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UniProtKB - Q13315 (ATM_HUMAN)

Protein

Serine-protein kinase ATM

Gene

ATM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. 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, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. 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. Phosphorylates ATF2 which stimulates its function in DNA damage response.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Activity regulationi

Inhibited by wortmannin.1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding, Kinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, DNA damage
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693548 Sensing of DNA Double Strand Breaks
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6803204 TP53 Regulates Transcription of Genes Involved in Cytochrome C Release
R-HSA-6803207 TP53 Regulates Transcription of Caspase Activators and Caspases
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-6804760 Regulation of TP53 Activity through Methylation
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-69541 Stabilization of p53
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-912446 Meiotic recombination
SignaLinkiQ13315
SIGNORiQ13315

Names & Taxonomyi

Protein namesi
Recommended name:
Serine-protein kinase ATM (EC:2.7.11.1)
Alternative name(s):
Ataxia telangiectasia mutated
Short name:
A-T mutated
Gene namesi
Name:ATM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000149311.17
HGNCiHGNC:795 ATM
MIMi607585 gene
neXtProtiNX_Q13315

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Involvement in diseasei

Ataxia telangiectasia (AT)27 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare recessive disorder characterized by progressive cerebellar ataxia, dilation of the blood vessels in the conjunctiva and eyeballs, immunodeficiency, growth retardation and sexual immaturity. Patients have a strong predisposition to cancer; about 30% of patients develop tumors, particularly lymphomas and leukemias. Cells from affected individuals are highly sensitive to damage by ionizing radiation and resistant to inhibition of DNA synthesis following irradiation.
See also OMIM:208900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010801224K → E in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs145053092EnsemblClinVar.1
Natural variantiVAR_010802292P → L in AT; associated with lymphoma; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs747727055EnsemblClinVar.1
Natural variantiVAR_010803323I → V in AT; loss of protein expression. 2 PublicationsCorresponds to variant dbSNP:rs587781511EnsemblClinVar.1
Natural variantiVAR_010808570F → S in AT. 1 PublicationCorresponds to variant dbSNP:rs777301065Ensembl.1
Natural variantiVAR_010809705 – 707YSS → FIP in AT; might be associated with susceptibility to cancer. 3
Natural variantiVAR_010812768N → D in AT. 1 Publication1
Natural variantiVAR_010813785R → C in AT. 1 PublicationCorresponds to variant dbSNP:rs587778065EnsemblClinVar.1
Natural variantiVAR_010815950L → R in AT. Corresponds to variant dbSNP:rs786203054EnsemblClinVar.1
Natural variantiVAR_0108161001L → Q in AT; associated with T-cell acute lymphoblastic leukemia. 1 Publication1
Natural variantiVAR_0772371046L → P in AT; loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs568461905EnsemblClinVar.1
Natural variantiVAR_0108191082H → L in AT. 1
Natural variantiVAR_0108201091E → D in AT. 1 Publication1
Natural variantiVAR_0108231420L → P in AT. 1 Publication1
Natural variantiVAR_0108261465L → P in AT; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs730881391EnsemblClinVar.1
Natural variantiVAR_0108271566P → R in AT. 1 Publication1
Natural variantiVAR_0108311743T → I in AT; associated with preleukemic T-cell proliferation; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs587779844EnsemblClinVar.1
Natural variantiVAR_0108321812 – 1813AF → V in AT. 1 Publication2
Natural variantiVAR_0108361913V → G in AT. 1 PublicationCorresponds to variant dbSNP:rs1060501688Ensembl.1
Natural variantiVAR_0108382016D → G in AT. 1 PublicationCorresponds to variant dbSNP:rs587781302EnsemblClinVar.1
Natural variantiVAR_0772382023G → R in AT; loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs11212587EnsemblClinVar.1
Natural variantiVAR_0108392063G → E in AT. Corresponds to variant dbSNP:rs866290641EnsemblClinVar.1
Natural variantiVAR_0108402067A → D in AT. 1 PublicationCorresponds to variant dbSNP:rs397514577EnsemblClinVar.1
Natural variantiVAR_0772392068L → S in AT; decreased protein abundance; loss of DNA damage induced protein autophosphorylation. 1 Publication1
Natural variantiVAR_0772402080Y → D in AT; loss of DNA damage induced protein autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs1064795467Ensembl.1
Natural variantiVAR_0108442218S → C in AT. 1 Publication1
Natural variantiVAR_0108452224 – 2227MALR → IS in AT. 4
Natural variantiVAR_0108462227R → C in AT. 1 PublicationCorresponds to variant dbSNP:rs564652222EnsemblClinVar.1
Natural variantiVAR_0108472246 – 2252CIKDILT → H in AT. 7
Natural variantiVAR_0108542424V → G in AT; also found in B-cell chronic lymphocytic leukemia and T-prolymphocytic leukemia; may be associated with increased risk for breast cancer; decreased phosphorylation of target proteins. 5 PublicationsCorresponds to variant dbSNP:rs28904921EnsemblClinVar.1
Natural variantiVAR_0108552427 – 2428Missing in AT; also found in T-prolymphocytic leukemia; lack of phosphorylation of target proteins. 4 Publications2
Natural variantiVAR_0108582470Y → D in AT. 1 PublicationCorresponds to variant dbSNP:rs876659365EnsemblClinVar.1
Natural variantiVAR_0108602491W → R in AT. 1 Publication1
Natural variantiVAR_0108612546 – 2548Missing in AT; also found in T-prolymphocytic leukemia and T-cell acute lymphoblastic leukemia; lack of phosphorylation of target proteins. 11 Publications3
Natural variantiVAR_0108622554H → D in AT; lack of phosphorylation of target proteins. 2 Publications1
Natural variantiVAR_0108642625 – 2626DA → EP in AT. Corresponds to variant dbSNP:rs267606668Ensembl.2
Natural variantiVAR_0108632625D → Q in AT; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_0772412627Y → H in AT; loss of protein expression. 1 Publication1
Natural variantiVAR_0108652656L → P in AT. 1 PublicationCorresponds to variant dbSNP:rs121434218EnsemblClinVar.1
Natural variantiVAR_0108662662Missing in AT. 1 Publication1
Natural variantiVAR_0108672663Missing in AT. 1
Natural variantiVAR_0108682668E → G in AT; unknown pathological significance; no effect on phosphorylation of target proteins. 2 Publications1
Natural variantiVAR_0108702702I → R in AT. Corresponds to variant dbSNP:rs876659735EnsemblClinVar.1
Natural variantiVAR_0108742726A → V in AT. 1
Natural variantiVAR_0108782824C → Y in AT. 1 PublicationCorresponds to variant dbSNP:rs876660927EnsemblClinVar.1
Natural variantiVAR_0108792827F → C in AT; mild; decreased phosphorylation of target proteins. 3 PublicationsCorresponds to variant dbSNP:rs121434216EnsemblClinVar.1
Natural variantiVAR_0108802829P → L in AT. 1 PublicationCorresponds to variant dbSNP:rs938431501EnsemblClinVar.1
Natural variantiVAR_0108812832R → C in AT; also found in B-cell non-Hodgkin lymphoma. 3 PublicationsCorresponds to variant dbSNP:rs587779872EnsemblClinVar.1
Natural variantiVAR_0772422834F → L in AT; decreased protein abundance. 1 Publication1
Natural variantiVAR_0108822849R → P in AT. 1 Publication1
Natural variantiVAR_0108842855 – 2856SV → RI in AT; lack of phosphorylation of target proteins. 1 PublicationCorresponds to variant dbSNP:rs587781353Ensembl.2
Natural variantiVAR_0108832855S → R in AT. Corresponds to variant dbSNP:rs780905851EnsemblClinVar.1
Natural variantiVAR_0108852860Missing in AT. 2 Publications1
Natural variantiVAR_0108862867G → R in AT. 2 Publications1
Natural variantiVAR_0108892904E → G in AT. 1 PublicationCorresponds to variant dbSNP:rs786202826EnsemblClinVar.1
Natural variantiVAR_0108902909R → G in AT. 1 Publication1
Natural variantiVAR_0772433003N → D in AT; decreased protein abundance. 4 PublicationsCorresponds to variant dbSNP:rs1137889Ensembl.1
Natural variantiVAR_0108933008R → C in AT; also found in T-prolymphocytic leukemia and mantle cell lymphoma; lack of phosphorylation of target proteins. 6 PublicationsCorresponds to variant dbSNP:rs587782292EnsemblClinVar.1
Defects in ATM may contribute to T-cell acute lymphoblastic leukemia (TALL) and T-prolymphocytic leukemia (TPLL). TPLL is characterized by a high white blood cell count, with a predominance of prolymphocytes, marked splenomegaly, lymphadenopathy, skin lesions and serous effusion. The clinical course is highly aggressive, with poor response to chemotherapy and short survival time. TPLL occurs both in adults as a sporadic disease and in younger AT patients.5 Publications
Defects in ATM may contribute to B-cell non-Hodgkin lymphomas (BNHL), including mantle cell lymphoma (MCL).3 Publications
Defects in ATM may contribute to B-cell chronic lymphocytic leukemia (BCLL). BCLL is the commonest form of leukemia in the elderly. It is characterized by the accumulation of mature CD5+ B-lymphocytes, lymphadenopathy, immunodeficiency and bone marrow failure.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi367S → A: Loss of IR-induced S-367 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-1893 nor S-1981 autophosphorylation. 1 Publication1
Mutagenesisi1807K → E: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi1893S → A: Loss of IR-induced S-1893 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1981 autophosphorylation. 1 Publication1
Mutagenesisi1941V → L: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi1981S → A: Loss of IR-induced S-1981 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1893 autophosphorylation. No dimer disruption. 2 Publications1
Mutagenesisi1981S → D or E: Disrupts the dimer. 2 Publications1
Mutagenesisi2019Y → C: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2039E → K: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi2338L → P: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2394S → L: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2452L → P: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2685S → T: No effect on phosphorylation of target proteins. 1 Publication1
Mutagenesisi2699P → L: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2708D → N: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi2730Q → P: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2870D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi2875N → K: Loss of kinase activity. 1 Publication1
Mutagenesisi3016K → R: Loss of DNA damage-inducible acetylation. Retains constitutive kinase activity, but blocks DNA damage-induced kinase activation. Disrupts dimer and abolishes S-1981 autophosphorylation. 1 Publication1
Mutagenesisi3018K → R: Retains DNA damage-inducible acetylation and S-1981 autophosphorylation. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Tumor suppressor

Organism-specific databases

DisGeNETi472
GeneReviewsiATM
MalaCardsiATM
MIMi208900 phenotype
OpenTargetsiENSG00000149311
Orphaneti100 Ataxia-telangiectasia
370109 Ataxia-telangiectasia variant
67038 B-cell chronic lymphocytic leukemia
370114 Combined cervical dystonia
52416 Mantle cell lymphoma
PharmGKBiPA61

Chemistry databases

ChEMBLiCHEMBL3797
DrugBankiDB00201 Caffeine
GuidetoPHARMACOLOGYi1934

Polymorphism and mutation databases

BioMutaiATM
DMDMi317373479

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000888402 – 3056Serine-protein kinase ATMAdd BLAST3055

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei367Phosphoserine; by autocatalysis1 Publication1
Modified residuei1893Phosphoserine; by autocatalysis1 Publication1
Modified residuei1981Phosphoserine; by autocatalysisCombined sources4 Publications1
Modified residuei1983PhosphoserineCombined sources1
Modified residuei2996PhosphoserineCombined sources1
Modified residuei3016N6-acetyllysine1 Publication1

Post-translational modificationi

Phosphorylated by NUAK1/ARK5. Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA damage-mediated activation of the kinase.5 Publications
Acetylation, on DNA damage, is required for activation of the kinase activity, dimer-monomer transition, and subsequent autophosphorylation on Ser-1981. Acetylated in vitro by KAT5/TIP60.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13315
MaxQBiQ13315
PaxDbiQ13315
PeptideAtlasiQ13315
PRIDEiQ13315
ProteomicsDBi59303

PTM databases

iPTMnetiQ13315
PhosphoSitePlusiQ13315

Expressioni

Tissue specificityi

Found in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, spleen, thymus, testis, ovary, small intestine, colon and leukocytes.

Inductioni

By ionizing radiation.

Gene expression databases

BgeeiENSG00000149311 Expressed in 229 organ(s), highest expression level in corpus callosum
CleanExiHS_ATM
ExpressionAtlasiQ13315 baseline and differential
GenevisibleiQ13315 HS

Organism-specific databases

HPAiCAB000102
HPA067142

Interactioni

Subunit structurei

Dimers or tetramers in inactive state. On DNA damage, autophosphorylation dissociates ATM into monomers rendering them catalytically active. Binds p53/TP53, ABL1, BRCA1, NBN/nibrin and TERF1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with RAD17; DNA damage promotes the association. Interacts with EEF1E1; the interaction, induced on DNA damage, up-regulates TP53. Interacts with DCLRE1C, KAT8, KAT5, NABP2, ATMIN and CEP164. Interacts with AP2B1 and AP3B2; the interaction occurs in cytoplasmic vesicles (By similarity). Interacts with TELO2 and TTI1. Interacts with DDX1. Interacts with BRAT1.By similarity18 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi106962, 195 interactors
CORUMiQ13315
DIPiDIP-182N
IntActiQ13315, 82 interactors
MINTiQ13315
STRINGi9606.ENSP00000278616

Chemistry databases

BindingDBiQ13315

Structurei

3D structure databases

ProteinModelPortaliQ13315
SMRiQ13315
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1960 – 2566FATPROSITE-ProRule annotationAdd BLAST607
Domaini2712 – 2962PI3K/PI4KPROSITE-ProRule annotationAdd BLAST251
Domaini3024 – 3056FATCPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1373 – 1382Interaction with ABL11 Publication10

Domaini

The FATC domain is required for interaction with KAT5.

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family. ATM subfamily.Curated

Phylogenomic databases

eggNOGiKOG0892 Eukaryota
ENOG410XNPY LUCA
GeneTreeiENSGT00670000098061
HOVERGENiHBG004304
InParanoidiQ13315
KOiK04728
OMAiYTLIHYI
OrthoDBiEOG091G002B
PhylomeDBiQ13315
TreeFamiTF101182

Family and domain databases

Gene3Di1.10.1070.11, 1 hit
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR015519 ATM
IPR003152 FATC_dom
IPR011009 Kinase-like_dom_sf
IPR000403 PI3/4_kinase_cat_dom
IPR036940 PI3/4_kinase_cat_sf
IPR018936 PI3/4_kinase_CS
IPR003151 PIK-rel_kinase_FAT
IPR014009 PIK_FAT
IPR021668 TAN
PANTHERiPTHR11139:SF96 PTHR11139:SF96, 1 hit
PfamiView protein in Pfam
PF02259 FAT, 1 hit
PF02260 FATC, 1 hit
PF00454 PI3_PI4_kinase, 1 hit
PF11640 TAN, 1 hit
SMARTiView protein in SMART
SM01343 FATC, 1 hit
SM00146 PI3Kc, 1 hit
SM01342 TAN, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51189 FAT, 1 hit
PS51190 FATC, 1 hit
PS00915 PI3_4_KINASE_1, 1 hit
PS00916 PI3_4_KINASE_2, 1 hit
PS50290 PI3_4_KINASE_3, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All

Q13315-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLVLNDLLI CCRQLEHDRA TERKKEVEKF KRLIRDPETI KHLDRHSDSK 
        60         70         80         90        100
QGKYLNWDAV FRFLQKYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL 
       110        120        130        140        150
VKYFIKCANR RAPRLKCQEL LNYIMDTVKD SSNGAIYGAD CSNILLKDIL 
       160        170        180        190        200
SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ DVHRVLVARI IHAVTKGCCS 
       210        220        230        240        250
QTDGLNSKFL DFFSKAIQCA RQEKSSSGLN HILAALTIFL KTLAVNFRIR 
       260        270        280        290        300
VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK 
       310        320        330        340        350
GAYESTKWRS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA 
       360        370        380        390        400
DICHQVFNED TRSLEISQSY TTTQRESSDY SVPCKRKKIE LGWEVIKDHL 
       410        420        430        440        450
QKSQNDFDLV PWLQIATQLI SKYPASLPNC ELSPLLMILS QLLPQQRHGE 
       460        470        480        490        500
RTPYVLRCLT EVALCQDKRS NLESSQKSDL LKLWNKIWCI TFRGISSEQI 
       510        520        530        540        550
QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACRPSCPAVC CLTLALTTSI 
       560        570        580        590        600
VPGTVKMGIE QNMCEVNRSF SLKESIMKWL LFYQLEGDLE NSTEVPPILH 
       610        620        630        640        650
SNFPHLVLEK ILVSLTMKNC KAAMNFFQSV PECEHHQKDK EELSFSEVEE 
       660        670        680        690        700
LFLQTTFDKM DFLTIVRECG IEKHQSSIGF SVHQNLKESL DRCLLGLSEQ 
       710        720        730        740        750
LLNNYSSEIT NSETLVRCSR LLVGVLGCYC YMGVIAEEEA YKSELFQKAK 
       760        770        780        790        800
SLMQCAGESI TLFKNKTNEE FRIGSLRNMM QLCTRCLSNC TKKSPNKIAS 
       810        820        830        840        850
GFFLRLLTSK LMNDIADICK SLASFIKKPF DRGEVESMED DTNGNLMEVE 
       860        870        880        890        900
DQSSMNLFND YPDSSVSDAN EPGESQSTIG AINPLAEEYL SKQDLLFLDM 
       910        920        930        940        950
LKFLCLCVTT AQTNTVSFRA ADIRRKLLML IDSSTLEPTK SLHLHMYLML 
       960        970        980        990       1000
LKELPGEEYP LPMEDVLELL KPLSNVCSLY RRDQDVCKTI LNHVLHVVKN 
      1010       1020       1030       1040       1050
LGQSNMDSEN TRDAQGQFLT VIGAFWHLTK ERKYIFSVRM ALVNCLKTLL 
      1060       1070       1080       1090       1100
EADPYSKWAI LNVMGKDFPV NEVFTQFLAD NHHQVRMLAA ESINRLFQDT 
      1110       1120       1130       1140       1150
KGDSSRLLKA LPLKLQQTAF ENAYLKAQEG MREMSHSAEN PETLDEIYNR 
      1160       1170       1180       1190       1200
KSVLLTLIAV VLSCSPICEK QALFALCKSV KENGLEPHLV KKVLEKVSET 
      1210       1220       1230       1240       1250
FGYRRLEDFM ASHLDYLVLE WLNLQDTEYN LSSFPFILLN YTNIEDFYRS 
      1260       1270       1280       1290       1300
CYKVLIPHLV IRSHFDEVKS IANQIQEDWK SLLTDCFPKI LVNILPYFAY 
      1310       1320       1330       1340       1350
EGTRDSGMAQ QRETATKVYD MLKSENLLGK QIDHLFISNL PEIVVELLMT 
      1360       1370       1380       1390       1400
LHEPANSSAS QSTDLCDFSG DLDPAPNPPH FPSHVIKATF AYISNCHKTK 
      1410       1420       1430       1440       1450
LKSILEILSK SPDSYQKILL AICEQAAETN NVYKKHRILK IYHLFVSLLL 
      1460       1470       1480       1490       1500
KDIKSGLGGA WAFVLRDVIY TLIHYINQRP SCIMDVSLRS FSLCCDLLSQ 
      1510       1520       1530       1540       1550
VCQTAVTYCK DALENHLHVI VGTLIPLVYE QVEVQKQVLD LLKYLVIDNK 
      1560       1570       1580       1590       1600
DNENLYITIK LLDPFPDHVV FKDLRITQQK IKYSRGPFSL LEEINHFLSV 
      1610       1620       1630       1640       1650
SVYDALPLTR LEGLKDLRRQ LELHKDQMVD IMRASQDNPQ DGIMVKLVVN 
      1660       1670       1680       1690       1700
LLQLSKMAIN HTGEKEVLEA VGSCLGEVGP IDFSTIAIQH SKDASYTKAL 
      1710       1720       1730       1740       1750
KLFEDKELQW TFIMLTYLNN TLVEDCVKVR SAAVTCLKNI LATKTGHSFW 
      1760       1770       1780       1790       1800
EIYKMTTDPM LAYLQPFRTS RKKFLEVPRF DKENPFEGLD DINLWIPLSE 
      1810       1820       1830       1840       1850
NHDIWIKTLT CAFLDSGGTK CEILQLLKPM CEVKTDFCQT VLPYLIHDIL 
      1860       1870       1880       1890       1900
LQDTNESWRN LLSTHVQGFF TSCLRHFSQT SRSTTPANLD SESEHFFRCC 
      1910       1920       1930       1940       1950
LDKKSQRTML AVVDYMRRQK RPSSGTIFND AFWLDLNYLE VAKVAQSCAA 
      1960       1970       1980       1990       2000
HFTALLYAEI YADKKSMDDQ EKRSLAFEEG SQSTTISSLS EKSKEETGIS 
      2010       2020       2030       2040       2050
LQDLLLEIYR SIGEPDSLYG CGGGKMLQPI TRLRTYEHEA MWGKALVTYD 
      2060       2070       2080       2090       2100
LETAIPSSTR QAGIIQALQN LGLCHILSVY LKGLDYENKD WCPELEELHY 
      2110       2120       2130       2140       2150
QAAWRNMQWD HCTSVSKEVE GTSYHESLYN ALQSLRDREF STFYESLKYA 
      2160       2170       2180       2190       2200
RVKEVEEMCK RSLESVYSLY PTLSRLQAIG ELESIGELFS RSVTHRQLSE 
      2210       2220       2230       2240       2250
VYIKWQKHSQ LLKDSDFSFQ EPIMALRTVI LEILMEKEMD NSQRECIKDI 
      2260       2270       2280       2290       2300
LTKHLVELSI LARTFKNTQL PERAIFQIKQ YNSVSCGVSE WQLEEAQVFW 
      2310       2320       2330       2340       2350
AKKEQSLALS ILKQMIKKLD ASCAANNPSL KLTYTECLRV CGNWLAETCL 
      2360       2370       2380       2390       2400
ENPAVIMQTY LEKAVEVAGN YDGESSDELR NGKMKAFLSL ARFSDTQYQR 
      2410       2420       2430       2440       2450
IENYMKSSEF ENKQALLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEL 
      2460       2470       2480       2490       2500
ALRALKEDRK RFLCKAVENY INCLLSGEEH DMWVFRLCSL WLENSGVSEV 
      2510       2520       2530       2540       2550
NGMMKRDGMK IPTYKFLPLM YQLAARMGTK MMGGLGFHEV LNNLISRISM 
      2560       2570       2580       2590       2600
DHPHHTLFII LALANANRDE FLTKPEVARR SRITKNVPKQ SSQLDEDRTE 
      2610       2620       2630       2640       2650
AANRIICTIR SRRPQMVRSV EALCDAYIIL ANLDATQWKT QRKGINIPAD 
      2660       2670       2680       2690       2700
QPITKLKNLE DVVVPTMEIK VDHTGEYGNL VTIQSFKAEF RLAGGVNLPK 
      2710       2720       2730       2740       2750
IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL 
      2760       2770       2780       2790       2800
TICTYKVVPL SQRSGVLEWC TGTVPIGEFL VNNEDGAHKR YRPNDFSAFQ 
      2810       2820       2830       2840       2850
CQKKMMEVQK KSFEEKYEVF MDVCQNFQPV FRYFCMEKFL DPAIWFEKRL 
      2860       2870       2880       2890       2900
AYTRSVATSS IVGYILGLGD RHVQNILINE QSAELVHIDL GVAFEQGKIL 
      2910       2920       2930       2940       2950
PTPETVPFRL TRDIVDGMGI TGVEGVFRRC CEKTMEVMRN SQETLLTIVE 
      2960       2970       2980       2990       3000
VLLYDPLFDW TMNPLKALYL QQRPEDETEL HPTLNADDQE CKRNLSDIDQ 
      3010       3020       3030       3040       3050
SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAI DPKNLSRLFP 

GWKAWV
Length:3,056
Mass (Da):350,687
Last modified:January 22, 2014 - v4
Checksum:iC0B4866E1E3199E2
GO

Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PIN0E9PIN0_HUMAN
Serine-protein kinase ATM
ATM
1,369Annotation score:
M0QXY8M0QXY8_HUMAN
Serine-protein kinase ATM
ATM
135Annotation score:
E9PRG7E9PRG7_HUMAN
Serine-protein kinase ATM
ATM
93Annotation score:
H0YDU7H0YDU7_HUMAN
Serine-protein kinase ATM
ATM
155Annotation score:
E9PIQ5E9PIQ5_HUMAN
Serine-protein kinase ATM
ATM
154Annotation score:
A0A087X0E9A0A087X0E9_HUMAN
Serine-protein kinase ATM
ATM
168Annotation score:
Q6P7P1Q6P7P1_HUMAN
ATM protein
ATM
112Annotation score:
H0YEC6H0YEC6_HUMAN
Serine-protein kinase ATM
ATM
77Annotation score:

Sequence cautioni

The sequence AAA86520 differs from that shown. Probable cloning artifact.Curated
The sequence AAA86520 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI37170 differs from that shown. Probable cloning artifact.Curated
The sequence AAI37170 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW67111 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46H → N in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti56N → I in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti313Y → N in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti488W → G in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti554T → A in AAC50289 (PubMed:8589678).Curated1
Sequence conflicti750K → N in AAC50289 (PubMed:8589678).Curated1
Sequence conflicti754Q → K in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti887E → G in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti1003Q → L in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti1049L → W in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti1089A → V in CAA62603 (PubMed:8789452).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04154523R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587779858EnsemblClinVar.1
Natural variantiVAR_05667845R → W. Corresponds to variant dbSNP:rs3218684EnsemblClinVar.1
Natural variantiVAR_01079849S → C5 PublicationsCorresponds to variant dbSNP:rs1800054EnsemblClinVar.1
Natural variantiVAR_010799126D → E2 PublicationsCorresponds to variant dbSNP:rs2234997EnsemblClinVar.1
Natural variantiVAR_041546140D → H1 PublicationCorresponds to variant dbSNP:rs55633650EnsemblClinVar.1
Natural variantiVAR_010800182V → L1 PublicationCorresponds to variant dbSNP:rs3218707EnsemblClinVar.1
Natural variantiVAR_010801224K → E in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs145053092EnsemblClinVar.1
Natural variantiVAR_041547250R → Q1 PublicationCorresponds to variant dbSNP:rs56123940EnsemblClinVar.1
Natural variantiVAR_010802292P → L in AT; associated with lymphoma; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs747727055EnsemblClinVar.1
Natural variantiVAR_010803323I → V in AT; loss of protein expression. 2 PublicationsCorresponds to variant dbSNP:rs587781511EnsemblClinVar.1
Natural variantiVAR_010804332Y → C in B-cell chronic lymphocytic leukemia. 1 Publication1
Natural variantiVAR_041548333S → F1 PublicationCorresponds to variant dbSNP:rs28904919EnsemblClinVar.1
Natural variantiVAR_041549337R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs138398778EnsemblClinVar.1
Natural variantiVAR_041550337R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs202160435EnsemblClinVar.1
Natural variantiVAR_010805350A → T in B-cell chronic lymphocytic leukemia. 1 PublicationCorresponds to variant dbSNP:rs371713984EnsemblClinVar.1
Natural variantiVAR_010806352I → T in B-cell chronic lymphocytic leukemia. 1 PublicationCorresponds to variant dbSNP:rs369203092EnsemblClinVar.1
Natural variantiVAR_041551410V → A1 PublicationCorresponds to variant dbSNP:rs56128736EnsemblClinVar.1
Natural variantiVAR_041552504N → S1 PublicationCorresponds to variant dbSNP:rs56365018EnsemblClinVar.1
Natural variantiVAR_010807514G → D2 PublicationsCorresponds to variant dbSNP:rs2235000EnsemblClinVar.1
Natural variantiVAR_041553540C → Y in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041554546L → V Polymorphism; no effect on phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs2227924EnsemblClinVar.1
Natural variantiVAR_010808570F → S in AT. 1 PublicationCorresponds to variant dbSNP:rs777301065Ensembl.1
Natural variantiVAR_041555582F → L1 PublicationCorresponds to variant dbSNP:rs2235006EnsemblClinVar.1
Natural variantiVAR_010809705 – 707YSS → FIP in AT; might be associated with susceptibility to cancer. 3
Natural variantiVAR_010810707S → P2 PublicationsCorresponds to variant dbSNP:rs4986761EnsemblClinVar.1
Natural variantiVAR_056679761T → S. Corresponds to variant dbSNP:rs2235011EnsemblClinVar.1
Natural variantiVAR_010812768N → D in AT. 1 Publication1
Natural variantiVAR_010813785R → C in AT. 1 PublicationCorresponds to variant dbSNP:rs587778065EnsemblClinVar.1
Natural variantiVAR_056680788S → R. Corresponds to variant dbSNP:rs641252EnsemblClinVar.1
Natural variantiVAR_056681814D → E. Corresponds to variant dbSNP:rs3218695EnsemblClinVar.1
Natural variantiVAR_041556848E → Q in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_010814858F → L Rare polymorphism. 6 PublicationsCorresponds to variant dbSNP:rs1800056EnsemblClinVar.1
Natural variantiVAR_041557872P → S1 PublicationCorresponds to variant dbSNP:rs3218673EnsemblClinVar.1
Natural variantiVAR_041558924R → W1 PublicationCorresponds to variant dbSNP:rs55723361EnsemblClinVar.1
Natural variantiVAR_041559935T → A1 PublicationCorresponds to variant dbSNP:rs35813135EnsemblClinVar.1
Natural variantiVAR_056682935T → M. Corresponds to variant dbSNP:rs3218708EnsemblClinVar.1
Natural variantiVAR_056683942L → F. Corresponds to variant dbSNP:rs3218688EnsemblClinVar.1
Natural variantiVAR_010815950L → R in AT. Corresponds to variant dbSNP:rs786203054EnsemblClinVar.1
Natural variantiVAR_0108161001L → Q in AT; associated with T-cell acute lymphoblastic leukemia. 1 Publication1
Natural variantiVAR_0108171040M → V Found in B-cell non-Hodgkin lymphoma; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs3092857EnsemblClinVar.1
Natural variantiVAR_0772371046L → P in AT; loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs568461905EnsemblClinVar.1
Natural variantiVAR_0108181054P → R Polymorphism; no effect on phosphorylation of target proteins. 9 PublicationsCorresponds to variant dbSNP:rs1800057EnsemblClinVar.1
Natural variantiVAR_0108191082H → L in AT. 1
Natural variantiVAR_0108201091E → D in AT. 1 Publication1
Natural variantiVAR_0415601179S → F in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0566841313E → Q. Corresponds to variant dbSNP:rs3092841EnsemblClinVar.1
Natural variantiVAR_0415611321M → I1 PublicationCorresponds to variant dbSNP:rs35184530EnsemblClinVar.1
Natural variantiVAR_0803001322L → I Polymorphism; no effect on phosphorylation of target proteins. 1 PublicationCorresponds to variant dbSNP:rs144535256EnsemblClinVar.1
Natural variantiVAR_0415621380H → Y1 PublicationCorresponds to variant dbSNP:rs3092856EnsemblClinVar.1
Natural variantiVAR_0415631382P → S1 PublicationCorresponds to variant dbSNP:rs55859590EnsemblClinVar.1
Natural variantiVAR_0108211407I → T in T-prolymphocytic leukemia. 1 PublicationCorresponds to variant dbSNP:rs1234250980Ensembl.1
Natural variantiVAR_0108221420L → F Rare polymorphism. 4 PublicationsCorresponds to variant dbSNP:rs1800058EnsemblClinVar.1
Natural variantiVAR_0108231420L → P in AT. 1 Publication1
Natural variantiVAR_0566851427A → T. Corresponds to variant dbSNP:rs2229021EnsemblClinVar.1
Natural variantiVAR_0108241454K → N1 PublicationCorresponds to variant dbSNP:rs148993589EnsemblClinVar.1
Natural variantiVAR_0108251463F → S Found in B-cell non-Hodgkin lymphoma; unknown pathological significance. 1 Publication1
Natural variantiVAR_0108261465L → P in AT; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs730881391EnsemblClinVar.1
Natural variantiVAR_0415641469I → M in a renal papillary cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs775047783Ensembl.1
Natural variantiVAR_0415651475Y → C1 Publication