P97377; -.
DR PRIDE; P97377; -.
DR ProteomicsDB; 281437; -. [P97377-1]
DR ProteomicsDB; 281438; -. [P97377-2]
DR Antibodypedia; 3404; 1749 antibodies from 50 providers.
DR DNASU; 12566; -.
DR Ensembl; ENSMUST00000026415; ENSMUSP00000026415; ENSMUSG00000025358. [P97377-2]
DR Ensembl; ENSMUST00000026416; ENSMUSP00000026416; ENSMUSG00000025358. [P97377-1]
DR GeneID; 12566; -.
DR KEGG; mmu:12566; -.
DR UCSC; uc007hny.2; mouse. [P97377-1]
DR CTD; 1017; -.
DR MGI; MGI:104772; Cdk2.
DR VEuPathDB; HostDB:ENSMUSG00000025358; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000159517; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; P97377; -.
DR OMA; HKEKCIY; -.
DR PhylomeDB; P97377; -.
DR TreeFam; TF101021; -.
DR BRENDA; 2.7.11.22; 3474.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-68911; G2 Phase.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-MMU-8849470; PTK6 Regulates Cell Cycle.
DR Reactome; R-MMU-9616222; Transcriptional regulation of granulopoiesis.
DR BioGRID-ORCS; 12566; 5 hits in 115 CRISPR screens.
DR ChiTaRS; Cdk2; mouse.
DR PRO; PR:P97377; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P97377; protein.
DR Bgee; ENSMUSG00000025358; Expressed in spermatocyte and 231 other tissues.
DR ExpressionAtlas; P97377; baseline and differential.
DR Genevisible; P97377; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0097123; C:cyclin A1-CDK2 complex; IDA:MGI.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IDA:MGI.
DR GO; GO:0097134; C:cyclin E1-CDK2 complex; IDA:MGI.
DR GO; GO:0097135; C:cyclin E2-CDK2 complex; IDA:MGI.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0000805; C:X chromosome; IDA:MGI.
DR GO; GO:0000806; C:Y chromosome; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IDA:BHF-UCL.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; ISO:MGI.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0035173; F:histone kinase activity; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0007099; P:centriole replication; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0016572; P:histone phosphorylation; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IGI:MGI.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0006813; P:potassium ion transport; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; ISO:MGI.
DR GO; GO:0051602; P:response to electrical stimulus; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IGI:MGI.
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; 2.
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 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Endosome; Kinase;
KW Magnesium; Meiosis; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..346
FT /note="Cyclin-dependent kinase 2"
FT /id="PRO_0000085771"
FT DOMAIN 4..334
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 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT SITE 9
FT /note="CDK7 binding"
FT /evidence="ECO:0000250"
FT SITE 88..89
FT /note="CDK7 binding"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="CDK7 binding"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 15
FT /note="Phosphotyrosine; by WEE1"
FT /evidence="ECO:0000269|PubMed:11585773"
FT MOD_RES 19
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 160
FT /note="Phosphothreonine; by CAK and CCRK"
FT /evidence="ECO:0000250|UniProtKB:P24941"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 197..244
FT /note="Missing (in isoform CDK2-alpha)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_004800"
FT MUTAGEN 15
FT /note="Y->F: Loss of tyrosine phosphorylation by WEE1 and
FT CABLES1."
FT /evidence="ECO:0000269|PubMed:11585773"
SQ SEQUENCE 346 AA; 38978 MW; D806BC2F150AEDFC CRC64;
MENFQKVEKI GEGTYGVVYK AKNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH
PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP LPLIKSYLFQ LLQGLAFCHS
HRVLHRDLKP QNLLINAEGS IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY
STAVDIWSLG CIFAEMHLVC TQHHAKCCGE HRRNGRHSLC PLCSYLEVAA SQGGGMTAVS
APHPVTRRAL FPGDSEIDQL FRIFRTLGTP DEVVWPGVTS MPDYKPSFPK WARQDFSKVV
PPLDEDGRSL LSQMLHYDPN KRISAKAALA HPFFQDVTKP VPHLRL
