Recombinant Human ATM protein (GST tag N-Terminus)
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Recombinant Human ATM protein (GST tag N-Terminus) is a Human Fragment protein, in the 1 to 138 aa range, expressed in Wheat germ, with >80%, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Serine-protein kinase ATM, Ataxia telangiectasia mutated, A-T mutated, ATM
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human ATM protein (GST tag N-Terminus) (AB131739)
12.5% SDS-PAGE using ab131739 stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ATM acts as a coordinator in cellular response to DNA damage highly interacting with multiple components of the DNA repair machinery. It forms a complex with proteins like NBS1 and MRN complex facilitating repair by recruiting and activating other proteins involved in homologous recombination and non-homologous end joining pathways. ATM also modulates p53 activity a primary response factor in cellular stress management linking ATM to control of cell cycle arrest and apoptosis. This positions ATM as an integral part of maintaining cellular integrity in face of genomic insult.
Pathways
ATM integrates neatly within the DNA damage response and cell cycle control pathways. ATM's operative relationship with the MRN complex and its role in the PI3K-related protein kinase family helps initiate appropriate repair processes upon DNA damage detection. Additionally ATM regulates the activity of proteins such as Chk2 which further propagates signals to p53 influencing decisions between cell cycle arrest and apoptosis. These interactions link ATM closely to essential processes like DNA repair and cell survival highlighting its role in genomic maintenance.
Specifications
Form
Liquid
Additional notes
Glutathione Sepharose
General info
Function
Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor (PubMed : 10550055, PubMed : 10839545, PubMed : 10910365, PubMed : 12556884, PubMed : 14871926, PubMed : 15064416, PubMed : 15448695, PubMed : 15456891, PubMed : 15790808, PubMed : 15916964, PubMed : 17923702, PubMed : 21757780, PubMed : 24534091, PubMed : 35076389, PubMed : 9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed : 10550055, PubMed : 10839545, PubMed : 10910365, PubMed : 12556884, PubMed : 14871926, PubMed : 15448695, PubMed : 15456891, PubMed : 15916964, PubMed : 17923702, PubMed : 24534091, PubMed : 9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed : 10550055, PubMed : 10766245, PubMed : 10802669, PubMed : 10839545, PubMed : 10910365, PubMed : 10973490, PubMed : 11375976, PubMed : 12086603, PubMed : 15456891, PubMed : 19965871, PubMed : 21757780, PubMed : 24534091, PubMed : 26240375, PubMed : 26774286, PubMed : 30612738, PubMed : 30886146, PubMed : 30952868, PubMed : 38128537, PubMed : 9733515, PubMed : 9843217). May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation (PubMed : 19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed : 15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed : 29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed : 15448695). Also involved in pexophagy by mediating phosphorylation of PEX5 : translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed : 26344566).
Sequence similarities
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Post-translational modifications
Phosphorylated by NUAK1/ARK5 (PubMed:12409306). Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA damage-mediated activation of the kinase (PubMed:12556884, PubMed:15790808, PubMed:16141325, PubMed:16858402, PubMed:21144835, PubMed:27664052). During the late stages of DNA damage response, dephosphorylated following deacetylation by SIRT7, leading to ATM deactivation (PubMed:30944854).. Acetylation, on DNA damage, is required for activation of the kinase activity, dimer-monomer transition, and subsequent autophosphorylation on Ser-1981 (PubMed:12556884, PubMed:16141325, PubMed:16858402, PubMed:17923702, PubMed:21144835). Acetylated in vitro by KAT5/TIP60 (PubMed:16141325). Deacetylated by SIRT7 during the late stages of DNA damage response, promoting ATM dephosphorylation and subsequent deactivation (PubMed:30944854).
Subcellular localisation
Nucleus
Target data
Product promise
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