{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P24941","secondaryAccessions":["A8K7C6","O75100"],"uniProtkbId":"CDK2_HUMAN","entryAudit":{"firstPublicDate":"1992-03-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1992-08-01","entryVersion":277,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cyclin-dependent kinase 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1396589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24670654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24728993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28216226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28666995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9030781"}],"value":"2.7.11.22"}]},"alternativeNames":[{"fullName":{"value":"Cell division protein kinase 2"}},{"fullName":{"value":"p33 protein kinase"}}]},"genes":[{"geneName":{"value":"CDK2"},"synonyms":[{"value":"CDKN2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10499802"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10884347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10995386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10995387"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11051553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11113184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12944431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15800615"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17495531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18372919"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19966300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20079829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20147522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20195506"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20935635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21262353"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21319273"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21596315"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24670654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24728993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28216226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28666995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29203878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41100585"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19238148"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561645"}],"value":"Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis (PubMed:10499802, PubMed:10884347, PubMed:10995386, PubMed:10995387, PubMed:11051553, PubMed:11113184, PubMed:12944431, PubMed:15800615, PubMed:17495531, PubMed:19966300, PubMed:20935635, PubMed:21262353, PubMed:21596315, PubMed:28216226, PubMed:28666995). Phosphorylates CABLES1, CTNNB1, CDK2AP2, ERCC6, NBN, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, SUV39H1, EZH2 (PubMed:10499802, PubMed:10995386, PubMed:10995387, PubMed:11051553, PubMed:11113184, PubMed:12944431, PubMed:15800615, PubMed:19966300, PubMed:20935635, PubMed:21262353, PubMed:21596315, PubMed:24728993, PubMed:28216226). Triggers duplication of centrosomes and DNA (PubMed:11051553). Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus (PubMed:18372919, PubMed:19238148, PubMed:19561645). Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in embryonic stem cells (ESCs) (PubMed:18372919, PubMed:19238148, PubMed:19561645). Activated by the CDK-activating kinase (CAK) complex consisting of CDK7, cyclin-H/CCNH and MAT1, which is a master regulator of CDK activity (PubMed:41100585). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase (PubMed:18372919, PubMed:19238148, PubMed:19561645). EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing (PubMed:20935635). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC (PubMed:19966300). Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis (PubMed:15800615, PubMed:20195506, PubMed:21319273). In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation (PubMed:15800615). Involved in regulation of telomere repair by mediating phosphorylation of NBN (PubMed:28216226). Phosphorylation of RB1 disturbs its interaction with E2F1 (PubMed:10499802). NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication (PubMed:11051553). Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase (PubMed:10995386, PubMed:10995387). Required for vitamin D-mediated growth inhibition by being itself inactivated (PubMed:20147522). Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner (PubMed:20079829). USP37 is activated by phosphorylation and thus triggers G1-S transition (PubMed:21596315). CTNNB1 phosphorylation regulates insulin internalization (PubMed:21262353). Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of the C-terminus of protein kinase B (PKB/AKT1 and PKB/AKT2), promoting its activation (PubMed:24670654)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1396589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24670654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24728993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28216226"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28666995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9030781"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.22","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1396589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24670654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28666995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9030781"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21565702"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21565702"}],"value":"Binds 2 Mg(2+) ions."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1396589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20147522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28666995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41100585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9030781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9334743"}],"value":"Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-160 activates it (PubMed:1396589, PubMed:41100585). Phosphorylated and activated by CDK7 in the CDK-activating kinase (CAK) complex, and reciprocally phosphorylating its activating kinase CDK7 (PubMed:41100585). Inhibited by 1,25-dihydroxyvitamin D(3) (1,25-(OH)(2)D(3)), AG-024322, N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), R547 (Ro-4584820), purine, pyrimidine and pyridine derivatives, 2-aminopyrimidines, paullones, thiazo derivatives, macrocyclic quinoxalin-2-one, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine, 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine (roscovitine, seliciclib and CYC202), SNS-032 (BMS-387032), triazolo[1,5-a]pyrimidines, staurosporine and olomoucine. Stimulated by MYC. Inactivated by CDKN1A (p21)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97377"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q63699"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10499802"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10884347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11980914"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12185076"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12839962"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12972555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15107404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15178429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15611625"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16325401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17095507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17373709"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17495531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17570665"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17937404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18656911"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19445729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19829063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21262353"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21406398"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21565702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23711367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23781148"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24670654"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28666995"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7630397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8610110"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8684460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8756328"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9334743"}],"value":"Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 (By similarity). Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC (PubMed:15611625). Interaction with SPDYA promotes kinase activation via a conformation change that alleviates obstruction of the substrate-binding cleft by the T-loop (PubMed:28666995). Found in a complex with both SPDYA and CDKN1B/KIP1 (PubMed:12972555, PubMed:28666995). Binds to RB1 and CDK7. Binding to CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63. Interacts with ANKRD17. Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements (PubMed:24670654, PubMed:8684460). Interacts with cyclins A, B1, B3, D, or E (PubMed:10499802, PubMed:10884347, PubMed:12185076, PubMed:23781148). Interacts with CDK2AP2 (PubMed:23781148)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P20248","geneName":"CCNA2","intActId":"EBI-457097"},"numberOfExperiments":34,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"O95067","geneName":"CCNB2","intActId":"EBI-375024"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P24385","geneName":"CCND1","intActId":"EBI-375001"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P30279","geneName":"CCND2","intActId":"EBI-748789"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P24864","geneName":"CCNE1","intActId":"EBI-519526"},"numberOfExperiments":25,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"O96020","geneName":"CCNE2","intActId":"EBI-375033"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P51946","geneName":"CCNH","intActId":"EBI-741406"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P50613","geneName":"CDK7","intActId":"EBI-1245958"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P38936","geneName":"CDKN1A","intActId":"EBI-375077"},"numberOfExperiments":32,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P46527","geneName":"CDKN1B","intActId":"EBI-519280"},"numberOfExperiments":32,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q16667","geneName":"CDKN3","intActId":"EBI-1031527"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P61024","geneName":"CKS1B","intActId":"EBI-456371"},"numberOfExperiments":28,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q09472","geneName":"EP300","intActId":"EBI-447295"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q969H0-4","geneName":"FBXW7","intActId":"EBI-6502391"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P22607","geneName":"FGFR3","intActId":"EBI-348399"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q14957","geneName":"GRIN2C","intActId":"EBI-8285963"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P06396","geneName":"GSN","intActId":"EBI-351506"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P01112","geneName":"HRAS","intActId":"EBI-350145"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q9Y6K9","geneName":"IKBKG","intActId":"EBI-81279"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"O95835","geneName":"LATS1","intActId":"EBI-444209"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q8TD08","geneName":"MAPK15","intActId":"EBI-1383794"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P06400","geneName":"RB1","intActId":"EBI-491274"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q9BY12","geneName":"SCAPER","intActId":"EBI-308519"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q9UQR0","geneName":"SCML2","intActId":"EBI-2513111"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q9UQR0-1","geneName":"SCML2","intActId":"EBI-16087037"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q9UBI4","geneName":"STOML1","intActId":"EBI-2681162"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q96PU4","geneName":"UHRF2","intActId":"EBI-625304"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P30274","geneName":"CCNA2","intActId":"EBI-15688654"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P51943","geneName":"Ccna2","intActId":"EBI-846980"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"P03129","geneName":"E7","intActId":"EBI-866453"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P24941","intActId":"EBI-375096"},"interactantTwo":{"uniProtKBAccession":"Q08619","geneName":"Ifi205b","intActId":"EBI-8064290"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"value":"Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)(2)D(3)"}]},"subcellularLocations":[{"location":{"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","id":"SL-0048"}},{"location":{"value":"Nucleus, Cajal body","id":"SL-0031"}},{"location":{"value":"Cytoplasm","id":"SL-0086"}},{"location":{"value":"Endosome","id":"SL-0101"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P24941-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"CDK2deltaT"}],"isoformIds":["P24941-2"],"sequenceIds":["VSP_041998"],"isoformSequenceStatus":"Described"}]},{"texts":[{"value":"Induced transiently by TGFB1 at an early phase of TGFB1-mediated apoptosis"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11113184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1396589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14597612"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16325401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17095507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17373709"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17570665"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20147522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20360007"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21565702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23781148"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28666995"}],"value":"Phosphorylated at Thr-160 by CDK7 in a CAK complex (PubMed:28666995). Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20079829"}],"value":"Nitrosylated after treatment with nitric oxide (DETA-NO)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. 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