Phospho-CDK (Tyr15) Antibody (YA9904)

Nucleus; Cytoplasm; Mitochondrion; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Cytoplasm, cytoskeleton, spindle

Tissue_specificity:Found in breast cancer tissue

Induction:Follows a cyclic expression; during interphase, accumulates gradually following G1, S to reach a critical threshold at the end of G2, which promotes self-activation and triggers onset of mitosis. Induced transiently by TGFB1 at an early phase of TGFB1-mediated apoptosis, but later repressed. Triggered by CKS1B during mitotic entry in breast cancer cells. Down-regulated under genotoxic stresses triggered by PKR/EIF2AK2-mediated phosphorylation

P06493 has 2 isomers: P06493-1: 34095 Da (predicted); P06493-2: 27503 Da (predicted).
Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity (PubMed:20360007). Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation (PubMed:7569953). Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts as a negative regulator of entry into mitosis (G2 to M transition) (PubMed:20360007). Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to keep CDK1-cyclin-B complexes inactive until the end of G2 (PubMed:20360007, PubMed:7569953). By the end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B are activated (PubMed:20360007). Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition (PubMed:20360007). Phosphorylation at Tyr-15 by WEE2 during oogenesis is required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, leading to prevent meiotic reentry (PubMed:29606300). Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation (PubMed:29606300). Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress (PubMed:20395957). This phosphorylation triggers CDK1 polyubiquitination and subsequent proteolysis, thus leading to G2 arrest (PubMed:20395957). In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage checkpoint (PubMed:19917613);Polyubiquitinated upon genotoxic stress

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin (PubMed:20360007). The cyclin subunit imparts substrate specificity to the complex (PubMed:20360007). Interacts with cyclins-B (CCNB1, CCNB2 and CCNB3) to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF) (PubMed:20360007, PubMed:2188730, PubMed:2344612). Promotes G2-M transition when in complex with a cyclin-B (PubMed:20360007). Can also form CDK1-cylin-D and CDK1-cyclin-E complexes that phosphorylate RB1 in vitro (PubMed:17459720). Associates with cyclins-A and B1 during S-phase in regenerating hepatocytes (PubMed:20360007). Interacts with DLGAP5 (PubMed:15145941). Binds to the CDK inhibitors CDKN1A/p21 and CDKN1B/p27. Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase (PubMed:12775724). Interacts with FANCC (PubMed:9242535). Interacts with CEP63; this interaction recruits CDK1 to centrosomes (PubMed:21406398). Interacts with CENPA (PubMed:25556658). Interacts with NR1D1 (PubMed:27238018). Interacts with proteasome subunit PSMA8; to participate in meiosis progression during spermatogenesis (By similarity)

P06493

CDK1; CDC2; CDC28A; CDKN1; P34CDC2; Cyclin-dependent kinase 1; CDK1; Cell division control protein 2 homolog; Cell division protein kinase 1; p34 protein kinase