Search Results
Overview
| Uniprot ID | P24941 |
|---|---|
| Protein Name | Cyclin-dependent kinase 2 |
| Gene Name | CDK2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 33 | TGEVVALKKIRLDTE |
| 34 | GEVVALKKIRLDTET |
| 9 | ENFQKVEKIGEGTYG |
Function
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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015030 | Cajal body |
| Biological Process | GO:0007265 | Ras protein signal transduction |
| Biological Process | GO:1905784 | regulation of anaphase-promoting complex-dependent catabolic process |
| Biological Process | GO:0120261 | regulation of heterochromatin organization |
| Biological Process | GO:0007346 | regulation of mitotic cell cycle |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0043247 | telomere maintenance in response to DNA damage |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0036064 | ciliary basal body |
| Cellular Component | GO:0000793 | condensed chromosome |
| Cellular Component | GO:0097123 | cyclin A1-CDK2 complex |
| Cellular Component | GO:0097124 | cyclin A2-CDK2 complex |
| Cellular Component | GO:0097134 | cyclin E1-CDK2 complex |
| Cellular Component | GO:0097135 | cyclin E2-CDK2 complex |
| Cellular Component | GO:0000307 | cyclin-dependent protein kinase holoenzyme complex |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005768 | endosome |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005667 | transcription regulator complex |
| Cellular Component | GO:0000805 | X chromosome |
| Cellular Component | GO:0000806 | Y chromosome |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0030332 | cyclin binding |
| Molecular Function | GO:0097472 | cyclin-dependent protein kinase activity |
| Molecular Function | GO:0004693 | cyclin-dependent protein serine/threonine kinase activity |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0106310 | protein serine kinase activity |
| Molecular Function | GO:0004674 | protein serine/threonine kinase activity |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0071732 | cellular response to nitric oxide |
| Biological Process | GO:0090398 | cellular senescence |
| Biological Process | GO:0007099 | centriole replication |
| Biological Process | GO:0051298 | centrosome duplication |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0000082 | G1/S transition of mitotic cell cycle |
| Biological Process | GO:0000086 | G2/M transition of mitotic cell cycle |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:0031571 | mitotic G1 DNA damage checkpoint signaling |
| Biological Process | GO:0120186 | negative regulation of protein localization to chromatin |
| Biological Process | GO:0018105 | peptidyl-serine phosphorylation |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:0045740 | positive regulation of DNA replication |
| Biological Process | GO:0031453 | positive regulation of heterochromatin formation |
| Biological Process | GO:0043687 | post-translational protein modification |
| Biological Process | GO:0006468 | protein phosphorylation |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.