Atm
entrez
11920
canonical
uniprot
Q62388
canonical
ensembl
ENSMUSG00000034218
resolver
ensp
ENSMUSP00000113388
resolver
ensp
ENSMUSP00000156344
resolver
enst
ENSMUST00000118282
resolver
enst
ENSMUST00000232179
resolver
genesymbol
Atm
resolver
uniprot
A0A384DV81
resolver
uniprot
B9EHX4
resolver
uniprot
E9QNY7
resolver
uniprot_entry
A0A384DV81_MOUSE
resolver
uniprot_entry
ATM_MOUSE
resolver
uniprot_entry
B9EHX4_MOUSE
resolver
uniprot_sec
E9QNY7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by the MRN (MRE11-RAD50-NBS1) complex in response to DNA double strand breaks (DSBs), which recruits ATM to DSBs and promotes its activation. Inhibited by wortmannin. {ECO:0000250|UniProtKB:Q13315}.
uniprot
proteins
amino_acid_sequence
MSLALNDLLICCRQLEHDRATERRKEVDKFKRLIQDPETVQHLDRHSDSKQGKYLNWDAVFRFLQKYIQKEMESLRTAKSNVSATTQSSRQKKMQEISSLVRYFIKCANKRAPRLKCQDLLNYVMDTVKDSSNGLTYGADCSNILLKDILSVRKYWCEVSQQQWLELFSLYFRLYLKPSQDINRVLVARIIHAVTRGCCSQTDGLPSKFLDLFSKAIQYARQEKSSPGLSHILAALNIFLKSLAVNFRKRVCEAGDEILPTLLYIWTQHRLNDSLKEVIIELIQLQIYIHHPQGARAPEEGAYESMKWKSILYNLYDLLVNEISHIGSRGKYSSGSRNIAVKENLIDLMADICYQLFDADTRSVEISQSYVTQRESTDYSVPCKRRKIDVGWEVIKDYLQKSQSDFDLVPWLQITTRLISKYPSSLPNCELSPLILILYQLLPQQRRGERIPYVLRCLKEVALCQGKKSNLESSQKSDLLKLWIKIWSITFRGISSGQTQTENFGLLEAIIQGSLVELDREFWKLFTGSACKPSSPSVCCLTLALSICVVPDAIKMGTEQSVCEANRSFSVKESIMRWLLFYQLEDDLEDSTELPPILQSNFPHLVVEKILVSLTMKNSKAAMKFFQSVPECEQHCEDKEEPSFSEVEELFLQTTFDKMDFLTTVKEYAVEKFQSSVGFSVQQNLKESLDHYLLGLSEQLLSNYSSEITSSETLVRCSSLLVGVLGCYCYMGIITEDEAHKSELFQKAKSLMQCAGESISLFKNKTNEESRIGSLRNVMHLCTSCLCIHTKHTPNKIASGFFLRLLTSKLMNDIADICKSLASCTKKPLDHGVHPGEDDEDGGGCDSLMEAEGPSSTGLSTAYPASSVSDANDYGENQNAVGAMSPLAADYLSKQDHLLLDMLRFLGRSVTASQSHTVSFRGADIRRKLLLLLDSSILDLMKPLHLHMYLVLLKDLPGNEHSLPMEDVVELLQPLSLVCSLHRRDQDVCKTILSNVLHIVTNLGQGSVDMESTRIAQGHFLTVMGAFWHLTKEKKCVFSVRMALVKCLQTLLEADPYSEWAILNVKGQDFPVNEAFSQFLADDHHQVRMLAAGSVNRLFQDMRQGDFSRSLKALPLKFQQTSFNNAYTTAEAGIRGLLCDSQNPDLLDEIYNRKSVLLMMIAVVLHCSPVCEKQALFALCKSVKENRLEPHLVKKVLEKVSESFGCRSLEDFMISHLDYLVLEWLNLQDTEYSLSSFPFMLLNYTSIEDFYRSCYKILIPHLVIRSHFDEVKSIANQIQKCWKSLLVDCFPKILVHILPYFAYEGTRDSYVSQKRETATKVYDTLKGEDFLGKQIDQVFISNLPEIVVELLMTLHETADSADSDASQSATALCDFSGDLDPAPNPPYFPSHVIQATFAYISNCHKTKFKSILEILSKIPDSYQKILLAICEQAAETNNVFKKHRILKIYHLFVSLLLKDIQSGLGGAWAFVLRDVIYTLIHYINKRSSHFTDVSLRSFSLCCDLLSRVCHTAVTQCKDALESHLHVIVGTLIPLVDYQEVQEQVLDLLKYLVIDNKDNKNLSVTIKLLDPFPDHVIFKDLRLTQQKIKYSGGPFSLLEEINHFLSVSAYNPLPLTRLEGLKDLRRQLEQHKDQMLDLLRASQDNPQDGIVVKLVVSLLQLSKMAVNQTGEREVLEAVGRCLGEIGPLDFSTIAVQHNKDVSYTKAYGLPEDRELQWTLIMLTALNNTLVEDSVKIRSAAATCLKNILATKIGHIFWENYKTSADPMLTYLQPFRTSRKKFLEVPRSVKEDVLEGLDAVNLWVPQSESHDIWIKTLTCAFLDSGGINSEILQLLKPMCEVKTDFCQMLLPYLIHDVLLQDTHESWRTLLSAHVRGFFTSCFKHSSQASRSATPANSDSESENFLRCCLDKKSQRTMLAVVDYLRRQKRPSSGTAFDDAFWLDLNYLEVAKVAQSCSAHFTALLYAEIYSDKKSTDEQEKRSPTFEEGSQGTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPLTRIRTYEHEATWEKALVTYDLETSISSSTRQSGIIQALQNLGLSHILSVYLKGLDYERREWCAELQELRYQAAWRNMQWGLCASAGQEVEGTSYHESLYNALQCLRNREFSTFYESLRYASLFRVKEVEELSKGSLESVYSLYPTLSRLQAIGELENSGELFSRSVTDRERSEAYWKWQKHSQLLKDSDFSFQEPLMALRTVILETLVQKEMERSQGACSKDILTKHLVEFSVLARTFKNTQLPERAIFKIKQYNSAICGISEWHLEEAQVFWAKKEQSLALSILKQMIKKLDSSFKDKENDAGLKVIYAECLRVCGSWLAETCLENPAVIMQTYLEKAVKVAGSYDGNSRELRNGQMKAFLSLARFSDTQYQRIENYMKSSEFENKQTLLKRAKEEVGLLREHKIQTNRYTVKVQRELELDECALRALREDRKRFLCKAVENYINCLLSGEEHDLWVFRLCSLWLENSGVSEVNGMMKKDGMKISSYKFLPLMYQLAARMGTKMTGGLGFHEVLNNLISRISLDHPHHTLFIILALANANKDEFLSKPETTRRSRITKSTSKENSHLDEDRTEAATRIIHSIRSKRCKMVKDMEALCDAYIILANMDASQWRAQRKGINIPANQPITKLKNLEDVVVPTMEIKVDPTGEYENLVTIKSFKTEFRLAGGLNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEYLVNSEDGAHRRYRPNDFSANQCQKKMMEVQKKSFEEKYDTFMTICQNFEPVFRYFCMEKFLDPAVWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLSRDIVDGMGITGVEGVFRRCCEKTMEVMRSSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDESDLHSTPNADDQECKQSLSDTDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAMDPKNLSRLFPGWKAWV
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
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:19047460). Recognizes the substrate consensus sequence [ST]-Q (PubMed:19047460). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (PubMed:11571274). 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 (By similarity). 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 (PubMed:19448632). Also involved in signal transduction and cell cycle control (By similarity). May function as a tumor suppressor (By similarity). Necessary for activation of ABL1 and SAPK (By similarity). Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, FBXO46, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4, UCHL3 and DCLRE1C (By similarity). May play a role in vesicle and/or protein transport (By similarity). Could play a role in T-cell development, gonad and neurological function (By similarity). Binds DNA ends (By similarity). Plays a role in replication-dependent histone mRNA degradation (By similarity). Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation (By similarity). Phosphorylates ATF2 which stimulates its function in DNA damage response (By similarity). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (By similarity). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q13315, ECO:0000269|PubMed:11571274, ECO:0000269|PubMed:19047460, ECO:0000269|PubMed:19448632}.
uniprot
proteins
mass_dalton
349418
uniprot
proteins
mutagenesis
MUTAGEN 367; /note="S->A: Retains genomic stability and cell cycle checkpoint correction and kinase activity towards downstream targets; when associated with A-1987. Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-1899 and A-1987."; /evidence="ECO:0000269|PubMed:19047460"; MUTAGEN 1899; /note="S->A: Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987."; /evidence="ECO:0000269|PubMed:19047460"; MUTAGEN 1987; /note="S->A: Retains genomic stability and cell cycle checkpoint correction and kinase activity towards downstream targets; when associated with A-367. Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987."; /evidence="ECO:0000269|PubMed:19047460
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by NUAK1/ARK5 (By similarity). Autophosphorylation on Ser-367, Ser-1899, Ser-1987 correlates with DNA damage-mediated activation of the kinase. {ECO:0000250, ECO:0000269|PubMed:19047460}.; PTM: Phosphorylated by NUAK1/ARK5. Autophosphorylation on Ser-367, Ser-1899, Ser-1987 correlates with DNA damage-mediated activation of the kinase. During the late stages of DNA damage response, dephosphorylated following deacetylation by SIRT7, leading to ATM deactivation. {ECO:0000250|UniProtKB:Q13315}.; PTM: Acetylation, on DNA damage, is required for activation of the kinase activity, dimer-monomer transition, and subsequent autophosphorylation on Ser-1987. Acetylated in vitro by KAT5/TIP60. Deacetylated by SIRT7 during the late stages of DNA damage response, promoting ATM dephosphorylation and subsequent deactivation. {ECO:0000250|UniProtKB:Q13315}.
uniprot
proteins
protein_family
ATM subfamily
uniprot
proteins
protein_family
PI3/PI4-kinase family
uniprot
proteins
pubmed
11571274
uniprot
proteins
pubmed
18833288
uniprot
proteins
pubmed
19047460
uniprot
proteins
pubmed
19448632
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25936915
uniprot
proteins
pubmed
30017584
uniprot
proteins
pubmed
8661102
uniprot
proteins
pubmed
8689683
uniprot
proteins
pubmed
9000145
uniprot
proteins
pubmed
9697112
uniprot
proteins
pubmed
9707615
uniprot
proteins
sequence_length
3066
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13315}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q13315}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25936915}. Peroxisome matrix {ECO:0000250|UniProtKB:Q13315}. Note=Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin. Translocated to peroxisomes in response to reactive oxygen species (ROS) by PEX5. {ECO:0000250|UniProtKB:Q13315}.
uniprot
proteins