DNA-PK (Phospho Thr2609) rabbit pAb
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DNA-PK (Phospho Thr2609) rabbit pAb
Background :
Catalytic activity:ATP + a protein = ADP + a phosphoprotein., enzyme regulation:Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation., function:Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V (D) J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V (D) J recombination by activation of the hairpin endonuclease artemis (DCLRE1C) . The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, c-myc/MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate TP53/p53 in the presence of supercoiled DNA is dependent on C1D., PTM:Phosphorylated upon DNA damage, probably by ATM or ATR. Autophosphorylated on Thr-2609, Thr-2638 and Thr-2647. Thr-2609 is a DNA damage-inducible phosphorylation site (inducible with ionizing radiation, IR) . Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair., similarity:Belongs to the PI3/PI4-kinase family., similarity:Contains 1 FAT domain., similarity:Contains 1 FATC domain., similarity:Contains 1 PI3K/PI4K domain., similarity:Contains 2 HEAT repeats., similarity:Contains 3 TPR repeats., subunit:DNA-PK is a heterotrimer of PRKDC and the Ku p70-p86 (XRCC6-XRCC5) dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D.Description :
Catalytic activity: ATP + a protein = ADP + a phosphoprotein. enzyme regulation: Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation. function: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V (D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V (D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, c-myc/MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate TP53/p53 in the presence of supercoiled DNA is dependent on C1D. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. Autophosphorylated on Thr-2609, Thr-2638 and Thr-2647. Thr-2609 is a DNA damage-inducible phosphorylation site (inducible with ionizing radiation, IR). Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair. similarity: Belongs to the PI3/PI4-kinase family. similarity: Contains 1 FAT domain. similarity: Contains 1 FATC domain. similarity: Contains 1 PI3K/PI4K domain. similarity: Contains 2 HEAT repeats. similarity: Contains 3 TPR repeats. subunit: DNA-PK is a heterotrimer of PRKDC and the Ku p70-p86 (XRCC6-XRCC5) dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D.UniProt :
P78527Swiss Prot :
P78527Reactivity :
Human; MouseImmunogen :
Synthesized peptide derived from human DNA-PK (Phospho Thr2609)Clonality :
PolyclonalSource :
RabbitApplications :
WB; ELISAConcentration :
1 mg/mlDilution :
WB 1:1000-2000 ELISA 1:5000-20000Molecular Weight :
450kDStorage Conditions :
-20°C/1 yearObserved Molecular Weight :
450kDFragment :
IgGSubcellular Location :
Nucleus . Nucleus, nucleolus .Other Product Names :
DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit; DNA-PKcs; EC 2.7.11.1; DNPK1; p460)Gene ID (Human) :
5591

